|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-1858 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1433.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 2 QDLSQRLAALSPEKRALLKQQLGKQGSRFNTFP------------LSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRV 69
Cdd:PRK12467 7 LRIARRFITLPLEKRRLYLEKMQEEGVSFANLPipqvrsaferipLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 70 DLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLIDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLA 149
Cdd:PRK12467 87 SALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 150 LLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQ 229
Cdd:PRK12467 167 LLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 230 LADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANR 309
Cdd:PRK12467 247 LGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 310 NRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLP- 388
Cdd:PRK12467 327 NRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTAt 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 389 ----DLHDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDAIRLELVYNTDLFKhERMLEMLEQY--SCLASQVSERDEMIS 462
Cdd:PRK12467 407 ggrdREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFE-ATTIERLATHwrNLLEAIVAEPRRRLG 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 463 RYSLV-STRASSVLPDPGAPISAHWEGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVV 541
Cdd:PRK12467 486 ELPLLdAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLV 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 542 AISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLriegaTDCQELDEWCRANSYCNLVLARNFAL 621
Cdd:PRK12467 566 GIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL-----TQSHLLAQLPVPAGLRSLCLDEPADL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 622 sgiLSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFT 701
Cdd:PRK12467 641 ---LCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFG 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 702 PLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQgmgedDLPSARIPSLRYAFVVGDALTRRHVARLY 781
Cdd:PRK12467 718 ALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ-----ASRVALPRPQRALVCGGEALQVDLLARVR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 782 AVAPHITCVNLYGSTETQRAVSYFVLPTASstespasvtalLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRS 861
Cdd:PRK12467 793 ALGPGARLINHYGPTETTVGVSTYELSDEE-----------RDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGG 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 862 PHLAFGYLDDPDQTNERFLVNPFTHQeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVAD 941
Cdd:PRK12467 862 AGLARGYHRRPALTAERFVPDPFGAD-GGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 942 AAVIIREDTPDNkQIVAYI--THHNEQVKP--VLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAAD 1017
Cdd:PRK12467 941 AVVLAQPGDAGL-QLVAYLvpAAVADGAEHqaTRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASA 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1018 EATLSLAtPQSPIQEELCLLWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASLIT 1097
Cdd:PRK12467 1020 VQATFVA-PQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVA 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1098 vsssskqelkepvLQAQAKRESEPKGPQRIFLderhgskmeqeesylfAASFAQERLWFLHRFEPESSAYHLFLAFELDG 1177
Cdd:PRK12467 1099 -------------AQQQGAQPALPDVDRDQPL----------------PLSYAQERQWFLWQLEPGSAAYHIPQALRLKG 1149
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1178 QFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQHLSLPAESESSLSqqalqAWLQQEIRRPFDLQQ 1257
Cdd:PRK12467 1150 PLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDEAQLK-----VYVEAEARQPFDLEQ 1224
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1258 APLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGISPQLAPLPLQYADYAVWQRAWLQEERQEKL 1337
Cdd:PRK12467 1225 GPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQ 1304
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1338 QRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVV 1417
Cdd:PRK12467 1305 LAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRV 1384
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1418 GTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFF 1497
Cdd:PRK12467 1385 GVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMF 1464
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1498 ALQ-NVPGDPISLEGLDVTQIRLDSNSAKFDLSWTWYqEDEKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRT 1576
Cdd:PRK12467 1465 NHQrDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTY-ESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPER 1543
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1577 PVSLLPLLSAAQRLHLLsLGHSSSPLPAAPSCGLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIG 1656
Cdd:PRK12467 1544 RLGELDLLDEAERRQIL-EGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVG 1622
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1657 PGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHEELKARWPHCP-CPLLCLDTLQER 1735
Cdd:PRK12467 1623 PEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDgLRSLVLDQEDDW 1702
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1736 YASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLL 1815
Cdd:PRK12467 1703 LEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLI 1782
|
1850 1860 1870 1880
....*....|....*....|....*....|....*....|...
gi 1574832895 1816 AGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLE 1858
Cdd:PRK12467 1783 NGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQ 1825
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-1851 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1173.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 7 RLAALSPEKRALLKQQLGKQG-----SRFNTFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVR 81
Cdd:PRK05691 645 TLAAFSAAVARQLAGGGAAQAaiarlPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 82 RHESLRTTFAMLNGEPIQVIRPNLTLQIPLIDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILL 161
Cdd:PRK05691 725 RHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLL 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 162 LNTHHIISDGWSLGVFLHELSLCYSAALAGNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPM 241
Cdd:PRK05691 805 VTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELAT 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 242 DHPRPAVQTSHGAVVSLLLPSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFF 321
Cdd:PRK05691 885 DHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFF 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 322 VNTLVLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPFDALLDELNPERSLShslLFQVFFN--MVNLPDLHdEWPDLKV 399
Cdd:PRK05691 965 INTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG---LFQVMFNhqQRDLSALR-RLPGLLA 1040
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 400 EHL-W-PREigSKFDLTLFVQEE-QDAIRLELVYNTDLFKHERMLEMLEQYSCLASQVSERDEM-ISRYSLVSTRASSVL 475
Cdd:PRK05691 1041 EELpWhSRE--AKFDLQLHSEEDrNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRaLGDVQLLDAAERAQL 1118
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 476 PDPGAPISAHWEGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAI 555
Cdd:PRK05691 1119 AQWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGL 1198
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 556 LGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLriegaTDCQELDEWCRANSYCNLVLArnfalSGILSQYASSAPAY 635
Cdd:PRK05691 1199 LAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL-----TQSHLLERLPQAEGVSAIALD-----SLHLDSWPSQAPGL 1268
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 636 RVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQE 715
Cdd:PRK05691 1269 HLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPG 1348
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 716 HMGDPGWLAQWMQGQEITIASFTPALLQLLTqgmgeDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGS 795
Cdd:PRK05691 1349 EHRDPQRIAELVQQYGVTTLHFVPPLLQLFI-----DEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGP 1423
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 796 TETQRAVSYFVLPTAsstespasvtallDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQT 875
Cdd:PRK05691 1424 TETAINVTHWQCQAE-------------DGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALT 1490
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 876 NERFLVNPFThQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTpDNKQ 955
Cdd:PRK05691 1491 AERFVPDPLG-EDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGA-AGAQ 1568
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 956 IVAYITHHNEQVKPVLSnLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPeaaDEATLSLATPQSPIQEELC 1035
Cdd:PRK05691 1569 LVGYYTGEAGQEAEAER-LKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEP---VWQQREHVEPRTELQQQIA 1644
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1036 LLWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIAslitvsssskqelkEPVLQAQA 1115
Cdd:PRK05691 1645 AIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFA--------------EQVARIQA 1710
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1116 KRESEPKGP-QRIflDERHGSKMeqeesylfaaSFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLAR 1194
Cdd:PRK05691 1711 AGERNSQGAiARV--DRSQPVPL----------SYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILR 1778
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1195 HESLRTSFVLQGEQLMQRIHAQLWLSLSQQHLS-LPAESESSlsqqALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPS 1273
Cdd:PRK05691 1779 HETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSaLPADARQQ----RLQQLADSEAHQPFDLERGPLLRACLVKAAEREH 1854
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1274 ILLLCLHHIIADGWSLGILLQELSLCYNAHVKGISPQLAPLPLQYADYAVWQRAWLQE-ERQEKLQrYWHGQLATAPALL 1352
Cdd:PRK05691 1855 YFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESgERQRQLD-YWKAQLGNEHPLL 1933
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1353 DLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGV 1432
Cdd:PRK05691 1934 ELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGL 2013
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1433 IGLFANTLVLRTDLSGDPSFLELLQRVREVTLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVP-GDPISLEG 1511
Cdd:PRK05691 2014 IGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLAG 2093
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1512 LDVTQIRLDSNSAKFDLSWTWYQEDEKsLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLH 1591
Cdd:PRK05691 2094 MTVEYLVNDARATKFDLNLEVTDLDGR-LGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQ 2172
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1592 LL-SLGhsSSPLPAAPSCGLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPS 1670
Cdd:PRK05691 2173 LLdSLA--GEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLE 2250
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1671 LLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHEEL----------KARWphcpcpllCLDTLQERYASLP 1740
Cdd:PRK05691 2251 MVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALfealgelpagVARW--------CLEDDAAALAAYS 2322
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1741 CEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQI 1820
Cdd:PRK05691 2323 DAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARV 2402
|
1850 1860 1870
....*....|....*....|....*....|.
gi 1574832895 1821 QLASQEQAsDPRQLASLLAQLPISILQATPT 1851
Cdd:PRK05691 2403 VLRAQGQW-GAEEICQLIREQQVSILGFTPS 2432
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-1858 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 954.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 80 VRRHESLRTTFAMLNG--EPIQVIRPNLtlQIPLIDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLE 157
Cdd:PRK12316 1603 VDRHEILRSGFLWQDGleQPLQVIHKQV--ELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGR 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 158 HILLLNTHHIISDGWSLGVFLHELSLCYsaalAGNSPtlPAPSLQYADYAAW--QRNWLKGENltnlldYWRKQLA--DM 233
Cdd:PRK12316 1681 HHLIYTNHHILMDGWSNAQLLGEVLQRY----AGQPV--AAPGGRYRDYIAWlqRQDAAASEA------FWKEQLAalEE 1748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 234 PPLLelpMDHPRPAVQTSHGAVVSLLLPSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANR--NR 311
Cdd:PRK12316 1749 PTRL---AQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRpaEL 1825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 312 TDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPF-----------DALLDelnperslshSLLfqV 380
Cdd:PRK12316 1826 PGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLydiqrwagqggEALFD----------SLL--V 1893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 381 FFNMVNLPDLHDEWP-DLKVEHLWPREiGSKFDLTLFVqEEQDAIRLELVYNTDLFKH---ERM----LEMLEQYSCLAS 452
Cdd:PRK12316 1894 FENYPVAEALKQGAPaGLVFGRVSNHE-QTNYPLTLAV-TLGETLSLQYSYDRGHFDAaaiERLdrhlLHLLEQMAEDAQ 1971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 453 Q---------VSERDEMISRYSlvstRASSVLP-DPGapisahwegtIHDLFAQQAHLRPENIAIIDEINTVSYGELEAR 522
Cdd:PRK12316 1972 AalgelalldAGERQRILADWD----RTPEAYPrGPG----------VHQRIAEQAARAPEAIAVVFGDQHLSYAELDSR 2037
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 523 SNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLeYVQRAHARGWLriegATDCQELD 602
Cdd:PRK12316 2038 ANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA-YMLEDSGAALL----LTQRHLLE 2112
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 603 EWCRANSYCNLVLARNFALSGilsqYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTD 682
Cdd:PRK12316 2113 RLPLPAGVARLPLDRDAEWAD----YPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPAD 2188
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 683 RYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMgDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPsariPSL 762
Cdd:PRK12316 2189 CELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRP----PAV 2263
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 763 RYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETqravsyFVLPTA--SSTESPAsvtallDKEVIPLGKGMPGAQIL 840
Cdd:PRK12316 2264 RVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEA------VVTPLLwkCRPQDPC------GAAYVPIGRALGNRRAY 2331
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 841 ILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIR 920
Cdd:PRK12316 2332 ILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAS-GERLYRTGDLARYRADGVVEYLGRIDHQVKIR 2410
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 921 GYRIELEEIEAILVEHPMVADAAVIIReDTPDNKQIVAYITHHNEQvKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLN 1000
Cdd:PRK12316 2411 GFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAA-EDLLAELRAWLAARLPAYMVPAHWVVLERLPLN 2488
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1001 ANGKVDRKALPAPEAADEATLSLAtPQSPIQEELCLLWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKFNSTLSL 1080
Cdd:PRK12316 2489 PNGKLDRKALPKPDVSQLRQAYVA-PQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPL 2567
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1081 RSLFEAPTIEGIASLITVSSSSKQELKEPVLQAQAkresepkgpqriflderhgskmeqeesylFAASFAQERLWFLHRF 1160
Cdd:PRK12316 2568 RILFERPTLAAFAASLESGQTSRAPVLQKVTRVQP-----------------------------LPLSHAQQRQWFLWQL 2618
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1161 EPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQHLSLPAESesslsqqA 1240
Cdd:PRK12316 2619 EPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADA-------A 2691
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1241 LQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGISPQLAPLPLQYAD 1320
Cdd:PRK12316 2692 IRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYAD 2771
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1321 YAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVLSHQQQVTLYMTLLA 1400
Cdd:PRK12316 2772 YAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLA 2851
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1401 AFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQAYSQQDMPFEKLVAE 1480
Cdd:PRK12316 2852 SFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEA 2931
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1481 LQPERSLAYNPLFQVFFALQNVPGDPISLEGLDVTQIRLDSNSAKFDLSWTWYqEDEKSLSAVIEYNTALFEPQRIAGMA 1560
Cdd:PRK12316 2932 LQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTW-ESAEGLGASLTYATDLFDARTVERLA 3010
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1561 TNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLL-SLGHSSSPLPAAPscGLHHLIEAQCERSSLQPALHAGSTTLTYRQL 1639
Cdd:PRK12316 3011 RHWQNLLRGMVENPQRSVDELAMLDAEERGQLLeAWNATAAEYPLER--GVHRLFEEQVERTPDAVALAFGEQRLSYAEL 3088
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1640 NQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHEELkaRW 1719
Cdd:PRK12316 3089 NRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHL--RL 3166
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1720 PHCP-CPLLCLDTLQERYASlpcEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAI 1798
Cdd:PRK12316 3167 PLAQgVQVLDLDRGDENYAE---ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQF 3243
|
1770 1780 1790 1800 1810 1820
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1799 TSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLE 1858
Cdd:PRK12316 3244 TTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE 3303
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
34-1397 |
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: 911.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLID 113
Cdd:COG1020 19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 114 LTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNS 193
Cdd:COG1020 99 LLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 194 PTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKALSQ 273
Cdd:COG1020 179 LPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALAR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 274 HEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAYA 353
Cdd:COG1020 259 RHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 354 HQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDLHDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDAIRLELVYNTD 433
Cdd:COG1020 339 HQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 434 LFKHERMLEMLEQYSCLASQVSERDEM-ISRYSLVS----TRASSVLPDPGAPISAhwEGTIHDLFAQQAHLRPENIAII 508
Cdd:COG1020 419 LFDAATIERMAGHLVTLLEALAADPDQpLGDLPLLTaaerQQLLAEWNATAAPYPA--DATLHELFEAQAARTPDAVAVV 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 509 DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARG 588
Cdd:COG1020 497 FGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 589 WLriegaTDcQELDEWCRANSYCNLVLArnfalSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHF 668
Cdd:COG1020 577 VL-----TQ-SALAARLPELGVPVLALD-----ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 669 LPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTqg 748
Cdd:COG1020 646 LAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL-- 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 749 mgedDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESPasvtalldkevI 828
Cdd:COG1020 724 ----DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGS-----------V 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 829 PLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFtHQEHDRLYRTGDLGRYLPDGNAE 908
Cdd:COG1020 789 PIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-GFPGARLYRTGDLARWLPDGNLE 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 909 FAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPVLSnLRAFVTQRLPAFMVP 988
Cdd:COG1020 868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAL-LRLALALLLPPYMVP 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 989 AHFVFMSRLPLNANGKVDRKALPAPEAADEATLSLATPQSPIQEELCLLWCELLGLkkVGITQNFFELGGHSLLATQLLA 1068
Cdd:COG1020 947 AAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVV--VGDDDFFFFGGGLGLLLLLALA 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1069 RINEKFNSTLSLRSLFEAPTIEGIASLITVSSSSKQELKEPVLQAQakresepkgpqriflderhgskmeqeesyLFAAS 1148
Cdd:COG1020 1025 RAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPL-----------------------------PLPPL 1075
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1149 FAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLwlslsQQHLSL 1228
Cdd:COG1020 1076 LLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVAL-----AAALAL 1150
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1229 PAESESSLSQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGIS 1308
Cdd:COG1020 1151 AALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAA 1230
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1309 PQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVLSH 1388
Cdd:COG1020 1231 LLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALA 1310
|
....*....
gi 1574832895 1389 QQQVTLYMT 1397
Cdd:COG1020 1311 LALLLLLLL 1319
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
6-1461 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 855.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 6 QRLAALSP-EKRALLkqqlgkQGSRFNTFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHE 84
Cdd:PRK12467 1095 QAVAAQQQgAQPALP------DVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 85 SLRTTFAMLNGEPIQVIRP--NLTLQIPLIDLTSLPEAEREASLQhainNEAHIPFDLKTGPLVRLALLRKSPLEHILLL 162
Cdd:PRK12467 1169 SLRTTFVQEDGRTRQVIHPvgSLTLEEPLLLAADKDEAQLKVYVE----AEARQPFDLEQGPLLRVGLLRLAADEHVLVL 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 163 NTHHIISDGWSLGVFLHELSLCYSAALAGNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMD 242
Cdd:PRK12467 1245 TLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTD 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 243 HPRPAVQTSHGAVVSLLLPSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFV 322
Cdd:PRK12467 1325 RPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFV 1404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 323 NTLVLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFN--MVNLPDLHdEWPDLKVE 400
Cdd:PRK12467 1405 NTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNhqRDDHQAQA-QLPGLSVE 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 401 HLWPREIGSKFDLTLFVQEEQDAIRLELVYNTDLFKHERMLEMLEQY-SCLASQVSERDEMISRYSLVSTRASSVLPDPG 479
Cdd:PRK12467 1484 SLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWlNLLQGLVADPERRLGELDLLDEAERRQILEGW 1563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 480 APISAHWEG--TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILG 557
Cdd:PRK12467 1564 NATHTGYPLarLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLA 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 558 ILKAGSTVLILDPSYPPARLLEYVQRAHARGWLriegaTDCQELDEWCRANSYCNLVLArnfALSGILSQYASSAPAYRV 637
Cdd:PRK12467 1644 ILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL-----TQSHLQARLPLPDGLRSLVLD---QEDDWLEGYSDSNPAVNL 1715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 638 GPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHM 717
Cdd:PRK12467 1716 APQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAH 1795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 718 GDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPsariPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTE 797
Cdd:PRK12467 1796 RDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP----LSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTE 1871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 798 TQRAVSYFVLPTASSTESPASvtalldkeviPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNE 877
Cdd:PRK12467 1872 TAVDVTHWTCRRKDLEGRDSV----------PIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAE 1941
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 878 RFLVNPFThQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIrEDTPDNKQIV 957
Cdd:PRK12467 1942 RFVADPFG-TVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLV 2019
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 958 AYIT-------HHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAADEATLSLAtPQSPI 1030
Cdd:PRK12467 2020 AYVVptdpglvDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVA-PQSEL 2098
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1031 QEELCLLWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKfNSTLSLRSLFEAPTIEGIASLitvsssSKQELKEPV 1110
Cdd:PRK12467 2099 EQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAV------AQEGDGTVS 2171
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1111 LQAQAKRESEPKGP-QRIFlderhgskmeqeesylfaasFAQERlwflhrfePESSAYHLFLAFELDGQFQPAAFEESLN 1189
Cdd:PRK12467 2172 IDQGPVTGDLPLLPiQQMF--------------------FADDI--------PERHHWNQSVLLEPREALDAELLEAALQ 2223
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1190 DLLARHESLRTSFVLQGEQL--MQRIHAQLWLSLSQQHlslpaesesSLSQQALQAWLQQEIRRPFDLQQAPLLRASLLH 1267
Cdd:PRK12467 2224 ALLVHHDALRLGFVQEDGGWsaMHRAPEQERRPLLWQV---------VVADKEELEALCEQAQRSLDLEEGPLLRAVLAT 2294
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1268 RGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGispQLAPLPLQYADYAVWQRAWLQEERQEKLQR---YWHGQ 1344
Cdd:PRK12467 2295 LPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGG---QPVKLPAKTSAFKAWAERLQTYAASAALADelgYWQAQ 2371
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1345 LATAPAllDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMvlshQQQVTLYMTL-----LAAFLLLLYRYSGQEDLVVgt 1419
Cdd:PRK12467 2372 LQGAST--ELPCDHPQGGLQRRHAASVTTHLDSEWTRRLL----QEAPAAYRTQvndllLTALARVIARWTGQASTLI-- 2443
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*...
gi 1574832895 1420 PIAGRQRREL-EGV-----IGLFANTLVLRtdLSGDPSFLELLQRVRE 1461
Cdd:PRK12467 2444 QLEGHGREDLfDEIdltrtVGWFTSLYPVK--LSPTASLATSIKTIKE 2489
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-1384 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 824.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1 MQDLSQRLAALSPEKRALLKQQLGKQGSRFNTFP------------LSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLR 68
Cdd:PRK12316 6 SLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPipagvssaerdrLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 69 VDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLIDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRL 148
Cdd:PRK12316 86 RQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 149 ALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRK 228
Cdd:PRK12316 166 RLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 229 QLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIAN 308
Cdd:PRK12316 246 QLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIAN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 309 RNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLP 388
Cdd:PRK12316 326 RNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 389 ---DLHDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDAIRLELVYNTDLFKHERMLEMLEQY-SCLASQVSERDEMISRY 464
Cdd:PRK12316 406 adiEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWqNLLRGMVENPQARVDEL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 465 SLVST--RASSVLPDPGAPISAHWEGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVA 542
Cdd:PRK12316 486 PMLDAeeRGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVG 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 543 ISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLriegaTDCQELDEWCRANSYCNLVLARnfaLS 622
Cdd:PRK12316 566 VAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL-----SQSHLGRKLPLAAGVQVLDLDR---PA 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 623 GILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTP 702
Cdd:PRK12316 638 AWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 703 LCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPSARIPSLRyafvvGDALTRRHVARLYA 782
Cdd:PRK12316 718 LMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCS-----GEALPADAQEQVFA 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 783 VAPHITCVNLYGSTETQRAVSYFvlptASSTESPASVtalldkeviPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSP 862
Cdd:PRK12316 793 KLPQAGLYNLYGPTEAAIDVTHW----TCVEEGGDSV---------PIGRPIANLACYILDANLEPVPVGVLGELYLAGR 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 863 HLAFGYLDDPDQTNERFLVNPFTHQEhdRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADA 942
Cdd:PRK12316 860 GLARGYHGRPGLTAERFVPSPFVAGE--RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 943 AVIIRedtpDNKQIVAYITHHNEQVKPVlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAADEATLS 1022
Cdd:PRK12316 938 AVLAV----DGKQLVGYVVLESEGGDWR-EALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGY 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1023 LAtPQSPIQEELCLLWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKfNSTLSLRSLFEAPTIEGIASLitvsssS 1102
Cdd:PRK12316 1013 VA-PRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLALV------A 1084
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1103 KQELKEPVLQAQAKRESEPKGPQRIFLDERHGSKMEQEESYLFAASfaqerlwflhrfEPessayhlflafeldgqFQPA 1182
Cdd:PRK12316 1085 KAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQAR------------QP----------------LDPD 1136
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1183 AFEESLNDLLARHESLRTSFVLQGEQLMQRI-HAQLWLSLSQQHlslpAESESSLSqqalqaWLQQEIRRPFDLQQAPLL 1261
Cdd:PRK12316 1137 RLGRALERLVAHHDALRLRFREEDGGWQQAYaAPQAGEVLWQRQ----AASEEELL------ALCEEAQRSLDLEQGPLL 1206
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1262 RASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYnahvkgiSPQLAPLPLQYADYAVWQRAwLQEERQEKL--QR 1339
Cdd:PRK12316 1207 RALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAY-------ADLDADLPARTSSYQAWARR-LHEHAGARAeeLD 1278
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|....*
gi 1574832895 1340 YWHGQLATAPAllDLPTDHPRPPIQTFVGARHQLHLPAELLEQLM 1384
Cdd:PRK12316 1279 YWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAERTRQLL 1321
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-1425 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 783.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 29 RFNTFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQ 108
Cdd:PRK12316 2599 RVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLR 2678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 109 IPLIDLTSLPEAereaSLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAA 188
Cdd:PRK12316 2679 IVLEDCAGVADA----AIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGA 2754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 189 LAGNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTAL 268
Cdd:PRK12316 2755 RRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSREL 2834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 269 KALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMT 348
Cdd:PRK12316 2835 LALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQA 2914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 349 LEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDLHDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDAIRLEL 428
Cdd:PRK12316 2915 LGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASL 2994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 429 VYNTDLFKHERMLEMLEQYSCLASQVSERDEM-ISRYSLVSTRASSVLPDPGAPISAHW--EGTIHDLFAQQAHLRPENI 505
Cdd:PRK12316 2995 TYATDLFDARTVERLARHWQNLLRGMVENPQRsVDELAMLDAEERGQLLEAWNATAAEYplERGVHRLFEEQVERTPDAV 3074
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 506 AIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAH 585
Cdd:PRK12316 3075 ALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSG 3154
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 586 ARGWLRiegatdcQELDEWCRANSYCNLVLARNfalsgiLSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPL 665
Cdd:PRK12316 3155 AQLLLS-------QSHLRLPLAQGVQVLDLDRG------DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL 3221
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 666 THFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPALLQLL 745
Cdd:PRK12316 3222 SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF 3301
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 746 TQgmgedDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPhitCVNLYGSTETqrAVSYFVLPTASSTESPAsvtalldk 825
Cdd:PRK12316 3302 LE-----EEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEA--TITVTHWQCVEEGKDAV-------- 3363
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 826 eviPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFthQEHDRLYRTGDLGRYLPDG 905
Cdd:PRK12316 3364 ---PIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF--VPGERLYRTGDLARYRADG 3438
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 906 NAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIiredTPDNKQIVAYITHHNEQVKpVLSNLRAFVTQRLPAF 985
Cdd:PRK12316 3439 VIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGD-LREALKAHLKASLPEY 3513
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 986 MVPAHFVFMSRLPLNANGKVDRKALPAPEAADEATLSLAtPQSPIQEELCLLWCELLGLKKVGITQNFFELGGHSLLATQ 1065
Cdd:PRK12316 3514 MVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVA-PVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQ 3592
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1066 LLARINEKfNSTLSLRSLFEAPTIEGIASLITVSssskqelkepvlQAQAKRESEPKGPQRIFLDERhgskmeqeesYLF 1145
Cdd:PRK12316 3593 VVSRARQA-GIRFTPKDLFQHQTIQGLARVARVG------------GGVAVDQGPVSGETLLLPIQQ----------QFF 3649
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1146 AASFAQERLWFLHrfepessayhlfLAFELDGQFQPAAFEESLNDLLARHESLRTSFVlQGEQLMQRIHAqlwlslsQQH 1225
Cdd:PRK12316 3650 EEPVPERHHWNQS------------LLLKPREALDAAALEAALQALVEHHDALRLRFV-EDAGGWTAEHL-------PVE 3709
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1226 LSLPAESESSLSQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVK 1305
Cdd:PRK12316 3710 LGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQ 3789
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1306 GISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPAllDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMv 1385
Cdd:PRK12316 3790 GEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSS--ELPCDHPQGALQNRHAASVQTRLDRELTRRLL- 3866
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|....*
gi 1574832895 1386 lshQQQVTLYMTL-----LAAFLLLLYRYSGQEDLVVGTPIAGRQ 1425
Cdd:PRK12316 3867 ---QQAPAAYRTQvndllLTALARVVCRWTGEASALVQLEGHGRE 3908
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
34-1425 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 714.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLID 113
Cdd:PRK05691 1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQD 1809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 114 LTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGN- 192
Cdd:PRK05691 1810 FSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRe 1889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 193 SPTLPAPsLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKALS 272
Cdd:PRK05691 1890 SPLEPLP-VQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFN 1968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 273 QHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAY 352
Cdd:PRK05691 1969 AQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQ 2048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 353 AHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLP-DLHDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDAIRLELVYN 431
Cdd:PRK05691 2049 SHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYS 2128
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 432 TDLFKHERMLEMLEQY-SCLASQVSERDEMISRYSLVSTRASSVLPDP--GAPISAHWEGTIHDLFAQQAHLRPENIAII 508
Cdd:PRK05691 2129 RDLFDEPRIARMAEHWqNLLEALLGDPQQRLAELPLLAAAEQQQLLDSlaGEAGEARLDQTLHGLFAAQAARTPQAPALT 2208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 509 DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARL----------L 578
Cdd:PRK05691 2209 FAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLhymiedsgigL 2288
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 579 EYVQRA--HARGWLRIEGATDCQELDewcransycnlvlarnfalSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPK 656
Cdd:PRK05691 2289 LLSDRAlfEALGELPAGVARWCLEDD-------------------AAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPK 2349
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 657 GVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMgDPGWLAQWMQGQEITIAS 736
Cdd:PRK05691 2350 GVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQW-GAEEICQLIREQQVSILG 2428
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 737 FTPALLQLLTQGMGEDDlpsARIPsLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETqravsyFVLPTASstesP 816
Cdd:PRK05691 2429 FTPSYGSQLAQWLAGQG---EQLP-VRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTET------VVMPLAC----L 2494
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 817 ASVTALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHqEHDRLYRTG 896
Cdd:PRK05691 2495 APEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAA-DGGRLYRTG 2573
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 897 DLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIReDTPDNKQIVAYIT-----HHNEQVKPVL 971
Cdd:PRK05691 2574 DLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVsavagQDDEAQAALR 2652
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 972 SNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAAdEATLSLATPQSPIQEELCLLWCELLGLKKVGITQ 1051
Cdd:PRK05691 2653 EALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPE-LNRQAYQAPRSELEQQLAQIWREVLNVERVGLGD 2731
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1052 NFFELGGHSLLATQLLARINEKfNSTLSLRSLFEAPTIEGIASLITVSSSSKQElkepvlQAQAKRESEPKGPQRiflde 1131
Cdd:PRK05691 2732 NFFELGGDSILSIQVVSRARQL-GIHFSPRDLFQHQTVQTLAAVATHSEAAQAE------QGPLQGASGLTPIQH----- 2799
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1132 rhgskmeqeesylfaasfaqerlWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQlmq 1211
Cdd:PRK05691 2800 -----------------------WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGR--- 2853
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1212 rihaqlWLSlsqQHLSLPAES---ESSLSQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWS 1288
Cdd:PRK05691 2854 ------WQA---EYRAVTAQEllwQVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVS 2924
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1289 LGILLQELSLCYNAHVKGISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPAllDLPTDHPRPPIQTFVG 1368
Cdd:PRK05691 2925 WRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRA--ELPCDRPQGGNLNRHA 3002
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 1369 ARHQLHLPAELLEQLMvlshQQQVTLYMTL-----LAAFLLLLYRYSGQEDLVVGTPIAGRQ 1425
Cdd:PRK05691 3003 QTVSVRLDAERTRQLL----QQAPAAYRTQvndllLTALARVLCRWSGQPSVLVQLEGHGRE 3060
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1146-1870 |
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: 659.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1146 AASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQH 1225
Cdd:COG1020 19 PLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1226 LSLPAESESslsQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVK 1305
Cdd:COG1020 99 LLVDLEALA---EAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1306 GISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMV 1385
Cdd:COG1020 176 GAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1386 LSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQ 1465
Cdd:COG1020 256 LARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1466 AYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPGDPISLEGLDVTQIRLDSNSAKFDLSWTWYqEDEKSLSAVIE 1545
Cdd:COG1020 336 AYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVV-ETGDGLRLTLE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1546 YNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLLSLGHSSSPLPAAPSCgLHHLIEAQCERSSLQP 1625
Cdd:COG1020 415 YNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADAT-LHELFEAQAARTPDAV 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1626 ALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQ 1705
Cdd:COG1020 494 AVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAG 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1706 LSLLLTHEELKARWPHCPCPLLCLDTLQerYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQS 1785
Cdd:COG1020 574 ARLVLTQSALAARLPELGVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQR 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1786 LLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETGWSGKA 1865
Cdd:COG1020 652 RYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALP 731
|
....*
gi 1574832895 1866 GLTLL 1870
Cdd:COG1020 732 SLRLV 736
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
226-1110 |
0e+00 |
|
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: 649.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 226 WRKQLaDMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTAlkalsqHEGVTLFMTTLALFQILLQRYTGRRDIVIGTP 305
Cdd:TIGR03443 2 WSERL-DNPTLSVLPHDYLRPANNRLVEATYSLQLPSAEVTA------GGGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 306 IANRNRTdiehvfgffvntLVLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPFDALLDELNPERSL-SHSLLFQVFFnm 384
Cdd:TIGR03443 75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAF-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 385 VNLPDL-HDEWPDlkvehlwpreiGSKFDLTLFVQEEQDAIRLELVYNTDLFKHERMLEMLEQYSCLASQVS-ERDEMIS 462
Cdd:TIGR03443 141 QDAPDNqQTTYST-----------GSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASsNPDEPIG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 463 RYSLVSTRASSVLPDPGAPIS-AHWEGTIHDLFAQQAHLRPENIAII---------DEINTVSYGELEARSNQLAHYLHA 532
Cdd:TIGR03443 210 KVSLITPSQKSLLPDPTKDLDwSGFRGAIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 533 QGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLRIEGATDCQELDEwcranSYCN 612
Cdd:TIGR03443 290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVR-----DYID 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 613 -----------LVLARNFALSG---------ILSQY---ASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFL 669
Cdd:TIGR03443 365 kelelrteipaLALQDDGSLVGgsleggetdVLAPYqalKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 670 PWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQGm 749
Cdd:TIGR03443 445 PWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQ- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 750 geddlPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESpasvtaLLD--KEV 827
Cdd:TIGR03443 524 -----ATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPSRSSDST------FLKnlKDV 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 828 IPLGKGMPGAQILILN--EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEH---------------- 889
Cdd:TIGR03443 593 MPAGKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkperefw 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 890 ----DRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYI----- 960
Cdd:TIGR03443 673 lgprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIvpqdk 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 961 -------------THHNEQV-------KPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPeaaDEAT 1020
Cdd:TIGR03443 753 sdeleefksevddEESSDPVvkglikyRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFP---DTAQ 829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1021 LSLATPQSPIQEELCLLWCELLGLK------------KVGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPT 1088
Cdd:TIGR03443 830 LAAVAKNRSASAADEEFTETEREIRdlwlellpnrpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPT 909
|
970 980 990
....*....|....*....|....*....|..
gi 1574832895 1089 IEGIA----------SLITVSSSSKQELKEPV 1110
Cdd:TIGR03443 910 IKGFAkevdrlkkgeELADEGDSEIEEEETVL 941
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
32-454 |
0e+00 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 647.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 32 TFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPL 111
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAG 191
Cdd:cd19531 81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 192 NSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKAL 271
Cdd:cd19531 161 RPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 272 SQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEA 351
Cdd:cd19531 241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 352 YAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDLHDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDAIRLELVYN 431
Cdd:cd19531 321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
|
410 420
....*....|....*....|...
gi 1574832895 432 TDLFKHERMLEMLEQYSCLASQV 454
Cdd:cd19531 401 TDLFDAATIERMAGHFQTLLEAI 423
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1148-1860 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 635.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1148 SFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLsqqHLS 1227
Cdd:PRK12467 53 SYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTI---PLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1228 LPAESESSLSQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGI 1307
Cdd:PRK12467 130 DLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1308 SPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVLS 1387
Cdd:PRK12467 210 EPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1388 HQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQAY 1467
Cdd:PRK12467 290 QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1468 SQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPGDPIS-----LEGLDVTQIRLDSNSAKFDLSWTWYqEDEKSLSA 1542
Cdd:PRK12467 370 AHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATGGRDregaqLPGLTVEELSWARHTAQFDLALDTY-ESAQGLWA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1543 VIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLLSlGHSSSPLPAAPSCgLHHLIEAQCERSS 1622
Cdd:PRK12467 449 AFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELV-RWNAPATEYAPDC-VHQLIEAQARQHP 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1623 LQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQ 1702
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLD 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1703 DAQLSLLLTHEELKARWPHCP-CPLLCLDTLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLL 1781
Cdd:PRK12467 607 DSGVRLLLTQSHLLAQLPVPAgLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVC 686
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1782 SLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:PRK12467 687 VIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQAS 765
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1145-1574 |
0e+00 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 590.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1145 FAASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQ 1224
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1225 HLS--LPAESESSLsqqalQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNA 1302
Cdd:cd19531 82 DLSglPEAEREAEA-----QRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1303 HVKGISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQ 1382
Cdd:cd19531 157 FLAGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1383 LMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREV 1462
Cdd:cd19531 237 LRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1463 TLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPGDPISLEGLDVTQIRLDSNSAKFDLSWTwYQEDEKSLSA 1542
Cdd:cd19531 317 ALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLS-LTETDGGLRG 395
|
410 420 430
....*....|....*....|....*....|..
gi 1574832895 1543 VIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19531 396 SLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1146-1860 |
2.11e-178 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 607.34 E-value: 2.11e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1146 AASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQH 1225
Cdd:PRK12316 51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFED 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1226 LSLPAESESSLSQQALQAWlqqEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVK 1305
Cdd:PRK12316 131 CSGLPEAEQEARLRDEAQR---ESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1306 GISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMV 1385
Cdd:PRK12316 208 GAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1386 LSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQ 1465
Cdd:PRK12316 288 TARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1466 AYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPGDP---ISLEGLDVTQIRLDSNSAKFDLSWTWYqEDEKSLSA 1542
Cdd:PRK12316 368 AQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADIealDTVAGLEFGQLEWKSRTTQFDLTLDTY-EKGGRLHA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1543 VIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLLSlGHSSSPLPAAPSCGLHHLIEAQCERSS 1622
Cdd:PRK12316 447 ALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVE-GWNATAAEYPLQRGVHRLFEEQVERTP 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1623 LQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQ 1702
Cdd:PRK12316 526 EAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1703 DAQLSLLLTHEELKARWP-HCPCPLLCLDTLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLL 1781
Cdd:PRK12316 606 DSGVQLLLSQSHLGRKLPlAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC 685
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1782 SLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:PRK12316 686 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE 764
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
489-1858 |
6.73e-163 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 559.79 E-value: 6.73e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAII------DEINTVSYGELEARSNQLAHYLHAQGIrPHDVVAISAQRCAALVLAILGILKAG 562
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 563 stvLILDPSYPP--------ARLLEYVQRAHARGWLRIEGATDC-QELDEWCRANSYCNLvlarnfALSGILSQYASSAP 633
Cdd:PRK05691 89 ---VIAVPAYPPesarrhhqERLLSIIADAEPRLLLTVADLRDSlLQMEELAAANAPELL------CVDTLDPALAEAWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 634 AYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLA--HD-----PLQREIFTPL-CV 705
Cdd:PRK05691 160 EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPlyHDmgligGLLQPIFSGVpCV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 706 gatiCIPDQEHMGDPgwlAQWMQGQEI---TIASFTPALLQLLTQGMGEDDLPSARIPSLRYAFVvGDALTRRHVARLYA 782
Cdd:PRK05691 240 ----LMSPAYFLERP---LRWLEAISEyggTISGGPDFAYRLCSERVSESALERLDLSRWRVAYS-GSEPIRQDSLERFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 783 vAPHITCvnlyGSTETQRAVSY-------FVlptaSSTESPASVTAL-LDKE--------------VIPLGKGMPGAQIL 840
Cdd:PRK05691 312 -EKFAAC----GFDPDSFFASYglaeatlFV----SGGRRGQGIPALeLDAEalarnraepgtgsvLMSCGRSQPGHAVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 841 ILnEAGNLAGIGE--LGEIYVRSPHLAFGYLDDPDQTNERFLvnpfthqEHD--RLYRTGDLGrYLPDGNAEFAGRNDLQ 916
Cdd:PRK05691 383 IV-DPQSLEVLGDnrVGEIWASGPSIAHGYWRNPEASAKTFV-------EHDgrTWLRTGDLG-FLRDGELFVTGRLKDM 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 917 VKIRGYRIELEEIEAILVEHPMVAD----AAVIIREDTPDNKQIVAYITHHNEQVKP---VLSNLRAFVTQrlpAFM-VP 988
Cdd:PRK05691 454 LIVRGHNLYPQDIEKTVEREVEVVRkgrvAAFAVNHQGEEGIGIAAEISRSVQKILPpqaLIKSIRQAVAE---ACQeAP 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 989 AHFVFMS--RLPLNANGKVDRKALPA-------------PEAADEATLSLATPQSPIQEELCLLWCELLGLKKVGITQNF 1053
Cdd:PRK05691 531 SVVLLLNpgALPKTSSGKLQRSACRLrladgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHF 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1054 FELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASLitvsssskqelkepVLQAQAKRESEPKGPQRIFLDERh 1133
Cdd:PRK05691 611 FLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAA--------------VARQLAGGGAAQAAIARLPRGQA- 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1134 gskmeqeesylFAASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRI 1213
Cdd:PRK05691 676 -----------LPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRI 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1214 HAQLWLSLSQQHLS-LPAESESSlsqqALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGIL 1292
Cdd:PRK05691 745 DAQGEFALQRIDLSdLPEAEREA----RAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNIL 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1293 LQELSLCYNAHVKGISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQ 1372
Cdd:PRK05691 821 LDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYS 900
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1373 LHLPAELLEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSF 1452
Cdd:PRK05691 901 LRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPF 980
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1453 LELLQRVREVTLQAYSQQDMPFEKLVAELQPERSlayNPLFQVFFALQNV-PGDPISLEGLDVTQIRLDSNSAKFDLSWT 1531
Cdd:PRK05691 981 TALLAQVRQATLGAQAHQDLPFEQLVEALPQARE---QGLFQVMFNHQQRdLSALRRLPGLLAEELPWHSREAKFDLQLH 1057
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1532 WYQEDEKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLLSLGHSssPLPAAPSCgLH 1611
Cdd:PRK05691 1058 SEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQA--PCAPAQAW-LP 1134
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1612 HLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPD 1691
Cdd:PRK05691 1135 ELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPD 1214
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1692 YPSQRLLWMAQDAQLSLLLTHEELKARWPHCP-CPLLCLDTLQerYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQ 1770
Cdd:PRK05691 1215 YPAERLAYMLADSGVELLLTQSHLLERLPQAEgVSAIALDSLH--LDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVG 1292
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1771 ISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATP 1850
Cdd:PRK05691 1293 NTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVP 1372
|
....*...
gi 1574832895 1851 TTWQLLLE 1858
Cdd:PRK05691 1373 PLLQLFID 1380
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
502-1010 |
2.95e-161 |
|
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: 502.83 E-value: 2.95e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYV 581
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 QRAHARgwlriegatdcqeldewcransycnLVLarnfalsgilsqyassapayrVGPNDIACLTFTSGSTGRPKGVLQR 661
Cdd:cd05930 81 EDSGAK-------------------------LVL---------------------TDPDDLAYVIYTSGSTGKPKGVMVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPAL 741
Cdd:cd05930 115 HRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 742 LQLLTQgmgedDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASstespasvta 821
Cdd:cd05930 195 LRLLLQ-----ELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDD---------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 822 lLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEhdRLYRTGDLGRY 901
Cdd:cd05930 260 -EEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGE--RMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 902 LPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThHNEQVKPVLSNLRAFVTQR 981
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV-PDEGGELDEEELRAHLAER 415
|
490 500
....*....|....*....|....*....
gi 1574832895 982 LPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05930 416 LPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-1105 |
1.53e-160 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 552.64 E-value: 1.53e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 11 LSPEKRALLKQQLGKQGSRFNTFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGpLRVDLLEKCIHLLVRRHESLRTTF 90
Cdd:PRK12316 4081 LAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGF 4159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 91 AMLN--GEPIQVIRPNLtlQIPLIDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHII 168
Cdd:PRK12316 4160 VWQGelGRPLQVVHKQV--SLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHIL 4237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 169 SDGWSLGVFLHELSLCYSaalaGNSPtlPAPSLQYADYAAWqrnwLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAV 248
Cdd:PRK12316 4238 MDGWSNSQLLGEVLERYS----GRPP--AQPGGRYRDYIAW----LQRQDAAASEAFWREQLAALDEPTRLAQAIARADL 4307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 249 QTSHG-AVVSLLLPSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANR--NRTDIEHVFGFFVNTL 325
Cdd:PRK12316 4308 RSANGyGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTL 4387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 326 VLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPfdalLDELNPERSLSHSLLFQVFFNMVNLP---DLHDEWP-DLKVEH 401
Cdd:PRK12316 4388 PVIATPRAQQSVVEWLQQVQRQNLALREHEHTP----LYEIQRWAGQGGEALFDSLLVFENYPvseALQQGAPgGLRFGE 4463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 402 LWPREIGSkFDLTLFVQEEqDAIRLELVYNTDLFKHERMLEMLEQYSCLASQVSERDEM-ISRYSLVStrassvlPDPGA 480
Cdd:PRK12316 4464 VTNHEQTN-YPLTLAVGLG-ETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRrLGELQLLE-------KAEQQ 4534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 481 PISAHWEGT---------IHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAAL 551
Cdd:PRK12316 4535 RIVALWNRTdagypatrcVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEM 4614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 552 VLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLriegaTDCQELDEWCRANSYCNLVLARNFALSGilsqYASS 631
Cdd:PRK12316 4615 MVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLL-----TQSHLLQRLPIPDGLASLALDRDEDWEG----FPAH 4685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 632 APAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICI 711
Cdd:PRK12316 4686 DPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVI 4765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 PDQEhMGDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDdlpsARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVN 791
Cdd:PRK12316 4766 RDDS-LWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERD----GEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFN 4840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 792 LYGSTETQravsyfVLPTASSTesPASVTALLDkeVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDD 871
Cdd:PRK12316 4841 GYGPTETT------VTVLLWKA--RDGDACGAA--YMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLER 4910
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 872 PDQTNERFLVNPFTHQeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADaAVIIREDTP 951
Cdd:PRK12316 4911 PALTAERFVPDPFGAP-GGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE-AVVIAQEGA 4988
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 952 DNKQIVAYITHHNEQVKPVLSN-------LRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAAdEATLSLA 1024
Cdd:PRK12316 4989 VGKQLVGYVVPQDPALADADEAqaelrdeLKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDAS-LLQQAYV 5067
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1025 TPQSPIQEELCLLWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASLITVSSSSKQ 1104
Cdd:PRK12316 5068 APRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
|
.
gi 1574832895 1105 E 1105
Cdd:PRK12316 5148 E 5148
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
33-1096 |
1.64e-141 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 476.46 E-value: 1.64e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 33 FPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIP-L 111
Cdd:PRK10252 8 LPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPeI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTSLPEAEREAslQHAINNEAHIPFDLKTG-PLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALA 190
Cdd:PRK10252 88 IDLRTQPDPHAAA--QALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 191 GN-SPTLPAPSLQ-----YADYAA---WQRNwlkgenltnlLDYWRKQLADMPPLLELPmdhPRPAVQTSHGA-VVSLLL 260
Cdd:PRK10252 166 GEpTPASPFTPFAdvveeYQRYRAseaWQRD----------AAFWAEQRRQLPPPASLS---PAPLPGRSASAdILRLKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 261 PSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTL 340
Cdd:PRK10252 233 EFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 341 LQRVKEMTLEAYAHQDIPFDALLDELN---PERSLSHSLL-FQVFFNMVNLPDLhdewpDLKVEHLwprEIGSKFDLTL- 415
Cdd:PRK10252 313 ATRLAAQLKKMRRHQRYDAEQIVRDSGraaGDEPLFGPVLnIKVFDYQLDFPGV-----QAQTHTL---ATGPVNDLELa 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 416 FVQEEQDAIRLELVYNTDLFKHERMLEMLEQYSCLASQVSERDemisrySLVSTRASSVLPDPGAPIsAHWEGTIH---- 491
Cdd:PRK10252 385 LFPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADP------ALLCGDVDILLPGEYAQL-AQVNATAVeipe 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 492 ----DLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLI 567
Cdd:PRK10252 458 ttlsALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 568 LDPSYPPARLleYVQRAHARGWLRIEGATDCQELDEWCRANSYC-NLVLARnfalsgilsqyASSAPAYRVGPNDIACLT 646
Cdd:PRK10252 538 LDTGYPDDRL--KMMLEDARPSLLITTADQLPRFADVPDLTSLCyNAPLAP-----------QGAAPLQLSQPHHTAYII 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 647 FTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQW 726
Cdd:PRK10252 605 FTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQF 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 727 MQGQEITIASFTPALLQLLTQGMGEDDLPSArIPSLRYAFVVGDALT---RRHVARLYAVAPHitcvNLYGSTETQRAVS 803
Cdd:PRK10252 685 FAEYGVTTTHFVPSMLAAFVASLTPEGARQS-CASLRQVFCSGEALPadlCREWQQLTGAPLH----NLYGPTEAAVDVS 759
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 804 YFvlptasstesPASVTALLDKEVIPLGKGMP--GAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLV 881
Cdd:PRK10252 760 WY----------PAFGEELAAVRGSSVPIGYPvwNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIA 829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 882 NPFTHQEhdRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADA---AVIIREDTP---DNKQ 955
Cdd:PRK10252 830 DPFAPGE--RMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAAAtggDARQ 907
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 956 IVAYITHHNEqVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPE-AADEATLSlatPQSPIQEEL 1034
Cdd:PRK10252 908 LVGYLVSQSG-LPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPElKAQVPGRA---PKTGTETII 983
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 1035 CLLWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASLI 1096
Cdd:PRK10252 984 AAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLL 1045
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-1121 |
2.39e-141 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 493.14 E-value: 2.39e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 33 FPLSFAQQRLwLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNG--EPIQVIRPNLTLQIP 110
Cdd:PRK12467 2647 YPLSPMQQGM-LFHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGEleEPLQVVYKQARLPFS 2725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 111 LIDLTSLPEAEreASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSaala 190
Cdd:PRK12467 2726 RLDWRDRADLE--QALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF---- 2799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 191 GNSPtlPAPSLQYADYAAWqrnwLKGENLTNLLDYWRKQLADM--PPLL--ELPMDHPRPAvqTSHGAVVSLLLPSEiST 266
Cdd:PRK12467 2800 GQPP--PAREGRYRDYIAW----LQAQDAEASEAFWKEQLAALeePTRLarALYPAPAEAV--AGHGAHYLHLDATQ-TR 2870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 267 ALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANR--NRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRV 344
Cdd:PRK12467 2871 QLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQV 2950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 345 KEMTLEAYAHQDIP-FDALLDELNPERSLSHSLLfqVFFNMVNLPDLHDEWP-DLKVEHLWPREIgSKFDLTLFVQEEqD 422
Cdd:PRK12467 2951 QAQNLALREFEHTPlADIQRWAGQGGEALFDSIL--VFENYPISEALKQGAPsGLRFGAVSSREQ-TNYPLTLAVGLG-D 3026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 423 AIRLELVYNTDLFKHERMLEMLEQYSCLASQVSE--RDEMISRYSLVSTRASSVLPDPGAPISAHWEG-TIHDLFAQQAH 499
Cdd:PRK12467 3027 TLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNnpAARLGELPTLAAHERRQVLHAWNATAAAYPSErLVHQLIEAQVA 3106
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 500 LRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLE 579
Cdd:PRK12467 3107 RTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY 3186
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 580 YVQRAHARGWLriegaTDCQELDEWCRANSYCNLVLARnfalsGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVL 659
Cdd:PRK12467 3187 MIEDSGVKLLL-----TQAHLLEQLPAPAGDTALTLDR-----LDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVG 3256
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 660 QRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMgDPGWLAQWMQGQEITIASFTP 739
Cdd:PRK12467 3257 VRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPP 3335
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 740 ALLQLLTQGMGEDDLPSaripsLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESPAsv 819
Cdd:PRK12467 3336 AYLQQFAEDAGGADCAS-----LDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPY-- 3408
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 820 talldkevIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFThQEHDRLYRTGDLG 899
Cdd:PRK12467 3409 --------APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFS-GSGGRLYRTGDLA 3479
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 900 RYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIReDTPDNKQIVAYITHHNEQvKPVLSNLRAFVT 979
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQ-GDWRETLRDHLA 3557
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 980 QRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAADEATlsLATPQSPIQEELCLLWCELLGLKKVGITQNFFELGGH 1059
Cdd:PRK12467 3558 ASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSRE--YVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGD 3635
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 1060 SLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASlitvSSSSKQELKEPVLQAQAKRESEP 1121
Cdd:PRK12467 3636 SLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAG----YSPLGDVPVNLLLDLNRLETGFP 3693
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
513-1013 |
1.55e-138 |
|
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: 442.73 E-value: 1.55e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLRI 592
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 EGAtdcqeldewcransycnlvlarnfalsGILsqyassapayrVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWM 672
Cdd:cd17647 100 RAA---------------------------GVV-----------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 673 RDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQGmged 752
Cdd:cd17647 142 AKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQ---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 753 dlPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESpasvtaLLD--KEVIPL 830
Cdd:cd17647 218 --ATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSDPT------FLKnlKDVMPA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 831 GKGMPGAQILILN--EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEH------------------- 889
Cdd:cd17647 290 GRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHwnyldkdnnepwrqfwlgp 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 890 -DRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQV- 967
Cdd:cd17647 370 rDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPd 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 968 -------------------------KPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAP 1013
Cdd:cd17647 450 desfaqedvpkevstdpivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1148-1574 |
1.63e-136 |
|
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: 433.39 E-value: 1.63e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1148 SFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSqqhLS 1227
Cdd:cd19540 5 SFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPD---LT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1228 LPAESESSLsqqalQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGI 1307
Cdd:cd19540 82 VVDVTEDEL-----AARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1308 SPQLAPLPLQYADYAVWQRAWLQEE--------RQeklQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAEL 1379
Cdd:cd19540 157 APDWAPLPVQYADYALWQRELLGDEddpdslaaRQ---LAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1380 LEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRV 1459
Cdd:cd19540 234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1460 REVTLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPGDPISLEGLDVTQIRLDSNSAKFDLSWTW---YQED 1536
Cdd:cd19540 314 RETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLterRDAD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1574832895 1537 EK--SLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19540 394 GApaGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
34-446 |
2.56e-134 |
|
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: 427.22 E-value: 2.56e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLiD 113
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDL-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 114 LTSLPEAEreasLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNS 193
Cdd:cd19540 82 VVDVTEDE----LAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 194 PTLPAPSLQYADYAAWQRNWLKGEN-----LTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTAL 268
Cdd:cd19540 158 PDWAPLPVQYADYALWQRELLGDEDdpdslAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 269 KALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMT 348
Cdd:cd19540 238 AALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 349 LEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDLHDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDA----- 423
Cdd:cd19540 318 LAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDAdgapa 397
|
410 420 430
....*....|....*....|....*....|.
gi 1574832895 424 -IRLELVYNTDLFKH-------ERMLEMLEQ 446
Cdd:cd19540 398 gLTGELEYATDLFDRstaerlaDRFVRVLEA 428
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
491-1010 |
5.79e-134 |
|
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: 428.62 E-value: 5.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 491 HDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDP 570
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 571 SYPPARLLEYVQRAHARGWLRIEGATDcqeldeWCRAnsycnlVLARNFALSGILSQYASSAPAYRVGPNDIACLTFTSG 650
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAA------RLPA------GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQ 730
Cdd:cd17646 149 STGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 731 EITIASFTPALLQLLTQGMGeddlpSARIPSLRYAFVVGDALTRRHVARLYAVaPHITCVNLYGSTETQRAVSYFVlpta 810
Cdd:cd17646 229 GVTTCHFVPSMLRVFLAEPA-----AGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWP---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 811 sstespasVTALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEhd 890
Cdd:cd17646 299 --------VRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGS-- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 891 RLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPV 970
Cdd:cd17646 369 RMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPD 448
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1574832895 971 LSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd17646 449 TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
492-1010 |
2.05e-130 |
|
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: 418.53 E-value: 2.05e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 492 DLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPS 571
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 572 YPPARLLEYVQRAHARGWLRIEGATDcqeldewcRANSYCNLVLarnfaLSGILSQYASSAPAYRVGPNDIACLTFTSGS 651
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAG--------RAGGLEVAVV-----IDEALDAGPAGNPAVPVSPDDLAYVMYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 652 TGRPKGVLQRHGPLTHFLpwMRDRFA-FTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQ 730
Cdd:cd12117 148 TGRPKGVAVTHRGVVRLV--KNTNYVtLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 731 EITIASFTPALLQLLTqgmgeDDLPSArIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTE-TQRAVSYFVLPT 809
Cdd:cd12117 226 GVTVLWLTAALFNQLA-----DEDPEC-FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnTTFTTSHVVTEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 810 ASSTESpasvtalldkevIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEh 889
Cdd:cd12117 300 DEVAGS------------IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGE- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 890 dRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThHNEQVKP 969
Cdd:cd12117 367 -RLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV-AEGALDA 444
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1574832895 970 VLsnLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd12117 445 AE--LRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
494-1011 |
2.24e-126 |
|
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: 407.50 E-value: 2.24e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 494 FAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYP 573
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 574 PARLLEYVQRAHARGWLRIEGATDCQELDEwcransycnlvLARNFALSGILSQYASSAPAYRVGPNDIACLTFTSGSTG 653
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVEL-----------VAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 654 RPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEIT 733
Cdd:cd17651 150 RPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRIS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 734 IASFTPALLQLLTQGMgedDLPSARIPSLRYAFVVGDALTRRH-VARLYAVAPHITCVNLYGSTETQrAVSYFVLPTASS 812
Cdd:cd17651 230 RVFLPTVALRALAEHG---RPLGVRLAALRYLLTGGEQLVLTEdLREFCAGLPGLRLHNHYGPTETH-VVTALSLPGDPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 813 TESpasvtalldkEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEhdRL 892
Cdd:cd17651 306 AWP----------APPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGA--RM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 893 YRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHnEQVKPVLS 972
Cdd:cd17651 374 YRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGD-PEAPVDAA 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 1574832895 973 NLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd17651 453 ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
515-944 |
2.62e-126 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 403.95 E-value: 2.62e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEARSNQLAHYLHAQ-GIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLrie 593
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 594 gaTDcQELDEWCRANSYCNLVLARNFALSGILSQyASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMR 673
Cdd:TIGR01733 78 --TD-SALASRLAGLVLPVILLDPLELAALDDAP-APPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 674 DRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGD-PGWLAQWMQGQEITIASFTPALLQLLtqgmgeD 752
Cdd:TIGR01733 154 RRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDdAALLAALIAEHPVTVLNLTPSLLALL------A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 753 DLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESPAsvtalldkevIPLGK 832
Cdd:TIGR01733 228 AALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP----------VPIGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 833 GMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEHDRLYRTGDLGRYLPDGNAEFAGR 912
Cdd:TIGR01733 298 PLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGR 377
|
410 420 430
....*....|....*....|....*....|..
gi 1574832895 913 NDLQVKIRGYRIELEEIEAILVEHPMVADAAV 944
Cdd:TIGR01733 378 IDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1148-1574 |
1.24e-125 |
|
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: 402.80 E-value: 1.24e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1148 SFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQHLS 1227
Cdd:cd19538 5 SFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1228 LPAESESSLsqqalqawLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGI 1307
Cdd:cd19538 85 VDEEELESE--------INEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1308 SPQLAPLPLQYADYAVWQRAWLQEERQEKLQ-----RYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQ 1382
Cdd:cd19538 157 APELAPLPVQYADYALWQQELLGDESDPDSLiarqlAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1383 LMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREV 1462
Cdd:cd19538 237 LLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1463 TLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPGDPISLEGLDvTQIRLDS-NSAKFDLS---WTWYQ-EDE 1537
Cdd:cd19538 317 NLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLE-AKLELRTvGSAKFDLTfelREQYNdGTP 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1574832895 1538 KSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19538 396 NGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
34-456 |
8.54e-125 |
|
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: 400.49 E-value: 8.54e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLiD 113
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 114 LTSLPEAEreasLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNS 193
Cdd:cd19538 82 IKEVDEEE----LESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 194 PTLPAPSLQYADYAAWQRNWLKGEN-----LTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTAL 268
Cdd:cd19538 158 PELAPLPVQYADYALWQQELLGDESdpdslIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 269 KALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMT 348
Cdd:cd19538 238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 349 LEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDLHDEWPDLKVEhLWPREIGS-KFDLTLFVQEE-----QD 422
Cdd:cd19538 318 LEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAK-LELRTVGSaKFDLTFELREQyndgtPN 396
|
410 420 430
....*....|....*....|....*....|....
gi 1574832895 423 AIRLELVYNTDLFKHERMLEMLEQYSCLASQVSE 456
Cdd:cd19538 397 GIEGFIEYRTDLFDHETIEALAQRYLLLLESAVE 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
493-1014 |
2.51e-120 |
|
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: 390.15 E-value: 2.51e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 493 LFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSY 572
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 573 PPARLlEYVQRAHARGWLRIEGATDCQELDEwcranSYCNLVLARNFalsgilSQYASSAPAYRVGPNDIACLTFTSGST 652
Cdd:cd17655 82 PEERI-QYILEDSGADILLTQSHLQPPIAFI-----GLIDLLDEDTI------YHEESENLEPVSKSDDLAYVIYTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 653 GRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEI 732
Cdd:cd17655 150 GKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 733 TIASFTPALLQLLTQgmgEDDLPSariPSLRYAFVVGDALTRRHVARLYAVAPH-ITCVNLYGSTETQRAVSYFVL-PTA 810
Cdd:cd17655 230 TIIDLTPAHLKLLDA---ADDSEG---LSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYQYePET 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 811 SSTESpasvtalldkevIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEhd 890
Cdd:cd17655 304 DQQVS------------VPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGE-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 891 RLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQvkpV 970
Cdd:cd17655 370 RMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKEL---P 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1574832895 971 LSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPE 1014
Cdd:cd17655 447 VAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
502-1010 |
9.31e-119 |
|
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: 383.97 E-value: 9.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLleyv 581
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 qrahargwlriegatdcqeldewcransycnlvlarnfalSGILsqyASSAPAYRVG-PNDIACLTFTSGSTGRPKGVLQ 660
Cdd:cd17643 77 ----------------------------------------AFIL---ADSGPSLLLTdPDDLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 661 RHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTP- 739
Cdd:cd17643 114 SHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPs 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 740 ALLQLLTqgmgEDDLPSARIPSLRYAFVVGDALTRRHVARLYA--VAPHITCVNLYGSTETQRAVSYFVLPTASSTESPA 817
Cdd:cd17643 194 AFYQLVE----AADRDGRDPLALRYVIFGGEALEAAMLRPWAGrfGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 818 SvtalldkeviPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFThQEHDRLYRTGD 897
Cdd:cd17643 270 S----------PIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFG-GPGSRMYRTGD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 898 LGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThHNEQVKPVLSNLRAF 977
Cdd:cd17643 339 LARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVV-ADDGAAADIAELRAL 417
|
490 500 510
....*....|....*....|....*....|...
gi 1574832895 978 VTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd17643 418 LKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
489-1011 |
1.24e-116 |
|
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: 378.32 E-value: 1.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLIL 568
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 569 DPSYPPARLLEYVQrahargwlriegatDCQeldewcransycnlvlarnfaLSGILSQyassapayrvgPNDIACLTFT 648
Cdd:cd17644 81 DPNYPQERLTYILE--------------DAQ---------------------ISVLLTQ-----------PENLAYVIYT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 649 SGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQ 728
Cdd:cd17644 115 SGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 729 GQEITIASFTPALLQLLTQGMGED--DLPSaripSLRYAFVVGDALTRRHVARLY-AVAPHITCVNLYGSTETQRAVSYF 805
Cdd:cd17644 195 QWQLTVLSLPPAYWHLLVLELLLStiDLPS----SLRLVIVGGEAVQPELVRQWQkNVGNFIQLINVYGPTEATIAATVC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 806 vLPTASSTESPASVtalldkeviPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFT 885
Cdd:cd17644 271 -RLTQLTERNITSV---------PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 886 HQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNE 965
Cdd:cd17644 341 SSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYE 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1574832895 966 qVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd17644 421 -ESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
34-457 |
2.73e-112 |
|
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: 364.39 E-value: 2.73e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTF-AMLNGEPIQVIRPNLTLQIPLI 112
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLvRDDGGVPRQEILPPGPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 113 DLtSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGN 192
Cdd:cd19539 83 DL-SDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 193 SPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLlELPMDHPRPAVQTSHGAVVSLLLPSEISTALKALS 272
Cdd:cd19539 162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPT-ALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 273 QHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAY 352
Cdd:cd19539 241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 353 AHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDL-HDEWPDLKVEHLWPREIGSKFDLTLFVQEEQDAIRLELVYN 431
Cdd:cd19539 321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGeLELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYA 400
|
410 420
....*....|....*....|....*.
gi 1574832895 432 TDLFKHERMLEMLEQYSCLASQVSER 457
Cdd:cd19539 401 TSLFDEETIQGFLADYLQVLRQLLAN 426
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
502-1011 |
8.66e-112 |
|
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: 364.00 E-value: 8.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYV 581
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 QRAHARgwlriegatdcqeldewcransycnLVLARnfalsgilsqyassapayrvGPNDIACLTFTSGSTGRPKGVLQR 661
Cdd:cd17649 81 EDSGAG-------------------------LLLTH--------------------HPRQLAYVIYTSGSTGTPKGVAVS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPAL 741
Cdd:cd17649 116 HGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 742 LQLLTQGMgeDDLPSARIPSLRYAFVVGDALTRRHVARlyAVAPHITCVNLYGSTETQRAVSYFVLPtASSTESPASVta 821
Cdd:cd17649 196 LQQLAEEA--DRTGDGRPPSLRLYIFGGEALSPELLRR--WLKAPVRLFNAYGPTEATVTPLVWKCE-AGAARAGASM-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 822 lldkeviPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFThQEHDRLYRTGDLGRY 901
Cdd:cd17649 269 -------PIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFG-APGSRLYRTGDLARW 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 902 LPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIReDTPDNKQIVAYITHHNEQVKPVL-SNLRAFVTQ 980
Cdd:cd17649 341 RDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELrAQLRTALRA 419
|
490 500 510
....*....|....*....|....*....|.
gi 1574832895 981 RLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd17649 420 SLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
502-1010 |
1.21e-111 |
|
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: 364.31 E-value: 1.21e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLlEYV 581
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 QRAHARGWLRIEGATDCqeldewcRANSYCNLVLARNFALSGilsqyASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQR 661
Cdd:cd12116 80 LEDAEPALVLTDDALPD-------RLPAGLPVLLLALAAAAA-----APAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPAL 741
Cdd:cd12116 148 HRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPAT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 742 LQLLTQGmGEDDLPSARipslryAFVVGDALTRRHVARLyaVAPHITCVNLYGSTETqravsyfvlpTASSTESPasVTA 821
Cdd:cd12116 228 WRMLLDA-GWQGRAGLT------ALCGGEALPPDLAARL--LSRVGSLWNLYGPTET----------TIWSTAAR--VTA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 822 llDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEHdRLYRTGDLGRY 901
Cdd:cd12116 287 --AAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGS-RLYRTGDLVRR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 902 LPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDnKQIVAYITHHnEQVKPVLSNLRAFVTQR 981
Cdd:cd12116 364 RADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGD-RRLVAYVVLK-AGAAPDAAALRAHLRAT 441
|
490 500
....*....|....*....|....*....
gi 1574832895 982 LPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd12116 442 LPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
502-1010 |
7.95e-111 |
|
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: 362.36 E-value: 7.95e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYV 581
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 QRAHARGWLrIEGatDCQELDEWCRansyCNLVLARNFALSGILsqyassAPAYRVGPNDIACLTFTSGSTGRPKGVLQR 661
Cdd:cd12114 81 ADAGARLVL-TDG--PDAQLDVAVF----DVLILDLDALAAPAP------PPPVDVAPDDLAYVIFTSGSTGTPKGVMIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPAL 741
Cdd:cd12114 148 HRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 742 LQLLtqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETqrAVSYFVLPTASSTESPASvta 821
Cdd:cd12114 228 LEML---LDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEA--SIWSIYHPIDEVPPDWRS--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 822 lldkevIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpFTHQEHDRLYRTGDLGRY 901
Cdd:cd12114 300 ------IPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARF----VTHPDGERLYRTGDLGRY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 902 LPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIReDTPDNKQIVAYITHHNEQVKPVLSNLRAFVTQR 981
Cdd:cd12114 370 RPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQT 448
|
490 500
....*....|....*....|....*....
gi 1574832895 982 LPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd12114 449 LPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
490-1010 |
6.83e-110 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 359.93 E-value: 6.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 490 IHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILD 569
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 570 PSYPPARLLEYVQRAHARgwlriegatdcqeldewcransycnLVLArnfalsgilSQyassapayrvgPNDIACLTFTS 649
Cdd:cd05918 81 PSHPLQRLQEILQDTGAK-------------------------VVLT---------SS-----------PSDAAYVIFTS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 650 GSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIP-DQEHMGDpgwLAQWMQ 728
Cdd:cd05918 116 GSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPsEEDRLND---LAGFIN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 729 GQEITIASFTPALLQLLTqgmgeddlPSArIPSLRYAFVVGDALTRRHVARLyavAPHITCVNLYGSTETqrAVSyfvlp 808
Cdd:cd05918 193 RLRVTWAFLTPSVARLLD--------PED-VPSLRTLVLGGEALTQSDVDTW---ADRVRLINAYGPAEC--TIA----- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 809 tASSTESPASVTALLdkevipLGKGMPGAQ-ILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNP---- 883
Cdd:cd05918 254 -ATVSPVVPSTDPRN------IGRPLGATCwVVDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlk 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 884 -FTHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHP---MVADAAVIIREDTPDNKQIVAY 959
Cdd:cd05918 327 qEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLpgaKEVVVEVVKPKDGSSSPQLVAF 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 960 ITHH----------------NEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05918 407 VVLDgsssgsgdgdslflepSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
490-1010 |
2.24e-108 |
|
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: 353.93 E-value: 2.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 490 IHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILD 569
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 570 PSYPPARLLEYVQRAHARgwlriegatdcqeldewcransycnLVLarnfalsgilsqyassapayrVGPNDIACLTFTS 649
Cdd:cd12115 81 PAYPPERLRFILEDAQAR-------------------------LVL---------------------TDPDDLAYVIYTS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 650 GSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQtdryslLSG-LAHDPLQ-----REIFTPLCVGATICIPDQE-HMGDPGW 722
Cdd:cd12115 115 GSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE------LAGvLASTSICfdlsvFELFGPLATGGKVVLADNVlALPDLPA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 723 LAqwmqgqEITIASFTP-ALLQLLTQgmgeDDLPsariPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRA 801
Cdd:cd12115 189 AA------EVTLINTVPsAAAELLRH----DALP----ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTY 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 802 VSYFVLPTASSTEspasvtalldkevIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLV 881
Cdd:cd12115 255 STVAPVPPGASGE-------------VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 882 NPFthQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIT 961
Cdd:cd12115 322 DPF--GPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIV 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1574832895 962 HHNEQvKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd12115 400 AEPGA-AGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1144-1858 |
8.91e-108 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 386.62 E-value: 8.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1144 LFAASFAQERLWFLHRFEPESSAYHLFLAFELDGqFQPAAFEESLNDLLARHESLRTSFVLQGE--QLMQRIHAQLWLSL 1221
Cdd:PRK12316 4102 IYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGElgRPLQVVHKQVSLPF 4180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1222 SQQHLSLPAESESSLsqqalQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYN 1301
Cdd:PRK12316 4181 AELDWRGRADLQAAL-----DALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYS 4255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1302 AHvkgispQLAPLPLQYADYAvwqrAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVG-ARHQLHLPAELL 1380
Cdd:PRK12316 4256 GR------PPAQPGGRYRDYI----AWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANGyGEHVRELDATAT 4325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1381 EQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGR--QRRELEGVIGLFANTLVLRTDLSGDPSFLELLQR 1458
Cdd:PRK12316 4326 ARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQ 4405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1459 VREVTLQAYSQQDMPFEklvaELQPERSLAYNPLFQVFFALQNVP-------GDPISLEGLDVTQirLDSNSAKFDLSWT 1531
Cdd:PRK12316 4406 VQRQNLALREHEHTPLY----EIQRWAGQGGEALFDSLLVFENYPvsealqqGAPGGLRFGEVTN--HEQTNYPLTLAVG 4479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1532 WyqedEKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLLSL-GHSSSPLPAAPScgL 1610
Cdd:PRK12316 4480 L----GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALwNRTDAGYPATRC--V 4553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1611 HHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDP 1690
Cdd:PRK12316 4554 HQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDP 4633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1691 DYPSQRLLWMAQDAQLSLLLTHEELKARWPhCPCPLLCLDTLQER-YASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGV 1769
Cdd:PRK12316 4634 EYPRERLAYMMEDSGAALLLTQSHLLQRLP-IPDGLASLALDRDEdWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGV 4712
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1770 QISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASqEQASDPRQLASLLAQLPISILQAT 1849
Cdd:PRK12316 4713 AVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRD-DSLWDPERLYAEIHEHRVTVLVFP 4791
|
....*....
gi 1574832895 1850 PTTWQLLLE 1858
Cdd:PRK12316 4792 PVYLQQLAE 4800
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
502-1011 |
8.66e-107 |
|
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: 349.24 E-value: 8.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYV 581
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 QRAHARgwlriegatdcqeldewcransycnLVLARnfalsgilsqyaSSAPAYrvgpndiacLTFTSGSTGRPKGVLQR 661
Cdd:cd17652 81 ADARPA-------------------------LLLTT------------PDNLAY---------VIYTSGSTGRPKGVVVT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHM--GDPgwLAQWMQGQEITIASFTP 739
Cdd:cd17652 115 HRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELlpGEP--LADLLREHRITHVTLPP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 740 ALLQLLtqgmgeddlPSARIPSLRYAFVVGDALTRRHVARLyavAPHITCVNLYGSTETqravsyfvlpTASSTESPASV 819
Cdd:cd17652 193 AALAAL---------PPDDLPDLRTLVVAGEACPAELVDRW---APGRRMINAYGPTET----------TVCATMAGPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 820 TAlldkEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFThQEHDRLYRTGDLG 899
Cdd:cd17652 251 GG----GVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFG-APGSRMYRTGDLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 900 RYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQvKPVLSNLRAFVT 979
Cdd:cd17652 326 RWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGA-APTAAELRAHLA 404
|
490 500 510
....*....|....*....|....*....|..
gi 1574832895 980 QRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd17652 405 ERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
498-1010 |
2.09e-106 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 348.47 E-value: 2.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 498 AHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARL 577
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 578 LEyvqrahargwlriegatdcqeldewcransycnlvlarnfalsgILSqyASSAPAYRVGPNDIACLTFTSGSTGRPKG 657
Cdd:cd05945 81 RE--------------------------------------------ILD--AAKPALLIADGDDNAYIIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 658 VLQRHGPLTHFLPWMRDRFAFTQTDRYsllsgLAHDPLQ-----REIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEI 732
Cdd:cd05945 115 VQISHDNLVSFTNWMLSDFPLGPGDVF-----LNQAPFSfdlsvMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGI 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 733 TIASFTPALLQLLtqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPtass 812
Cdd:cd05945 190 TVWVSTPSFAAMC---LLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVT---- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 813 tesPASVTALldkEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfTHQEHDRL 892
Cdd:cd05945 263 ---PEVLDGY---DRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF-----FPDEGQRA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 893 YRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIT--HHNEQVKPV 970
Cdd:cd05945 332 YRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpkPGAEAGLTK 411
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1574832895 971 LsnLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05945 412 A--IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-1096 |
3.15e-106 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 381.44 E-value: 3.15e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 33 FPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEP-IQVIRPNLTLQIPL 111
Cdd:PRK05691 3258 YPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETmLQVIHKPGRTPIDY 3337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAG 191
Cdd:PRK05691 3338 LDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEG 3417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 192 NSPTLPAPSlQYADYAAWqrnwLKGENLTNLLDYWRKQLADMPPLLELPMDHP--RPAVQTSHGAVVS---LLLPSEIST 266
Cdd:PRK05691 3418 REAQLPVPP-RYRDYIGW----LQRQDLAQARQWWQDNLRGFERPTPIPSDRPflREHAGDSGGMVVGdcyTRLDAADGA 3492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 267 ALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANR--NRTDIEHVFGFFVNTLVLRI---DVASELNFRTLL 341
Cdd:PRK05691 3493 RLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVqlpAAGQRCSVRQWL 3572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 342 QRVKEMTLEAYAHQDIPFDALLD--ELNPERSLSHSLLfqVFFNMVNLPDLHDEWPDLKVEHLWPReIGSKFDLTLfVQE 419
Cdd:PRK05691 3573 QGLLDSNMELREYEYLPLVAIQEcsELPKGQPLFDSLF--VFENAPVEVSVLDRAQSLNASSDSGR-THTNFPLTA-VCY 3648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 420 EQDAIRLELVYNTDLFKHERMLEMLEQYS-CLASQVSERDEMISRYSLVSTRASSVLPDpGAPISAH---WEGTIHDLFA 495
Cdd:PRK05691 3649 PGDDLGLHLSYDQRYFDAPTVERLLGEFKrLLLALVQGFHGDLSELPLLGEQERDFLLD-GCNRSERdypLEQSYVRLFE 3727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 496 QQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPA 575
Cdd:PRK05691 3728 AQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQ 3807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 576 RLLEYVQRAhaRGWLRIEGATdCQE-----LDEWCRANSYCNLVLARNFAlsgilSQYASSAPAYRVGPNDIACLTFTSG 650
Cdd:PRK05691 3808 RLQRIIELS--RTPVLVCSAA-CREqaralLDELGCANRPRLLVWEEVQA-----GEVASHNPGIYSGPDNLAYVIYTSG 3879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKGVL-QRHGPLTHFL---PWM----RDRFAFTQTDRY--SLLSGLAhdplqreifTPLcVGATICIPDQEHMGDP 720
Cdd:PRK05691 3880 STGLPKGVMvEQRGMLNNQLskvPYLalseADVIAQTASQSFdiSVWQFLA---------APL-FGARVEIVPNAIAHDP 3949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 721 GWLAQWMQGQEITIASFTPALLQlltqGMGEDDlpSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQR 800
Cdd:PRK05691 3950 QGLLAHVQAQGITVLESVPSLIQ----GMLAED--RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSD 4023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 801 AVSYFVLPTASSTESpasvtalldkeVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFL 880
Cdd:PRK05691 4024 DVAFFRVDLASTRGS-----------YLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFV 4092
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 881 VNPFThQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQIVAYI 960
Cdd:PRK05691 4093 PHPFG-APGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEG-VNGKHLVGYL 4170
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 961 THHNEQVKPvlSNLRAFVTQRL----PAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAADEATLSLATPQSPIQEELCL 1036
Cdd:PRK05691 4171 VPHQTVLAQ--GALLERIKQRLraelPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLAT 4248
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1037 LWCELLGLKKVGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASLI 1096
Cdd:PRK05691 4249 IWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
31-470 |
1.04e-105 |
|
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: 346.63 E-value: 1.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 31 NTFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAM-LNGEPIQVIRPNLTLQI 109
Cdd:pfam00668 3 DEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPFEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 110 PLIDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAAL 189
Cdd:pfam00668 83 EIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 190 AGNSPTLPaPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALK 269
Cdd:pfam00668 163 KGEPLPLP-PKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 270 ALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTL 349
Cdd:pfam00668 242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 350 EAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDlHDEWPDLK-------VEHLWPREIgSKFDLTLFVQEEQD 422
Cdd:pfam00668 322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLG-QDSQEEEFqlseldlSVSSVIEEE-AKYDLSLTASERGG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1574832895 423 AIRLELVYNTDLFKHERMLEMLEQYSCLASQVSER-DEMISRYSLVSTR 470
Cdd:pfam00668 400 GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHpSQPLSELDLLSDA 448
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
490-1019 |
1.05e-102 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 337.94 E-value: 1.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 490 IHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILD 569
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 570 PSYPPARLLEYVQRAHARgwlriegatdcqeldewcransycnLVLArnfalsgilsqyassapayrvgpndiACLTFTS 649
Cdd:COG0318 81 PRLTAEELAYILEDSGAR-------------------------ALVT--------------------------ALILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 650 GSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGATICIPDQehmGDPGWLAQWMQ 728
Cdd:COG0318 110 GTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPR---FDPERVLELIE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 729 GQEITIASFTPALLQLLTQgmgEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVApHITCVNLYGSTETQRAVSYfvLP 808
Cdd:COG0318 187 RERVTVLFGVPTMLARLLR---HPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTV--NP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 809 TASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqe 888
Cdd:COG0318 261 EDPGERRPGSV-----------GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 889 HDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHnEQVK 968
Cdd:COG0318 321 RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR-PGAE 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 969 PVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAADEA 1019
Cdd:COG0318 400 LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGAL 450
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
491-1011 |
2.74e-99 |
|
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: 327.59 E-value: 2.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 491 HDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDP 570
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 571 SYPPARLleyvqrahargwlriegatdcqeldEWCRANSYCNLVLARnfalsgilsqyassapayrvgPNDIACLTFTSG 650
Cdd:cd17645 81 DYPGERI-------------------------AYMLADSSAKILLTN---------------------PDDLAYVIYTSG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQ 730
Cdd:cd17645 115 STGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 731 EITIaSFTPAllQLLTQGMGEDDlpsariPSLRYAFVVGDALTRrhvarlyAVAPHITCVNLYGSTE-TQRAVSYFVLPT 809
Cdd:cd17645 195 GITI-SFLPT--GAAEQFMQLDN------QSLRVLLTGGDKLKK-------IERKGYKLVNNYGPTEnTVVATSFEIDKP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 810 ASStespasvtalldkevIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEh 889
Cdd:cd17645 259 YAN---------------IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGE- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 890 dRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThHNEQVKP 969
Cdd:cd17645 323 -RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT-APEEIPH 400
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1574832895 970 vlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd17645 401 --EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1148-1570 |
1.67e-98 |
|
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: 324.72 E-value: 1.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1148 SFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGeqlmQRIHAQLWLSLSQQHLS 1227
Cdd:cd19539 5 SFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDD----GGVPRQEILPPGPAPLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1228 LPAESESSLSQQALQAWLQQE-IRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKG 1306
Cdd:cd19539 81 VRDLSDPDSDRERRLEELLRErESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1307 ISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATApALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVL 1386
Cdd:cd19539 161 PAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVAALREL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1387 SHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQA 1466
Cdd:cd19539 240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1467 YSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPGDPISLEG-LDVTQIRLDSNSAKFDLSWTwYQEDEKSLSAVIE 1545
Cdd:cd19539 320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGgLSYTEGSDIPDGAKFDLNLT-VTEEGTGLRGSLG 398
|
410 420
....*....|....*....|....*
gi 1574832895 1546 YNTALFEPQRIAGMATNMLVVLQSL 1570
Cdd:cd19539 399 YATSLFDEETIQGFLADYLQVLRQL 423
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1146-1593 |
3.24e-98 |
|
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: 325.06 E-value: 3.24e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1146 AASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQ-LMQRIHAQLWLSLSQQ 1224
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGePVQVILEERPFELEII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1225 HLSLPAESESslsQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHV 1304
Cdd:pfam00668 86 DISDLSESEE---EEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1305 KGISPQLAPLPlQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLM 1384
Cdd:pfam00668 163 KGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1385 VLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTL 1464
Cdd:pfam00668 242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1465 QAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVPG-----DPISLEGLDVTQIRLDSNSAKFDLSWTWYqEDEKS 1539
Cdd:pfam00668 322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGqdsqeEEFQLSELDLSVSSVIEEEAKYDLSLTAS-ERGGG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1574832895 1540 LSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLL 1593
Cdd:pfam00668 401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
502-1010 |
1.16e-95 |
|
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: 317.49 E-value: 1.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLlEYV 581
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL-QYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 qrahargwlriegATDcqeldewcransycnlvlarnfalsgilsqyaSSAPAYRVGPNDIACLTFTSGSTGRPKGVLQR 661
Cdd:cd17650 80 -------------LED--------------------------------SGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFLPWMRDRFAF-TQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFTPA 740
Cdd:cd17650 115 HRNVAHAAHAWRREYELdSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 741 LLQLLtqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYA-VAPHITCVNLYGSTETQRAVSYFVLptasstespaSV 819
Cdd:cd17650 195 LIRPV---MAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAArFGQGMRIINSYGVTEATIDSTYYEE----------GR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 820 TALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEhdRLYRTGDLG 899
Cdd:cd17650 262 DPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGE--RMYRTGDLA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 900 RYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThhnEQVKPVLSNLRAFVT 979
Cdd:cd17650 340 RWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV---AAATLNTAELRAFLA 416
|
490 500 510
....*....|....*....|....*....|.
gi 1574832895 980 QRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd17650 417 KELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
492-1010 |
3.77e-94 |
|
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: 312.71 E-value: 3.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 492 DLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPS 571
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 572 YPPARLlEYVQRahargwlriegatdcqeldewcraNSYCNLVLarnfalsgilsqYASSapayrvgPNDIACLTFTSGS 651
Cdd:cd17653 81 LPSARI-QAILR------------------------TSGATLLL------------TTDS-------PDDLAYIIFTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 652 TGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDqehMGDPgwLAQwmQGQE 731
Cdd:cd17653 117 TGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD---PSDP--FAH--VART 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 732 ITIASFTPALLQLltqgmgeddLPSARIPSLRYAFVVGDALTRRHVARLyavAPHITCVNLYGSTETQRAVSYfvlptas 811
Cdd:cd17653 190 VDALMSTPSILST---------LSPQDFPNLKTIFLGGEAVPPSLLDRW---SPGRRLYNAYGPTECTISSTM------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 812 stespasvTALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEhdR 891
Cdd:cd17653 251 --------TELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGS--R 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 892 LYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEA-ILVEHPMVADAAVIIREDTpdnkqIVAYIThhNEQVkpV 970
Cdd:cd17653 321 MYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGR-----LVAFVT--PETV--D 391
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1574832895 971 LSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd17653 392 VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
502-1011 |
9.04e-93 |
|
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: 310.17 E-value: 9.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYV 581
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 582 QRAHARGWLriegatdcqeldewcrANSYCNLVLARNFAL----SGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKG 657
Cdd:cd17656 82 LDSGVRVVL----------------TQRHLKSKLSFNKSTilleDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 658 VLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASF 737
Cdd:cd17656 146 VQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 738 TPALLQLLTQGMG-EDDLPSaripSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESP 816
Cdd:cd17656 226 PVAFLKFIFSEREfINRFPT----CVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 817 asvtalldkeviPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFthQEHDRLYRTG 896
Cdd:cd17656 302 ------------PIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF--DPNERMYRTG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 897 DLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThhNEQVKPVlSNLRA 976
Cdd:cd17656 368 DLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNI-SQLRE 444
|
490 500 510
....*....|....*....|....*....|....*
gi 1574832895 977 FVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd17656 445 YLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
35-280 |
2.01e-89 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 291.17 E-value: 2.01e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 35 LSFAQQRLWLLDqlnPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLIDL 114
Cdd:COG4908 1 LSPAQKRFLFLE---PGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 115 TSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNSP 194
Cdd:COG4908 78 SALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 195 TLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKALSQH 274
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*.
gi 1574832895 275 EGVTLF 280
Cdd:COG4908 238 HGATVN 243
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
33-456 |
4.66e-89 |
|
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: 297.78 E-value: 4.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 33 FPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQ-IPL 111
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFrIEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTSLpeAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAG 191
Cdd:cd19066 82 IDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 192 nSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKAL 271
Cdd:cd19066 160 -KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 272 SQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEA 351
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 352 YAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNLPDLHDEWPDLK---VEHLWprEIGSKFDLTLFVQEEQDA-IRLE 427
Cdd:cd19066 319 IEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIfttPVYTS--SEGTVFDLDLEASEDPDGdLLLR 396
|
410 420
....*....|....*....|....*....
gi 1574832895 428 LVYNTDLFKHERMLEMLEQYSCLASQVSE 456
Cdd:cd19066 397 LEYSRGVYDERTIDRFAERYMTALRQLIE 425
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1144-1858 |
4.27e-88 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 322.68 E-value: 4.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1144 LFAASFAQERLWFLHRFEPESSAYHLFLAFELDGqFQPAAFEESLNDLLARHESLRTSFVLQG--EQLMQRIHAQLWLSL 1221
Cdd:PRK12316 1556 IYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDglEQPLQVIHKQVELPF 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1222 SQQHLSLPAESESSLSQQALQawlqqEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYN 1301
Cdd:PRK12316 1635 AELDWRGREDLGQALDALAQA-----ERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYA 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1302 AHVkgispqLAPLPLQYADYAvwqrAWLQEERQEKLQRYWHGQLATapalLDLPT---DHPRPPIQTFVGARHQLHLPAE 1378
Cdd:PRK12316 1710 GQP------VAAPGGRYRDYI----AWLQRQDAAASEAFWKEQLAA----LEEPTrlaQAARTEDGQVGYGDHQQLLDPA 1775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1379 LLEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRrELEGV---IGLFANTLVLRTDLSGDPSFLEL 1455
Cdd:PRK12316 1776 QTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPA-ELPGIeqqIGLFINTLPVIAAPRPDQSVADW 1854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1456 LQRVREVTLQAYSQQDMPfeklVAELQPERSLAYNPLFQVFFALQNVP-------GDPISLEGLDVtqirldSNSAKFDL 1528
Cdd:PRK12316 1855 LQEVQALNLALREHEHTP----LYDIQRWAGQGGEALFDSLLVFENYPvaealkqGAPAGLVFGRV------SNHEQTNY 1924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1529 SWTWYQEDEKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLLSlgHSSSPLPAAPS- 1607
Cdd:PRK12316 1925 PLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILA--DWDRTPEAYPRg 2002
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1608 CGLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVP 1687
Cdd:PRK12316 2003 PGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1688 LDPDYPSQRLLWMAQDAQLSLLLTHEELKARWPhCPCPLLCLD-TLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRP 1766
Cdd:PRK12316 2083 LDPNYPAERLAYMLEDSGAALLLTQRHLLERLP-LPAGVARLPlDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLP 2161
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1767 KGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIqLASQEQASDPRQLASLLAQLPISIL 1846
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTIL 2240
|
730
....*....|..
gi 1574832895 1847 QATPTTWQLLLE 1858
Cdd:PRK12316 2241 DFPPVYLQQLAE 2252
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
502-1011 |
3.47e-87 |
|
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: 293.15 E-value: 3.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQG-IRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLley 580
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 581 vqrahargwlriegatdcqeldewcransycnlvlarNFALSgilsqyASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQ 660
Cdd:cd17648 78 -------------------------------------QFILE------DTGARVVITNSTDLAYAIYTSGTTGKPKGVLV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 661 RHGPLTHFLPWMRDRFAFTQTDRYSLL--SGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQEITIASFT 738
Cdd:cd17648 115 EHGSVVNLRTSLSERYFGRDNGDEAVLffSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 739 PALLQLLtqgmgedDLpsARIPSLRYAFVVGDALTRRHVARLYAVAPHITcVNLYGSTETqravsyfvlpTASSTESPAS 818
Cdd:cd17648 195 PSVLQQY-------DL--ARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLI-INAYGPTET----------TVTNHKRFFP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 819 VTALLDKEvipLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPF-THQE-----HDRL 892
Cdd:cd17648 255 GDQRFDKS---LGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqTEQErargrNARL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 893 YRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIRED-----TPDNKQIVAYITHHNEQV 967
Cdd:cd17648 332 YKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLPEPGHV 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1574832895 968 KPvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd17648 412 PE--SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
32-383 |
6.45e-87 |
|
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: 291.28 E-value: 6.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 32 TFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAM--LNGEPIQVIRPNLTLQI 109
Cdd:cd19532 1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTdpEDGEPMQGVLASSPLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 110 PLIDLTSLPEAEREAslqHAINNeaHIpFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYsaal 189
Cdd:cd19532 81 EHVQISDEAEVEEEF---ERLKN--HV-YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 190 agNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLEL-PMDH--PRPAVQTSHGAVVSLLLPSEIST 266
Cdd:cd19532 151 --NGQPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlPFAKvkSRPPLTRYDTHTAERRLDAALAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 267 ALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKE 346
Cdd:cd19532 229 RIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 1574832895 347 MTLEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFN 383
Cdd:cd19532 309 KAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFIN 345
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
34-452 |
2.64e-86 |
|
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: 289.93 E-value: 2.64e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPLID 113
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 114 LTSlpEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNS 193
Cdd:cd20483 83 LSE--AADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 194 P-TLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPP---LLELPMDHpRPAVQTSHGAVVSLLLPSEISTALK 269
Cdd:cd20483 161 LaTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDaskLLPFAKAE-RPPVKDYERSTVEATLDKELLARMK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 270 ALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTL 349
Cdd:cd20483 240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 350 EAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVnlpdLHDEWP-----DLKVEHLWPREIGSKFDLTLFVQEEQD-A 423
Cdd:cd20483 320 EAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ----VHGKFPeydtgDFKFTDYDHYDIPTACDIALEAEEDPDgG 395
|
410 420 430
....*....|....*....|....*....|
gi 1574832895 424 IRLELVYNTDLFKHERMLEMLEQYS-CLAS 452
Cdd:cd20483 396 LDLRLEFSTTLYDSADMERFLDNFVtFLTS 425
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
494-920 |
7.65e-83 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 279.20 E-value: 7.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 494 FAQQAHLRPENIAI-IDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSY 572
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 573 PPARLLEYVQRAHAR-----GWLRIEGATDCQELDEwcraNSYCNLVLARNFALSGILS------QYASSAPAYRVGPND 641
Cdd:pfam00501 81 PAEELAYILEDSGAKvlitdDALKLEELLEALGKLE----VVKLVLVLDRDPVLKEEPLpeeakpADVPPPPPPPPDPDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 642 IACLTFTSGSTGRPKGVLQRHGPLTHFLPWM----RDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGATICIPDQEH 716
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDfGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 717 MGDPGWLAQWMQGQEITIASFTPALLQLLTQgmgEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPhITCVNLYGST 796
Cdd:pfam00501 237 ALDPAALLELIERYKVTVLYGVPTLLNMLLE---AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 797 ETQrAVSYFVLPTASSTESPASVtalldkeviplGKGMPGAQILILNEA-GNLAGIGELGEIYVRSPHLAFGYLDDPDQT 875
Cdd:pfam00501 313 ETT-GVVTTPLPLDEDLRSLGSV-----------GRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELT 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1574832895 876 NERFLvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIR 920
Cdd:pfam00501 381 AEAFD--------EDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
32-454 |
1.67e-82 |
|
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: 278.82 E-value: 1.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 32 TFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPL 111
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTSLPEAEreaSLQHaINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAG 191
Cdd:cd20484 81 EDISSLKESE---IIAY-LREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 192 NSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKAL 271
Cdd:cd20484 157 KQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 272 SQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEA 351
Cdd:cd20484 237 ARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 352 YAHQDIPFDALLDELNPERSLSHSLLFQV------FFNMVNLPDLHDEWPD-LKVEHLwpREIGS--KFDLTLFVQEEQD 422
Cdd:cd20484 317 LDHAAYPFPAMVRDLNIPRSQANSPVFQVaffyqnFLQSTSLQQFLAEYQDvLSIEFV--EGIHQegEYELVLEVYEQED 394
|
410 420 430
....*....|....*....|....*....|..
gi 1574832895 423 AIRLELVYNTDLFKHERMLEMLEQYSCLASQV 454
Cdd:cd20484 395 RFTLNIKYNPDLFDASTIERMMEHYVKLAEEL 426
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1181-1860 |
6.08e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 295.53 E-value: 6.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1181 PAAFEESLNDLLARHESLRTSFVLQG--EQLMQRIHAQLWLSLSQQHLSLPAESESSLSQQALQawlqqEIRRPFDLQQA 1258
Cdd:PRK12467 2682 VERFRTAWQAVIDRHEILRSGFLWDGelEEPLQVVYKQARLPFSRLDWRDRADLEQALDALAAA-----DRQQGFDLLSA 2756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1259 PLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSlcynAHVKGISPqlAPLPLQYADYAvwqrAWLQEERQEKLQ 1338
Cdd:PRK12467 2757 PLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVL----QRYFGQPP--PAREGRYRDYI----AWLQAQDAEASE 2826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1339 RYWHGQLA--TAPALLdLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLV 1416
Cdd:PRK12467 2827 AFWKEQLAalEEPTRL-ARALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVC 2905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1417 VGTPIAGR--QRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQAYSQQDMPfeklVAELQPERSLAYNPLFQ 1494
Cdd:PRK12467 2906 FGATVAGRpaQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTP----LADIQRWAGQGGEALFD 2981
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1495 VFFALQNVPGDPISLEGLDvTQIRLDSNSAkfdLSWTWYQED-----EKSLSAVIEYNTALFEPQRIAGMATNMLVVLQS 1569
Cdd:PRK12467 2982 SILVFENYPISEALKQGAP-SGLRFGAVSS---REQTNYPLTlavglGDTLELEFSYDRQHFDAAAIERLAESFDRLLQA 3057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1570 LCQEPRTPVSLLPLLSAAQRLHLLSLGHSSSPLPAAPSCgLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHL 1649
Cdd:PRK12467 3058 MLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERL-VHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHR 3136
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1650 LRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHEELKARWPHcPCPLLCL 1729
Cdd:PRK12467 3137 LIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPA-PAGDTAL 3215
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1730 DTLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLE 1809
Cdd:PRK12467 3216 TLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER 3295
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 1810 LYLPLLAGAQIQLASQEQaSDPRQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:PRK12467 3296 FLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAEDA 3345
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1625-1875 |
1.24e-78 |
|
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: 269.16 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd12116 4 TAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTHEELKARWPHCpCPLLCLDtlqERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQ 1784
Cdd:cd12116 84 EPALVLTDDALPDRLPAG-LPVLLLA---LAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1785 SLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETGWSGK 1864
Cdd:cd12116 160 ERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGR 239
|
250
....*....|.
gi 1574832895 1865 AGLTLLSGAKP 1875
Cdd:cd12116 240 AGLTALCGGEA 250
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1147-1395 |
4.08e-75 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 250.34 E-value: 4.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1147 ASFAQERLWFLhrfEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQHL 1226
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1227 S--LPAESESSLsqqalQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHV 1304
Cdd:COG4908 78 SalPEPEREAEL-----EELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1305 KGISPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLM 1384
Cdd:COG4908 153 EGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALK 232
|
250
....*....|.
gi 1574832895 1385 VLSHQQQVTLY 1395
Cdd:COG4908 233 ALAKAHGATVN 243
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1147-1574 |
2.98e-70 |
|
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: 243.54 E-value: 2.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1147 ASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQlwlSLSQQHL 1226
Cdd:cd19546 7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDA---DAARPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1227 SLPAESESSLSQQALQAWLqqeirRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKG 1306
Cdd:cd19546 84 PVVPATEEELPALLADRAA-----HLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1307 ISPQLAPLPLQYADYAVWQRAWLQEERQ------EKLQrYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELL 1380
Cdd:cd19546 159 RAPERAPLPLQFADYALWERELLAGEDDrdsligDQIA-YWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1381 EQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRR-ELEGVIGLFANTLVLRTDLSGDPSFLELLQRV 1459
Cdd:cd19546 238 ARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1460 REVTLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQ---NVPGDPISLEGLDVTQIRLDSNSAKFDLSWT---WY 1533
Cdd:cd19546 318 REAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRdddNDPWDAPELPGLRTSPVPLGTEAMELDLSLAlteRR 397
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1574832895 1534 QED--EKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19546 398 NDDgdPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1144-1574 |
1.86e-69 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 240.77 E-value: 1.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1144 LFAASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLS-LS 1222
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFrIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1223 QQHLSLPAESESSLSQQALQAWlqqeiRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNA 1302
Cdd:cd19066 81 IIDLRNLADPEARLLELIDQIQ-----QTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1303 HVKGiSPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQ 1382
Cdd:cd19066 156 AERQ-KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1383 LMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREV 1462
Cdd:cd19066 235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1463 TLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNVP-GDPISLEGLDVTQIRLDSNSAKFDLSWTWYQEDEKSLS 1541
Cdd:cd19066 315 SREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQqQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDPDGDLL 394
|
410 420 430
....*....|....*....|....*....|...
gi 1574832895 1542 AVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19066 395 LRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
34-457 |
4.49e-69 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 239.80 E-value: 4.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLN-GEPIQVIRPNLTLQIPLI 112
Cdd:cd19543 3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRKLPWREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 113 DLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAGN 192
Cdd:cd19543 83 DLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 193 SPTLPAPSlQYADYAAwqrnWLKGENLTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPSEISTALKALS 272
Cdd:cd19543 163 PPSLPPVR-PYRDYIA----WLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 273 QHEGVTLfmTTL--ALFQILLQRYTGRRDIVIGTPIANRNR--TDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMT 348
Cdd:cd19543 238 RQHGVTL--NTVvqGAWALLLSRYSGRDDVVFGTTVSGRPAelPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 349 LEAYAHQDIPfdalLDELNpERSLSHSLLFQ---VFFNMVNLPDLHDEWPD--LKVEHLWPREiGSKFDLTLFVQEEqDA 423
Cdd:cd19543 316 LELREHEYVP----LYEIQ-AWSEGKQALFDhllVFENYPVDESLEEEQDEdgLRITDVSAEE-QTNYPLTVVAIPG-EE 388
|
410 420 430
....*....|....*....|....*....|....
gi 1574832895 424 IRLELVYNTDLFKHERMLEMLEQYSCLASQVSER 457
Cdd:cd19543 389 LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
641-1006 |
1.28e-68 |
|
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: 235.26 E-value: 1.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDqehMGDP 720
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 721 GWLAQWMQGQEITIASFTPALLQLLTQGMGEDDlpsARIPSLRYAFVVGDALtRRHVARLYAVAPHITCVNLYGSTETQR 800
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAG---YDLSSLRALVSGGAPL-PPELLERFEEAPGIKLVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 801 AVSYfvLPTASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFl 880
Cdd:cd04433 154 TVAT--GPPDDDARKPGSV-----------GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 881 vnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYI 960
Cdd:cd04433 220 --------EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVV 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1574832895 961 tHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVD 1006
Cdd:cd04433 292 -VLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1150-1851 |
1.38e-67 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 252.66 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1150 AQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLsqqhLSLP 1229
Cdd:PRK10252 13 AQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPL----PEII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1230 AESESSLSQQALQAWLQQEIRRPFDLQQA-PLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGIS 1308
Cdd:PRK10252 89 DLRTQPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1309 PQLAPLPLQ---YADYAVWQrawlQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMV 1385
Cdd:PRK10252 169 TPASPFTPFadvVEEYQRYR----ASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGAFRQLAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1386 LSHQQQ--------VTLYMTllaafllllyRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQ 1457
Cdd:PRK10252 245 QASGVQrpdlalalVALWLG----------RLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1458 RVREVTLQAYSQQDMPFEKLVAELQ---PERSLaYNPLFQVffalqnVPGD-PISLEGLDVTQIRLDSNSAKfDLSWTWY 1533
Cdd:PRK10252 315 RLAAQLKKMRRHQRYDAEQIVRDSGraaGDEPL-FGPVLNI------KVFDyQLDFPGVQAQTHTLATGPVN-DLELALF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1534 QEDEKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLLSLGHSSSPLPAAPscgLHHL 1613
Cdd:PRK10252 387 PDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETT---LSAL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1614 IEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYP 1693
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1694 SQRLLWMAQDAQLSLLLTHEELKARWPHCP-CPLLCLDTLQERYASLPCEDLQeacsPAQLAYVIYTSGSTGRPKGVQIS 1772
Cdd:PRK10252 544 DDRLKMMLEDARPSLLITTADQLPRFADVPdLTSLCYNAPLAPQGAAPLQLSQ----PHHTAYIIFTSGSTGRPKGVMVG 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1773 HGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPT 1851
Cdd:PRK10252 620 QTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPS 698
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
32-446 |
5.27e-67 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 233.42 E-value: 5.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 32 TFPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPL 111
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTSLPEAEREAslQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAG 191
Cdd:cd19533 81 IDLSGDPDPEGAA--QQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 192 -NSPTLPAPSL--------QYADYAAWQRNwlkgenltnlLDYWRKQLADMPPLLELpmdhPRPAVQTSHGAVV-SLLLP 261
Cdd:cd19533 159 rPAPPAPFGSFldlveeeqAYRQSERFERD----------RAFWTEQFEDLPEPVSL----ARRAPGRSLAFLRrTAELP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 262 SEISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRIDVASELNFRTLL 341
Cdd:cd19533 225 PELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 342 QRVKEMTLEAYAHQDIPFDALLDELNPERSLSHslLFQVFFNmVNLPDLHDEWPDLKVEhlwPREI--GSKFDLTLFVQE 419
Cdd:cd19533 305 AQVSRELRSLLRHQRYRYEDLRRDLGLTGELHP--LFGPTVN-YMPFDYGLDFGGVVGL---THNLssGPTNDLSIFVYD 378
|
410 420 430
....*....|....*....|....*....|....*.
gi 1574832895 420 EQD--AIRLELVYNTDLF------KH-ERMLEMLEQ 446
Cdd:cd19533 379 RDDesGLRIDFDANPALYsgedlaRHqERLLRLLEE 414
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1148-1574 |
1.73e-65 |
|
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: 229.51 E-value: 1.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1148 SFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQqhls 1227
Cdd:cd20484 5 SEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1228 lpaESESSLSQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGI 1307
Cdd:cd20484 81 ---EDISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1308 SPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVLS 1387
Cdd:cd20484 158 QPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1388 HQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQAY 1467
Cdd:cd20484 238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1468 SQQDMPFEKLVAELQPERSLAYNPLFQVFFALQNV--PGDPISL-----EGLDVTQIRLDSNSAKFDLSW-TWYQEDEKS 1539
Cdd:cd20484 318 DHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFlqSTSLQQFlaeyqDVLSIEFVEGIHQEGEYELVLeVYEQEDRFT 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1574832895 1540 LSavIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd20484 398 LN--IKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1148-1497 |
1.94e-63 |
|
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: 223.10 E-value: 1.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1148 SFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGE--QLMQRIHAQLWLSLSQQH 1225
Cdd:cd19532 5 SFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEdgEPMQGVLASSPLRLEHVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1226 LSLPAESESSLsqqalqawlqQEIR-RPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNahv 1304
Cdd:cd19532 85 ISDEAEVEEEF----------ERLKnHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1305 kgiSPQLAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPA---LLDLPTDHPRPPIQTFVGARHQLHLPAELLE 1381
Cdd:cd19532 152 ---GQPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEplpLLPFAKVKSRPPLTRYDTHTAERRLDAALAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1382 QLMVLSHQQQVT---LYMTLLAAFLlllYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQR 1458
Cdd:cd19532 229 RIKEASRKLRVTpfhFYLAALQVLL---ARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKE 305
|
330 340 350
....*....|....*....|....*....|....*....
gi 1574832895 1459 VREVTLQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFF 1497
Cdd:cd19532 306 TRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFI 344
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
491-1010 |
3.12e-63 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 227.30 E-value: 3.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 491 HDLFAQQAHLRPENIAII-----DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTV 565
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 566 LILDPSYPPARLLEYVQRAHAR------GWLRIEGATDCQE-LDEWCRA-----------NSYCNLVLARNFALSGILSQ 627
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKvlitadGGLRGGKVIDLKEkVDEALEElpslehvivvgRTGADVPMEGDLDWDELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 628 YASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRH-GPLTHFLPWMR--------DRFaFTQTDR-------YSLLSgla 691
Cdd:COG0365 172 ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHgGYLVHAATTAKyvldlkpgDVF-WCTADIgwatghsYIVYG--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 692 hdplqreiftPLCVGATICI-PDQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQgMGEDDLPSARIPSLRYAFVVGD 770
Cdd:COG0365 248 ----------PLLNGATVVLyEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMK-AGDEPLKKYDLSSLRLLGSAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 771 ALTRRHVARLYAVApHITCVNLYGSTETqraVSYFVLPTASSTESPASvtalldkevipLGKGMPGAQILILNEAGNLAG 850
Cdd:COG0365 317 PLNPEVWEWWYEAV-GVPIVDGWGQTET---GGIFISNLPGLPVKPGS-----------MGKPVPGYDVAVVDEDGNPVP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 851 IGELGEIYVRSPHLAF--GYLDDPDQTNERFlvnpftHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEE 928
Cdd:COG0365 382 PGEEGELVIKGPWPGMfrGYWNDPERYRETY------FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 929 IEAILVEHPMVADAAVIIREDtPDNKQ-IVAYIT-HHNEQVKPVLSN-LRAFVTQRLPAFMVPAHFVFMSRLPLNANGKV 1005
Cdd:COG0365 456 IESALVSHPAVAEAAVVGVPD-EIRGQvVKAFVVlKPGVEPSDELAKeLQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
....*
gi 1574832895 1006 DRKAL 1010
Cdd:COG0365 535 MRRLL 539
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
34-446 |
6.84e-62 |
|
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: 219.27 E-value: 6.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVI------RPNLTL 107
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldadaaRPELPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 108 qiplidltsLPEAEREasLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSA 187
Cdd:cd19546 86 ---------VPATEEE--LPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 188 ALAGNSPTLPAPSLQYADYAAWQRNWLKGEN-----LTNLLDYWRKQLADMPPLLELPMDHPRPAVQTSHGAVVSLLLPS 262
Cdd:cd19546 155 RREGRAPERAPLPLQFADYALWERELLAGEDdrdslIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 263 EISTALKALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRN-RTDIEHVFGFFVNTLVLRIDVASELNFRTLL 341
Cdd:cd19546 235 EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 342 QRVKEMTLEAYAHQDIPFDALLDELNPERSLSHSLLFQVFFNMVNlpDLHDEW-----PDLKVEHLWPREIGSKFDLTLF 416
Cdd:cd19546 315 GRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRD--DDNDPWdapelPGLRTSPVPLGTEAMELDLSLA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1574832895 417 VQEEQ------DAIRLELVYNTDLFKH-------ERMLEMLEQ 446
Cdd:cd19546 393 LTERRnddgdpDGLDGSLRYAADLFDRataaalaRRLVRVLEQ 435
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1151-1574 |
9.38e-62 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 218.61 E-value: 9.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1151 QERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQG-EQLMQRIHAQL---WLSLSQQHL 1226
Cdd:cd19543 8 QEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGlGEPLQVVLKDRklpWRELDLSHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1227 SlPAESESSLsqqalQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKG 1306
Cdd:cd19543 88 S-EAEQEAEL-----EALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1307 ISPQLAPLPlQYADYAvwqrAWLQEERQEKLQRYWHGQLATAPALLDLPTDHPRPPIQTFVGARHQLHLPAELLEQLMVL 1386
Cdd:cd19543 162 QPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1387 SHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQrRELEGV---IGLFANTLVLRTDLSGDPSFLELLQRVREVT 1463
Cdd:cd19543 237 ARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQAQQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1464 LQAYSQQDMPFeklvAELQpERSLAYNPLFQVFFALQNVPGDPISLE-----GLDVTQIRLDSNSaKFDLSWTWYQEDEk 1538
Cdd:cd19543 316 LELREHEYVPL----YEIQ-AWSEGKQALFDHLLVFENYPVDESLEEeqdedGLRITDVSAEEQT-NYPLTVVAIPGEE- 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 1574832895 1539 sLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19543 389 -LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1635-1870 |
2.84e-61 |
|
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: 216.75 E-value: 2.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1635 TYRQLNQQANQLAHLLRQ-HGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHE 1713
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1714 ELKARWPHCPCPLLCLDTLQERY--ASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSP 1791
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAAldDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1792 HDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASD-PRQLASLLAQLPISILQATPTTWQLLLETGWSGKAGLTLL 1870
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDdAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1148-1570 |
4.64e-60 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. 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: 213.66 E-value: 4.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1148 SFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHAQLWLSLSQQHLS 1227
Cdd:cd20483 5 STFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1228 LPAESESSLSQQALQAWlqqeiRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGI 1307
Cdd:cd20483 85 EAADPEAALDQLVRNLR-----RQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1308 SPQ-LAPLPLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPA---LLDLPTDHpRPPIQTFVGARHQLHLPAELLEQL 1383
Cdd:cd20483 160 DLAtVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDaskLLPFAKAE-RPPVKDYERSTVEATLDKELLARM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1384 MVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVT 1463
Cdd:cd20483 239 KRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1464 LQAYSQQDMPFEKLVAELQPERSLAYNPLFQVFFALQnVPGD--PISLEGLDVTQIRLDSNSAKFDLSWTWYQEDEKSLS 1541
Cdd:cd20483 319 LEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-VHGKfpEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDGGLD 397
|
410 420
....*....|....*....|....*....
gi 1574832895 1542 AVIEYNTALFEPQRIAGMATNMLVVLQSL 1570
Cdd:cd20483 398 LRLEFSTTLYDSADMERFLDNFVTFLTSV 426
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1624-1860 |
1.19e-59 |
|
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: 213.16 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:cd05930 3 AVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLLLTHeelkarwphcpcpllcldtlqeryaslpcedlqeacsPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSL 1783
Cdd:cd05930 83 SGAKLVLTD-------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 1784 QSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQEL 202
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
489-1010 |
4.17e-59 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 213.22 E-value: 4.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDlFAQQahlRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLIL 568
Cdd:PRK04813 7 TIEE-FAQT---QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 569 DPSYPPARLLEYVQRAHARGWLRIE----GATDCQELDEwcransycnlvlarnFALSGILSQYASSAPAYRVGPNDIAC 644
Cdd:PRK04813 83 DVSSPAERIEMIIEVAKPSLIIATEelplEILGIPVITL---------------DELKDIFATGNPYDFDHAVKGDDNYY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 645 LTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDR------YSL-LSGLAhdplqreIFTPLCVGATICIPDQEHM 717
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQflnqapYSFdLSVMD-------LYPTLASGGTLVALPKDMT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 718 GDPGWLAQWMQGQEITIASFTPALLQLLtqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTE 797
Cdd:PRK04813 221 ANFKQLFETLPQLPINVWVSTPSFADMC---LLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 798 TQRAVSyfvlptasSTEspasVTA-LLDK-EVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQT 875
Cdd:PRK04813 298 ATVAVT--------SIE----ITDeMLDQyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 876 NERFlvnpFTHQEHdRLYRTGDLGrYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIiredtPDNK- 954
Cdd:PRK04813 366 AEAF----FTFDGQ-PAYHTGDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-----PYNKd 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 955 ----QIVAYITHHNEQVKPVL---SNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK04813 435 hkvqYLIAYVVPKEEDFEREFeltKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1614-1870 |
1.66e-58 |
|
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: 211.05 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1614 IEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYP 1693
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1694 SQRLLWMAQDAQLSLLLTHEELKARWPHCPCPLLCLDtlQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISH 1773
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLD--QPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1774 GALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTW 1853
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250
....*....|....*..
gi 1574832895 1854 QLLLETGWSGKAGLTLL 1870
Cdd:cd17651 239 RALAEHGRPLGVRLAAL 255
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1613-1872 |
1.47e-55 |
|
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: 202.43 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1613 LIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDY 1692
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1693 PSQRLLWMAQDAQLSLLLTHEELKARWPHCPCPLLCLDTLQERyaslPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQIS 1772
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAG----PAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1773 HgALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTT 1852
Cdd:cd12117 158 H-RGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL 236
|
250 260
....*....|....*....|.
gi 1574832895 1853 WQLLLETGWSGKAGL-TLLSG 1872
Cdd:cd12117 237 FNQLADEDPECFAGLrELLTG 257
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1625-1871 |
5.35e-54 |
|
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: 196.82 E-value: 5.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd17649 4 VALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTHEelkarwphcpcpllcldtlqeryaslpcedlqeacsPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQ 1784
Cdd:cd17649 84 GAGLLLTHH------------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1785 SLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLE----TG 1860
Cdd:cd17649 128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEeadrTG 207
|
250
....*....|.
gi 1574832895 1861 WSGKAGLTLLS 1871
Cdd:cd17649 208 DGRPPSLRLYI 218
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
489-1018 |
1.23e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 197.72 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAG------ 562
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGavlhpi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 563 -----------------STVLILDPSYPP--ARLLEYVQraHARGWLRIEGATDCQELDEWcransycnlvlarnFALSG 623
Cdd:PRK06187 87 nirlkpeeiayilndaeDRVVLVDSEFVPllAAILPQLP--TVRTVIVEGDGPAAPLAPEV--------------GEYEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 624 ILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHdplqreIFT-- 701
Cdd:PRK06187 151 LLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFH------VHAwg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 702 ----PLCVGATICIPDQEhmgDPGWLAQWMQGQEITIASFTPALLQLLtqgMGEDDLPSARIPSLRYAFVVGDALTrRHV 777
Cdd:PRK06187 225 lpylALMAGAKQVIPRRF---DPENLLDLIETERVTFFFAVPTIWQML---LKAPRAYFVDFSSLRLVIYGGAALP-PAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 778 ARLYAVAPHITCVNLYGSTETqravsyfvlptassteSPASVTALLDKEVIPL-------GKGMPGAQILILNEAGNL-- 848
Cdd:PRK06187 298 LREFKEKFGIDLVQGYGMTET----------------SPVVSVLPPEDQLPGQwtkrrsaGRPLPGVEARIVDDDGDElp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 849 AGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGR-NDLqVKIRGYRIELE 927
Cdd:PRK06187 362 PDGGEVGEIIVRGPWLMQGYWNRPEATAETI---------DGGWLHTGDVGYIDEDGYLYITDRiKDV-IISGGENIYPR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 928 EIEAILVEHPMVADAAVIireDTPDNK---QIVAYIT-HHNEQVKPvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANG 1003
Cdd:PRK06187 432 ELEDALYGHPAVAEVAVI---GVPDEKwgeRPVAVVVlKPGATLDA--KELRAFLRGRLAKFKLPKRIAFVDELPRTSVG 506
|
570
....*....|....*
gi 1574832895 1004 KVDRKALPAPEAADE 1018
Cdd:PRK06187 507 KILKRVLREQYAEGK 521
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
521-1010 |
6.07e-53 |
|
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: 193.81 E-value: 6.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 521 ARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGST---VLI-LDPSYPPARLLEYVQRAHARGWLRIEGAT 596
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglVFVpLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 597 D--------CQELDEWCRANSycnLVLARnfalsgilsqyaSSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHF 668
Cdd:cd05922 81 DrlrdalpaSPDPGTVLDADG---IRAAR------------ASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 669 LPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAqwMQGQEITIASFTPALLQLLTQg 748
Cdd:cd05922 146 ARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWED--LREHGATGLAGVPSTYAMLTR- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 749 MGEDDlpsARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYfvLPTASSTESPASVtalldkevi 828
Cdd:cd05922 223 LGFDP---AKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTY--LPPERILEKPGSI--------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 829 plGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNpfthqehDRLYrTGDLGRYLPDGNAE 908
Cdd:cd05922 289 --GLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGG-------GVLH-TGDLARRDEDGFLF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 909 FAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPVLSNLRAfvtqRLPAFMVP 988
Cdd:cd05922 359 IVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAE----RLPPYKVP 434
|
490 500
....*....|....*....|..
gi 1574832895 989 AHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05922 435 ATVRVVDELPLTASGKVDYAAL 456
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1611-1858 |
4.84e-52 |
|
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: 192.11 E-value: 4.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1611 HHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDP 1690
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1691 DYPSQRLLWMAQDAQLSLLLTHEELKARWPHCPCPLLCLDTlqeRYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQ 1770
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDE---ALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1771 ISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATP 1850
Cdd:cd17646 158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
|
....*...
gi 1574832895 1851 TTWQLLLE 1858
Cdd:cd17646 238 SMLRVFLA 245
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
506-1005 |
6.24e-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: 191.66 E-value: 6.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 506 AIIDEIN--TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARL------ 577
Cdd:cd05911 1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELahqlki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 578 ------------LEYVQRAhARGWLRI----------EGATDCQELDEWCRANSYCNLVLARNfalsgilsqyassapay 635
Cdd:cd05911 81 skpkviftdpdgLEKVKEA-AKELGPKdkiivlddkpDGVLSIEDLLSPTLGEEDEDLPPPLK----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 636 rVGPNDIACLTFTSGSTGRPKGVLQRHGPLT--HFLPWMRDRFAFTQTDRYSLLSGLAH-DPLQREIFTPLCvGATICI- 711
Cdd:cd05911 143 -DGKDDTAAILYSSGTTGLPKGVCLSHRNLIanLSQVQTFLYGNDGSNDVILGFLPLYHiYGLFTTLASLLN-GATVIIm 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 --PDQEHMgdpgwlAQWMQGQEITIASFTPALLQLLTQgmgEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITC 789
Cdd:cd05911 221 pkFDSELF------LDLIEKYKITFLYLVPPIAAALAK---SPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 790 VNLYGSTETQRAVSYfvlpTASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLA-GIGELGEIYVRSPHLAFGY 868
Cdd:cd05911 292 KQGYGMTETGGILTV----NPDGDDKPGSV-----------GRLLPNVEAKIVDDDGKDSlGPNEPGEICVRGPQVMKGY 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 869 LDDPDQTNErflvnpftHQEHDRLYRTGDLGRYLPDGNAEFAGR-NDLqVKIRGYRIELEEIEAILVEHPMVADAAVIIR 947
Cdd:cd05911 357 YNNPEATKE--------TFDEDGWLHTGDIGYFDEDGYLYIVDRkKEL-IKYKGFQVAPAELEAVLLEHPGVADAAVIGI 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 948 EDTPDNKQIVAYIthhneqvkpVLSN--------LRAFVTQRLPAFmvpAHF----VFMSRLPLNANGKV 1005
Cdd:cd05911 428 PDEVSGELPRAYV---------VRKPgekltekeVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKI 485
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
496-1007 |
2.02e-51 |
|
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: 188.59 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 496 QQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILdpsyppa 575
Cdd:cd17631 3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 576 rlleyvqrahargwlriegatdcqeldewcransycnlvlarNFALSG--ILSQYASSAPayRVGPNDIACLTFTSGSTG 653
Cdd:cd17631 76 ------------------------------------------NFRLTPpeVAYILADSGA--KVLFDDLALLMYTSGTTG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 654 RPKGVLQRHGPLT-HFLPWMRDrFAFTQTDRYSLLSGLAH-DPLQREIFTPLCVGATICIPDQEhmgDPGWLAQWMQGQE 731
Cdd:cd17631 112 RPKGAMLTHRNLLwNAVNALAA-LDLGPDDVLLVVAPLFHiGGLGVFTLPTLLRGGTVVILRKF---DPETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 732 ITIASFTPALLQLLTQgmgEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHItcVNLYGSTETQRAVSyfVLPTAS 811
Cdd:cd17631 188 VTSFFLVPTMIQALLQ---HPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKF--VQGYGMTETSPGVT--FLSPED 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 812 STESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDR 891
Cdd:cd17631 261 HRRKLGSA-----------GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF---------RDG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 892 LYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIRedtPDNK--QIVAYITHHNEQVKP 969
Cdd:cd17631 321 WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGV---PDEKwgEAVVAVVVPRPGAEL 397
|
490 500 510
....*....|....*....|....*....|....*...
gi 1574832895 970 VLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:cd17631 398 DEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
492-1010 |
4.49e-51 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 188.54 E-value: 4.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 492 DLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPS 571
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 572 YPPARLLEYVQRAHARGwlriegatdcqeldewcransycnLVLARNFAlsGILSQYASSAPAYRVGPNDIACLTFTSGS 651
Cdd:cd05936 83 YTPRELEHILNDSGAKA------------------------LIVAVSFT--DLLAAGAPLGERVALTPEDVAVLQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 652 TGRPKGVLQRHGPLTH----------FLPWMRDRF--------AFTQTdryslLSGLAhdplqreiftPLCVGATICI-- 711
Cdd:cd05936 137 TGVPKGAMLTHRNLVAnalqikawleDLLEGDDVVlaalplfhVFGLT-----VALLL----------PLALGATIVLip 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 -PDqehmgDPGWLAQwMQGQEITIASFTPALLQLLtqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVaphiTCV 790
Cdd:cd05936 202 rFR-----PIGVLKE-IRKHRVTIFPGVPTMYIAL---LNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEEL----TGV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 791 NL---YGSTETqravsyfvlptassteSPasVTAL--LDKEVIP--LGKGMPGAQILILNEAGNLAGIGELGEIYVRSPH 863
Cdd:cd05936 269 PIvegYGLTET----------------SP--VVAVnpLDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQ 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 864 LAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGR-NDLqVKIRGYRIELEEIEAILVEHPMVADA 942
Cdd:cd05936 331 VMKGYWNRPEETAEAF---------VDGWLRTGDIGYMDEDGYFFIVDRkKDM-IIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 943 AVIireDTPDNKQ---IVAYITHHNEQvKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05936 401 AVV---GVPDPYSgeaVKAFVVLKEGA-SLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1613-1856 |
2.75e-50 |
|
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: 187.15 E-value: 2.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1613 LIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDY 1692
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1693 PSQRLLWMAQDAQLSLLLTHEELKARWPHCP-CPLLCLDTLQERYAslpcEDLQEACSPAQLAYVIYTSGSTGRPKGVQI 1771
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGlIDLLDEDTIYHEES----ENLEPVSKSDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1772 SHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPT 1851
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPA 237
|
....*
gi 1574832895 1852 TWQLL 1856
Cdd:cd17655 238 HLKLL 242
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
33-455 |
4.30e-50 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 184.57 E-value: 4.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 33 FPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLN-GEPIQVIRPNLTLQIPL 111
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTslPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILL-LNTHHIISDGWSLGVFLHELSLCYSAALA 190
Cdd:cd19536 82 LDLT--PLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 191 GNSPTLPaPSLQYADYAAWQRnwlKGENLTNLLDYWRKQL--ADMPPLLELPMDHPRPAVQTShgavvSLLLPSEISTAL 268
Cdd:cd19536 160 YKPLSLP-PAQPYRDFVAHER---ASIQQAASERYWREYLagATLATLPALSEAVGGGPEQDS-----ELLVSVPLPVRS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 269 KALSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNR--TDIEHVFGFFVNTLVLRIDvASELNFRTLLQRVKE 346
Cdd:cd19536 231 RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVT-LSEETVEDLLKRAQE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 347 MTLEAYAHQDIPFDALldelnpERSLSHSLLFQVFFNMVNLP--DLHDEWPDLK--VEHLWPREIGSKFDLTLFVQEEQD 422
Cdd:cd19536 310 QELESLSHEQVPLADI------QRCSEGEPLFDSIVNFRHFDldFGLPEWGSDEgmRRGLLFSEFKSNYDVNLSVLPKQD 383
|
410 420 430
....*....|....*....|....*....|...
gi 1574832895 423 AIRLELVYNTDLFKHERMLEMLEQYSCLASQVS 455
Cdd:cd19536 384 RLELKLAYNSQVLDEEQAQRLAAYYKSAIAELA 416
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1625-1872 |
7.00e-49 |
|
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: 182.47 E-value: 7.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd12114 4 TAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTHEELKARWPHCPCPLLCLDTLQERYASLPCEDLQeacsPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQ 1784
Cdd:cd12114 84 GARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVA----PDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1785 SLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETGWSGK 1864
Cdd:cd12114 160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQ 239
|
250
....*....|...
gi 1574832895 1865 AG-----LTLLSG 1872
Cdd:cd12114 240 ALlpslrLVLLSG 252
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1625-1859 |
3.81e-48 |
|
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: 179.43 E-value: 3.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd17643 4 VAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTheelkarwphcpcpllcldtlqeryaslpcedlqeacSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQ 1784
Cdd:cd17643 84 GPSLLLT-------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1785 SLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLET 1859
Cdd:cd17643 127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1610-1860 |
4.21e-48 |
|
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: 179.94 E-value: 4.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLLTHeelkarwphcpcpllcldtlqeryaslpcedlqeacsPAQLAYVIYTSGSTGRPKGV 1769
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQ-------------------------------------PENLAYVIYTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1770 QISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQAT 1849
Cdd:cd17644 125 MIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLP 204
|
250
....*....|.
gi 1574832895 1850 PTTWQLLLETG 1860
Cdd:cd17644 205 PAYWHLLVLEL 215
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
485-1010 |
7.17e-48 |
|
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: 181.11 E-value: 7.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 485 HWEG-TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGS 563
Cdd:COG1021 21 YWRGeTLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 564 T-VLILdpsyPPARLLE---YVQRAHARGWL---RIEGaTDCQEL-DEWCRANSYCNLVL----ARNF-ALSGILSQyAS 630
Cdd:COG1021 101 IpVFAL----PAHRRAEishFAEQSEAVAYIipdRHRG-FDYRALaRELQAEVPSLRHVLvvgdAGEFtSLDALLAA-PA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 631 SAPAYRVGPNDIACLTFTSGSTGRPKGVlqrhgPLTHflpwmRDRF----------AFTQTDRYslLSGL--AHD-PLQR 697
Cdd:COG1021 175 DLSEPRPDPDDVAFFQLSGGTTGLPKLI-----PRTH-----DDYLysvrasaeicGLDADTVY--LAALpaAHNfPLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 698 E-IFTPLCVGATI-CIPDqehmGDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDlpsARIPSLRYAFVVGDALTRR 775
Cdd:COG1021 243 PgVLGVLYAGGTVvLAPD----PSPDTAFPLIERERVTVTALVPPLALLWLDAAERSR---YDLSSLRVLQVGGAKLSPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 776 HVARlyaVAPHITC--VNLYGSTETqrAVSYfvlptasstespasvTALLD-KEVI------PLGkgmPGAQILILNEAG 846
Cdd:COG1021 316 LARR---VRPALGCtlQQVFGMAEG--LVNY---------------TRLDDpEEVIlttqgrPIS---PDDEVRIVDEDG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 847 NLAGIGELGEIYVRSPHLAFGYLDDPDQtNERflvnPFTHqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVkIR-GYRIE 925
Cdd:COG1021 373 NPVPPGEVGELLTRGPYTIRGYYRAPEH-NAR----AFTP---DGFYRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 926 LEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPVlsNLRAFVTQR-LPAFMVPAHFVFMSRLPLNANGK 1004
Cdd:COG1021 444 AEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLA--ELRRFLRERgLAAFKLPDRLEFVDALPLTAVGK 521
|
....*.
gi 1574832895 1005 VDRKAL 1010
Cdd:COG1021 522 IDKKAL 527
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1625-1852 |
1.02e-47 |
|
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: 177.83 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd17652 4 PAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTHeelkarwphcpcpllcldtlqeryaslpcedlqeacsPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQ 1784
Cdd:cd17652 84 RPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1785 SLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQ-------LPISILQATPTT 1852
Cdd:cd17652 127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREhrithvtLPPAALAALPPD 201
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
489-1010 |
2.18e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 178.94 E-value: 2.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLIL 568
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 569 DPSYPPARLLEYVQRAHARGWLRIEG-------ATDC---QELDEWCRANSYCNLVlARNFALSGILSQYASSAPAYRVG 638
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLflgvdysATTRlpaLEHVVICETEEDDPHT-EKMKTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLT-HFLPWMrDRFAFTQTDRYsllsgLAHDP------LQREIFTPLCVGATICI 711
Cdd:PRK07656 165 PDDVADILFTSGTTGRPKGAMLTHRQLLsNAADWA-EYLGLTEGDRY-----LAANPffhvfgYKAGVNAPLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 pdqEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQ--GMGEDDLPSARIpslryaFVVGDA-----LTRRHVARLyava 784
Cdd:PRK07656 239 ---LPVFDPDEVFRLIETERITVLPGPPTMYNSLLQhpDRSAEDLSSLRL------AVTGAAsmpvaLLERFESEL---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 785 PHITCVNLYGSTETQravsyfvlPTAssTESPASVtallDKEVIP--LGKGMPGAQILILNEAGNLAGIGELGEIYVRSP 862
Cdd:PRK07656 306 GVDIVLTGYGLSEAS--------GVT--TFNRLDD----DRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 863 HLAFGYLDDPDQTNErflvnpfTHQEHDRLYrTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADA 942
Cdd:PRK07656 372 NVMKGYYDDPEATAA-------AIDADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEA 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 943 AVIireDTPDNK--QIV-AYI-THHNEQVKPvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK07656 444 AVI---GVPDERlgEVGkAYVvLKPGAELTE--EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1151-1858 |
6.55e-47 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 186.91 E-value: 6.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1151 QERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQ-GEQLMQRIHA--------QLWLSL 1221
Cdd:PRK05691 3264 QEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNaGETMLQVIHKpgrtpidyLDWRGL 3343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1222 SQqhlslpAESESSLSQQALQawlqqEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYN 1301
Cdd:PRK05691 3344 PE------DGQEQRLQALHKQ-----EREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYT 3412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1302 AHVKGISPQLAPLPlQYADYAvwqrAWLQEERQEKLQRYWHGQLATAPALLDLPTDhpRPPIQTFVGARHQL-------H 1374
Cdd:PRK05691 3413 ALGEGREAQLPVPP-RYRDYI----GWLQRQDLAQARQWWQDNLRGFERPTPIPSD--RPFLREHAGDSGGMvvgdcytR 3485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1375 LPAELLEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGR--QRRELEGVIGLFANTLVLRTDLSGDP-- 1450
Cdd:PRK05691 3486 LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVQLPAAGqr 3565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1451 -SFLELLQRVREVTLQAYSQQDMPfekLVAeLQPERSLAY-NPLFQVFFALQNVPgdpISLEGLDVTQ-IRLDSNSAK-- 1525
Cdd:PRK05691 3566 cSVRQWLQGLLDSNMELREYEYLP---LVA-IQECSELPKgQPLFDSLFVFENAP---VEVSVLDRAQsLNASSDSGRth 3638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1526 --FDLSWTWYQEDEKSLSavIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTPVSLLPLLSAAQRLHLL-SLGHSSSPL 1602
Cdd:PRK05691 3639 tnFPLTAVCYPGDDLGLH--LSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLdGCNRSERDY 3716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1603 PAAPScgLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTG 1682
Cdd:PRK05691 3717 PLEQS--YVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAG 3794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1683 AAYVPLDPDYPSQRLLWMAQDAQLSLLLTH----EELKARWPHCPCP----LLCLDTLQERyaSLPCEDLQEACSPAQLA 1754
Cdd:PRK05691 3795 AGYLPLDPGLPAQRLQRIIELSRTPVLVCSaacrEQARALLDELGCAnrprLLVWEEVQAG--EVASHNPGIYSGPDNLA 3872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1755 YVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQL 1834
Cdd:PRK05691 3873 YVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGL 3952
|
730 740
....*....|....*....|....
gi 1574832895 1835 ASLLAQLPISILQATPTTWQLLLE 1858
Cdd:PRK05691 3953 LAHVQAQGITVLESVPSLIQGMLA 3976
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1150-1574 |
1.49e-46 |
|
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: 174.09 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1150 AQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIhaqlwLSLSQQHLSLP 1229
Cdd:cd19533 7 AQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWI-----DPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1230 AESESSLSQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGISP 1309
Cdd:cd19533 82 DLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1310 QLAPLPlQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPALLDLPtdhPRPPIQTFVGARHQLHLPAELLEQLMVLSHQ 1389
Cdd:cd19533 162 PPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLA---RRAPGRSLAFLRRTAELPPELTRTLLEAAEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1390 QQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLRTDLSGDPSFLELLQRVREVTLQAYSQ 1469
Cdd:cd19533 238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1470 QDMPFEKLVAELQPERSLAynPLFQVFFALQnvPGDPISLEGLDVTQIRLDSNSAKFDLS-WTWYQEDEKSLSAVIEYNT 1548
Cdd:cd19533 318 QRYRYEDLRRDLGLTGELH--PLFGPTVNYM--PFDYGLDFGGVVGLTHNLSSGPTNDLSiFVYDRDDESGLRIDFDANP 393
|
410 420
....*....|....*....|....*.
gi 1574832895 1549 ALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19533 394 ALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1610-1858 |
3.41e-46 |
|
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: 173.66 E-value: 3.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLLTheelkarwphcpcpllcldtlqeryaslpcedlqeacSPAQLAYVIYTSGSTGRPKGV 1769
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT-------------------------------------DPDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1770 QISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQAsdprqLASLLAQLPISILQAT 1849
Cdd:cd12115 124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLA-----LPDLPAAAEVTLINTV 198
|
....*....
gi 1574832895 1850 PTTWQLLLE 1858
Cdd:cd12115 199 PSAAAELLR 207
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
506-1010 |
2.50e-45 |
|
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: 171.11 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 506 AIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLlEYVqrah 585
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDY-AYI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 586 argwlriegATDCQeldewcransyCNLVlarnfalsgilsqYASSApayrvgpnDIACLTFTSGSTGRPKGVLQRH-GP 664
Cdd:cd05919 78 ---------ARDCE-----------ARLV-------------VTSAD--------DIAYLLYSSGTTGPPKGVMHAHrDP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 665 LTHFLPWMRDRFAFTQTDRYSLLS------GLAHDplqreIFTPLCVGATICIpdqehmgDPGWLAQwmQGQEITIASFT 738
Cdd:cd05919 117 LLFADAMAREALGLTPGDRVFSSAkmffgyGLGNS-----LWFPLAVGASAVL-------NPGWPTA--ERVLATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 739 PALL--------QLLTQGmgedDLPSARIPSLRYAFVVGDALTRrhvARLYAVAPHITC--VNLYGSTETqraVSYFVLP 808
Cdd:cd05919 183 PTVLygvptfyaNLLDSC----AGSPDALRSLRLCVSAGEALPR---GLGERWMEHFGGpiLDGIGATEV---GHIFLSN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 809 TASSTEsPASvtalldkevipLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLvnpfthqe 888
Cdd:cd05919 253 RPGAWR-LGS-----------TGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 889 hDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQV- 967
Cdd:cd05919 313 -GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAp 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1574832895 968 -KPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05919 392 qESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
514-1010 |
4.79e-45 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 171.73 E-value: 4.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 514 VSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSY-------------------PP 574
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYkkaefefyladlgsklvltPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 575 ARLLEYVQRAHARGWLRIEGATDCQELDEWCRANSycnlvlarnfaLSGILSQYASSAPAYRVGPNDIACLTFTSGSTGR 654
Cdd:cd05926 95 GELGPASRAASKLGLAILELALDVGVLIRAPSAES-----------LSNLLADKKNAKSEGVPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 655 PKGVlqrhgPLTH--FLPWMRD---RFAFTQTDR----------YSLLSGLahdplqreiFTPLCVGATICIPdqehmgd 719
Cdd:cd05926 164 PKGV-----PLTHrnLAASATNitnTYKLTPDDRtlvvmplfhvHGLVASL---------LSTLAAGGSVVLP------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 720 PGWLA----QWMQGQEITIASFTPALLQLLTqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAV--APHITCvnlY 793
Cdd:cd05926 223 PRFSAstfwPDVRDYNATWYTAVPTIHQILL--NRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATfgAPVLEA---Y 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 794 GSTETQRAVSYFVLPTasSTESPASVtalldkeviplGKGMpGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPD 873
Cdd:cd05926 298 GMTEAAHQMTSNPLPP--GPRKPGSV-----------GKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 874 QTNERFLVNPFthqehdrlYRTGDLGRYLPDGNAEFAGRndlqVK---IR-GYRIELEEIEAILVEHPMVADAAVIireD 949
Cdd:cd05926 364 ANAEAAFKDGW--------FRTGDLGYLDADGYLFLTGR----IKeliNRgGEKISPLEVDGVLLSHPAVLEAVAF---G 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574832895 950 TPDNK---QIVAYIThHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05926 429 VPDEKygeEVAAAVV-LREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
490-1010 |
5.55e-45 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 171.78 E-value: 5.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 490 IHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILD 569
Cdd:cd05959 6 ATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 570 PSYPPARLLEYVQRAHARGwLRIEGATdCQELDEWCR--ANSYCNLVL---ARNFALSGILSQY----ASSAPAYRVGPN 640
Cdd:cd05959 86 TLLTPDDYAYYLEDSRARV-VVVSGEL-APVLAAALTksEHTLVVLIVsggAGPEAGALLLAELvaaeAEQLKPAATHAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLQRHGPLTHFLP-WMRDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGAT-ICIPDQEhm 717
Cdd:cd05959 164 DPAFWLYSSGSTGRPKGVVHLHADIYWTAElYARNVLGIREDDVCFSAAKLFFAyGLGNSLTFPLSVGATtVLMPERP-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 718 gDPGWLAQWMQGQEITIASFTPALLQLLT--QGMGEDDLPSaripsLRYAFVVGDALTRrHVARLYAVAPHITCVNLYGS 795
Cdd:cd05959 242 -TPAAVFKRIRRYRPTVFFGVPTLYAAMLaaPNLPSRDLSS-----LRLCVSAGEALPA-EVGERWKARFGLDILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 796 TEtqrAVSYFVLPTASSTESPASvtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQT 875
Cdd:cd05959 315 TE---MLHIFLSNRPGRVRYGTT------------GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 876 NERFLvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQ 955
Cdd:cd05959 380 RDTFQ---------GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTK 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 956 IVAYITHHNEQVKPVLS--NLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05959 451 PKAFVVLRPGYEDSEALeeELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1614-1860 |
1.22e-44 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 168.26 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1614 IEAQCERSSLQPAL-HAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDY 1692
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1693 PSQRLLWMAQDAQLSLLLTHEELKAR-------WPHCPCPLLCLDTL-----QERYASLPCEDLQ----EACSPAQLAYV 1756
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEellealgKLEVVKLVLVLDRDpvlkeEPLPEEAKPADVPppppPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1757 IYTSGSTGRPKGVQISHGA----LLSFLLSLQSLLSLSPHDRWLAITSISFDIA-GLELYLPLLAGAQIQLASQEQASDP 1831
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNlvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260
....*....|....*....|....*....
gi 1574832895 1832 RQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAG 269
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
515-1011 |
4.08e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 167.08 E-value: 4.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPArLLEYVQRaHARgwlrieg 594
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGD-ELAYIID-HSG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 595 atdcqeldewcransyCNLVLArnfalsgilsqyassapayrvgpnDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRD 674
Cdd:cd05934 76 ----------------AQLVVV------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSAR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 675 RFAFTQTDRYSLLSGLAH-DPLQREIFTPLCVGATICIPDQEHMGdpGWLAQwMQGQEITIASFTPALLQLLtqgMGEDD 753
Cdd:cd05934 116 RFGLGEDDVYLTVLPLFHiNAQAVSVLAALSVGATLVLLPRFSAS--RFWSD-VRRYGATVTNYLGAMLSYL---LAQPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 754 LPSARIPSLRYAFVVG------DALTRRHVARLyavaphitcVNLYGSTETqravsyfvlptasstesPASVTALLDKEV 827
Cdd:cd05934 190 SPDDRAHRLRAAYGAPnppelhEEFEERFGVRL---------LEGYGMTET-----------------IVGVIGPRDEPR 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 828 IP--LGKGMPGAQILILNEAGNLAGIGELGEIYVRS--PHLAF-GYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYL 902
Cdd:cd05934 244 RPgsIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGlrGWGFFkGYYNMPEATAEAM---------RNGWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 903 PDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVI-----IREDtpdnkQIVAY-ITHHNEQVKPVlsNLRA 976
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVavpdeVGED-----EVKAVvVLRPGETLDPE--ELFA 387
|
490 500 510
....*....|....*....|....*....|....*
gi 1574832895 977 FVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:cd05934 388 FCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
34-443 |
9.37e-44 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 165.05 E-value: 9.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 34 PLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPnltlqiplid 113
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSS---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 114 ltSLPEAEREASLqhAINNEAHIPFDLKTGPLVRlALLRKSplehILLLNTHHIISDGWSLGVFLHELSLCYsaalagNS 193
Cdd:cd19537 73 --SPPRVQRVDTL--DVWKEINRPFDLEREDPIR-VFISPD----TLLVVMSHIICDLTTLQLLLREVSAAY------NG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 194 PTLPAPSLQYADYAAWQRnWLKGENLtnllDYWRKQLADMPPLLelpmDHPRPAVQTSHGAVVSLLLPSEISTALKALSQ 273
Cdd:cd19537 138 KLLPPVRREYLDSTAWSR-PASPEDL----DFWSEYLSGLPLLN----LPRRTSSKSYRGTSRVFQLPGSLYRSLLQFST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 274 HEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANRNRTDIEHVFGFFVNTLVLRI--DVASELNFRTLLQRVKEMTLEA 351
Cdd:cd19537 209 SSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIrfPSSSDASAADFLRAVRRSSQAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 352 YAHQdIPFDALLDELN-PERSLSHSlLFQVffnMV--NLPDLHDEW---PDLKVEHLWPReiGSKFDLTL-FVQEEQDAI 424
Cdd:cd19537 289 LAHA-IPWHQLLEHLGlPPDSPNHP-LFDV---MVtfHDDRGVSLAlpiPGVEPLYTWAE--GAKFPLMFeFTALSDDSL 361
|
410
....*....|....*....
gi 1574832895 425 RLELVYNTDLFKHERMLEM 443
Cdd:cd19537 362 LLRLEYDTDCFSEEEIDRI 380
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1610-1851 |
2.41e-43 |
|
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: 166.18 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLLTHeelkarwphcpcpllcldtlqeryaslpcedlqeacSPAQLAYVIYTSGSTGRPKGV 1769
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1770 QISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDprQLASLLAQLPISILQAT 1849
Cdd:cd05918 125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLT 202
|
..
gi 1574832895 1850 PT 1851
Cdd:cd05918 203 PS 204
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
505-1010 |
2.43e-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: 165.16 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 505 IAIIDEINTVSYGELEARSNQLAHYLHAQG-IRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLlEYVqr 583
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL-EYV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 584 ahargwlriegatdcqeldewcRANSYCNLVLarnfalsgilsqyassapayrvgpnDIACLTFTSGSTGRPKGVLQRHG 663
Cdd:cd05941 80 ----------------------ITDSEPSLVL-------------------------DPALILYTSGTTGRPKGVVLTHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 664 PLTHFLPWMRDRFAFTQTDRysLLSGLahdPLQR------EIFTPLCVGATIcipdqEHMG--DPGWLAQWMQGQEITIA 735
Cdd:cd05941 113 NLAANVRALVDAWRWTEDDV--LLHVL---PLHHvhglvnALLCPLFAGASV-----EFLPkfDPKEVAISRLMPSITVF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 736 SFTPA----LLQLLTQGMGEDDLPSARIP-SLRYaFVVGDALTRRHV-ARLYAVAPHiTCVNLYGSTETQRAVSyfvlpt 809
Cdd:cd05941 183 MGVPTiytrLLQYYEAHFTDPQFARAAAAeRLRL-MVSGSAALPVPTlEEWEAITGH-TLLERYGMTEIGMALS------ 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 810 assteSPasvtalLDKEVIP--LGKGMPGAQILIL-NEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfth 886
Cdd:cd05941 255 -----NP------LDGERRPgtVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF------- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 887 qEHDRLYRTGDLGRYLPDGNAEFAGR-NDLQVKIRGYRIELEEIEAILVEHPMVADAAVIireDTPDNKQ---IVAYITH 962
Cdd:cd05941 317 -TDDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVI---GVPDPDWgerVVAVVVL 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1574832895 963 HNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05941 393 RAGAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
514-1010 |
1.29e-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: 162.89 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 514 VSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLrie 593
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 594 gatdcqeldewcransycnlvlarnfalsgilsqyassapayrVGPNDIACLTFTSGSTGRPKGVLQRHG-PLTHfLPWM 672
Cdd:cd05972 78 -------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSyPLGH-IPTA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 673 RDRFAFTQTDRYSLLSglahDP-----LQREIFTPLCVGATICIPDQEHMGDPGWLaQWMQGQEITIASFTPALLQLLTQ 747
Cdd:cd05972 114 AYWLGLRPDDIHWNIA----DPgwakgAWSSFFGPWLLGATVFVYEGPRFDAERIL-ELLERYGVTSFCGPPTAYRMLIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 748 gmgeDDLPSARIPSLRYAFVVGDALTRRhVARLYAVAPHITCVNLYGSTETQRAVSYFvlptasstespasvtalLDKEV 827
Cdd:cd05972 189 ----QDLSSYKFSHLRLVVSAGEPLNPE-VIEWWRAATGLPIRDGYGQTETGLTVGNF-----------------PDMPV 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 828 IP--LGKGMPGAQILILNEAGNLAGIGELGEIYVR-SPHLAF-GYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLP 903
Cdd:cd05972 247 KPgsMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlPPPGLFlGYVGDPEKTEASI---------RGDYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 904 DGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQIV-AYI--THHNEQVKPVLSNLRAFVTQ 980
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPD-PVRGEVVkAFVvlTSGYEPSEELAEELQGHVKK 396
|
490 500 510
....*....|....*....|....*....|
gi 1574832895 981 RLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
485-1010 |
2.10e-42 |
|
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: 163.65 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 485 HWEG-TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGS 563
Cdd:cd05920 11 YWQDePLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 564 TVLILDPSYPPARLLEYVQRAhargwlrieGATDCQELDEWCRANSycnLVLARnfalsgilsQYASSAPayrvgpnDIA 643
Cdd:cd05920 91 VPVLALPSHRRSELSAFCAHA---------EAVAYIVPDRHAGFDH---RALAR---------ELAESIP-------EVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 644 CLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHD-PLQRE-IFTPLCVGATICIPDQehmGDPG 721
Cdd:cd05920 143 LFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNfPLACPgVLGTLLAGGRVVLAPD---PSPD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 722 WLAQWMQGQEITIASFTPALLQLLTQGMGEddlPSARIPSLRYAFVVGDALTRRHVARLYAVaphITCV--NLYGSTETq 799
Cdd:cd05920 220 AAFPLIEREGVTVTALVPALVSLWLDAAAS---RRADLSSLRLLQVGGARLSPALARRVPPV---LGCTlqQVFGMAEG- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 800 rAVSYfvlptasstespasvTALLDKEVIPL---GKGM-PGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQt 875
Cdd:cd05920 293 -LLNY---------------TRLDDPDEVIIhtqGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEH- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 876 NERflvnPFTHqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQ 955
Cdd:cd05920 356 NAR----AFTP---DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGER 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 956 IVAYITHHNEQVKpvLSNLRAFVTQR-LPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05920 429 SCAFVVLRDPPPS--AAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
40-456 |
3.41e-42 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 160.55 E-value: 3.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 40 QRLWLLDQLNPGNaSYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFA--MLNGEPIQVIRPNLTLQIPLI--DLT 115
Cdd:cd19542 8 QEGMLLSQLRSPG-LYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVesSAEGTFLQVVLKSLDPPIEEVetDED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 116 SLPEAEREASLQHAINNEahipfdlktgPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAalagnspT 195
Cdd:cd19542 87 SLDALTRDLLDDPTLFGQ----------PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------Q 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 196 LPAPSLQYADYAAWQRnwlkGENLTNLLDYWRKQLADMPPLLElpmdhprPAVQTSHGAVVSLLLPSEISTALKALSQHE 275
Cdd:cd19542 150 LLPPAPPFSDYISYLQ----SQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCASL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 276 GVTlfMTTL--ALFQILLQRYTGRRDIVIGTPIANRN--RTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEA 351
Cdd:cd19542 219 GVT--LASLfqAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 352 YAHQDIPFDALLDELN--PERSLSHSLLfqVFFNMVNLPDLHDEWPDLKVEHLWprEIGSKFDLTLFVQEEQDAIRLELV 429
Cdd:cd19542 297 LPHQHLSLREIQRALGlwPSGTLFNTLV--SYQNFEASPESELSGSSVFELSAA--EDPTEYPVAVEVEPSGDSLKVSLA 372
|
410 420
....*....|....*....|....*..
gi 1574832895 430 YNTDLFKHERMLEMLEQYSCLASQVSE 456
Cdd:cd19542 373 YSTSVLSEEQAEELLEQFDDILEALLA 399
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
486-1010 |
6.24e-41 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 160.68 E-value: 6.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 486 W-EGTIHDLFAQQAHLRPENIAIIDEINTV-SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGS 563
Cdd:PRK06087 20 WgDASLADYWQQTARAMPDKIAVVDNHGASyTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 564 TVLILDPSYPPARLLEYVQRAHARGWLrieGATdcqeldeWCRANSYCNLVLA---------------------RNFALS 622
Cdd:PRK06087 100 VSVPLLPSWREAELVWVLNKCQAKMFF---APT-------LFKQTRPVDLILPlqnqlpqlqqivgvdklapatSSLSLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 623 GILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDP-LQREIFT 701
Cdd:PRK06087 170 QIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATgFLHGVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 702 PLCVGATICIpdQEHMGDPGWLAQ-------WMQGQeitiasfTPALLQLLTqgmgEDDLPSARIPSLRYaFVVGDALTR 774
Cdd:PRK06087 250 PFLIGARSVL--LDIFTPDACLALleqqrctCMLGA-------TPFIYDLLN----LLEKQPADLSALRF-FLCGGTTIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 775 RHVARlYAVAPHITCVNLYGSTETqraVSYFVLPTASSTESPASVTalldkeviplGKGMPGAQILILNEAGNLAGIGEL 854
Cdd:PRK06087 316 KKVAR-ECQQRGIKLLSVYGSTES---SPHAVVNLDDPLSRFMHTD----------GYAAAGVEIKVVDEARKTLPPGCE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 855 GEIYVRSPHLAFGYLDDPDQTNeRFLvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDlQVKIR-GYRIELEEIEAIL 933
Cdd:PRK06087 382 GEEASRGPNVFMGYLDEPELTA-RAL-------DEEGWYYSGDLCRMDEAGYIKITGRKK-DIIVRgGENISSREVEDIL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 934 VEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPVLSNLRAFV-TQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK06087 453 LQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
489-1006 |
8.96e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 159.67 E-value: 8.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKA------- 561
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAravpvnv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 562 ----------------GSTVLILDPSYPP--ARLLEyvQRAHARGWLRIEGATDcqeLDEWCRANSYCNLVlarnfalsg 623
Cdd:PRK07798 84 nyryvedelryllddsDAVALVYEREFAPrvAEVLP--RLPKLRTLVVVEDGSG---NDLLPGAVDYEDAL--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 624 ilsqyASSAPAYRVG---PNDIACLtFTSGSTGRPKGVLQRH---------------GPLTHFLPWMRDRFAFTQTDRYS 685
Cdd:PRK07798 150 -----AAGSPERDFGersPDDLYLL-YTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAAGPGMRRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 686 LLSGLAHDPLQREIFTPLCVGATICIPDQEHMgDPGWLAQWMQGQEITIASFT------PaLLQLLTQGmGEDDLPSAri 759
Cdd:PRK07798 224 PAPPLMHGAGQWAAFAALFSGQTVVLLPDVRF-DADEVWRTIEREKVNVITIVgdamarP-LLDALEAR-GPYDLSSL-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 760 pslryaFVV---GDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESPasvtalldkeviplgKGMPG 836
Cdd:PRK07798 299 ------FAIasgGALFSPSVKEALLELLPNVVLTDSIGSSETGFGGSGTVAKGAVHTGGP---------------RFTIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 837 AQILILNEAGN--LAGIGELGEIyVRSPHLAFGYLDDPDQTNERFlvnpFTHQEHdRLYRTGDLGRYLPDGNAEFAGRND 914
Cdd:PRK07798 358 PRTVVLDEDGNpvEPGSGEIGWI-ARRGHIPLGYYKDPEKTAETF----PTIDGV-RYAIPGDRARVEADGTITLLGRGS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 915 LQVKIRGYRIELEEIEAILVEHPMVADAAVIIRedtPDNK--QIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFV 992
Cdd:PRK07798 432 VCINTGGEKVFPEEVEEALKAHPDVADALVVGV---PDERwgQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIW 508
|
570
....*....|....
gi 1574832895 993 FMSRLPLNANGKVD 1006
Cdd:PRK07798 509 FVDEVQRSPAGKAD 522
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
515-1014 |
8.76e-40 |
|
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: 154.97 E-value: 8.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLRIEg 594
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 595 atdcqELDEwcransycnlvlarnfalsgilsqyassapayRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRD 674
Cdd:cd05969 81 -----ELYE--------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 675 RFAFTQTDRY------SLLSGLAHDplqreIFTPLCVGATICIPDQEHmgDPGWLAQWMQGQEITIASFTPALLQLLtqg 748
Cdd:cd05969 124 VLDLHPDDIYwctadpGWVTGTVYG-----IWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRML--- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 749 MGEDDLPSAR--IPSLRYAFVVGDALTRRHVA---RLYAVAPHITcvnlYGSTETQravSYFVLPTASSTESPASvtall 823
Cdd:cd05969 194 MKEGDELARKydLSSLRFIHSVGEPLNPEAIRwgmEVFGVPIHDT----WWQTETG---SIMIANYPCMPIKPGS----- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 824 dkevipLGKGMPGAQILILNEAGNLAGIGELGEIYVRS--PHLAFGYLDDPDQTNERFLvnpfthqehDRLYRTGDLGRY 901
Cdd:cd05969 262 ------MGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFI---------DGWYLTGDLAYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 902 LPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThHNEQVKP---VLSNLRAFV 978
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFIS-LKEGFEPsdeLKEEIINFV 405
|
490 500 510
....*....|....*....|....*....|....*.
gi 1574832895 979 TQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPE 1014
Cdd:cd05969 406 RQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
513-1005 |
1.34e-39 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 154.08 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAIS-AQRCAALVLAiLGILKAGSTVLILDPSYPPARLLEYVQRAHARgwlr 591
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQlPNWWEFAVLY-LACLRIGAVTNPILPFFREHELAFILRRAKAK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 592 iegatdcqeldewcransycNLVLARNFALSGILSQyassapayrvgPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPW 671
Cdd:cd05903 76 --------------------VFVVPERFRQFDPAAM-----------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 672 MRDRFAFTQTDRYSLLSGLAHDP-LQREIFTPLCVGATICIPDqehMGDPGWLAQWMQGQEITIASFTPALLQLLTQGMG 750
Cdd:cd05903 125 YAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVLQD---IWDPDKALALMREHGVTFMMGATPFLTDLLNAVE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 751 EDDlpsARIPSLRYaFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSyfvlptaSSTESPASVTALLDkevipl 830
Cdd:cd05903 202 EAG---EPLSRLRT-FVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVT-------SITPAPEDRRLYTD------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 831 GKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFA 910
Cdd:cd05903 265 GRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA---------PEGWFRTGDLARLDEDGYLRIT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 911 GRNDlQVKIR-GYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThHNEQVKPVLSNLRAFVT-QRLPAFMVP 988
Cdd:cd05903 336 GRSK-DIIIRgGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVV-TKSGALLTFDELVAYLDrQGVAKQYWP 413
|
490
....*....|....*..
gi 1574832895 989 AHFVFMSRLPLNANGKV 1005
Cdd:cd05903 414 ERLVHVDDLPRTPSGKV 430
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1144-1574 |
3.96e-39 |
|
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: 152.22 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1144 LFAASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQL-MQRIHAQLWLSLS 1222
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQpVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1223 QQHLSLPAESESSLSqqalqAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILL-LCLHHIIADGWSLGILLQELSLCYN 1301
Cdd:cd19536 81 ELDLTPLEEQLDPLR-----AYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1302 AHVKGISPQLAPlPLQYADYAVWQRAWLQeerQEKLQRYWHGQL-----ATAPALLDLPTDHPRPPIQTFVGARhqlhlP 1376
Cdd:cd19536 156 QLLEYKPLSLPP-AQPYRDFVAHERASIQ---QAASERYWREYLagatlATLPALSEAVGGGPEQDSELLVSVP-----L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1377 AELLEQlmvLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGR--QRRELEGVIGLFANTLVLRTDLSgDPSFLE 1454
Cdd:cd19536 227 PVRSRS---LAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTLS-EETVED 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1455 LLQRVREVTLQAYSQQDMPfeklVAELQpeRSLAYNPLFQVFFALQNVP-GDPISLEGLDVTQIR--LDSNSAKFDLSWT 1531
Cdd:cd19536 303 LLKRAQEQELESLSHEQVP----LADIQ--RCSEGEPLFDSIVNFRHFDlDFGLPEWGSDEGMRRglLFSEFKSNYDVNL 376
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1574832895 1532 WYQEDEKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19536 377 SVLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
489-1010 |
1.04e-38 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 152.66 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINT--VSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVL 566
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 567 ILDPSYPPARLLEYVQRAHARGWLRIEGATDCQELdewcransycNLVLARNFALS-----GILSQYASSAPAYRVGPND 641
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAVIAVDAQVMDAI----------FQSGVRVLALSdlvglGEPESAGPLIEDPPREPEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 642 IACLTFTSGSTGRPKGVL--QRHgplthflpwMRDRFAFTQTD------RYSLLSGLAhdPLQREI-FTPLCVGA----- 707
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVipQRA---------AESRVLFMSTQaglrhgRHNVVLGLM--PLYHVIgFFAVLVAAlaldg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 708 TICIPDQEhmgDPGWLAQWMQGQEITIASFTPALLQLLTqgmGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPhI 787
Cdd:cd05923 221 TYVVVEEF---DPADALKLIEQERVTSLFATPTHLDALA---AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP-G 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 788 TCVNLYGSTETqravsyfvlptasstespasVTALLDKEVIPLGKGMPG----AQIL-ILNEAGNLAGIGELGEIYV-RS 861
Cdd:cd05923 294 EKVNIYGTTEA--------------------MNSLYMRDARTGTEMRPGffseVRIVrIGGSPDEALANGEEGELIVaAA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 862 PHLAF-GYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVA 940
Cdd:cd05923 354 ADAAFtGYLNQPEATAKKL---------QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVT 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 941 DAAVIIREDTPDNKQIVAYITHHneQVKPVLSNLRAF-VTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05923 425 EVVVIGVADERWGQSVTACVVPR--EGTLSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
489-1010 |
1.02e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 149.54 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPhDVVAISAQRCAALVLAILGILKAGSTVLIL 568
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 569 DPSYPPARLLEYVQRAHA-------RGWLRIEGAtDCQ--ELDEWCRANSycnlvlarNFALSGILSQYASSAPAYrvgp 639
Cdd:PRK07638 81 DIKWKQDELKERLAISNAdmivterYKLNDLPDE-EGRviEIDEWKRMIE--------KYLPTYAPIENVQNAPFY---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 640 ndiacLTFTSGSTGRPKGVLQRHGPLTH-FLPWMRDrFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIpdqEHMG 718
Cdd:PRK07638 148 -----MGFTSGSTGKPKAFLRAQQSWLHsFDCNVHD-FHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL---MRKF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 719 DPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPSARIPSlryafvvGDALTRRHVARLYAVAPHITCVNLYGSTET 798
Cdd:PRK07638 219 IPNQVLDKLETENISVMYTVPTMLESLYKENRVIENKMKIISS-------GAKWEAEAKEKIKNIFPYAKLYEFYGASEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 799 QrAVSYFVlpTASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDpdqtner 878
Cdd:PRK07638 292 S-FVTALV--DEESERRPNSV-----------GRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 879 flVNPFTHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVA 958
Cdd:PRK07638 351 --GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVA 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 959 YItHHNEQVKpvlsNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK07638 429 II-KGSATKQ----QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
503-1010 |
3.21e-37 |
|
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: 147.23 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 503 ENIAIIDEI---NTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLe 579
Cdd:cd17654 3 RPALIIDQTtsdTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 580 yvqrahargwlRIEGATDCQELDEWCRansycNLVLARNFALSGIlsQYASSAPAyrvgpnDIACLTFTSGSTGRPKGVL 659
Cdd:cd17654 82 -----------TVMKKCHVSYLLQNKE-----LDNAPLSFTPEHR--HFNIRTDE------CLAYVIHTSGTTGTPKIVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 660 QRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWM-QGQEITIASFT 738
Cdd:cd17654 138 VPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQAT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 739 PALLQLLTQGMGEDDLPSArIPSLRYAFVVGDAL-------TRRHVArlyavaPHITCVNLYGSTETQRAVSYFVLPTAS 811
Cdd:cd17654 218 PTLFRRFGSQSIKSTVLSA-TSSLRVLALGGEPFpslvilsSWRGKG------NRTRIFNIYGITEVSCWALAYKVPEED 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 812 STEspasvtalldkeviPLGKGMPGAQILILNEAGNlAGIGEL---GEIYVrsphlafGYLDDPDQTnerflvnPFThqe 888
Cdd:cd17654 291 SPV--------------QLGSPLLGTVIEVRDQNGS-EGTGQVflgGLNRV-------CILDDEVTV-------PKG--- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 889 hdRLYRTGDLGRyLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIRedtpDNKQIVAYIThHNEQVK 968
Cdd:cd17654 339 --TMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLS----DQQRLIAFIV-GESSSS 410
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1574832895 969 PVLSNLRAFVtqrLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd17654 411 RIHKELQLTL---LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
484-1013 |
8.01e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 147.83 E-value: 8.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 484 AHWEGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAI-------- 555
Cdd:PRK06188 8 LHSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIgaaqlagl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 556 -------LG-------ILK-AGSTVLILDPSYPPARLLEYVQRAHA-RGWLRI---EGATDcqeldewcransycnlvla 616
Cdd:PRK06188 88 rrtalhpLGslddhayVLEdAGISTLIVDPAPFVERALALLARVPSlKHVLTLgpvPDGVD------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 617 rnfalsgILSQYASSAPAYRV---GPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHd 693
Cdd:PRK06188 149 -------LLAAAAKFGPAPLVaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 694 plqreiftplcVGATICIPDQEHMG--------DPGWLAQWMQGQEITIASFTPALLQLLtqgMGEDDLPSARIPSLRYA 765
Cdd:PRK06188 221 -----------AGGAFFLPTLLRGGtvivlakfDPAEVLRAIEEQRITATFLVPTMIYAL---LDHPDLRTRDLSSLETV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 766 FVVGDALT----RRHVARLYAVAphitcVNLYGSTETQRAVSYfvLPTAS-STESPASVTALldkeviplGKGMPGAQIL 840
Cdd:PRK06188 287 YYGASPMSpvrlAEAIERFGPIF-----AQYYGQTEAPMVITY--LRKRDhDPDDPKRLTSC--------GRPTPGLRVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 841 ILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIR 920
Cdd:PRK06188 352 LLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF---------RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 921 GYRIELEEIEAILVEHPMVADAAVIireDTPDNK--QIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLP 998
Cdd:PRK06188 423 GFNVFPREVEDVLAEHPAVAQVAVI---GVPDEKwgEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLP 499
|
570
....*....|....*
gi 1574832895 999 LNANGKVDRKALPAP 1013
Cdd:PRK06188 500 LTALGKPDKKALRAR 514
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1146-1573 |
8.12e-37 |
|
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: 144.64 E-value: 8.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1146 AASFAQERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRI-----HAQLwls 1220
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYsssppRVQR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1221 lsQQHLSLpaesesslsqqalqawlQQEIRRPFDLQQAPLLRASLlhrgsEPSILLLCLHHIIADGWSLGILLQELSLCY 1300
Cdd:cd19537 80 --VDTLDV-----------------WKEINRPFDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLREVSAAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1301 NAHvkgispQLAPLPLQYADYAVWQRAWLQEERQeklqrYWHGQLATAPalldlPTDHPRPPI-QTFVGARHQLHLPAEL 1379
Cdd:cd19537 136 NGK------LLPPVRREYLDSTAWSRPASPEDLD-----FWSEYLSGLP-----LLNLPRRTSsKSYRGTSRVFQLPGSL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1380 LEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRRELEGVIGLFANTLVLR--TDLSGDPSFLELLQ 1457
Cdd:cd19537 200 YRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFLR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1458 RVREVTLQAYSQQdMPFEKLVAELQPERSLAYNPLFQ--VFFALQNVPGDPISLEGLDVTQIRldSNSAKFDLSWTWYQE 1535
Cdd:cd19537 280 AVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDvmVTFHDDRGVSLALPIPGVEPLYTW--AEGAKFPLMFEFTAL 356
|
410 420 430
....*....|....*....|....*....|....*...
gi 1574832895 1536 DEKSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQE 1573
Cdd:cd19537 357 SDDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1611-1845 |
2.20e-36 |
|
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: 144.62 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1611 HHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDP 1690
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1691 DYPSQRLLWMAQDAQLSLLLTheelkarwphcpcpllcldtlqeryaslpcedlqeacSPAQLAYVIYTSGSTGRPKGVQ 1770
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLT-------------------------------------NPDDLAYVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1771 ISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISI 1845
Cdd:cd17645 124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITI 198
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
514-1010 |
2.58e-36 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 144.50 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 514 VSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLlEYvqrahargwlRIe 593
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEAL-EY----------RL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 594 gatdcqeldewcrANSYCNLVLARnfalsgilsqyassapayrvGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWM- 672
Cdd:cd05971 75 -------------SNSGASALVTD--------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVq 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 673 --------RDRFAFTQTDrYSLLSGLAhdplqrEIFTP-LCVGATICIPDQEHMgDPGWLAQWMQGQEITIASFTPALLQ 743
Cdd:cd05971 122 fpfnlfprDGDLYWTPAD-WAWIGGLL------DVLLPsLYFGVPVLAHRMTKF-DPKAALDLMSRYGVTTAFLPPTALK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 744 LLTQgMGEDDLPSARipSLRYAFVVGDALTRRHVA---RLYAVAPHitcvNLYGSTETQRAVSyfvlptasstespaSVT 820
Cdd:cd05971 194 MMRQ-QGEQLKHAQV--KLRAIATGGESLGEELLGwarEQFGVEVN----EFYGQTECNLVIG--------------NCS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 821 ALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPH-LAF-GYLDDPDQTNERFlVNPFthqehdrlYRTGDL 898
Cdd:cd05971 253 ALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpVAFlGYWNNPSATEKKM-AGDW--------LLTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 899 GRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYItHHNEQVKP---VLSNLR 975
Cdd:cd05971 324 GRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFV-VLNPGETPsdaLAREIQ 402
|
490 500 510
....*....|....*....|....*....|....*
gi 1574832895 976 AFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05971 403 ELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
490-1010 |
9.87e-36 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 144.64 E-value: 9.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 490 IHDLFAQQAHLRPENIAII--DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLI 567
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 568 LDPSYPPARLLEYVQRAHARGWLrIEGATDCQELDEWCRANSYCNLVLARNFALSGILSQY--ASSAPAYRV------GP 639
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVL-IDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHldAATEPTPATstpeglRP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 640 NDiACLTFTSGSTGRPKGVlqrhgplthflPWMRDRFAftqTDRYSLLSGLAHDP---------------LQREIFTPLC 704
Cdd:PRK05852 177 DD-AMIMFTGGTTGLPKMV-----------PWTHANIA---SSVRAIITGYRLSPrdatvavmplyhghgLIAALLATLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 VGATICIPDQEHMGDPGWLAQwMQGQEITIASFTPALLQLLTQGMGEDDLPSARiPSLRYAFVVGDALTRR--HVARLYA 782
Cdd:PRK05852 242 SGGAVLLPARGRFSAHTFWDD-IKAVGATWYTAVPTIHQILLERAATEPSGRKP-AALRFIRSCSAPLTAEtaQALQTEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 783 VAPhITCVnlYGSTETQRAVSYFVLPTASSTESPASVTALLDKEViplgkgmpGAQILILNEAGNLAGIGELGEIYVRSP 862
Cdd:PRK05852 320 AAP-VVCA--FGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRST--------GAQIRIVGSDGLPLPAGAVGEVWLRGT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 863 HLAFGYLDDPDQTNERFLvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADA 942
Cdd:PRK05852 389 TVVRGYLGDPTITAANFT---------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 943 AVIIREDTPDNKQIVAYITHHnEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK05852 460 AVFGVPDQLYGEAVAAVIVPR-ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
515-1010 |
1.11e-35 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 142.66 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARgwLRIEG 594
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGAR--LVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 595 ATDCQELDEwcransycnlvlarnfalsgilsqyassapayrvgpnDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRD 674
Cdd:cd05973 80 AANRHKLDS-------------------------------------DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 675 RFAFTQTDRYSLLSglahDP-----LQREIFTPLCVGaticIPDQEHMGDPGWLAQWMQGQEITIASFT--PALLQLLTQ 747
Cdd:cd05973 123 AVDLRPEDSFWNAA----DPgwaygLYYAITGPLALG----HPTILLEGGFSVESTWRVIERLGVTNLAgsPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 748 gmgeDDLPSARIP--SLRYAFVVGDALTRrHVARLYAVAPHITCVNLYGSTETQravsyFVLPTASSTESPASVTALldk 825
Cdd:cd05973 195 ----AGAEVPARPkgRLRRVSSAGEPLTP-EVIRWFDAALGVPIHDHYGQTELG-----MVLANHHALEHPVHAGSA--- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 826 eviplGKGMPGAQILILNEAGNLAGIGELGEIYV---RSPHLAF-GY--LDDPDQTNerflvnpfthqehdRLYRTGDLG 899
Cdd:cd05973 262 -----GRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMWFrGYqlPDTPAIDG--------------GYYLTGDTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 900 RYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAY-ITHHNEQVKPVLSN-LRAF 977
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFvVLRGGHEGTPALADeLQLH 402
|
490 500 510
....*....|....*....|....*....|...
gi 1574832895 978 VTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05973 403 VKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1625-1851 |
2.13e-35 |
|
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: 141.84 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd17650 4 IAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTHeelkarwphcpcpllcldtlqeryaslpcedlqeacsPAQLAYVIYTSGSTGRPKGVQISHG--ALLSFLLS 1782
Cdd:cd17650 84 GAKLLLTQ-------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRnvAHAAHAWR 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1783 LQSLLSLSPHdRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPT 1851
Cdd:cd17650 127 REYELDSFPV-RLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPA 194
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
488-1012 |
9.31e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 141.99 E-value: 9.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 488 GTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLI 567
Cdd:PRK07788 49 GPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 568 LDPSYPPARLLEYVQRahargwlriEGATdcqeldewcransycNLVLARNFAlsGILSQYASSAPAYRV--------GP 639
Cdd:PRK07788 129 LNTGFSGPQLAEVAAR---------EGVK---------------ALVYDDEFT--DLLSALPPDLGRLRAwggnpdddEP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 640 NDIACLTF------------------------TSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLS------G 689
Cdd:PRK07788 183 SGSTDETLddliagsstaplpkppkpggivilTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPApmfhatG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 690 LAHDPLQ---------REIFTPLCVGATIcipdQEHmgdpgwlaqwmqgqEITIASFTPALLQLLTQgMGEDDLPSARIP 760
Cdd:PRK07788 263 WAHLTLAmalgstvvlRRRFDPEATLEDI----AKH--------------KATALVVVPVMLSRILD-LGPEVLAKYDTS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 761 SLRYAFVVGDALTRRHVARLYAVAPHITCvNLYGSTEtqraVSYFVLPT-ASSTESPASVtalldkeviplGKGMPGAQI 839
Cdd:PRK07788 324 SLKIIFVSGSALSPELATRALEAFGPVLY-NLYGSTE----VAFATIATpEDLAEAPGTV-----------GRPPKGVTV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 840 LILNEAGNLAGIGELGEIYVRSpHLAF-GYLDDPDQtnerflvnpfthQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVK 918
Cdd:PRK07788 388 KILDENGNEVPRGVVGRIFVGN-GFPFeGYTDGRDK------------QIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 919 IRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYI-THHNEQVKPvlSNLRAFVTQRLPAFMVPAHFVFMSRL 997
Cdd:PRK07788 455 SGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVvKAPGAALDE--DAIKDYVRDNLARYKVPRDVVFLDEL 532
|
570
....*....|....*
gi 1574832895 998 PLNANGKVDRKALPA 1012
Cdd:PRK07788 533 PRNPTGKVLKRELRE 547
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1341-1856 |
1.08e-34 |
|
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: 145.98 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1341 WHGQLaTAPALLDLPTDHPRPPIQTFVGARHQLHLPAElleqlmVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTP 1420
Cdd:TIGR03443 2 WSERL-DNPTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1421 IAGRQRrelegviglfanTLVLRTDLSGDPSFLELLQRVREVTLQAYSQQDMPFEKLVAELQPERSLAYNP-LFQV-FFA 1498
Cdd:TIGR03443 75 SNKSGR------------PFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLaFQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1499 LQNVPGDPISlEGLDV-TQIRLDSNSAKFDLSwtwyqedekslsavIEYNTALFEPQRIAGMATNMLVVLQSLCQEPRTP 1577
Cdd:TIGR03443 143 APDNQQTTYS-TGSTTdLTVFLTPSSPELELS--------------IYYNSLLFSSDRITIVADQLAQLLSAASSNPDEP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1578 VSLLPLLSAAQRLHLlslghsssPLPAAPS--CG----LHHLIEAQCER-----------SSLQPAlhAGSTTLTYRQLN 1640
Cdd:TIGR03443 208 IGKVSLITPSQKSLL--------PDPTKDLdwSGfrgaIHDIFADNAEKhpdrtcvvetpSFLDPS--SKTRSFTYKQIN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1641 QQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQR------------LLWMAQDAQLSL 1708
Cdd:TIGR03443 278 EASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraLIVIEKAGTLDQ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1709 LLT---HEELKARwphCPCPLLCL----------------DTLQ--ERYASLPCEDLQEACSPAQLAyviYTSGSTGRPK 1767
Cdd:TIGR03443 358 LVRdyiDKELELR---TEIPALALqddgslvggsleggetDVLApyQALKDTPTGVVVGPDSNPTLS---FTSGSEGIPK 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1768 GVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQ 1847
Cdd:TIGR03443 432 GVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTH 511
|
....*....
gi 1574832895 1848 ATPTTWQLL 1856
Cdd:TIGR03443 512 LTPAMGQLL 520
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1625-1877 |
1.55e-34 |
|
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: 139.30 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd05945 8 PAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTheelkarwphcpcpllcldtlqeryaslpcedlqeacSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQ 1784
Cdd:cd05945 88 KPALLIA-------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWML 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1785 SLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETGwsgk 1864
Cdd:cd05945 131 SDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSP---- 206
|
250
....*....|...
gi 1574832895 1865 aglTLLSGAKPSL 1877
Cdd:cd05945 207 ---TFTPESLPSL 216
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
489-1010 |
1.90e-34 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 140.45 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEIN--TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVL 566
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 567 ILDPSYPPARLLEYVQRAHARGWLriegaTDCQELDEWCRANSYCNLV----LARNFALSGILSQYASSAPAYRVGPNDI 642
Cdd:cd05904 86 TANPLSTPAEIAKQVKDSGAKLAF-----TTAELAEKLASLALPVVLLdsaeFDSLSFSDLLFEADEAEPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 643 ACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFA--FTQTDRYSLLSGLAHdplqreIF-------TPLCVGATICIpd 713
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFH------IYglssfalGLLRLGATVVV-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 714 qehMG--DPGWLAQWMQGQEITIASFTPA-LLQLLTQGMGED-DLPSaripsLRYAFVVGDALTRRHVARLYAVAPHITC 789
Cdd:cd05904 233 ---MPrfDLEELLAAIERYKVTHLPVVPPiVLALVKSPIVDKyDLSS-----LRQIMSGAAPLGKELIEAFRAKFPNVDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 790 VNLYGSTETQrAVSYFVLPTASSTESPASVtalldkeviplGKGMPGAQILILN-EAGNLAGIGELGEIYVRSPHLAFGY 868
Cdd:cd05904 305 GQGYGMTEST-GVVAMCFAPEKDRAKYGSV-----------GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 869 LDDPDQTNERFLVnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIRE 948
Cdd:cd05904 373 LNNPEATAATIDK--------EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYP 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 949 DtPDNKQI-VAYIthhneqVKPVLSNL-----RAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05904 445 D-EEAGEVpMAFV------VRKPGSSLtedeiMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
489-1005 |
3.19e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 140.07 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAG------ 562
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGavhvpv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 563 -----------------STVLILDPS-YPPARLLEYVQRAHARGWLRIEGATDCQelDEWcransycnlvlaRNFAlsGI 624
Cdd:PRK08316 92 nfmltgeelayildhsgARAFLVDPAlAPTAEAALALLPVDTLILSLVLGGREAP--GGW------------LDFA--DW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 625 LSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTH-FLPWMRDrFAFTQTDRysllsGLAHDPL----QREI 699
Cdd:PRK08316 156 AEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAeYVSCIVA-GDMSADDI-----PLHALPLyhcaQLDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 700 F--TPLCVGATICIPDQEhmgDPGWLAQWMQGQEITiASFTP-----ALLQlltqgmgEDDLPSARIPSLRYAFVVGDAL 772
Cdd:PRK08316 230 FlgPYLYVGATNVILDAP---DPELILRTIEAERIT-SFFAPptvwiSLLR-------HPDFDTRDLSSLRKGYYGASIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 773 TRRHVARLYAVAPHITCVNLYGSTEtqravsyfVLPTAsstespasvTALLDKEVI--PLGKGMPG--AQILILNEAGNL 848
Cdd:PRK08316 299 PVEVLKELRERLPGLRFYNCYGQTE--------IAPLA---------TVLGPEEHLrrPGSAGRPVlnVETRVVDDDGND 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 849 AGIGELGEIYVRSPHLAFGYLDDPDQTNERFLvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEE 928
Cdd:PRK08316 362 VAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR---------GGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASRE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 929 IEAILVEHPMVADAAVIireDTPDNKQIVAY----ITHHNEQVKPvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGK 1004
Cdd:PRK08316 433 VEEALYTHPAVAEVAVI---GLPDPKWIEAVtavvVPKAGATVTE--DELIAHCRARLAGFKVPKRVIFVDELPRNPSGK 507
|
.
gi 1574832895 1005 V 1005
Cdd:PRK08316 508 I 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1610-1875 |
1.68e-33 |
|
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: 136.48 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLLTheelkarwphcpcpllcldtlqeryaslpcedlqeacspaqlAYVIYTSGSTGRPKGV 1769
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1770 QISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIA-GLELYLPLLAGAQIQLASqeqASDPRQLASLLAQLPISILQA 1848
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFG 195
|
250 260 270
....*....|....*....|....*....|.
gi 1574832895 1849 TPTTWQLLLETGWSGKAGL----TLLSGAKP 1875
Cdd:COG0318 196 VPTMLARLLRHPEFARYDLsslrLVVSGGAP 226
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
475-1024 |
2.47e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 138.93 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 475 LPDPGAPISahwegtIHDLFAQQAHLRPENIAII--------DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQ 546
Cdd:PRK07529 18 LAARDLPAS------TYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 547 RCAALVLAILG---------------------ILK-AGSTVLILDPSYPPARLLEYVQRA-----HARGWLRIEGATDCQ 599
Cdd:PRK07529 92 NLPETHFALWGgeaagianpinpllepeqiaeLLRaAGAKVLVTLGPFPGTDIWQKVAEVlaalpELRTVVEVDLARYLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 600 ELDEWCransycnLVLARNFALSGIL-------SQYASSA-PAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFlPW 671
Cdd:PRK07529 172 GPKRLA-------VPLIRRKAHARILdfdaelaRQPGDRLfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 672 MRDRFAFTQTDRySLLSGLahdPLqreiF----------TPLCVGATICIPDQEHMGDPGWLAQ-W--MQGQEITIASFT 738
Cdd:PRK07529 244 LGALLLGLGPGD-TVFCGL---PL----FhvnallvtglAPLARGAHVVLATPQGYRGPGVIANfWkiVERYRINFLSGV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 739 PALL-QLLTQGMGEDDlpsarIPSLRYAFvVGDALTRRHVARLYAVAPHITCVNLYGSTETqravsyfvlpTASSTESPA 817
Cdd:PRK07529 316 PTVYaALLQVPVDGHD-----ISSLRYAL-CGAAPLPVEVFRRFEAATGVRIVEGYGLTEA----------TCVSSVNPP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 818 svtallDKEVIP--LGKGMPGAQ--ILILNEAGNL---AGIGELGEIYVRSPHLAFGYLdDPDQTNERFLvnpfthqeHD 890
Cdd:PRK07529 380 ------DGERRIgsVGLRLPYQRvrVVILDDAGRYlrdCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL--------ED 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 891 RLYRTGDLGRYLPDGNAEFAGR-NDLqvKIR-GYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIthhneQVK 968
Cdd:PRK07529 445 GWLNTGDLGRIDADGYFWLTGRaKDL--IIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYV-----QLK 517
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 969 P----VLSNLRAFVTQRLP---AfmVPAHFVFMSRLPLNANGKVDRKALPAPEAADEATLSLA 1024
Cdd:PRK07529 518 PgasaTEAELLAFARDHIAeraA--VPKHVRILDALPKTAVGKIFKPALRRDAIRRVLRAALR 578
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
513-1010 |
4.15e-33 |
|
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: 134.91 E-value: 4.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYL-HAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHargwlr 591
Cdd:cd05958 10 EWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 592 iegatdcqeldewcRANSYCNLVLARNfalsgilsqyassapayrvgpNDIACLTFTSGSTGRPKGVLQRH-GPLTHFLP 670
Cdd:cd05958 84 --------------ITVALCAHALTAS---------------------DDICILAFTSGTTGAPKATMHFHrDPLASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 671 WMRDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGATICIPdqehmgdPGWLAQWMQGqeiTIASFTPALLQLLTQGM 749
Cdd:cd05958 129 YAVNVLRLREDDRFVGSPPLAFTfGLGGVLLFPFGVGASGVLL-------EEATPDLLLS---AIARYKPTVLFTAPTAY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 750 ----GEDDLPSARIPSLRYAFVVGDALTRRhVARLYAVAPHITCVNLYGSTEtqrAVSYFVlptaSSTESPASVTALldk 825
Cdd:cd05958 199 ramlAHPDAAGPDLSSLRKCVSAGEALPAA-LHRAWKEATGIPIIDGIGSTE---MFHIFI----SARPGDARPGAT--- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 826 eviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPhLAFGYLDDPDQTnerflvnpfTHQEHDRLYrTGDLGRYLPDG 905
Cdd:cd05958 268 -----GKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-TGCRYLADKRQR---------TYVQGGWNI-TGDTYSRDPDG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 906 NAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQIV-AYITHHNEQV-KPVL-SNLRAFVTQRL 982
Cdd:cd05958 332 YFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPD-ESRGVVVkAFVVLRPGVIpGPVLaRELQDHAKAHI 410
|
490 500
....*....|....*....|....*...
gi 1574832895 983 PAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05958 411 APYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
477-1005 |
8.44e-33 |
|
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: 136.55 E-value: 8.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 477 DPGAPISAHWEGTIHDLFAQ--QAHLR--PENIAIIDE------INTVSYGELEARSNQLAHYLHAQGIRPHDVVAI--- 543
Cdd:cd17634 38 APGAPSIKWFEDATLNLAANalDRHLRenGDRTAIIYEgddtsqSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIymp 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 544 ----------SAQRCAALVLAILG----------ILKAGSTVLIL-DPSYPPARLLEYVQRAHARGWLRIEGATDCQELD 602
Cdd:cd17634 118 mipeaavamlACARIGAVHSVIFGgfapeavagrIIDSSSRLLITaDGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 603 ewcRANSYCNLVLARNFALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPW-MRDRFAFTQT 681
Cdd:cd17634 198 ---RTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 682 DRYSLLSGL----AHDPLqreIFTPLCVGATICIPDQEHMG-DPGWLAQWMQGQEITIASFTPALLQLLTQGmGEDDLPS 756
Cdd:cd17634 275 DIYWCTADVgwvtGHSYL---LYGPLACGATTLLYEGVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAA-GDDAIEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 757 ARIPSLRYAFVVGDALTRRHVARLYAVAPHITC--VNLYGSTETQRAVSYfVLPTASSTESPASVTALldkeviplgkgm 834
Cdd:cd17634 351 TDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCpvVDTWWQTETGGFMIT-PLPGAIELKAGSATRPV------------ 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 835 PGAQILILNEAGNLAGIGELGEIYVRS--PHLAFGYLDDPDqtneRFLVNPFThqEHDRLYRTGDLGRYLPDGNAEFAGR 912
Cdd:cd17634 418 FGVQPAVVDNEGHPQPGGTEGNLVITDpwPGQTRTLFGDHE----RFEQTYFS--TFKGMYFSGDGARRDEDGYYWITGR 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 913 NDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIT-HHNEQVKPVLSN-LRAFVTQRLPAFMVPAH 990
Cdd:cd17634 492 SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVlNHGVEPSPELYAeLRNWVRKEIGPLATPDV 571
|
570
....*....|....*
gi 1574832895 991 FVFMSRLPLNANGKV 1005
Cdd:cd17634 572 VHWVDSLPKTRSGKI 586
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1633-1858 |
9.53e-33 |
|
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: 134.52 E-value: 9.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTH 1712
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1713 EelkarwpHCPCPLlcldtLQERYASLPCEDL--QEACS-------PAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSL 1783
Cdd:cd17656 93 R-------HLKSKL-----SFNKSTILLEDPSisQEDTSnidyinnSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1784 QSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLE 1858
Cdd:cd17656 161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS 235
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
496-1010 |
1.04e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 134.70 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 496 QQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPA 575
Cdd:PRK03640 10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 576 RLLeyVQRAHArgwlrieGATdcqeldewcransycNLVLARNFA--LSGILSQYASSAPAYRVGP---------NDIAC 644
Cdd:PRK03640 90 ELL--WQLDDA-------EVK---------------CLITDDDFEakLIPGISVKFAELMNGPKEEaeiqeefdlDEVAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 645 LTFTSGSTGRPKGVLQRHGplTHFLPWMRDRFAFTQTDRYSLL--------SGLAhdplqrEIFTPLCVGATICIpdQEH 716
Cdd:PRK03640 146 IMYTSGTTGKPKGVIQTYG--NHWWSAVGSALNLGLTEDDCWLaavpifhiSGLS------ILMRSVIYGMRVVL--VEK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 717 MgDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPSaripSLRyAFVVGDALTRRHVARLyAVAPHITCVNLYGST 796
Cdd:PRK03640 216 F-DAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPS----SFR-CMLLGGGPAPKPLLEQ-CKEKGIPVYQSYGMT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 797 ETqraVSYFV-LPTASSTESPASVtalldkeviplGKGMPGAQILILNEaGNLAGIGELGEIYVRSPHLAFGYLDDPDQT 875
Cdd:PRK03640 289 ET---ASQIVtLSPEDALTKLGSA-----------GKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDAT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 876 NERFlvnpfthqeHDRLYRTGDLGrYL-PDGNAEFAGR-NDLQVKiRGYRIELEEIEAILVEHPMVADAAVIIREDTPDN 953
Cdd:PRK03640 354 RETF---------QDGWFKTGDIG-YLdEEGFLYVLDRrSDLIIS-GGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 954 KQIVAYITHHneqVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK03640 423 QVPVAFVVKS---GEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
509-945 |
1.37e-32 |
|
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: 133.49 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 509 DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGstvLILDPSYPparlleyvqraharg 588
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIG---AVPVPIYP--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 589 wlriegaTDCQELDEWCRANSYCNLVLARNfalsgilsqyassapayrvgPNDIACLTFTSGSTGRPKGVLQRHGPLTHF 668
Cdd:cd05907 63 -------TSSAEQIAYILNDSEAKALFVED--------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSN 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 669 LPWMRDRFAFTQTDRYSLLSGLAHDPLQREI-FTPLCVGATICIPdqehmGDPGWLAQWMQGQEITIASFTPALLQLLTQ 747
Cdd:cd05907 116 ALALAERLPATEGDRHLSFLPLAHVFERRAGlYVPLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 748 GMGEDDLPS--------ARIPSLRYAFVVGDALTRRhVARLYAvAPHITCVNLYGSTETQRAVSyFVLPTassTESPASV 819
Cdd:cd05907 191 AIKVKAVPGlkrklfdlAVGGRLRFAASGGAPLPAE-LLHFFR-ALGIPVYEGYGLTETSAVVT-LNPPG---DNRIGTV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 820 talldkeviplGKGMPGAQIlilneagnlaGIGELGEIYVRSPHLAFGYLDDPDQTNERFLvnpfthqeHDRLYRTGDLG 899
Cdd:cd05907 265 -----------GKPLPGVEV----------RIADDGEILVRGPNVMLGYYKNPEATAEALD--------ADGWLHTGDLG 315
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1574832895 900 RYLPDGNAEFAGR-NDLQVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:cd05907 316 EIDEDGFLHITGRkKDLIITSGGKNISPEPIENALKASPLISQAVVI 362
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1612-1851 |
1.63e-31 |
|
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: 130.12 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1612 HLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPD 1691
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1692 YPSQRLLWMAQDAQLSLLLTheelkarwphcpcpllcldtlqeryaslpcedlqeACSPAQLAYVIYTSGSTGRPKGVQI 1771
Cdd:cd17653 81 LPSARIQAILRTSGATLLLT-----------------------------------TDSPDDLAYIIFTSGSTGIPKGVMV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1772 SHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASqeqASDPrqLASLLAQLpiSILQATPT 1851
Cdd:cd17653 126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD---PSDP--FAHVARTV--DALMSTPS 198
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
509-1010 |
1.68e-30 |
|
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: 128.52 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 509 DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISA---QRCAALVLAILG--------------------ILKAGSTV 565
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGmgavlhtinprlfpeqiayiINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 566 LILDPSYPParLLEYV--QRAHARGWLRIEGATDcQELDEWCRANSYCNLVlarnfalsgilsqyASSAPAY---RVGPN 640
Cdd:cd12119 101 VFVDRDFLP--LLEAIapRLPTVEHVVVMTDDAA-MPEPAGVGVLAYEELL--------------AAESPEYdwpDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLQRHGPLthFLPWM----RDRFAFTQTDRYSLLSGLAHD-----PlqreiFTPLCVGATICI 711
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSL--VLHAMaallTDGLGLSESDVVLPVVPMFHVnawglP-----YAAAMVGAKLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 PDQeHMgDPGWLAQWMQGQEITIASFTPALLQLLTQGMgedDLPSARIPSLRYAFVVGDALTRrHVARLYAvAPHITCVN 791
Cdd:cd12119 237 PGP-YL-DPASLAELIEREGVTFAAGVPTVWQGLLDHL---EANGRDLSSLRRVVIGGSAVPR-SLIEAFE-ERGVRVIH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 792 LYGSTETQRAVSYFVLPTASSTESPASVTALLDKEviplGKGMPGAQILILNEAGN-LAGIGE-LGEIYVRSPHLAFGYL 869
Cdd:cd12119 310 AWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQ----GRPVPGVELRIVDDDGReLPWDGKaVGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 870 DDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGR-NDLqVKIRGYRIELEEIEAILVEHPMVADAAVIIRe 948
Cdd:cd12119 386 KNDEESEALT---------EDGWLRTGDVATIDEDGYLTITDRsKDV-IKSGGEWISSVELENAIMAHPAVAEAAVIGV- 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 949 dtPDNK---QIVAYIT-HHNEQVKPvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd12119 455 --PHPKwgeRPLAVVVlKEGATVTA--EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
489-1010 |
2.25e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 128.32 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLIL 568
Cdd:PRK06164 11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 569 DPSYPPARLLEYVQRAHARgWLRIEGA------------------TDCQELDEWCRANSYC-NLVLARNFALSGILSQYA 629
Cdd:PRK06164 91 NTRYRSHEVAHILGRGRAR-WLVVWPGfkgidfaailaavppdalPPLRAIAVVDDAADATpAPAPGARVQLFALPDPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 630 SSAPAYRVGPNDIACLTFT-SGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRY-------------SLLSGLAHdpl 695
Cdd:PRK06164 170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLlaalpfcgvfgfsTLLGALAG--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 696 qreiftplcvGATICIpdqEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQGMGED-DLPSARIpslryaFVVGDALTR 774
Cdd:PRK06164 247 ----------GAPLVC---EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERaDFPSARL------FGFASFAPA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 775 RHVARLYAVAPHITCVNLYGSTETQRAVSyfvlptASSTESPASVTALldkeviplGKGM---PGAQILILN-EAGNLAG 850
Cdd:PRK06164 308 LGELAALARARGVPLTGLYGSSEVQALVA------LQPATDPVSVRIE--------GGGRpasPEARVRARDpQDGALLP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 851 IGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIE 930
Cdd:PRK06164 374 DGESGEIEIRAPSLMRGYLDNPDATARAL--------TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 931 AILVEHPMVADAAVIirEDTPDNKQIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLP--LNANG-KVDR 1007
Cdd:PRK06164 446 HALEALPGVAAAQVV--GATRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPvtESANGaKIQK 523
|
...
gi 1574832895 1008 KAL 1010
Cdd:PRK06164 524 HRL 526
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1156-1574 |
4.66e-30 |
|
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: 125.11 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1156 FLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQG--EQLMQRIHAQLWLSLsqQHLSLPAESE 1233
Cdd:cd19542 11 MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSaeGTFLQVVLKSLDPPI--EEVETDEDSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1234 SSLSQQalqawlqqEIRRPFDLQQaPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAhvkgispQLAP 1313
Cdd:cd19542 89 DALTRD--------LLDDPTLFGQ-PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------QLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1314 LPLQYADYAvwqrAWLQEERQEKLQRYWHGQLATA-----PALLDLPTDHPR-----PPIQTFVGARHQLHLPAELLEQL 1383
Cdd:cd19542 153 PAPPFSDYI----SYLQSQSQEESLQYWRKYLQGAspcafPSLSPKRPAERSlsstrRSLAKLEAFCASLGVTLASLFQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1384 ---MVLSHqqqvtlymtllaafllllyrYSGQEDLVVGTPIAGRQ--RRELEGVIGLFANTLVLRTDLSGDPSFLELLQR 1458
Cdd:cd19542 229 awaLVLAR--------------------YTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1459 VREVTLQAYSQQDMPFEKLVAELQPERSLaynPLFQVFFALQNVPGDP-ISLEGLDVTQIRLDSNSAKFDLsWTWYQEDE 1537
Cdd:cd19542 289 LQQQYLRSLPHQHLSLREIQRALGLWPSG---TLFNTLVSYQNFEASPeSELSGSSVFELSAAEDPTEYPV-AVEVEPSG 364
|
410 420 430
....*....|....*....|....*....|....*..
gi 1574832895 1538 KSLSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19542 365 DSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
492-1010 |
5.39e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 126.54 E-value: 5.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 492 DLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPS 571
Cdd:PRK06145 6 ASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 572 YPPARLLEYVQRAHARGWLRIEgatdcqELDewcransyCNLVLARNFALSGILSQYASS---------APAYRVGPNDI 642
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLLVDE------EFD--------AIVALETPKIVIDAAAQADSRrlaqggleiPPQAAVAPTDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 643 ACLTFTSGSTGRPKGVLQRHGPLThflpWMR-DRFA---FTQTDRYSLLSGLAH-DPLQREIFTPLCVGATICIpdqEHM 717
Cdd:PRK06145 152 VRLMYTSGTTDRPKGVMHSYGNLH----WKSiDHVIalgLTASERLLVVGPLYHvGAFDLPGIAVLWVGGTLRI---HRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 718 GDPGWLAQWMQGQEITIASFTPALL-QLLTqgmgeddLPSA---RIPSLRYAFVVGD---ALTRRHVARLYAVAPHItcv 790
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWMAPVMLsRVLT-------VPDRdrfDLDSLAWCIGGGEktpESRIRDFTRVFTRARYI--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 791 NLYGSTETqravsyfvlptaSSTESPASVTALLDKeVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLD 870
Cdd:PRK06145 295 DAYGLTET------------CSGDTLMEAGREIEK-IGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 871 DPDQTNERFLvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDT 950
Cdd:PRK06145 362 DPEKTAEAFY---------GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDD 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 951 PDNKQIVAYIThHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK06145 433 RWGERITAVVV-LNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
478-1010 |
1.20e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 126.69 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 478 PGAPISAHWEGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILG 557
Cdd:PRK06178 23 PREPEYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 558 ILKAG------------------------STVLILDpsyppaRLLEYVQRAHARGWLRIEGATdcqELDEWCRANSYCNL 613
Cdd:PRK06178 103 ILKLGavhvpvsplfrehelsyelndagaEVLLALD------QLAPVVEQVRAETSLRHVIVT---SLADVLPAEPTLPL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 614 ---VLARNFALSGILSQYAS------SAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGpltHFLPWMRDRFAFTQTDRY 684
Cdd:PRK06178 174 pdsLRAPRLAAAGAIDLLPAlractaPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 685 S--LLSGLAHDPLQRE---IFTPLCVGATICIpdqehmgdpgwLAQW--------MQGQEITIASFT-PALLQLL-TQGM 749
Cdd:PRK06178 251 DsvFLSFLPEFWIAGEnfgLLFPLFSGATLVL-----------LARWdavafmaaVERYRVTRTVMLvDNAVELMdHPRF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 750 GEDDLPSaripsLRYAFVVG--DALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYfvlptassTESPASVTALLDKEV 827
Cdd:PRK06178 320 AEYDLSS-----LRQVRVVSfvKKLNPDYRQRWRALTGSVLAEAAWGMTETHTCDTF--------TAGFQDDDFDLLSQP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 828 IPLGKGMPGAQILILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGN 906
Cdd:PRK06178 387 VFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL---------RDGWLHTGDIGKIDEQGF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 907 AEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQI-VAYIthhneQVKP----VLSNLRAFVTQR 981
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPD-PDKGQVpVAFV-----QLKPgadlTAAALQAWCREN 531
|
570 580
....*....|....*....|....*....
gi 1574832895 982 LPAFMVPaHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK06178 532 MAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
496-1010 |
2.70e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 124.59 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 496 QQAHLRPENIAIIDEINTVSYGELEARSNQLAHYL-HAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPP 574
Cdd:PRK06839 10 KRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 575 ARLLEYVQRAHARgwlRIEGATDCQELDEWCRANSYcnlvLARNFALSGiLSQYASSAPAYRVGPND----IACltFTSG 650
Cdd:PRK06839 90 NELIFQLKDSGTT---VLFVEKTFQNMALSMQKVSY----VQRVISITS-LKEIEDRKIDNFVEKNEsasfIIC--YTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKG-VLQRHgplTHFLPWMRDRFA--FTQTDRYSLLSGLAH-DPLQREIFTPLCVGATICIPDQehmGDPGWLAQW 726
Cdd:PRK06839 160 TTGKPKGaVLTQE---NMFWNALNNTFAidLTMHDRSIVLLPLFHiGGIGLFAFPTLFAGGVIIVPRK---FEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 727 MQGQEITIASFTPALLQLLTQGMgedDLPSARIPSLRYaFVVGDA-----LTRRHVARLYAVAPHitcvnlYGSTETQRA 801
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCS---KFETTNLQSVRW-FYNGGApcpeeLMREFIDRGFLFGQG------FGMTETSPT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 802 VsyFVLPTASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlv 881
Cdd:PRK06839 304 V--FMLSEEDARRKVGSI-----------GKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 882 npfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIT 961
Cdd:PRK06839 369 -------QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIV 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1574832895 962 HHNEQVKpVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK06839 442 KKSSSVL-IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
647-1007 |
2.94e-29 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 120.59 E-value: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 647 FTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIpdqEHMGDPGWLAQW 726
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 727 MQGQEITIASFTPALLQLLTQgmgeDDLPSARIPSLryaFVVGDALTRRHVARLYAVAPHITCVNLYGSTETqravSYfv 806
Cdd:cd17633 84 INQYNATVIYLVPTMLQALAR----TLEPESKIKSI---FSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL----SF-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 807 lptasstespasVTALLDKEVIP---LGKGMPGAQILILNEAGnlagiGELGEIYVRSPHLAFGYLDdpdqtnERFlVNP 883
Cdd:cd17633 151 ------------ITYNFNQESRPpnsVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVR------GGF-SNP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 884 fthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNkQIVAYITHH 963
Cdd:cd17633 207 ------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFG-EIAVALYSG 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1574832895 964 NEQVKPvlsNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:cd17633 280 DKLTYK---QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
641-1010 |
1.37e-28 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 118.59 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATIcipdqeHMGDP 720
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAEL------VLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 721 GW-LAQWMQGQEITIASFTPA-LLQLLtqgmgEDDLPSARIPSLRYAFVVGDALTRRHVARlyAVAPHITCVNLYGSTET 798
Cdd:cd17630 75 NQaLAEDLAPPGVTHVSLVPTqLQRLL-----DSGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 799 QRAVsyfvlptassTESPASVTALLDkevipLGKGMPGAQILILNEagnlagigelGEIYVRSPHLAFGYLDDPdqtner 878
Cdd:cd17630 148 ASQV----------ATKRPDGFGRGG-----VGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 879 fLVNPFTHQEhdrLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIireDTPDNK---Q 955
Cdd:cd17630 197 -LVPEFNEDG---WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV---GVPDEElgqR 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 956 IVAYITHHNEqvkPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd17630 270 PVAVIVGRGP---ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
486-1013 |
1.68e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 122.56 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 486 WEGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTV 565
Cdd:PRK13382 41 EGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 566 LILDPSYPPARLLEYVQRAHARGWLRIEGATDC--QELDEWCRANSYCNLVLARNFALSGILSQ-YASSAPAYRVGPNDI 642
Cdd:PRK13382 121 LLLNTSFAGPALAEVVTREGVDTVIYDEEFSATvdRALADCPQATRIVAWTDEDHDLTVEVLIAaHAGQRPEPTGRKGRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 643 ACLTftSGSTGRPKGVlqRH------GPLTHFL---PW-----------MRDRFAFTQTdrySLLSGLAHDPLQREIFTP 702
Cdd:PRK13382 201 ILLT--SGTTGTPKGA--RRsgpggiGTLKAILdrtPWraeeptvivapMFHAWGFSQL---VLAASLACTIVTRRRFDP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 703 lcvGATICIPDQEHMgdpgwlaqwmqgqeiTIASFTPALLQLLTQgMGEDDLPSARIPSLRYAFVVGDALtRRHVARLYA 782
Cdd:PRK13382 274 ---EATLDLIDRHRA---------------TGLAVVPVMFDRIMD-LPAEVRNRYSGRSLRFAAASGSRM-RPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 783 VAPHITCVNLYGSTETQRAvsyfvlptasSTESPASVTALLDKEviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSP 862
Cdd:PRK13382 334 DQFGDVIYNNYNATEAGMI----------ATATPADLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRND 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 863 HLAFGYldDPDQTNERflvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADA 942
Cdd:PRK13382 400 TQFDGY--TSGSTKDF----------HDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 943 AVIIREDTPDNKQIVAYITHhNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAP 1013
Cdd:PRK13382 468 AVIGVDDEQYGQRLAAFVVL-KPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
639-1006 |
1.78e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 119.41 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLtFTSGSTGRPKGVLQRH---------GPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPL-----QREIFTPLC 704
Cdd:cd05924 3 ADDLYIL-YTGGTTGMPKGVMWRQedifrmlmgGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLmhgtgSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 VGATICIPDQEHMGDPGW-LAQWMQGQEITIA--SFTPALLQLLTQGMGEDdlpsarIPSLRYAFVVGDALTRRHVARLY 781
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWrTIEKHKVTSMTIVgdAMARPLIDALRDAGPYD------LSSLFAISSGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 782 AVAPHITCVNLYGSTETQRAVSYFVLPTASSTES---PASVTALLDkeviPLGKGMPGaqililneagnlaGIGELGEIy 858
Cdd:cd05924 156 ELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPftrANPDTVVLD----DDGRVVPP-------------GSGGVGWI- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 859 VRSPHLAFGYLDDPDQTNERFLVnpfthQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPM 938
Cdd:cd05924 218 ARRGHIPLGYYGDEAKTAETFPE-----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPA 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 939 VADAAVIIRedtPDNK--QIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVD 1006
Cdd:cd05924 293 VYDVLVVGR---PDERwgQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
513-1010 |
1.79e-28 |
|
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: 120.53 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDpsyppARLLEYvqrahargwlri 592
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN-----TRLTPN------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 egatdcqELdewcransycnlvlarnfalsgiLSQYASSAPAYrvgpNDIACLTFTSGSTGRPKGVLQRHGplTHFlpW- 671
Cdd:cd05912 64 -------EL-----------------------AFQLKDSDVKL----DDIATIMYTSGTTGKPKGVQQTFG--NHW--Ws 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 672 ---MRDRFAFTQTDRYSL------LSGLAhdplqrEIFTPLCVGATICIPDQEhmgDPGWLAQWMQGQEITIASFTPALL 742
Cdd:cd05912 106 aigSALNLGLTEDDNWLCalplfhISGLS------ILMRSVIYGMTVYLVDKF---DAEQVLHLINSGKVTIISVVPTML 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 743 QLLTQgmgedDLPSARIPSLRYAFVVGDALTRRHVARlyAVAPHITCVNLYGSTETqraVSYFV-LPTASSTESPASVta 821
Cdd:cd05912 177 QRLLE-----ILGEGYPNNLRCILLGGGPAPKPLLEQ--CKEKGIPVYQSYGMTET---CSQIVtLSPEDALNKIGSA-- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 822 lldkeviplGKGMPGAQILILNEAGNLAGIGElgeIYVRSPHLAFGYLDDPDQTNERFLVNPFthqehdrlyRTGDLGrY 901
Cdd:cd05912 245 ---------GKPLFPVELKIEDDGQPPYEVGE---ILLKGPNVTKGYLNRPDATEESFENGWF---------KTGDIG-Y 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 902 L-PDGNAEFAGR-NDLQVKiRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHneqvKPV-LSNLRAFV 978
Cdd:cd05912 303 LdEEGFLYVLDRrSDLIIS-GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE----RPIsEEELIAYC 377
|
490 500 510
....*....|....*....|....*....|..
gi 1574832895 979 TQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05912 378 SEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
496-1010 |
3.92e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 121.34 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 496 QQAHLRPENIAII--DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAI-------------SAQRCAALVLAILGILK 560
Cdd:PRK13391 5 IHAQTTPDKPAVImaSTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIfmennlrylevcwAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 561 AGSTVLILDPSypPARLLeYVQRAHARGwlriegatdCQELDEWCRANSYCnLVLARNFALSGILSqYASSAPAYRVGPN 640
Cdd:PRK13391 85 PAEAAYIVDDS--GARAL-ITSAAKLDV---------ARALLKQCPGVRHR-LVLDGDGELEGFVG-YAEAVAGLPATPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIAC----LTFTSGSTGRPKGVL--------QRHGPLTHFLpwmRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGAT 708
Cdd:PRK13391 151 ADESlgtdMLYSSGTTGRPKGIKrplpeqppDTPLPLTAFL---QRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 709 ICIpdQEHMgDPGWLAQWMQGQEITIASFTPAL----LQLLTQGMGEDDLPSARIpsLRYAFVVGDALTRRHVARLYAVA 784
Cdd:PRK13391 228 VIV--MEHF-DAEQYLALIEEYGVTHTQLVPTMfsrmLKLPEEVRDKYDLSSLEV--AIHAAAPCPPQVKEQMIDWWGPI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 785 PHitcvNLYGSTEtqrAVSYFVLPTASSTESPASVtalldkeviplGKGMPGaQILILNEAGNLAGIGELGEIYVRSPHl 864
Cdd:PRK13391 303 IH----EYYAATE---GLGFTACDSEEWLAHPGTV-----------GRAMFG-DLHILDDDGAELPPGEPGTIWFEGGR- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 865 AFGYLDDPDQTNErflvnpfTHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAV 944
Cdd:PRK13391 363 PFEYLNDPAKTAE-------ARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAV 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 945 IireDTPDNKQivayithhNEQVKPVL-------------SNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK13391 436 F---GVPNEDL--------GEEVKAVVqpvdgvdpgpalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
485-1010 |
4.29e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 121.70 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 485 HWEG-TIHDLFAQQAHLRPENIAIID------EINTVSYGELEARSNQLAHYLHAQGIRPHDVVAI-------------S 544
Cdd:PRK13295 20 HWHDrTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCqlpnwweftvlylA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 545 AQRCAALVLAILGILK----------AGSTVLILdPS----YPPARLLEYVQRA--HARGWLRIEGATdcqeldewcrAN 608
Cdd:PRK13295 100 CSRIGAVLNPLMPIFRerelsfmlkhAESKVLVV-PKtfrgFDHAAMARRLRPElpALRHVVVVGGDG----------AD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 609 SYCNLVLARNF----ALSGILsqyASSAPayrvGPNDIACLTFTSGSTGRPKGVLqrHGPLTHF---LPWMRdRFAFTQT 681
Cdd:PRK13295 169 SFEALLITPAWeqepDAPAIL---ARLRP----GPDDVTQLIYTSGTTGEPKGVM--HTANTLManiVPYAE-RLGLGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 682 DRYSLLSGLAHDP-LQREIFTPLCVGATICIPDQehmGDPGWLAQWMQGQEI--TIASfTPALLQlLTQGMGEDDLPsar 758
Cdd:PRK13295 239 DVILMASPMAHQTgFMYGLMMPVMLGATAVLQDI---WDPARAAELIRTEGVtfTMAS-TPFLTD-LTRAVKESGRP--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 759 IPSLRyAFVVGDA-----LTRRHVARLYAvaphiTCVNLYGSTETqravsyfvlpTASSTESPASVtalLDKEVIPLGKG 833
Cdd:PRK13295 311 VSSLR-TFLCAGApipgaLVERARAALGA-----KIVSAWGMTEN----------GAVTLTKLDDP---DERASTTDGCP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 834 MPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRN 913
Cdd:PRK13295 372 LPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA----------DGWFDTGDLARIDADGYIRISGRS 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 914 DlQVKIRG-YRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIThhneqVKP----VLSNLRAFV-TQRLPAFMV 987
Cdd:PRK13295 442 K-DVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVV-----PRPgqslDFEEMVEFLkAQKVAKQYI 515
|
570 580
....*....|....*....|...
gi 1574832895 988 PAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK13295 516 PERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
496-1018 |
5.29e-28 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 121.54 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 496 QQAHLRPENIAIID----------EINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTV 565
Cdd:PRK09274 14 RAAQERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 566 LILDPSYPPARLLEYVQRAHARGWLRIEGATDCQELDEWCRANSYCNLVLARNFALSG------ILSQYASSAPAYRVGP 639
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLARRLFGWGKPSVRRLVTVGGRLLWGGttlatlLRDGAAAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 640 NDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRysllsGLAHDPLqreiFT--PLCVGATICIPDqehM 717
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI-----DLPTFPL----FAlfGPALGMTSVIPD---M 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 718 G-------DPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPsarIPSLRYAFVVGDALTRRHVARLYAVAPHITCV 790
Cdd:PRK09274 242 DptrpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIK---LPSLRRVISAGAPVPIAVIERFRAMLPPDAEI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 791 -NLYGSTEtqravsyfVLPTAS--STESPASVTALLDK-EVIPLGKGMPGAQILI----------LNEAGNLAgIGELGE 856
Cdd:PRK09274 319 lTPYGATE--------ALPISSieSREILFATRAATDNgAGICVGRPVDGVEVRIiaisdapipeWDDALRLA-TGEIGE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 857 IYVRSPHLAFGYLDDPDQTnerfLVNPFTHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEH 936
Cdd:PRK09274 390 IVVAGPMVTRSYYNRPEAT----RLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTH 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 937 PMVADAA-VIIredTPDNKQIVAYIThhneQVKPVLSNLRAFVTQRLPAF-------MVPAHFVFMSRLPLNA--NGKVD 1006
Cdd:PRK09274 466 PGVKRSAlVGV---GVPGAQRPVLCV----ELEPGVACSKSALYQELRALaaahphtAGIERFLIHPSFPVDIrhNAKIF 538
|
570
....*....|..
gi 1574832895 1007 RKALpAPEAADE 1018
Cdd:PRK09274 539 REKL-AVWAAKQ 549
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
489-945 |
8.45e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 121.36 E-value: 8.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAII----DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAG-S 563
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALRekedGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGaV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 564 TVlildPSYP--PARLLEYV------------QRAHARGWLRIEGAT---------DCQELDEWCRANSYCNLV-LARNF 619
Cdd:COG1022 92 TV----PIYPtsSAEEVAYIlndsgakvlfveDQEQLDKLLEVRDELpslrhivvlDPRGLRDDPRLLSLDELLaLGREV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 620 ALSGILSQYASSapayrVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRY-SLLSgLAHdPLQRE 698
Cdd:COG1022 168 ADPAELEARRAA-----VKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTlSFLP-LAH-VFERT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 699 I-FTPLCVGATICIPD-------------------------------QEHMGDPGWLAQWM------QGQEITIASFT-- 738
Cdd:COG1022 241 VsYYALAAGATVAFAEspdtlaedlrevkptfmlavprvwekvyagiQAKAEEAGGLKRKLfrwalaVGRRYARARLAgk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 739 --PALLQL------------LTQGMGeddlpsariPSLRYAfVVGDALTRRHVARLYAVApHITCVNLYGSTETqravsy 804
Cdd:COG1022 321 spSLLLRLkhaladklvfskLREALG---------GRLRFA-VSGGAALGPELARFFRAL-GIPVLEGYGLTET------ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 805 fvlptassteSPAsVTALLDKEVIP--LGKGMPGAQIlilneagnlaGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVn 882
Cdd:COG1022 384 ----------SPV-ITVNRPGDNRIgtVGPPLPGVEV----------KIAEDGEILVRGPNVMKGYYKNPEATAEAFDA- 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 883 pfthqehDRLYRTGDLGRYLPDGNaefagrndlqVKIRGyRI-EL-----------EEIEAILVEHPMVADAAVI 945
Cdd:COG1022 442 -------DGWLHTGDIGELDEDGF----------LRITG-RKkDLivtsggknvapQPIENALKASPLIEQAVVV 498
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
53-456 |
8.87e-28 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 118.17 E-value: 8.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 53 ASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLN-GEPIQVIRPNLTLQIplidltslpeaEREASLQHAIN 131
Cdd:cd19545 20 GAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDsGGLLQVVVKESPISW-----------TESTSLDEYLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 132 NEAHIPFDLKtGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYsaalAGNSPTLPAPSLQYADYaawqr 211
Cdd:cd19545 89 EDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----QGEPVPQPPPFSRFVKY----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 212 nwLKGENLTNLLDYWRKQLADMPPlLELPMdHPRPAVQTSHGAVV--SLLLPSeistalkalSQHEGVTLFMTTLALFQI 289
Cdd:cd19545 159 --LRQLDDEAAAEFWRSYLAGLDP-AVFPP-LPSSRYQPRPDATLehSISLPS---------SASSGVTLATVLRAAWAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 290 LLQRYTGRRDIVIGTPIANRNR--TDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAYAHQDIPFDALLdELN 367
Cdd:cd19545 226 VLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIR-RLG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 368 PErsLSHSLLFQvffNMVNL-PDLHDEWPDLKVEHLWPREIGSK-FD---LTLFVQEEQDAIRLELVYNTDLFKHERMLE 442
Cdd:cd19545 305 PD--ARAACNFQ---TLLVVqPALPSSTSESLELGIEEESEDLEdFSsygLTLECQLSGSGLRVRARYDSSVISEEQVER 379
|
410
....*....|....
gi 1574832895 443 MLEQYSCLASQVSE 456
Cdd:cd19545 380 LLDQFEHVLQQLAS 393
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
513-1009 |
9.76e-28 |
|
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: 120.42 E-value: 9.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGiRPHDVVAISAQRCAALVLAILGILKAGstvLILDPSYPP------ARLLEYVQRAHA 586
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAG---AIAVPLPPPtpgrhaERLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 587 RGWLRIEGATDcqELDEWCRanSYCNLVLARNFALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLT 666
Cdd:cd05931 100 RVVLTTAAALA--AVRAFAA--SRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 667 HFLPWMRDRFAFTQTDRY-SLLSgLAHD-PLQREIFTPLCVGAT-ICIPDQEHMGDPgwlAQWMQgqeiTI----ASFTP 739
Cdd:cd05931 176 ANVRQIRRAYGLDPGDVVvSWLP-LYHDmGLIGGLLTPLYSGGPsVLMSPAAFLRRP---LRWLR----LIsryrATISA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 740 A---LLQLLTQGMGEDDLPSARIPSLRYAFVVG-----DALTR------RHVARLYAVAPHitcvnlYG---ST------ 796
Cdd:cd05931 248 ApnfAYDLCVRRVRDEDLEGLDLSSWRVALNGAepvrpATLRRfaeafaPFGFRPEAFRPS------YGlaeATlfvsgg 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 797 --ETQRAVSYFVLPTASSTESPASVTALLDKEVIPLGKGMPGAQILILNEAGN-LAGIGELGEIYVRSPHLAFGYLDDPD 873
Cdd:cd05931 322 ppGTGPVVLRVDRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 874 QTNERFlvNPFTHQEHDRLYRTGDLGrYLPDGNAEFAGR-NDLQVkIRGYRIELEEIEAILVEHP--MVADAAVIIREDT 950
Cdd:cd05931 402 ATAETF--GALAATDEGGWLRTGDLG-FLHDGELYITGRlKDLII-VRGRNHYPQDIEATAEEAHpaLRPGCVAAFSVPD 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 951 PDNKQIVAYITHHNEQVKPVLSNLRAFVTQRLP-AFMVPAH-FVFMSR--LPLNANGKVDRKA 1009
Cdd:cd05931 478 DGEERLVVVAEVERGADPADLAAIAAAIRAAVArEHGVAPAdVVLVRPgsIPRTSSGKIQRRA 540
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
641-1005 |
2.35e-27 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 115.29 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLQRHGP-LTHFLPWMrDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGATIcIPDQehMG 718
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQtLRAAAAWA-DCADLTEDDRYLIINPFFHTfGYKAGIVACLLTGATV-VPVA--VF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 719 DPGWLAQWMQGQEITIASFTPALLQLLtqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTET 798
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSL---LDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 799 qravsyfVLPTASSTESPASVTAlldkevIPLGKGMPGAQIlilneagnlaGIGELGEIYVRSPHLAFGYLDDPDQTNER 878
Cdd:cd17638 154 -------GVATMCRPGDDAETVA------TTCGRACPGFEV----------RIADDGEVLVRGYNVMQGYLDDPEATAEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 879 FLVNPFTHqehdrlyrTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVA 958
Cdd:cd17638 211 IDADGWLH--------TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKA 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1574832895 959 YITHHNEQVKPVlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKV 1005
Cdd:cd17638 283 FVVARPGVTLTE-EDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
513-1014 |
2.57e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 118.17 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHylhaqGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLri 592
Cdd:PRK07787 25 VLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 eGATDcQELDewcransycnlvlarnfALSGI-LSQYASSAPAY-RVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLP 670
Cdd:PRK07787 98 -GPAP-DDPA-----------------GLPHVpVRLHARSWHRYpEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 671 WMRDRFAFTQTDrySLLSGLahdPLQR------EIFTPLCVGATIcipdqEHMGDPgwlaqwmqgqeiTIASFTPALLQL 744
Cdd:PRK07787 159 ALAEAWQWTADD--VLVHGL---PLFHvhglvlGVLGPLRIGNRF-----VHTGRP------------TPEAYAQALSEG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 745 LTQGMG--------EDDLPSARipSLRYA--FVVGDALTRRHV-ARLYAVAPHiTCVNLYGSTETQRAVSYFvlptASST 813
Cdd:PRK07787 217 GTLYFGvptvwsriAADPEAAR--ALRGArlLVSGSAALPVPVfDRLAALTGH-RPVERYGMTETLITLSTR----ADGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 814 ESPASVtalldkeviplGKGMPGAQILILNEAGN-LAGIGE-LGEIYVRSPHLAFGYLDDPDQTNERFLVnpfthqehDR 891
Cdd:PRK07787 290 RRPGWV-----------GLPLAGVETRLVDEDGGpVPHDGEtVGELQVRGPTLFDGYLNRPDATAAAFTA--------DG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 892 LYRTGDLGRYLPDGNAEFAGRN--DLqVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEqvkP 969
Cdd:PRK07787 351 WFRTGDVAVVDPDGMHRIVGREstDL-IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD---V 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1574832895 970 VLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPE 1014
Cdd:PRK07787 427 AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
469-1007 |
4.22e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 118.72 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 469 TRASSVLPDPGAPISAhweGTIHDLFAQQAHLRPENIAIIDEINTV--SYGELEARSNQLAHYLHAQGIRPHDVVAISAQ 546
Cdd:PRK12583 2 PQPSYYQGGGDKPLLT---QTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 547 RCAALVLAILGILKAGSTVLILDPSYPpARLLEY-VQRAHARGWLRIEG--ATD--------CQELDEWCRANSYC---- 611
Cdd:PRK12583 79 NCAEWLLTQFATARIGAILVNINPAYR-ASELEYaLGQSGVRWVICADAfkTSDyhamlqelLPGLAEGQPGALACerlp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 612 ---NLVLARNFALSGILSQYASSAPAYRVGPNDIACLT------------FTSGSTGRPKGVLQRHGPLTHFLPWMRDRF 676
Cdd:PRK12583 158 elrGVVSLAPAPPPGFLAWHELQARGETVSREALAERQasldrddpiniqYTSGTTGFPKGATLSHHNILNNGYFVAESL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 677 AFTQTDRYSLLSGLAHdplqreIF-----TPLC--VGATICIPdQEHMgDPGWLAQWMQGQEITIASFTPALL--QLLTQ 747
Cdd:PRK12583 238 GLTEHDRLCVPVPLYH------CFgmvlaNLGCmtVGACLVYP-NEAF-DPLATLQAVEEERCTALYGVPTMFiaELDHP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 748 GMGEDDLPSaripsLRYAFVVGD----ALTRRHVARLyavapHITCVNL-YGSTETQravsyfvlPTASSTespaSVTAL 822
Cdd:PRK12583 310 QRGNFDLSS-----LRTGIMAGApcpiEVMRRVMDEM-----HMAEVQIaYGMTETS--------PVSLQT----TAADD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 823 LDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHqehdrlyrTGDLGRYL 902
Cdd:PRK12583 368 LERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMH--------TGDLATMD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 903 PDGNAEFAGRNDlQVKIR-GYRIELEEIEAILVEHPMVADAAVIireDTPDNK---QIVAYITHHNEQvKPVLSNLRAFV 978
Cdd:PRK12583 440 EQGYVRIVGRSK-DMIIRgGENIYPREIEEFLFTHPAVADVQVF---GVPDEKygeEIVAWVRLHPGH-AASEEELREFC 514
|
570 580
....*....|....*....|....*....
gi 1574832895 979 TQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:PRK12583 515 KARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
639-1007 |
7.68e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 114.30 E-value: 7.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLqrhgpLTHF-----LPWMRDRFAFTQTDRYSLLSGLAHdplqreIF-----TPLCV--G 706
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGAT-----LTHHnivnnGYFIGERLGLTEQDRLCIPVPLFH------CFgsvlgVLACLthG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 707 ATICIPdqEHMGDPGWLAQWMQGQEITIASFTPAL-LQLLTQgmgeDDLPSARIPSLRYAFVVG----DALTRRHVARLY 781
Cdd:cd05917 70 ATMVFP--SPSFDPLAVLEAIEKEKCTALHGVPTMfIAELEH----PDFDKFDLSSLRTGIMAGapcpPELMKRVIEVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 782 AVAPHITcvnlYGSTETQrAVSyfvlpTASSTESPasvtalLDKEVIPLGKGMPGAQILILNEAGN-LAGIGELGEIYVR 860
Cdd:cd05917 144 MKDVTIA----YGMTETS-PVS-----TQTRTDDS------IEKRVNTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 861 SPHLAFGYLDDPDQTNErflvnpfTHqEHDRLYRTGDLGRYLPDGNAEFAGR-NDLqvKIRG-YRIELEEIEAILVEHPM 938
Cdd:cd05917 208 GYSVMKGYWNDPEKTAE-------AI-DGDGWLHTGDLAVMDEDGYCRIVGRiKDM--IIRGgENIYPREIEEFLHTHPK 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 939 VADAAVIireDTPDNK---QIVAYITHHNEQvKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:cd05917 278 VSDVQVV---GVPDERygeEVCAWIRLKEGA-ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
509-1021 |
8.74e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 117.69 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 509 DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARG 588
Cdd:PRK04319 69 SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 589 ------WLRIEGATDCQELDewcransYCNLVLARNFALSGILS-----QYASSAPAYR-VGPNDIACLTFTSGSTGRPK 656
Cdd:PRK04319 149 littpaLLERKPADDLPSLK-------HVLLVGEDVEEGPGTLDfnalmEQASDEFDIEwTDREDGAILHYTSGSTGKPK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 657 GVLQRHGP-LTHflpWMRDRFA--FTQTDRY------SLLSGLAHDplqreIFTPLCVGATICIpDQEHMgDPGWLAQWM 727
Cdd:PRK04319 222 GVLHVHNAmLQH---YQTGKYVldLHEDDVYwctadpGWVTGTSYG-----IFAPWLNGATNVI-DGGRF-SPERWYRIL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 728 QGQEITIASFTPALLQLLtQGMGEDDLPSARIPSLRYAFVVGDALTRRHV---ARLYAVAPHITcvnlYGSTET--QRAV 802
Cdd:PRK04319 292 EDYKVTVWYTAPTAIRML-MGAGDDLVKKYDLSSLRHILSVGEPLNPEVVrwgMKVFGLPIHDN----WWMTETggIMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 803 SYFVLPTassteSPASvtalldkevipLGKGMPGAQILILNEAGNLAGIGELGEIYVRS--PHLAFGYLDDPDQTNERFL 880
Cdd:PRK04319 367 NYPAMDI-----KPGS-----------MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYFA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 881 vnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQIV-AY 959
Cdd:PRK04319 431 ---------GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD-PVRGEIIkAF 500
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 960 IT-----HHNEQVKpvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPE----AADEATL 1021
Cdd:PRK04319 501 VAlrpgyEPSEELK---EEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWElglpEGDLSTM 568
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
487-1016 |
1.15e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 116.98 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 487 EGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQ-GIRPHDVVAISAQRCAALVLAILGILKAGSTV 565
Cdd:PRK08314 9 ETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 566 LILDPSYPPARLLEYVQRAHAR----------------GWLRIEGATDCQELD-----------EWCRAN-SYCNLVLAR 617
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARvaivgselapkvapavGNLRLRHVIVAQYSDylpaepeiavpAWLRAEpPLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 618 NFALSGILSQyASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFlpwmrdrfAFTQTDRYSLLS---GLAHDP 694
Cdd:PRK08314 169 VVAWKEALAA-GLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMAN--------AVGSVLWSNSTPesvVLAVLP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 695 L------QREIFTPLCVGATICIpdqehMgdPGW----LAQWMQGQEITIASFTPALL-QLLTQ-GMGEDDLPSaripsL 762
Cdd:PRK08314 240 LfhvtgmVHSMNAPIYAGATVVL-----M--PRWdreaAARLIERYRVTHWTNIPTMVvDFLASpGLAERDLSS-----L 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 763 RYafVVG------DALTRRhVARLYAvaphITCVNLYGSTETqravsyfVLPTASSTESPASVTALldkeviplgkGMP- 835
Cdd:PRK08314 308 RY--IGGggaampEAVAER-LKELTG----LDYVEGYGLTET-------MAQTHSNPPDRPKLQCL----------GIPt 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 836 -GAQILILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLvnpfthqEHD--RLYRTGDLGRYLPDGNAEFAG 911
Cdd:PRK08314 364 fGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI-------EIDgkRFFRTGDLGRMDEEGYFFITD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 912 RNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQV-KPVLSNLRAFVTQRLPAFMVPAH 990
Cdd:PRK08314 437 RLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgKTTEEEIIAWAREHMAAYKYPRI 516
|
570 580
....*....|....*....|....*.
gi 1574832895 991 FVFMSRLPLNANGKVDRKALPAPEAA 1016
Cdd:PRK08314 517 VEFVDSLPKSGSGKILWRQLQEQEKA 542
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1626-1855 |
2.01e-26 |
|
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: 115.19 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1626 ALHAGSTTLTYRQLNQQANQLAHLLRQHGIG-PGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd17648 5 AVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTheelkarwphcpcpllcldtlqeryaslpcedlqeacSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQ 1784
Cdd:cd17648 85 GARVVIT-------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 1785 SLLSLSPHD--RWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQL 1855
Cdd:cd17648 128 ERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQ 200
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
487-1010 |
7.19e-26 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 114.86 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 487 EGTIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVL 566
Cdd:PRK06155 20 ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 567 ILDPSYPPARLLEYVQRAHAR-------GWLRIEGATDCQE-LDEWCRANSYCNLVLARNFALSGiLSQYASSAPAYRVG 638
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARllvveaaLLAALEAADPGDLpLPAVWLLDAPASVSVPAGWSTAP-LPPLDAPAPAAAVQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGpltHFLPW---MRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIpdQE 715
Cdd:PRK06155 179 PGDTAAILYTSGTTGPSKGVCCPHA---QFYWWgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL--EP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 716 HMGDPGWLAQwMQGQEITIASFTPALLQ-LLTQGMGEDDlpsaRIPSLRYAFVVGdalTRRHVARLYAVAPHITCVNLYG 794
Cdd:PRK06155 254 RFSASGFWPA-VRRHGATVTYLLGAMVSiLLSQPARESD----RAHRVRVALGPG---VPAALHAAFRERFGVDLLDGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 795 STETQravsyFVLPTASSTESPASvtalldkevipLGKGMPGAQILILNEAGNLAGIGELGEIYVRS--PH-LAFGYLDD 871
Cdd:PRK06155 326 STETN-----FVIAVTHGSQRPGS-----------MGRLAPGFEARVVDEHDQELPDGEPGELLLRAdePFaFATGYFGM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 872 PDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVI-IREDT 950
Cdd:PRK06155 390 PEKTVEAW---------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFpVPSEL 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 951 PDNKQIVAYITHHNEQVKPVlsNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK06155 461 GEDEVMAAVVLRDGTALEPV--ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
513-1010 |
7.80e-26 |
|
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: 114.69 E-value: 7.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPsyPPARLLEYVQRAHARGWLRI 592
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTV--PPTYDEPNARLRKLRHIWQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 EGA----TDC---QELDEWCRANSYCNLVLArnfaLSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRH--- 662
Cdd:cd05906 117 LGSpvvlTDAelvAEFAGLETLSGLPGIRVL----SIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHrni 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 663 -------------GPLTHFLPWMR-DRFAftqtdrysllsGLAHDPLQreiftPLCVGA-TICIPDQEHMGDP-GWLaQW 726
Cdd:cd05906 193 larsagkiqhnglTPQDVFLNWVPlDHVG-----------GLVELHLR-----AVYLGCqQVHVPTEEILADPlRWL-DL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 727 MQGQEITIaSFTPA-LLQLLTQGMGEDDLPSARIPSLRYAFVVGDA-----------LTRRHVARLYAVAPHitcvnlYG 794
Cdd:cd05906 256 IDRYRVTI-TWAPNfAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAvvaktirrllrLLEPYGLPPDAIRPA------FG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 795 STETQRAVSYfvlptASSTESPASVTALldkEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQ 874
Cdd:cd05906 329 MTETCSGVIY-----SRSFPTYDHSQAL---EFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 875 TNERFLvnpfthqeHDRLYRTGDLGrYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVAD---AAVIIREDTP 951
Cdd:cd05906 401 NAEAFT--------EDGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 952 DNKQ-IVAYITHHNEQVK--PVLSNLRAFVTQRL---PAFMVPahfVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05906 472 ETEElAIFFVPEYDLQDAlsETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
473-1016 |
8.28e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 114.31 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 473 SVLPDpgAPISAHWegTIHDLFAQQAHLRPENIAIIDEIN--TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAA 550
Cdd:PLN02246 12 SKLPD--IYIPNHL--PLHDYCFERLSEFSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 551 LVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARgwLRIEGATDCQELDEWCRANSYCNLVLARNFA----LSGILS 626
Cdd:PLN02246 88 FVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK--LIITQSCYVDKLKGLAEDDGVTVVTIDDPPEgclhFSELTQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 627 QYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRD----RFAFTQTDR----------YSLLSGLah 692
Cdd:PLN02246 166 ADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFHSDDVilcvlpmfhiYSLNSVL-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 693 dplqreiftpLC---VGATICIpdqehMG--DPGWLAQWMQGQEITIASFTPALLQLLTQG--MGEDDLPSARIpSLRYA 765
Cdd:PLN02246 244 ----------LCglrVGAAILI-----MPkfEIGALLELIQRHKVTIAPFVPPIVLAIAKSpvVEKYDLSSIRM-VLSGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 766 FVVGDALTRRHVARLyavaPHITCVNLYGSTETQRAVSYfvlptassteSPAsvtalLDKEVIPLGKGMPG-----AQIL 840
Cdd:PLN02246 308 APLGKELEDAFRAKL----PNAVLGQGYGMTEAGPVLAM----------CLA-----FAKEPFPVKSGSCGtvvrnAELK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 841 ILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHqehdrlyrTGDLGrYLPDGNAEF-AGRNDLQVK 918
Cdd:PLN02246 369 IVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLH--------TGDIG-YIDDDDELFiVDRLKELIK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 919 IRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHN------EQVKpvlsnlrAFVTQRLpAFMVPAHFV 992
Cdd:PLN02246 440 YKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNgseiteDEIK-------QFVAKQV-VFYKRIHKV 511
|
570 580
....*....|....*....|....*
gi 1574832895 993 -FMSRLPLNANGKVDRKALPAPEAA 1016
Cdd:PLN02246 512 fFVDSIPKAPSGKILRKDLRAKLAA 536
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
514-1010 |
9.99e-26 |
|
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: 112.57 E-value: 9.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 514 VSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARgwLRIE 593
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK--VAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 594 GAtdcqELDewcransycnlvlarnfalsgilsqyassapayrvgpnDIACLTFTSGSTGRPKGVLqrhgpLTHFLPWmr 673
Cdd:cd05935 80 GS----ELD--------------------------------------DLALIPYTSGTTGLPKGCM-----HTHFSAA-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 674 drFAFTQTDRYSLLSG----LAHDPL------QREIFTPLCVGATICIpdqehMG--DPGWLAQWMQGQEITIASFTPAL 741
Cdd:cd05935 111 --ANALQSAVWTGLTPsdviLACLPLfhvtgfVGSLNTAVYVGGTYVL-----MArwDRETALELIEKYKVTFWTNIPTM 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 742 LQLL--TQGMGEDDLPSARIpslryaFVVGDALTRRHVA-RLYAVAPhITCVNLYGSTETQravsyfvlptassteSPAS 818
Cdd:cd05935 184 LVDLlaTPEFKTRDLSSLKV------LTGGGAPMPPAVAeKLLKLTG-LRFVEGYGLTETM---------------SQTH 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 819 VTALLDKEVIPLGKGMPGAQILILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNErflvnPFTHQEHDRLYRTGD 897
Cdd:cd05935 242 TNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEE-----SFIEIKGRRFFRTGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 898 LGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNE-QVKPVLSNLRA 976
Cdd:cd05935 317 LGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyRGKVTEEDIIE 396
|
490 500 510
....*....|....*....|....*....|....
gi 1574832895 977 FVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05935 397 WAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
69-356 |
1.52e-25 |
|
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: 111.81 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 69 VDL--LEKCIHLLVRRHESLRTTFamL-NGEpiQVIRPNLTL-QIPLIDLTSLPEAEREASLQHAINNEAHIPFDLKTGP 144
Cdd:cd19535 37 LDPdrLERAWNKLIARHPMLRAVF--LdDGT--QQILPEVPWyGITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 145 L--VRLALLRKSplEHILLLNTHHIISDGWSLGVFLHELSLCYsaalAGNSPTLPAPSLQYADYAAWQRNwLKGENLTNL 222
Cdd:cd19535 113 LfdIRLSLLPEG--RTRLHLSIDLLVADALSLQILLRELAALY----EDPGEPLPPLELSFRDYLLAEQA-LRETAYERA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 223 LDYWRKQLADMP-----PLLELPMDHPRPAVQTSHGavvslLLPSEISTALKALSQHEGVTLFMTTLALFQILLQRYTGR 297
Cdd:cd19535 186 RAYWQERLPTLPpapqlPLAKDPEEIKEPRFTRREH-----RLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQ 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 298 RDIVIGTPIANRNRT--DIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMTLEAYAHQD 356
Cdd:cd19535 261 PRFLLNLTLFNRLPLhpDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSS 321
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
33-383 |
2.07e-25 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 111.57 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 33 FPLSFAQQrlWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLNGEPIQVIRPNLTLQIPL- 111
Cdd:cd19534 2 VPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 -IDLTSLPEAEReasLQHAInNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALA 190
Cdd:cd19534 80 vVDLSSLAQAAA---IEALA-AEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 191 GNSPTLPaPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPPllELPMDHPRPAvqtSHGAVVSLLLPSEISTAL-- 268
Cdd:cd19534 156 GEPIPLP-SKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYW--GLPKDPEQTY---GDARTVSFTLDEEETEALlq 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 269 ---KALsQHEGVTLFMTTLALfqiLLQRYTGRRDIVI---------GTPIANRNRTdiehvFGFFVNTLVLRIDVASELN 336
Cdd:cd19534 230 eanAAY-RTEINDLLLAALAL---AFQDWTGRAPPAIfleghgreeIDPGLDLSRT-----VGWFTSMYPVVLDLEASED 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1574832895 337 FRTLLQRVKEMtLEAYAHQDIPFDaLLDELNPER--SLSHSLLFQVFFN 383
Cdd:cd19534 301 LGDTLKRVKEQ-LRRIPNKGIGYG-ILRYLTPEGtkRLAFHPQPEISFN 347
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
493-1010 |
3.55e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 112.44 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 493 LFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGStvlILDP-- 570
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA---VWVPtn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 571 --SYPParllEYVQRAHARGWLRIEGATDCQELDEWCRANS-YCNLVLARNFALSG-----ILSQYA-SSAPAYRVGPND 641
Cdd:PRK07470 89 frQTPD----EVAYLAEASGARAMICHADFPEHAAAVRAASpDLTHVVAIGGARAGldyeaLVARHLgARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 642 IACLTFTSGSTGRPKGVLQRHGPLthflpwmrdrfAFTQTDRYS-LLSGLAHDplQREIFT-PLCVGA------------ 707
Cdd:PRK07470 165 PCWFFFTSGTTGRPKAAVLTHGQM-----------AFVITNHLAdLMPGTTEQ--DASLVVaPLSHGAgihqlcqvarga 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 708 -TICIPDQEHMGDPGW--LAQWmqgqEITIASFTPALLQLLTqgmgEDdlPSARipslRYafvvgDALTRRHVarLYAVA 784
Cdd:PRK07470 232 aTVLLPSERFDPAEVWalVERH----RVTNLFTVPTILKMLV----EH--PAVD----RY-----DHSSLRYV--IYAGA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 785 PhitcvnLYgSTETQRA--------VSYFVLP--TASSTESPASVTALLDKEVIPLGK-GMP--GAQILILNEAGNLAGI 851
Cdd:PRK07470 291 P------MY-RADQKRAlaklgkvlVQYFGLGevTGNITVLPPALHDAEDGPDARIGTcGFErtGMEVQIQDDEGRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 852 GELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGR-NDLQVKiRGYRIELEEIE 930
Cdd:PRK07470 364 GETGEICVIGPAVFAGYYNNPEANAKAF---------RDGWFRTGDLGHLDARGFLYITGRaSDMYIS-GGSNVYPREIE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 931 AILVEHPMVADAAVIireDTPDNKQ-------IVAyithhNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANG 1003
Cdd:PRK07470 434 EKLLTHPAVSEVAVL---GVPDPVWgevgvavCVA-----RDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYG 505
|
....*..
gi 1574832895 1004 KVDRKAL 1010
Cdd:PRK07470 506 KITKKMV 512
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
510-1012 |
4.62e-25 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 112.97 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 510 EINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGW 589
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 590 LRIEGATD-------CQELDEWCRAN-SYCNLVLARNFALSGILSQYASSAP----------AYRVGPNDIACLTFTSGS 651
Cdd:cd05968 168 ITADGFTRrgrevnlKEEADKACAQCpTVEKVVVVRHLGNDFTPAKGRDLSYdeeketagdgAERTESEDPLMIIYTSGT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 652 TGRPKGVLQRHG--PLTHFLPwMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICI----PDQEhmgDPGWLAQ 725
Cdd:cd05968 248 TGKPKGTVHVHAgfPLKAAQD-MYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgaPDHP---KADRLWR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 726 WMQGQEITIASFTPALLQLLtQGMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVA--PHITCVNLYGSTETQRAV- 802
Cdd:cd05968 324 MVEDHEITHLGLSPTLIRAL-KPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkGRNPIINYSGGTEISGGIl 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 803 -SYFVLPTAsstesPASVTALLdkeviplgkgmPGAQILILNEAGNLAgIGELGEIYVRSPHLAF--GYLDDPDQTNERF 879
Cdd:cd05968 403 gNVLIKPIK-----PSSFNGPV-----------PGMKADVLDESGKPA-RPEVGELVLLAPWPGMtrGFWRDEDRYLETY 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 880 LvnpfthQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAY 959
Cdd:cd05968 466 W------SRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCF 539
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 960 -ITHHNEQVKPVLSN-LRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPA 1012
Cdd:cd05968 540 vVLKPGVTPTEALAEeLMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
33-457 |
6.92e-25 |
|
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: 110.09 E-value: 6.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 33 FPLSFAQQRLWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFAMLN-GEPIQVIRPNLTLQIPL 111
Cdd:cd19547 2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 112 IDLTSLPEAEREASLQHAINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTHHIISDGWSLGVFLHELSLCYSAALAG 191
Cdd:cd19547 82 LDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 192 NSPTLpAPSLQYADYAAWQR-NWLKGENLTNlldYWRKQLADMPPlleLPMDHPrPAVQTSHGAVVSLLLPSEISTALKA 270
Cdd:cd19547 162 REPQL-SPCRPYRDYVRWIRaRTAQSEESER---FWREYLRDLTP---SPFSTA-PADREGEFDTVVHEFPEQLTRLVNE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 271 LSQHEGVTLFMTTLALFQILLQRYTGRRDIVIGTPIANR--NRTDIEHVFGFFVNTLVLRIDVASELNFRTLLQRVKEMT 348
Cdd:cd19547 234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 349 LEAYAHQDIPFDALLDELNPERsLSHSLLFQVFFNMVNLPDlhDEWPD----LKVEHLWPREiGSKFDLTLFVQEEQDaI 424
Cdd:cd19547 314 ATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPE--DNLPGddlsIQIIDLHAQE-KTEYPIGLIVLPLQK-L 388
|
410 420 430
....*....|....*....|....*....|...
gi 1574832895 425 RLELVYNTDLFKHERMLEMLEQYSCLASQVSER 457
Cdd:cd19547 389 AFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRR 421
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1173-1459 |
7.74e-25 |
|
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: 109.88 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1173 FELDGQ-FQPAAFEESLNDLLARHESLRTSFVLQGEQlmqRIHAQL-WLSLSQQHLSL--PAESESSLsqqalqawlqQE 1248
Cdd:cd19535 30 LEFDGEdLDPDRLERAWNKLIARHPMLRAVFLDDGTQ---QILPEVpWYGITVHDLRGlsEEEAEAAL----------EE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1249 IR-----RPFDLQQAPL--LRASLLHRGsePSILLLCLHHIIADGWSLGILLQELSLCYNAHVKgispQLAPLPLQYADY 1321
Cdd:cd19535 97 LRerlshRVLDVERGPLfdIRLSLLPEG--RTRLHLSIDLLVADALSLQILLRELAALYEDPGE----PLPPLELSFRDY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1322 AVWQRAwLQEERQEKLQRYWHGQLATAPALLDLPT-------DHPRppiqtFVgaRHQLHLPAELLEQLMVLSHQQQVTL 1394
Cdd:cd19535 171 LLAEQA-LRETAYERARAYWQERLPTLPPAPQLPLakdpeeiKEPR-----FT--RREHRLSAEQWQRLKERARQHGVTP 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 1395 YMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQRR--ELEGVIGLFANTLVLRTDLSGDPSFLELLQRV 1459
Cdd:cd19535 243 SMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLhpDVNDVVGDFTSLLLLEVDGSEGQSFLERARRL 309
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
498-1010 |
1.10e-24 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 109.96 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 498 AHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSyPPARL 577
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQ-LPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 578 LEYVQRAhargwLRIEGATDCQELDEWcransycnlvlarnFALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKG 657
Cdd:PRK09029 92 LEELLPS-----LTLDFALVLEGENTF--------------SALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 658 VLqrHGPLTHF------LPWMrdrfAFTQTDRYsLLS-GLAHDPLQREIFTPLCVGATICIPDQEHmgdpgwLAQWMQGq 730
Cdd:PRK09029 153 AV--HTAQAHLasaegvLSLM----PFTAQDSW-LLSlPLFHVSGQGIVWRWLYAGATLVVRDKQP------LEQALAG- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 731 eITIASFTPALLQLLtqgmgeddLPSARIPSLRYAFVVGDA-----LTRRhvarlyAVAPHITCVNLYGSTEtqravsyf 805
Cdd:PRK09029 219 -CTHASLVPTQLWRL--------LDNRSEPLSLKAVLLGGAaipveLTEQ------AEQQGIRCWCGYGLTE-------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 806 vlptASSTespasVTAlldKEVIPL---GKGMPGAQILILNeagnlagigelGEIYVRSPHLAFGYLDDPdqtnerfLVN 882
Cdd:PRK09029 276 ----MAST-----VCA---KRADGLagvGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQG-------QLV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 883 PFTHQehDRLYRTGDLGRyLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITH 962
Cdd:PRK09029 326 PLVND--EGWFATRDRGE-WQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVES 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 963 HNEQvkpVLSNLRAFVTQRLPAFMVPAHFVfmsRLP---LNANGKVDRKAL 1010
Cdd:PRK09029 403 DSEA---AVVNLAEWLQDKLARFQQPVAYY---LLPpelKNGGIKISRQAL 447
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
491-1010 |
1.89e-24 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 110.28 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 491 HDLFAQQAHLRPENIAII-----DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTV 565
Cdd:cd05970 20 YDVVDAMAKEYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 566 lILDPSYPPARLLEY-VQRAHARGWL---------RIEGA-TDC-----------QELDEWCRANSYCNlvlarnfALSG 623
Cdd:cd05970 100 -IPATHQLTAKDIVYrIESADIKMIVaiaednipeEIEKAaPECpskpklvwvgdPVPEGWIDFRKLIK-------NASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 624 ILSQyaSSAPAYRVGpNDIACLTFTSGSTGRPKGVLQRHG-PLTHFLPWM------RDRFAFTQTDrysllSGLAhDPLQ 696
Cdd:cd05970 172 DFER--PTANSYPCG-EDILLVYFSSGTTGMPKMVEHDFTyPLGHIVTAKywqnvrEGGLHLTVAD-----TGWG-KAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 697 REIFTPLCVGATICIPDQEhMGDPGWLAQWMQGQEITIASFTPALLQLLTQgmgeDDLPSARIPSLRYAFVVGDALTRrH 776
Cdd:cd05970 243 GKIYGQWIAGAAVFVYDYD-KFDPKALLEKLSKYGVTTFCAPPTIYRFLIR----EDLSRYDLSSLRYCTTAGEALNP-E 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 777 VARLYAVAPHITCVNLYGSTETQRAVSYFVLPTASstesPASvtalldkevipLGKGMPGAQILILNEAGNLAGIGELGE 856
Cdd:cd05970 317 VFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPK----PGS-----------MGKPAPGYEIDLIDREGRSCEAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 857 IYVRS----PHLAF-GYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEA 931
Cdd:cd05970 382 IVIRTskgkPVGLFgGYYKDAEKTAEVW---------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVES 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 932 ILVEHPMVADAAVIIREDtPDNKQIVAYITHHNEQVKP--VLSN-LRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRK 1008
Cdd:cd05970 453 ALIQHPAVLECAVTGVPD-PIRGQVVKATIVLAKGYEPseELKKeLQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRV 531
|
..
gi 1574832895 1009 AL 1010
Cdd:cd05970 532 EI 533
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
639-1010 |
3.49e-24 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 108.96 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDR----------YSLLSGLahdplqreiFTPLCVGAT 708
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVvfgalpffhsFGLTGCL---------WLPLLSGIK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 709 I-CIPDQEHmgdPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLpsariPSLRYAFVVGDALtRRHVARLYAVAPHI 787
Cdd:cd05909 217 VvFHPNPLD---YKKIPELIYDKKATILLGTPTFLRGYARAAHPEDF-----SSLRLVVAGAEKL-KDTLRQEFQEKFGI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 788 TCVNLYGSTETQRAVSyfvLPTASSTESPASVtalldkeviplGKGMPGAQILILNEAGNL-AGIGELGEIYVRSPHLAF 866
Cdd:cd05909 288 RILEGYGTTECSPVIS---VNTPQSPNKEGTV-----------GRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVML 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 867 GYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEH-PMVADAAVI 945
Cdd:cd05909 354 GYLNEPELTSFAF---------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVV 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 946 IREDTPDNKQIVAYITHHNEQVkpvlSNLRAFVTQ-RLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05909 425 SVPDGRKGEKIVLLTTTTDTDP----SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1624-1850 |
6.46e-24 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 108.06 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:PRK04813 18 FPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLLLTHEELKARwpHCPCPLLCLDTLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSL 1783
Cdd:PRK04813 98 AKPSLIIATEELPLE--ILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 1784 QSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATP 1850
Cdd:PRK04813 176 LEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTP 242
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1609-1890 |
7.98e-24 |
|
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: 107.95 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1609 GLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPL 1688
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1689 DPDYPSQRLLWMAQDAQLSLLLTHEE----LKARWPHCP--CPLLCLDTLQERYASLPCE---DLQEA-----------C 1748
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSErldlLHPALPGCHdlRTLIIVGDPAHASEGHPGEepaSWPKLlalgdadpphpV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1749 SPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDiAGL-ELYLPLLAGAQIQLasqEQ 1827
Cdd:TIGR03098 161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFD-YGFnQLTTAFYVGATVVL---HD 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1828 ASDPRQLASLLAQLPISILQATPTTWQLLLETGWSGKAGLTLL----SGAK--PSLLISLAACCPVAKP 1890
Cdd:TIGR03098 237 YLLPRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRyltnSGGAmpRATLSRLRSFLPNARL 305
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
641-1007 |
1.24e-23 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 104.27 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLQRHGPL----THFLPWMRdrfaFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEh 716
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLiaanLQLIHAMG----LTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 717 mgDPGWLAQWMQGQEIT-IASFTPALLQLLTQgmgEDDLPSArIPSLRYafVVG----DALTRRHV---ARLYAvaphit 788
Cdd:cd17637 76 --DPAEALELIEEEKVTlMGSFPPILSNLLDA---AEKSGVD-LSSLRH--VLGldapETIQRFEEttgATFWS------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 789 cvnLYGSTETQRAVSYfvlptASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGY 868
Cdd:cd17637 142 ---LYGQTETSGLVTL-----SPYRERPGSA-----------GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 869 LDDPDQTNERFLvNPFTHqehdrlyrTGDLGRYLPDGNAEFAGRN---DLqVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:cd17637 203 WNLPELTAYTFR-NGWHH--------TGDLGRFDEDGYLWYAGRKpekEL-IKPGGENVYPAEVEKVILEHPAIAEVCVI 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 946 ireDTPDNKqivayithHNEQVKPVLS----------NLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:cd17637 273 ---GVPDPK--------WGEGIKAVCVlkpgatltadELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
469-1010 |
1.25e-23 |
|
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: 108.42 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 469 TRASSVLPDPGAPISAHW--EGTI---HDLFAQQAHLRPENIAII------DEINTVSYGELEARSNQLAHYLHAQGIRP 537
Cdd:cd05966 29 KPWDKVLDWSKGPPFIKWfeGGKLnisYNCLDRHLKERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSLGVKK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 538 HDVVAISAQRCAALVLAILG-----------------------ILKAGSTVLI-LDPSY---PPARLLEYVQRAhargwl 590
Cdd:cd05966 109 GDRVAIYMPMIPELVIAMLAcarigavhsvvfagfsaesladrINDAQCKLVItADGGYrggKVIPLKEIVDEA------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 591 rIEGATDCQELDEWCRANSYCNLVLARNFALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRH-GPLTHFL 669
Cdd:cd05966 183 -LEKCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTgGYLLYAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 670 PWMRDRFAFTQTDRY------------SLLsglahdplqreIFTPLCVGATICI----PDQEhmgDPGWLAQWMQGQEIT 733
Cdd:cd05966 262 TTFKYVFDYHPDDIYwctadigwitghSYI-----------VYGPLANGATTVMfegtPTYP---DPGRYWDIVEKHKVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 734 IASFTPALLQLLtQGMGEDDLPSARIPSLRYAFVVGDALT-------RRHVARlyavaPHITCVNLYGSTETQravSYFV 806
Cdd:cd05966 328 IFYTAPTAIRAL-MKFGDEWVKKHDLSSLRVLGSVGEPINpeawmwyYEVIGK-----ERCPIVDTWWQTETG---GIMI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 807 LPTASSTES-PASVTalldkevIPLgkgmPGAQILILNEAGNLAGIGELGEIYVRS--PHLAFGYLDDPdqtnERFLVNP 883
Cdd:cd05966 399 TPLPGATPLkPGSAT-------RPF----FGIEPAILDEEGNEVEGEVEGYLVIKRpwPGMARTIYGDH----ERYEDTY 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 884 FTHQEHdrLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIT-H 962
Cdd:cd05966 464 FSKFPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlK 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1574832895 963 HNEQVKPVLSN-LRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05966 542 DGEEPSDELRKeLRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
513-1004 |
1.77e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 106.91 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAI-------------SAQRCAALVLAILGILKA----------GSTVLILD 569
Cdd:PRK08276 11 VVTYGELEARSNRLAHGLRALGLREGDVVAIllennpeffevywAARRSGLYYTPINWHLTAaeiayivddsGAKVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 570 PSY-PPARLLEYVQRAHARGWLRIEGATD-CQELDEWcransycnlvlarnfalsgiLSQYASSAPAYRVGPNDIAcltF 647
Cdd:PRK08276 91 AALaDTAAELAAELPAGVPLLLVVAGPVPgFRSYEEA--------------------LAAQPDTPIADETAGADML---Y 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 648 TSGSTGRPKGVLQrhgPLTHFLP--------WMRDRFAFTQTD-RYSLLSGLAHD-PLQREIFTPLCVGATICIP--DQE 715
Cdd:PRK08276 148 SSGTTGRPKGIKR---PLPGLDPdeapgmmlALLGFGMYGGPDsVYLSPAPLYHTaPLRFGMSALALGGTVVVMEkfDAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 716 HMgdpgwLAQwMQGQEITIASFTPALL-QLLTqgmgeddLPsariPSLRYAFvvgDALTRRHVArlYAVAP---HIT--- 788
Cdd:PRK08276 225 EA-----LAL-IERYRVTHSQLVPTMFvRMLK-------LP----EEVRARY---DVSSLRVAI--HAAAPcpvEVKram 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 789 ------CVN-LYGSTETQRAvsyfvlpTASSTES----PASVtalldkeviplGKGMPGaQILILNEAGNLAGIGELGEI 857
Cdd:PRK08276 283 idwwgpIIHeYYASSEGGGV-------TVITSEDwlahPGSV-----------GKAVLG-EVRILDEDGNELPPGEIGTV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 858 YVRSPHLAFGYLDDPDQTNErflvnpfthQEHDRLYRT-GDLGrYL-PDGNAEFAGRNDLQVKIRGYRIELEEIEAILVE 935
Cdd:PRK08276 344 YFEMDGYPFEYHNDPEKTAA---------ARNPHGWVTvGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVT 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 936 HPMVADAAVIireDTPDNKqivayithHNEQVKPVL-------------SNLRAFVTQRLPAFMVPAHFVFMSRLPLNAN 1002
Cdd:PRK08276 414 HPKVADVAVF---GVPDEE--------MGERVKAVVqpadgadagdalaAELIAWLRGRLAHYKCPRSIDFEDELPRTPT 482
|
..
gi 1574832895 1003 GK 1004
Cdd:PRK08276 483 GK 484
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
514-945 |
2.06e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 105.73 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 514 VSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAhargwlrie 593
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 594 GATDCQeLDEWCRANsycnlvlarnfalsgilsqyassapayrvgpnDIACLTFTSGSTGRPKGVLQRHG--PLTHF--L 669
Cdd:cd05974 72 GAVYAA-VDENTHAD--------------------------------DPMLLYFTSGTTSKPKLVEHTHRsyPVGHLstM 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 670 PWMRDRFAFTQTDRYSllSGLAHDPLQrEIFTPLCVGATICIPDQEHMgDPGWLAQWMQGQEITIASFTPALLQLLTQgm 749
Cdd:cd05974 119 YWIGLKPGDVHWNISS--PGWAKHAWS-CFFAPWNAGATVFLFNYARF-DAKRVLAALVRYGVTTLCAPPTVWRMLIQ-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 750 geDDLPSARIPsLRYAFVVGDALTRRHVARLYAvAPHITCVNLYGSTETqravsyfvlpTASSTESPASVTalldkEVIP 829
Cdd:cd05974 193 --QDLASFDVK-LREVVGAGEPLNPEVIEQVRR-AWGLTIRDGYGQTET----------TALVGNSPGQPV-----KAGS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 830 LGKGMPGAQILILNEAGNLAGIGELGEIY--VRSPHLAFGYLDDPDQTnerflvnpfTHQEHDRLYRTGDLGRYLPDGNA 907
Cdd:cd05974 254 MGRPLPGYRVALLDPDGAPATEGEVALDLgdTRPVGLMKGYAGDPDKT---------AHAMRGGYYRTGDIAMRDEDGYL 324
|
410 420 430
....*....|....*....|....*....|....*...
gi 1574832895 908 EFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:cd05974 325 TYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVV 362
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
485-1028 |
3.72e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.40 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 485 HWEGTIhdlfAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGST 564
Cdd:PRK07786 18 NWVNQL----ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 565 VLILDPSYPPARLLEYVQRAHARGWLrIEG-----ATDCQELDEwcranSYCNLVLARNFALSGILS---QYASSAPAYR 636
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVV-TEAalapvATAVRDIVP-----LLSTVVVAGGSSDDSVLGyedLLAEAGPAHA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 637 VG--PNDIACLT-FTSGSTGRPKGVLQRHGPLT-HFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICI- 711
Cdd:PRK07786 168 PVdiPNDSPALImYTSGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIy 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 PdqehMG--DPGWLAQWMQGQEITIASFTPALLQLLTqgmgEDDLPSARIPSLRY----AFVVGDALTRRhvarLYAVAP 785
Cdd:PRK07786 248 P----LGafDPGQLLDVLEAEKVTGIFLVPAQWQAVC----AEQQARPRDLALRVlswgAAPASDTLLRQ----MAATFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 786 HITCVNLYGSTETqravsyfvlptassteSPasVTALLD-KEVI----PLGKGMPGAQILILNEAGNLAGIGELGEIYVR 860
Cdd:PRK07786 316 EAQILAAFGQTEM----------------SP--VTCMLLgEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 861 SPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVA 940
Cdd:PRK07786 378 APTLMSGYWNNPEATAEAF---------AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 941 DAAVIIREDTPDNKQIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVD----RKALPAPEAA 1016
Cdd:PRK07786 449 EVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNV 528
|
570
....*....|..
gi 1574832895 1017 DEATLSLATPQS 1028
Cdd:PRK07786 529 ERRSASAGFTER 540
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1612-1857 |
5.45e-23 |
|
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: 105.23 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1612 HLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPD 1691
Cdd:TIGR01734 4 EAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1692 YPSQRLLWMAQDAQLSLLLTHEELKARWPHCPcpLLCLDTLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQI 1771
Cdd:TIGR01734 84 IPSERIEMIIEAAGPELVIHTAELSIDAVGTQ--IITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1772 SHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPT 1851
Cdd:TIGR01734 162 SHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPS 241
|
....*.
gi 1574832895 1852 TWQLLL 1857
Cdd:TIGR01734 242 FVDMCL 247
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
502-1005 |
9.33e-23 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 104.30 E-value: 9.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 502 PENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGStVLI-----LDpsyppAR 576
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGA-VLNalntrLD-----AE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 577 LLEYVQRaHARgwlriegatdcqeldewCRAnsycnLVLARNFALSGILSQYASSAPAYRvgPND----IAcLTFTSGST 652
Cdd:cd12118 92 EIAFILR-HSE-----------------AKV-----LFVDREFEYEDLLAEGDPDFEWIP--PADewdpIA-LNYTSGTT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 653 GRPKGVLQRHgplthflpwmrdRFAFTQTDRYSLLSGLAHDPL---QREIF---------TPLCVGAT-ICIPDQehmgD 719
Cdd:cd12118 146 GRPKGVVYHH------------RGAYLNALANILEWEMKQHPVylwTLPMFhcngwcfpwTVAAVGGTnVCLRKV----D 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 720 PGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPsarIPSLRYAFVVGDALTRRHVARLYAVAPHITCVnlYGSTETQ 799
Cdd:cd12118 210 AKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARP---LPHRVHVMTAGAPPPAAVLAKMEELGFDVTHV--YGLTETY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 800 RAVSYFVLPTASSTESPASVTALLDKEVIPLgKGMPGAQILILNEAGNLAGIGE-LGEIYVRSPHLAFGYLDDPDQTNER 878
Cdd:cd12118 285 GPATVCAWKPEWDELPTEERARLKARQGVRY-VGLEEVDVLDPETMKPVPRDGKtIGEIVFRGNIVMKGYLKNPEATAEA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 879 FlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIRedtPDNK---Q 955
Cdd:cd12118 364 F---------RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVAR---PDEKwgeV 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1574832895 956 IVAYITHHnEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSrLPLNANGKV 1005
Cdd:cd12118 432 PCAFVELK-EGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1151-1574 |
1.02e-22 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 103.55 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1151 QERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQG-EQLMQRIHAQL---WLSL--SQQ 1224
Cdd:cd19547 8 QEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLappWALLdwSGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1225 HLSLPAESESSLSQQALQAWlqqeirrpFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHV 1304
Cdd:cd19547 88 DPDRRAELLERLLADDRAAG--------LSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1305 KGISPQLAPLPlQYADYAVWQRAwlQEERQEKLQRYWHGQLA--TAPALLDLPTDHPrppiQTFVGARHQlhLPAELLEQ 1382
Cdd:cd19547 160 HGREPQLSPCR-PYRDYVRWIRA--RTAQSEESERFWREYLRdlTPSPFSTAPADRE----GEFDTVVHE--FPEQLTRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1383 LMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVVGTPIAGRQrRELEG---VIGLFANTLVLRTDLSGDPSFLELLQRV 1459
Cdd:cd19547 231 VNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PELEGsehMVGIFINTIPLRIRLDPDQTVTGLLETI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1460 REVTLQAYSQQDMPFEKLVAELQPERsLAYNPLFQVFFALQNVPGDPISLEGLDVTQIRLDSNSaKFDLSWTWYQEDEKS 1539
Cdd:cd19547 310 HRDLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLHAQE-KTEYPIGLIVLPLQK 387
|
410 420 430
....*....|....*....|....*....|....*
gi 1574832895 1540 LSAVIEYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19547 388 LAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
501-1010 |
1.42e-22 |
|
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: 105.09 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 501 RPENIAII------DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGST---------- 564
Cdd:cd05967 64 RGDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsvvfggfaa 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 565 ------------VLILDPSY--PPARLLEYVQRAHARGWLRIEGATDCQELDewcRANSYCNLV-LARNFALSGILSQyA 629
Cdd:cd05967 144 kelasriddakpKLIVTASCgiEPGKVVPYKPLLDKALELSGHKPHHVLVLN---RPQVPADLTkPGRDLDWSELLAK-A 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 630 SSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPW-MRDRFAFTQTDRYSLLSGLA----HdplQREIFTPLC 704
Cdd:cd05967 220 EPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWsMRNIYGIKPGDVWWAASDVGwvvgH---SYIVYGPLL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 VGATICIPDQEHMG--DPGwlAQWMQGQEITIAS-FT-P-ALLQLLTQGMGEDDLPSARIPSLRYAFVVG---DALTRRH 776
Cdd:cd05967 297 HGATTVLYEGKPVGtpDPG--AFWRVIEKYQVNAlFTaPtAIRAIRKEDPDGKYIKKYDLSSLRTLFLAGerlDPPTLEW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 777 VARLYAVaPHItcvNLYGSTETQRAVSyfvlptasstespASVTALLDKEVIP--LGKGMPGAQILILNEAGNLAGIGEL 854
Cdd:cd05967 375 AENTLGV-PVI---DHWWQTETGWPIT-------------ANPVGLEPLPIKAgsPGKPVPGYQVQVLDEDGEPVGPNEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 855 GEIYVRSPhLAFGYLDDPDQTNERFLVNPFthQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILV 934
Cdd:cd05967 438 GNIVIKLP-LPPGCLLTLWKNDERFKKLYL--SKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 935 EHPMVADAAVI-IREDTPDNKQIVAYI--THHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05967 515 SHPAVAECAVVgVRDELKGQVPLGLVVlkEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
513-945 |
1.51e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 103.31 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLRI 592
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 EGAtdcqeldewcransycnlvlarnfalsgilsqyassapayrvgpNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWM 672
Cdd:cd05910 82 PKA--------------------------------------------DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 673 RDRFAFTQTDRysllsGLAHDPLqREIFTPLcVGATICIPDQEHM----GDPGWLAQWMQGQEITIASFTPALLQLLTQG 748
Cdd:cd05910 118 RQLYGIRPGEV-----DLATFPL-FALFGPA-LGLTSVIPDMDPTrparADPQKLVGAIRQYGVSIVFGSPALLERVARY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 749 MGEDDLPsarIPSLRYAFVVGDALTRRHVARLY-AVAPHITCVNLYGSTETqravsyfvLPTAS--STESPASVTALLDK 825
Cdd:cd05910 191 CAQHGIT---LPSLRRVLSAGAPVPIALAARLRkMLSDEAEILTPYGATEA--------LPVSSigSRELLATTTAATSG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 826 EV-IPLGKGMPGAQILILneAGNLAGI-----------GELGEIYVRSPHLAFGYLDDPDQTNerflvnpfTHQEHDR-- 891
Cdd:cd05910 260 GAgTCVGRPIPGVRVRII--EIDDEPIaewddtlelprGEIGEITVTGPTVTPTYVNRPVATA--------LAKIDDNse 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 892 --LYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:cd05910 330 gfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
484-1025 |
1.53e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 104.32 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 484 AHWEGTIHDLFAQQAHLRPENIAI--IDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKA 561
Cdd:PRK05857 10 PQLPSTVLDRVFEQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 562 GSTVLILDPSYPPARLLEYVQRAHARGWLRIE----GATDCQELDEWCRANSYCNLVLARNFALSGILSqYASSAPAYrv 637
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERFCQITDPAAALVAPgskmASSAVPEALHSIPVIAVDIAAVTRESEHSLDAA-SLAGNADQ-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 638 GPNDIACLTFTSGSTGRPKGVLqrhgplthfLPwMRDRFAFTQTDRYSLLSGL-------AHDPLQRE-------IFTPL 703
Cdd:PRK05857 167 GSEDPLAMIFTSGTTGEPKAVL---------LA-NRTFFAVPDILQKEGLNWVtwvvgetTYSPLPAThigglwwILTCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 704 CVGAtICIPDQEHMGDpgwLAQWMQGQEITIASFTPALLQLLtqgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAV 783
Cdd:PRK05857 237 MHGG-LCVTGGENTTS---LLEILTTNAVATTCLVPTLLSKL---VSELKSANATVPSLRLVGYGGSRAIAADVRFIEAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 784 AphITCVNLYGSTETqrAVSYFVLPTASSTESPASVTAlldkevipLGKGMPGAQILILNEAG---NLAGIGE---LGEI 857
Cdd:PRK05857 310 G--VRTAQVYGLSET--GCTALCLPTDDGSIVKIEAGA--------VGRPYPGVDVYLAATDGigpTAPGAGPsasFGTL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 858 YVRSPHLAFGYLDDPDQTNERFLvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHP 937
Cdd:PRK05857 378 WIKSPANMLGYWNNPERTAEVLI---------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 938 MVADAAVIireDTPDNK------QIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMV-PAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK05857 449 GVREAACY---EIPDEEfgalvgLAVVASAELDESAARALKHTIAARFRRESEPMArPSTIVIVTDIPRTQSGKVMRASL 525
|
570
....*....|....*
gi 1574832895 1011 PApeAADEATLSLAT 1025
Cdd:PRK05857 526 AA--AATADKARVVV 538
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
493-1010 |
2.15e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 103.42 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 493 LFAqqAHLRPENIAI-IDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPS 571
Cdd:PRK07514 9 LRA--AFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 572 YPPARlLEY----------VQRAHARGWLR----IEGATDCQELDEwcransycnlvlarnfALSGILSQYASSAPA--- 634
Cdd:PRK07514 87 YTLAE-LDYfigdaepalvVCDPANFAWLSkiaaAAGAPHVETLDA----------------DGTGSLLEAAAAAPDdfe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 635 -YRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRysLLSGLahdPlqreIF----------TPL 703
Cdd:PRK07514 150 tVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDV--LIHAL---P----IFhthglfvatnVAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 704 CVGATIcipdqehmgdpgwlaqwmqgqeITIASFTP-ALLQLLTQG---MGeddlpsarIPSLRYAFVVGDALTRRHVA- 778
Cdd:PRK07514 221 LAGASM----------------------IFLPKFDPdAVLALMPRAtvmMG--------VPTFYTRLLQEPRLTREAAAh 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 779 -RLY--AVAP--------------HiTCVNLYGSTEtqravsyfvlpTASSTESPasvtalLDKEVIP--LGKGMPGAQI 839
Cdd:PRK07514 271 mRLFisGSAPllaethrefqertgH-AILERYGMTE-----------TNMNTSNP------YDGERRAgtVGFPLPGVSL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 840 LILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFthqehdrlYRTGDLGRYLPDGNAEFAGRN-DLqV 917
Cdd:PRK07514 333 RVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF--------FITGDLGKIDERGYVHIVGRGkDL-I 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 918 KIRGYRIELEEIEAILVEHPMVADAAViIREDTPDNKQIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRL 997
Cdd:PRK07514 404 ISGGYNVYPKEVEGEIDELPGVVESAV-IGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDEL 482
|
570
....*....|...
gi 1574832895 998 PLNANGKVDRKAL 1010
Cdd:PRK07514 483 PRNTMGKVQKNLL 495
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
514-1010 |
2.17e-22 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 103.95 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 514 VSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPaRLLEYvQrahargwLRIE 593
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTP-RELEH-Q-------LKDS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 594 GATdcqeldewcransycNLVLARNFA-------------------------LSGILSQY----------ASSAPAYR-- 636
Cdd:PRK07059 120 GAE---------------AIVVLENFAttvqqvlaktavkhvvvasmgdllgFKGHIVNFvvrrvkkmvpAWSLPGHVrf 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 637 ----------------VGPNDIACLTFTSGSTGRPKG-----------VLQRHGplthflpWMRDrfAFTQTDRYSLLSG 689
Cdd:PRK07059 185 ndalaegarqtfkpvkLGPDDVAFLQYTGGTTGVSKGatllhrnivanVLQMEA-------WLQP--AFEKKPRPDQLNF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 690 LAHDPLQrEIFTpLCV---------GATICIPDQEHMgdPGWLAQWMQGQeitIASFtPALLQLLTQGMGEDDLPSARIP 760
Cdd:PRK07059 256 VCALPLY-HIFA-LTVcgllgmrtgGRNILIPNPRDI--PGFIKELKKYQ---VHIF-PAVNTLYNALLNNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 761 SLRYAFVVGDALtRRHVARLYAVAPHITCVNLYGSTETQravsyfvlPTAssTESPASVTALLDKEVIPLgkgmPGAQIL 840
Cdd:PRK07059 328 KLIVANGGGMAV-QRPVAERWLEMTGCPITEGYGLSETS--------PVA--TCNPVDATEFSGTIGLPL----PSTEVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 841 ILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFthqehdrlYRTGDLGRYLPDGNAEFAGRNDLQVKIR 920
Cdd:PRK07059 393 IRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF--------FRTGDVGVMDERGYTKIVDRKKDMILVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 921 GYRIELEEIEAILVEHPMVADAAVIireDTPDnkqivayiTHHNEQVK-------PVLS--NLRAFVTQRLPAFMVPAHF 991
Cdd:PRK07059 465 GFNVYPNEIEEVVASHPGVLEVAAV---GVPD--------EHSGEAVKlfvvkkdPALTeeDVKAFCKERLTNYKRPKFV 533
|
570
....*....|....*....
gi 1574832895 992 VFMSRLPLNANGKVDRKAL 1010
Cdd:PRK07059 534 EFRTELPKTNVGKILRREL 552
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
513-1008 |
4.80e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 103.16 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHAR---GW 589
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARvaiVW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 590 LRIegATDCQELdewcRANSYCNLVLARN----------FALSGIL-----SQYASSAPA-------------------- 634
Cdd:PRK05605 137 DKV--APTVERL----RRTTPLETIVSVNmiaampllqrLALRLPIpalrkARAALTGPApgtvpwetlvdaaiggdgsd 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 635 ---YRVGPNDIACLTFTSGSTGRPKGVLQRHGPLT-------HFLPWMRDrfaftQTDRYsllsgLAHDPLqreiFTplC 704
Cdd:PRK05605 211 vshPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFanaaqgkAWVPGLGD-----GPERV-----LAALPM----FH--A 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 VGATICIPDQEHMG---------DPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPsarIPSLRYAFVVGDALTRR 775
Cdd:PRK05605 275 YGLTLCLTLAVSIGgelvllpapDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVD---LSGVRNAFSGAMALPVS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 776 HVARLYAVaphiTCVNL---YGSTETqravSYFVL--PtASSTESPASVTalldkevIPLgkgmPGAQILILNEAgNLA- 849
Cdd:PRK05605 352 TVELWEKL----TGGLLvegYGLTET----SPIIVgnP-MSDDRRPGYVG-------VPF----PDTEVRIVDPE-DPDe 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 850 --GIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELE 927
Cdd:PRK05605 411 tmPDGEEGELLVRGPQVFKGYWNRPEETAKSF---------LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 928 EIEAILVEHPMVADAAV--IIREDTPDNkqIVAYITHHN-EQVKPvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGK 1004
Cdd:PRK05605 482 EVEEVLREHPGVEDAAVvgLPREDGSEE--VVAAVVLEPgAALDP--EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGK 557
|
....
gi 1574832895 1005 VDRK 1008
Cdd:PRK05605 558 VRRR 561
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
641-1007 |
6.03e-22 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 99.64 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLQRHGPL-THFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGD 719
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 720 PgwLAQWMQGQEITIASFTPALLQLLTQgMGEDDLpsARIPSLRYaFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQ 799
Cdd:cd17635 82 S--LFKILTTNAVTTTCLVPTLLSKLVS-ELKSAN--ATVPSLRL-IGYGGSRAIAADVRFIEATGLTNTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 800 RAVsyfVLPTASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERF 879
Cdd:cd17635 156 TAL---CLPTDDDSIEINAV-----------GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 880 LvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAViirEDTPDN---KQI 956
Cdd:cd17635 222 I---------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAC---YEISDEefgELV 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 957 VAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:cd17635 290 GLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
513-1010 |
6.17e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 102.59 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQ-GIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARG--W 589
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAlvY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 590 LRIEGA--------TDCQELDEwcrANSYCNLVLARNFALSGILSQYASSAPAYR-----------------------VG 638
Cdd:PRK12492 129 LNMFGKlvqevlpdTGIEYLIE---AKMGDLLPAAKGWLVNTVVDKVKKMVPAYHlpqavpfkqalrqgrglslkpvpVG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSG-----LAHDPLQR-EIFTPLCV------G 706
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEgqevmIAPLPLYHiYAFTANCMcmmvsgN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 707 ATICIPDQEHMgdPGWLaqwmqgQEITIASFTpALLQLLT---QGMGEDDLPSARIPSLRYAFVVGDALTRRhVARLYAV 783
Cdd:PRK12492 286 HNVLITNPRDI--PGFI------KELGKWRFS-ALLGLNTlfvALMDHPGFKDLDFSALKLTNSGGTALVKA-TAERWEQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 784 APHITCVNLYGSTETQravsyfvlPTASSteSPASVTALLDKEVIPLgkgmPGAQILILNEAGNLAGIGELGEIYVRSPH 863
Cdd:PRK12492 356 LTGCTIVEGYGLTETS--------PVAST--NPYGELARLGTVGIPV----PGTALKVIDDDGNELPLGERGELCIKGPQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 864 LAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAA 943
Cdd:PRK12492 422 VMKGYWQQPEATAEAL--------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCA 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 944 VIireDTPDNKQivayithhNEQVK-------PVLS--NLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK12492 494 AI---GVPDERS--------GEAVKlfvvardPGLSveELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
515-1010 |
6.25e-22 |
|
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: 102.16 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEARSNQLAHYL-HAQGIRPHDVVAISAQRCAALVLAILGILKAGsTVLILDPSYPPARLLEY-VQRAHARGWLRI 592
Cdd:cd05928 43 SFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTG-LVFIPGTIQLTAKDILYrLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 EG--------ATDCQELDewcransyCNLVLARN-----FALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVL 659
Cdd:cd05928 122 DElapevdsvASECPSLK--------TKLLVSEKsrdgwLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 660 QRHGPLTH-FLPWMRDRFAFTQTDRYSLLS--GLAHDPLQrEIFTPLCVGATICIpdqEHMG--DPGWLAQWMQGQEITI 734
Cdd:cd05928 194 HSHSSLGLgLKVNGRYWLDLTASDIMWNTSdtGWIKSAWS-SLFEPWIQGACVFV---HHLPrfDPLVILKTLSSYPITT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 735 ASFTPALLQLLTQgmgeDDLPSARIPSLRYAFVVGDALTRRHVARLyavaPHITCVNL---YGSTETqravsyfVLPTAS 811
Cdd:cd05928 270 FCGAPTVYRMLVQ----QDLSSYKFPSLQHCVTGGEPLNPEVLEKW----KAQTGLDIyegYGQTET-------GLICAN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 812 STE---SPASvtalldkevipLGKGMPGAQILILNEAGNLAGIGELGEIYVR-SPHLAFG----YLDDPDQTNERFLVNp 883
Cdd:cd05928 335 FKGmkiKPGS-----------MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIRPFGlfsgYVDNPEKTAATIRGD- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 884 fthqehdrLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQIV------ 957
Cdd:cd05928 403 --------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPD-PIRGEVVkafvvl 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 958 --AYITHHNEQvkpVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05928 474 apQFLSHDPEQ---LTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
639-1010 |
1.80e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 98.32 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLThFLPWMRDRFA-FTQTDrySLLSGLahdPLQR------EIFTPLCVGATICI 711
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWMLALNSlFDPDD--VLLCGL---PLFHvngsvvTLLTPLASGAHVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 PDQEHMGDPGWLAQ-W--MQGQEITIASFTPALLQLLTQGMGEDDlpsarIPSLRYAFVVGDALTRRHVARLYAvAPHIT 788
Cdd:cd05944 75 AGPAGYRNPGLFDNfWklVERYRITSLSTVPTVYAALLQVPVNAD-----ISSLRFAMSGAAPLPVELRARFED-ATGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 789 CVNLYGSTETQRAVSyfvLPTASSTESPASVtalldkeviplGKGMPGAQ--ILILNEAGNL---AGIGELGEIYVRSPH 863
Cdd:cd05944 149 VVEGYGLTEATCLVA---VNPPDGPKRPGSV-----------GLRLPYARvrIKVLDGVGRLlrdCAPDEVGEICVAGPG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 864 LAFGYLDDPDQTNerflvnpftHQEHDRLYRTGDLGRYLPDGNAEFAGR-NDLqvKIRG-YRIELEEIEAILVEHPMVAD 941
Cdd:cd05944 215 VFGGYLYTEGNKN---------AFVADGWLNTGDLGRLDADGYLFITGRaKDL--IIRGgHNIDPALIEEALLRHPAVAF 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574832895 942 AAVIIREDTPDNKQIVAYIthhneQVKPVLS----NLRAFVTQRLPA-FMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05944 284 AGAVGQPDAHAGELPVAYV-----QLKPGAVveeeELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
500-1028 |
1.81e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 102.03 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 500 LRPENIAIIDEINTVSYGeleaRSNQLAHYlhAQGIRPHDVVAISAQRCAAlVLAILGiLKAGSTVLILDPSYPpaRLLE 579
Cdd:PRK06060 1 MRNGNLAGLLAEQASEAG----WYDRPAFY--AADVVTHGQIHDGAARLGE-VLRNRG-LSSGDRVLLCLPDSP--DLVQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 580 YVQRAHARGWLRIEGATDCQELDE-WCRANSYCNLV-----LARNFALSGILSQYASSAPAYRVGPNDI--------ACL 645
Cdd:PRK06060 71 LLLACLARGVMAFLANPELHRDDHaLAARNTEPALVvtsdaLRDRFQPSRVAEAAELMSEAARVAPGGYepmggdalAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 646 TFTSGSTGRPKGVLQRHGPLTHFLPWM-RDRFAFTQTD------RYSLLSGLAHdplqrEIFTPLCVGATICIPDqehmg 718
Cdd:PRK06060 151 TYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDtglcsaRMYFAYGLGN-----SVWFPLATGGSAVINS----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 719 dpgwLAQWMQGQEITIASFTPALL----QLLTQGMGEDDLPSARipSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYG 794
Cdd:PRK06060 221 ----APVTPEAAAILSARFGPSVLygvpNFFARVIDSCSPDSFR--SLRCVVSAGEALELGLAERLMEFFGGIPILDGIG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 795 STETQRAvsyFVLPTASstespasvtallDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQ 874
Cdd:PRK06060 295 STEVGQT---FVSNRVD------------EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 875 --TNERFLvnpfthQEHDRLYRTGDlgrylpdGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVI-IREDTP 951
Cdd:PRK06060 360 pvANEGWL------DTRDRVCIDSD-------GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVaVRESTG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 952 DNKQIVAYITHHNEQV-KPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAADEA-TLSLATPQS 1028
Cdd:PRK06060 427 ASTLQAFLVATSGATIdGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIwELSLTEPGS 505
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1610-1857 |
4.80e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 99.49 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLLTHEE-------LKARWPHC-------PCPLLCLDTLQERYASL----PCEDLQEACSPA 1751
Cdd:PRK06187 88 IRLKPEEIAYILNDAEDRVVLVDSEfvpllaaILPQLPTVrtvivegDGPAAPLAPEVGEYEELlaaaSDTFDFPDIDEN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1752 QLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSIsFDIAGLEL-YLPLLAGAQIQLASQeqaSD 1830
Cdd:PRK06187 168 DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVIPRR---FD 243
|
250 260
....*....|....*....|....*..
gi 1574832895 1831 PRQLASLLAQLPISILQATPTTWQLLL 1857
Cdd:PRK06187 244 PENLLDLIETERVTFFFAVPTIWQMLL 270
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
499-1010 |
2.25e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 97.37 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 499 HLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLL 578
Cdd:PRK10946 34 HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 579 EYVQ----------RAHARgwlriegATDCQELDEWCRANSYCNLVLARN----FALSGILSQYASSAPAYRVGPNDIAC 644
Cdd:PRK10946 114 AYASqiepalliadRQHAL-------FSDDDFLNTLVAEHSSLRVVLLLNddgeHSLDDAINHPAEDFTATPSPADEVAF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 645 LTFTSGSTGRPKGVLQRHG----------PLTHFLPWMRDRFAFTQTDRYSLLSG-------------LAHDPlqreift 701
Cdd:PRK10946 187 FQLSGGSTGTPKLIPRTHNdyyysvrrsvEICGFTPQTRYLCALPAAHNYPMSSPgalgvflaggtvvLAPDP------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 702 plcvGATICIPDQEHmgdpgwlaqwmqgQEITIASFTPALLQLLTQGMGEDDLpSARIPSLRYAFVVGDALTRRHVARLY 781
Cdd:PRK10946 260 ----SATLCFPLIEK-------------HQVNVTALVPPAVSLWLQAIAEGGS-RAQLASLKLLQVGGARLSETLARRIP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 782 AVaphITCV--NLYGSTETqrAVSYfvlptasstespasvTALLDKEVIPL---GKGM-PGAQILILNEAGNLAGIGELG 855
Cdd:PRK10946 322 AE---LGCQlqQVFGMAEG--LVNY---------------TRLDDSDERIFttqGRPMsPDDEVWVADADGNPLPQGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 856 EIYVRSPHLAFGYLDDPDQTNERFLVNPFthqehdrlYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVE 935
Cdd:PRK10946 382 RLMTRGPYTFRGYYKSPQHNASAFDANGF--------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLR 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 936 HPMVADAAVIIREDTPDNKQIVAYIThHNEQVKPVLsnLRAFVTQRLPA-FMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK10946 454 HPAVIHAALVSMEDELMGEKSCAFLV-VKEPLKAVQ--LRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
489-988 |
6.87e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 96.48 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVlil 568
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVV--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 569 dpsyppaRLLEYVQR----AHArgwLRIEGA------TDCQELDEWCR-----ANSYCNLVLARNFALSGI--LSQYASS 631
Cdd:PRK08279 115 -------ALLNTQQRgavlAHS---LNLVDAkhlivgEELVEAFEEARadlarPPRLWVAGGDTLDDPEGYedLAAAAAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 632 APAY------RVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDR-YSLLSgLAHDplqreifTPLC 704
Cdd:PRK08279 185 APTTnpasrsGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVlYCCLP-LYHN-------TGGT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 V--------GATICI----------PDqehmgdpgwlaqwmqgqeitIASFTPALLQ--------LLTQGMGEDDlpsaR 758
Cdd:PRK08279 257 VawssvlaaGATLALrrkfsasrfwDD--------------------VRRYRATAFQyigelcryLLNQPPKPTD----R 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 759 IPSLRYAFVVG------DALTRRhvarlYAVaPHItcVNLYGSTETQraVSYF----------VLPTASSTesPASVTAl 822
Cdd:PRK08279 313 DHRLRLMIGNGlrpdiwDEFQQR-----FGI-PRI--LEFYAASEGN--VGFInvfnfdgtvgRVPLWLAH--PYAIVK- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 823 LDKEviplgKGMPgaqilILNEAGNL-----AGIGEL-GEIYVRSPhlaF-GYLdDPDQTNERFLVNPFthQEHDRLYRT 895
Cdd:PRK08279 380 YDVD-----TGEP-----VRDADGRCikvkpGEVGLLiGRITDRGP---FdGYT-DPEASEKKILRDVF--KKGDAWFNT 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 896 GDLGRYLPDGNAEFAGR-NDLqvkirgYRIELE-----EIEAILVEHPMVADAAV----IirEDTPDNKQIVAYITHHNE 965
Cdd:PRK08279 444 GDLMRDDGFGHAQFVDRlGDT------FRWKGEnvattEVENALSGFPGVEEAVVygveV--PGTDGRAGMAAIVLADGA 515
|
570 580
....*....|....*....|...
gi 1574832895 966 QVKPvlSNLRAFVTQRLPAFMVP 988
Cdd:PRK08279 516 EFDL--AALAAHLYERLPAYAVP 536
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
515-1013 |
1.21e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 94.77 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPP---ARLLE----YVQRAHAR 587
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPeeiAYILEdsgaRVLIAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 588 GWLRIEGA--TDCQEL---------------DEWCRANsycnlvlARNFALSGILSQYASSAPAYRVGPndiACLTFTSG 650
Cdd:PRK12406 93 LLHGLASAlpAGVTVLsvptppeiaaayrisPALLTPP-------AGAIDWEGWLAQQEPYDGPPVPQP---QSMIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKGVLQRHGPLTHFLPWMRDR---FAFTQTDRySLLSG-LAHD-PLQREIFTPLCVGATICIPdqehMGDPGWLAQ 725
Cdd:PRK12406 163 TTGHPKGVRRAAPTPEQAAAAEQMRaliYGLKPGIR-ALLTGpLYHSaPNAYGLRAGRLGGVLVLQP----RFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 726 WMQGQEITIASFTPAL-LQLLtqgmgedDLPSAR-----IPSLRyaFVV-GDALTRRHVARlyAV----APHItcVNLYG 794
Cdd:PRK12406 238 LIERHRITHMHMVPTMfIRLL-------KLPEEVrakydVSSLR--HVIhAAAPCPADVKR--AMiewwGPVI--YEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 795 STETQRAVsyfvlpTASSTES---PASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLA-FGYLD 870
Cdd:PRK12406 305 STESGAVT------FATSEDAlshPGTV-----------GKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPdFTYHN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 871 DPDQTNErflvnpfthQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDT 950
Cdd:PRK12406 368 KPEKRAE---------IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDA 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 951 PDNKQIVAYITHHnEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAP 1013
Cdd:PRK12406 439 EFGEALMAVVEPQ-PGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
647-1010 |
1.57e-19 |
|
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: 94.37 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 647 FTSGSTGRPKGVLQRH-GPLTHFLPWM--RDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIpdQEHMgDPGWL 723
Cdd:cd05929 132 YSGGTTGRPKGIKRGLpGGPPDNDTLMaaALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVL--MEKF-DPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 724 AQWMQGQEITIASFTPALLQLLTQgmgeddLPSAripsLRYAFVVGDALTRRHVA---------RLYAVAPHITcVNLYG 794
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLK------LPEA----VRNAYDLSSLKRVIHAAapcppwvkeQWIDWGGPII-WEYYG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 795 STETQRavsyfvLPTASSTE---SPASVtalldkeviplGKGMpGAQILILNEAGNLAGIGELGEIYVRSPHlAFGYLDD 871
Cdd:cd05929 278 GTEGQG------LTIINGEEwltHPGSV-----------GRAV-LGKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTND 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 872 PDQTNERFlvnpfthqeHDRLYRT-GDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDT 950
Cdd:cd05929 339 PEKTAAAR---------NEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDE 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 951 PDNKQIVAYI-THHNEQVKPVLS-NLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05929 410 ELGQRVHAVVqPAPGADAGTALAeELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-302 |
1.69e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 96.78 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 6 QRLAALSPEKRALLKQQlgkqGSRFNTFPLSFAQQrlWLLDQLNPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHES 85
Cdd:PRK05691 2769 QTLAAVATHSEAAQAEQ----GPLQGASGLTPIQH--WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDA 2842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 86 LRTTFAMLNGEPIQVIRPnLTLQIPLIDLTSLPEAEREAslqhaINNEAHIPFDLKTGPLVRLALLRKSPLEHILLLNTH 165
Cdd:PRK05691 2843 LRLRFSQADGRWQAEYRA-VTAQELLWQVTVADFAECAA-----LFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIH 2916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 166 HIISDGWSLGVFLHELSLCYSAALAGNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADmpPLLELPMDHPR 245
Cdd:PRK05691 2917 HLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGG--PRAELPCDRPQ 2994
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 246 PAVQTSHGAVVSLLLPSEISTALkaLSQ-----HEGVT-LFMTTLALfqiLLQRYTGRRDIVI 302
Cdd:PRK05691 2995 GGNLNRHAQTVSVRLDAERTRQL--LQQapaayRTQVNdLLLTALAR---VLCRWSGQPSVLV 3052
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1632-1879 |
1.70e-19 |
|
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: 93.69 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1632 TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLT 1711
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1712 HEELkarwphcpCPLLCLDTLQERYASLPcedlqeacSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSP 1791
Cdd:cd17654 95 NKEL--------DNAPLSFTPEHRHFNIR--------TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1792 HDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLP-ISILQATPT-----TWQLLLETGWSGKA 1865
Cdd:cd17654 159 EDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHrITVLQATPTlfrrfGSQSIKSTVLSATS 238
|
250
....*....|....*..
gi 1574832895 1866 GL-TLLSG--AKPSLLI 1879
Cdd:cd17654 239 SLrVLALGgePFPSLVI 255
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1155-1360 |
4.81e-19 |
|
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: 92.31 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1155 WFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQGEQLMQRIHaqlwlSLSQQHLSLPAESES 1234
Cdd:cd19534 10 WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIR-----GDVEELFRLEVVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1235 SLSQQALQAWLQQEIRRPFDLQQAPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAHVKGISPQLaPL 1314
Cdd:cd19534 85 SLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPL-PS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1574832895 1315 PLQYADYAVWQRAWLQEERQEKLQRYWHGQLATAPAllDLPTDHPR 1360
Cdd:cd19534 164 KTSFQTWAELLAEYAQSPALLEELAYWRELPAADYW--GLPKDPEQ 207
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1151-1461 |
5.21e-19 |
|
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: 91.73 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1151 QERLWFLHRFEPESSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVLQG--E--QLMQRiHAQL---WLSLSQ 1223
Cdd:cd19544 8 QEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGlsEpvQVVWR-QAELpveELTLDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1224 QHLS---LPAESESSlsqqalqawlqqeiRRPFDLQQAPLLRASLLH-RGSEPSILLLCLHHIIADGWSLGILLQELslc 1299
Cdd:cd19544 87 GDDAlaqLRARFDPR--------------RYRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1300 yNAHVKGISPQLAPlPLQYADYAVwqRAWLQEERQEKlQRYWHGQLA-----TAP-ALLDLPTDhprppiqtfvGAR--- 1370
Cdd:cd19544 150 -QAILAGRAAALPP-PVPYRNFVA--QARLGASQAEH-EAFFREMLGdvdepTAPfGLLDVQGD----------GSDite 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1371 HQLHLPAELLEQL--------------------MVLShqqqvtlymtllaafllllyRYSGQEDLVVGTPIAGRQR--RE 1428
Cdd:cd19544 215 ARLALDAELAQRLraqarrlgvspaslfhlawaLVLA--------------------RCSGRDDVVFGTVLSGRMQggAG 274
|
330 340 350
....*....|....*....|....*....|...
gi 1574832895 1429 LEGVIGLFANTLVLRTDLsGDPSFLELLQRVRE 1461
Cdd:cd19544 275 ADRALGMFINTLPLRVRL-GGRSVREAVRQTHA 306
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
495-1010 |
6.50e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 92.56 E-value: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 495 AQQAHLRPENIAIIDEINTV--SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSY 572
Cdd:PRK09088 2 AFHARLQPQRLAAVDLALGRrwTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 573 PPARLLEYVQRAHARGWLRIEGATDCQELDEwcransycnlvlarnfALSGILSQYASSAPAYR--VGPNDIACLTFTSG 650
Cdd:PRK09088 82 SASELDALLQDAEPRLLLGDDAVAAGRTDVE----------------DLAAFIASADALEPADTpsIPPERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKGVLqrhgplthflpwMRDRFAFTQTDRYSLLSGLAHDP-------------LQREIFTPLCVGATICIPDqehm 717
Cdd:PRK09088 146 TSGQPKGVM------------LSERNLQQTAHNFGVLGRVDAHSsflcdapmfhiigLITSVRPVLAVGGSILVSN---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 718 G-DPGWLAQWMQGQEITIASF--TPALLQLLTQGMGEDdlpSARIPSLRyAFVVGDAltrRHVAR--LYAVAPHITCVNL 792
Cdd:PRK09088 210 GfEPKRTLGRLGDPALGITHYfcVPQMAQAFRAQPGFD---AAALRHLT-ALFTGGA---PHAAEdiLGWLDDGIPMVDG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 793 YGSTEtqrAVSYFVLPTASstespasvtALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDP 872
Cdd:PRK09088 283 FGMSE---AGTVFGMSVDC---------DVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 873 DQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPD 952
Cdd:PRK09088 351 QATARAF--------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQW 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 953 NKQIVAYITHHNEQVKPvLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK09088 423 GEVGYLAIVPADGAPLD-LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
497-1005 |
1.59e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 91.22 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 497 QAHLRPENIAII--DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPP 574
Cdd:PRK13390 6 HAQIAPDRPAVIvaETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 575 ARLLEYVQRAHARGwLRIEGATDCQEldewCRANSYCNLVLARNFALSGILSQYASSAPAyrvGPNDI-----ACLTFTS 649
Cdd:PRK13390 86 PEADYIVGDSGARV-LVASAALDGLA----AKVGADLPLRLSFGGEIDGFGSFEAALAGA---GPRLTeqpcgAVMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 650 GSTGRPKGVL------QRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPgwl 723
Cdd:PRK13390 158 GTTGFPKGIQpdlpgrDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQAT--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 724 AQWMQGQEITIASFTPALLQLLTQgMGEDDLPSARIPSLRyafvvgdaltrrhvARLYAVAPhitCvnlygSTETQRAVS 803
Cdd:PRK13390 235 LGHVERYRITVTQMVPTMFVRLLK-LDADVRTRYDVSSLR--------------AVIHAAAP---C-----PVDVKHAMI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 804 YFVLPTA----SSTEspASVTALLDKEVIPLGKGMPGAQIL----ILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQT 875
Cdd:PRK13390 292 DWLGPIVyeyySSTE--AHGMTFIDSPDWLAHPGSVGRSVLgdlhICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 876 NERflvnpfTHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQ 955
Cdd:PRK13390 370 AAA------QHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPD-PEMGE 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 956 IVAYITHHNEQVKP---VLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKV 1005
Cdd:PRK13390 443 QVKAVIQLVEGIRGsdeLARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
487-1005 |
2.82e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 91.03 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 487 EGTIHDLFAQQAHLRPENIAIIDEINTV--SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGST 564
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 565 VLILDPSYPPARLlEYVQRAHARGWLRIEGA---TD----CQELDEWCRANSYCNLVLAR-------------------N 618
Cdd:PRK08315 95 LVTINPAYRLSEL-EYALNQSGCKALIAADGfkdSDyvamLYELAPELATCEPGQLQSARlpelrrviflgdekhpgmlN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 619 F----ALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLqrhgpLTHF--LP---WMRDRFAFTQTDRYSL--- 686
Cdd:PRK08315 174 FdellALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGAT-----LTHRniLNngyFIGEAMKLTEEDRLCIpvp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 687 --------LSGLAhdplqreiftplCV--GATICIPDQEHmgDPGWLAQWMQGQEITiasftpALLQLLTQGMGEDDLPS 756
Cdd:PRK08315 249 lyhcfgmvLGNLA------------CVthGATMVYPGEGF--DPLATLAAVEEERCT------ALYGVPTMFIAELDHPD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 757 -AR--IPSLRYAFVVGDA----LTRRHVARLYAvaPHITCVnlYGSTETQrAVSyfvlpTASSTESPasvtalLDKEVIP 829
Cdd:PRK08315 309 fARfdLSSLRTGIMAGSPcpieVMKRVIDKMHM--SEVTIA--YGMTETS-PVS-----TQTRTDDP------LEKRVTT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 830 LGKGMPGAQILILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAE 908
Cdd:PRK08315 373 VGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI--------DADGWMHTGDLAVMDEEGYVN 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 909 FAGRndlqVK---IRG----YRIELEEieaILVEHPMVADAAVIireDTPDNK---QIVAYIT-HHNEQVKPvlSNLRAF 977
Cdd:PRK08315 445 IVGR----IKdmiIRGgeniYPREIEE---FLYTHPKIQDVQVV---GVPDEKygeEVCAWIIlRPGATLTE--EDVRDF 512
|
570 580
....*....|....*....|....*...
gi 1574832895 978 VTQRLPAFMVPAHFVFMSRLPLNANGKV 1005
Cdd:PRK08315 513 CRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1610-1875 |
3.35e-18 |
|
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: 89.93 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLLTHEelkarwphcpcpllcldTLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGV 1769
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAV-----------------SFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1770 QISHGALLS--FLLSLQSLLSLSPHDRWLAITSIsFDIAGLE--LYLPLLAGAQIQLasqEQASDPRQLASLLAQLPISI 1845
Cdd:cd05936 144 MLTHRNLVAnaLQIKAWLEDLLEGDDVVLAALPL-FHVFGLTvaLLLPLALGATIVL---IPRFRPIGVLKEIRKHRVTI 219
|
250 260 270
....*....|....*....|....*....|....
gi 1574832895 1846 LQATPTTWQLLLETGWSGKAGLTLL----SGAKP 1875
Cdd:cd05936 220 FPGVPTMYIALLNAPEFKKRDFSSLrlciSGGAP 253
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
831-1006 |
3.88e-18 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 88.13 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 831 GKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFA 910
Cdd:cd17636 166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT---------RGGWHHTNDLGRREPDGSLSFV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 911 GRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIireDTPDNK--QIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVP 988
Cdd:cd17636 237 GPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI---GVPDPRwaQSVKAIVVLKPGASVTEAELIEHCRARIASYKKP 313
|
170
....*....|....*...
gi 1574832895 989 AHFVFMSRLPLNANGKVD 1006
Cdd:cd17636 314 KSVEFADALPRTAGGADD 331
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
489-1010 |
4.30e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 90.13 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAIIDE-----INTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGS 563
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFEssggvVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 564 TVLILDpsyppARLL----EYVQRAHARGWLRIEGA---TDCQELDEwcRANSYCNLVLAR--NFALSGI--LSQYASSA 632
Cdd:PRK08008 88 IMVPIN-----ARLLreesAWILQNSQASLLVTSAQfypMYRQIQQE--DATPLRHICLTRvaLPADDGVssFTQLKAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 633 PA---YRV--GPNDIACLTFTSGSTGRPKGVLQRHGPLT---HFLPWmrdRFAFTQTDRYSLLSGLAHDPLQREIFTP-L 703
Cdd:PRK08008 161 PAtlcYAPplSTDDTAEILFTSGTTSRPKGVVITHYNLRfagYYSAW---QCALRDDDVYLTVMPAFHIDCQCTAAMAaF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 704 CVGATICIPDQEHMGdpgwlAQWMQGQEI--TIASFTPALLQ-LLTQGMGEDDlpsaRIPSLRYAFVV-------GDALT 773
Cdd:PRK08008 238 SAGATFVLLEKYSAR-----AFWGQVCKYraTITECIPMMIRtLMVQPPSAND----RQHCLREVMFYlnlsdqeKDAFE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 774 RRHVARLYavaphitcvNLYGSTETQRAVSyfvlptassTESPAsvtallDKEVIP-LGKGMPGAQILILNEAGNLAGIG 852
Cdd:PRK08008 309 ERFGVRLL---------TSYGMTETIVGII---------GDRPG------DKRRWPsIGRPGFCYEAEIRDDHNRPLPAG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 853 ELGEIYVRS---PHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEI 929
Cdd:PRK08008 365 EIGEICIKGvpgKTIFKEYYLDPKATAKVL--------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVEL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 930 EAILVEHPMVADAAVIIREDTPDNKQIVAYIThHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKA 1009
Cdd:PRK08008 437 ENIIATHPKIQDIVVVGIKDSIRDEAIKAFVV-LNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKN 515
|
.
gi 1574832895 1010 L 1010
Cdd:PRK08008 516 L 516
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
490-1020 |
3.68e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 87.40 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 490 IHDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILD 569
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 570 PSYPpARLLEYvqRAHARG----------WLRIEGATDCQELD----------------------EWCRANSYCNLVLAR 617
Cdd:PRK06710 106 PLYT-ERELEY--QLHDSGakvilcldlvFPRVTNVQSATKIEhvivtriadflpfpknllypfvQKKQSNLVVKVSESE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 618 NFALSGILSQYASSAPAYRVGP-NDIACLTFTSGSTGRPKGVLQRHGPLTH---------------------FLPWMRdR 675
Cdd:PRK06710 183 TIHLWNSVEKEVNTGVEVPCDPeNDLALLQYTGGTTGFPKGVMLTHKNLVSntlmgvqwlynckegeevvlgVLPFFH-V 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 676 FAFTQTDRYSLLSGLAhdplqreiftplcvgaTICIPDqehmGDPGWLAQWMQGQEITIASFTPALLQLLTQG--MGEDD 753
Cdd:PRK06710 262 YGMTAVMNLSIMQGYK----------------MVLIPK----FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSplLKEYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 754 LPSARipslryAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETqravsyfvlptassteSPASVTALLDKEVIPLGKG 833
Cdd:PRK06710 322 ISSIR------ACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES----------------SPVTHSNFLWEKRVPGSIG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 834 MP----GAQILILnEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEF 909
Cdd:PRK06710 380 VPwpdtEAMIMSL-ETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL---------QDGWLHTGDVGYMDEDGFFYV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 910 AGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPVlSNLRAFVTQRLPAFMVPA 989
Cdd:PRK06710 450 KDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSE-EELNQFARKYLAAYKVPK 528
|
570 580 590
....*....|....*....|....*....|....
gi 1574832895 990 HFVFMSRLPLNANGKVDRKALPAPEA---ADEAT 1020
Cdd:PRK06710 529 VYEFRDELPKTTVGKILRRVLIEEEKrknEDEQT 562
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
491-1115 |
4.45e-17 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 87.84 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 491 HDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDP 570
Cdd:COG3319 4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 571 SYPPARLLEYVQRAHARGWLRIEGATDCQELDEWcransycnLVLARNFALSGILSQYASSAPAYRVGPNDIACLTFTSG 650
Cdd:COG3319 84 LALALAAAAAALLLAALALLLALLAALALALLAL--------LLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDQEHMGDPGWLAQWMQGQ 730
Cdd:COG3319 156 GGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 731 EITIASFTPALLQLLTQGMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVLPTA 810
Cdd:COG3319 236 LLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 811 sstespasvtalldkevIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHQEHD 890
Cdd:COG3319 316 -----------------GPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 891 RLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHhneQVKPV 970
Cdd:COG3319 379 RLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVA---AAALA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 971 LSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAADEATLSLATPQsPIQEELCLLWCELLGLKKVGIT 1050
Cdd:COG3319 456 AAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAA-ALELALALLLLLLLGLGLVGDD 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1051 QNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASLITVSSSSKQELKEPVLQAQA 1115
Cdd:COG3319 535 DDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGG 599
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
491-1012 |
4.58e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 86.97 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 491 HDLFAQQAHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDP 570
Cdd:PRK13383 38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 571 SYPpARLLEYVQRAHArgwLRIEGATDcqELDEWCRANSYCNLVLARNFALSGILSQYASSAPAYRVgpndiacLTFTSG 650
Cdd:PRK13383 118 EFR-SDALAAALRAHH---ISTVVADN--EFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRI-------VLLTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 651 STGRPKGVLQRHGPLTHFLPWMR--DRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIpdQEHMGDPGWLAQWMQ 728
Cdd:PRK13383 185 TTGKPKGVPRAPQLRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLT--HRHFDAEAALAQASL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 729 GQEITIASFTPALLQLLtqgmgedDLPS---AR--IPSLRYAFVVGDALTRRhVARLYAVAPHITCVNLYGSTETqrAVS 803
Cdd:PRK13383 263 HRADAFTAVPVVLARIL-------ELPPrvrARnpLPQLRVVMSSGDRLDPT-LGQRFMDTYGDILYNGYGSTEV--GIG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 804 YFVLPtASSTESPASVtalldkeviplGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTnerfLVnp 883
Cdd:PRK13383 333 ALATP-ADLRDAPETV-----------GKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKA----VV-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 884 fthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIT-H 962
Cdd:PRK13383 395 ------DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVlH 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1574832895 963 HNEQVKPvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPA 1012
Cdd:PRK13383 469 PGSGVDA--AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
489-912 |
5.06e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.41 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 489 TIHDLFAQQAHLRPENIAII------DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAG 562
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAqrepghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 563 STVLILDPSYPP-----ARL----------LEYVQRA--HARGwLRIEGATDCqeldEWCRANSYCNLVLARNFA-LSGI 624
Cdd:PRK12582 130 VPAAPVSPAYSLmshdhAKLkhlfdlvkprVVFAQSGapFARA-LAALDLLDV----TVVHVTGPGEGIASIAFAdLAAT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 625 LSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYS-LLSGL--AHDPLQREIFT 701
Cdd:PRK12582 205 PPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPvSLDWMpwNHTMGGNANFN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 702 PLCV-GATICIPDQEHMgdPGWLAQWMQG-QEITIASF--TPALLQLLTQGMGEDD-LPSARIPSLRYAFVVGDALTRRH 776
Cdd:PRK12582 285 GLLWgGGTLYIDDGKPL--PGMFEETIRNlREISPTVYgnVPAGYAMLAEAMEKDDaLRRSFFKNLRLMAYGGATLSDDL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 777 VARLYAVAPHIT-----CVNLYGSTETQravsyfvlPTASSTESPASVTALldkevipLGKGMPGAQIlilneagNLAGI 851
Cdd:PRK12582 363 YERMQALAVRTTghripFYTGYGATETA--------PTTTGTHWDTERVGL-------IGLPLPGVEL-------KLAPV 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 852 GELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYL-PDGNAE---FAGR 912
Cdd:PRK12582 421 GDKYEVRVKGPNVTPGYHKDPELTAAAF--------DEEGFYRLGDAARFVdPDDPEKgliFDGR 477
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1624-1860 |
6.36e-17 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 86.70 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGS-----TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLL 1698
Cdd:COG0365 25 KVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1699 WMAQDAQLSLLLTHEE---------LKARW----PHCPCP--LLCLDTLQERYASLPCEDLQEA-------CSPAQL--- 1753
Cdd:COG0365 105 DRIEDAEAKVLITADGglrggkvidLKEKVdealEELPSLehVIVVGRTGADVPMEGDLDWDELlaaasaeFEPEPTdad 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1754 --AYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLS-LSPHDRWLAITSISFdIAGL--ELYLPLLAGA-QIQLASQEQ 1827
Cdd:COG0365 185 dpLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLdLKPGDVFWCTADIGW-ATGHsyIVYGPLLNGAtVVLYEGRPD 263
|
250 260 270
....*....|....*....|....*....|...
gi 1574832895 1828 ASDPRQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:COG0365 264 FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAG 296
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1164-1574 |
7.70e-17 |
|
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: 85.04 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1164 SSAYHLFLAFELDGQFQPAAFEESLNDLLARHESLRTSFVL-QGEQLMQRIHaqlwlslsqQHLSLPAESESSLSQQALQ 1242
Cdd:cd19545 19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQsDSGGLLQVVV---------KESPISWTESTSLDEYLEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1243 AWlqqeiRRPFDLQQaPLLRASLLHRGSEPSILLLCLHHIIADGWSLGILLQELSLCYNAhvkgispQLAPLPLQYADYA 1322
Cdd:cd19545 90 DR-----AAPMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG-------EPVPQPPPFSRFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1323 vwqrAWLQEERQEKLQRYWHGQLATAPAlLDLPTdHPRPPIQTFVGA--RHQLHLPAelleqlmvlSHQQQVTLYMTLLA 1400
Cdd:cd19545 157 ----KYLRQLDDEAAAEFWRSYLAGLDP-AVFPP-LPSSRYQPRPDAtlEHSISLPS---------SASSGVTLATVLRA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1401 AFLLLLYRYSGQEDLVVGT-------PIAGrqrreLEGVIGLFANTLVLRTDLSGDPSFLELLQRVrevtlQAYSQQDMP 1473
Cdd:cd19545 222 AWALVLSRYTGSDDVVFGVtlsgrnaPVPG-----IEQIVGPTIATVPLRVRIDPEQSVEDFLQTV-----QKDLLDMIP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1474 FE----KLVAELQPERSLAynPLFQVFFALQnVPGDPISLEGLDVTQIRLDSNSAKFDlswTWY-----QEDEKSLSAVI 1544
Cdd:cd19545 292 FEhtglQNIRRLGPDARAA--CNFQTLLVVQ-PALPSSTSESLELGIEEESEDLEDFS---SYGltlecQLSGSGLRVRA 365
|
410 420 430
....*....|....*....|....*....|
gi 1574832895 1545 EYNTALFEPQRIAGMATNMLVVLQSLCQEP 1574
Cdd:cd19545 366 RYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1610-1814 |
8.00e-17 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 86.69 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPAL---HAGS-TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAY 1685
Cdd:COG1022 13 LPDLLRRRAARFPDRVALrekEDGIwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1686 VPLDPDYPSQRLLWMAQDAQLSLLLTHEE-----LKARWPHCPC----------------PLLCLDTLQERYASLPC--- 1741
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVEDQeqldkLLEVRDELPSlrhivvldprglrddpRLLSLDELLALGREVADpae 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574832895 1742 -EDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLaitsisfdiagleLYLPL 1814
Cdd:COG1022 173 lEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-------------SFLPL 233
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
476-1010 |
8.59e-17 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 86.04 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 476 PDPGAPISAHWEGTIHDLFAQQAHLRPENIAIIDEINTV--SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVL 553
Cdd:cd17642 5 PGPFYPLEDGTAGEQLHKAMKRYASVPGTIAFTDAHTGVnySYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 554 AILGILKAGSTVLILDPSYPPARLLEYVQRAHARgwLRIEGATDCQELDEWCRANSYCN--LVLARNFALSGILSQY--- 628
Cdd:cd17642 85 PVIAGLFIGVGVAPTNDIYNERELDHSLNISKPT--IVFCSKKGLQKVLNVQKKLKIIKtiIILDSKEDYKGYQCLYtfi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 629 ASSAP----AYRVGPN------DIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRD-RFAFTQTDRYSLLSGLA--HDPL 695
Cdd:cd17642 163 TQNLPpgfnEYDFKPPsfdrdeQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGNQIIPDTAILTVIPfhHGFG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 696 QREIFTPLCVGATICIpdqEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQGMGED--------DLPSARIPSLRYafv 767
Cdd:cd17642 243 MFTTLGYLICGFRVVL---MYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDkydlsnlhEIASGGAPLSKE--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 768 VGDALTRR-HVarlyavaPHITcvNLYGSTETQRAVsyfvLPTASSTESPASVtalldkeviplGKGMPGAQILILN-EA 845
Cdd:cd17642 317 VGEAVAKRfKL-------PGIR--QGYGLTETTSAI----LITPEGDDKPGAV-----------GKVVPFFYAKVVDlDT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 846 GNLAGIGELGEIYVRSPHLAFGYLDDPDQTNErfLVNpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIE 925
Cdd:cd17642 373 GKTLGPNERGELCVKGPMIMKGYVNNPEATKA--LID------KDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 926 LEEIEAILVEHPMVADAAVIIREDtPDNKQIVAYITHHNEQVKPVLSNLRAFV-TQRLPAFMVPAHFVFMSRLPLNANGK 1004
Cdd:cd17642 445 PAELESILLQHPKIFDAGVAGIPD-EDAGELPAAVVVLEAGKTMTEKEVMDYVaSQVSTAKRLRGGVKFVDEVPKGLTGK 523
|
....*.
gi 1574832895 1005 VDRKAL 1010
Cdd:cd17642 524 IDRRKI 529
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
55-344 |
1.02e-16 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 84.80 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 55 YNIAAAIRFAGPLRVDLLEKCIHLLVRRHESLRTTFA--MLNgEPIQVIRPNLTLqiPLIDLTSLPEAEREASLQHAINn 132
Cdd:cd19544 24 YLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILweGLS-EPVQVVWRQAEL--PVEELTLDPGDDALAQLRARFD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 133 EAHIPFDLKTGPLVRLALLRKSPL-EHILLLNTHHIISDGWSLGVFLHELSLCysaaLAGNSPTLPAPsLQYADYAAWQR 211
Cdd:cd19544 100 PRRYRLDLRQAPLLRAHVAEDPANgRWLLLLLFHHLISDHTSLELLLEEIQAI----LAGRAAALPPP-VPYRNFVAQAR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 212 NwlkGENLTNLLDYWRKQLADmppllelpMDHP-----RPAVQTSHGAVV--SLLLPSEISTALKALSQHEGV---TLFM 281
Cdd:cd19544 175 L---GASQAEHEAFFREMLGD--------VDEPtapfgLLDVQGDGSDITeaRLALDAELAQRLRAQARRLGVspaSLFH 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 282 TTLALfqiLLQRYTGRRDIVIGTPIANRNR--TDIEHVFGFFVNTLVLRIDVAsELNFRTLLQRV 344
Cdd:cd19544 244 LAWAL---VLARCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLRVRLG-GRSVREAVRQT 304
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1624-1858 |
1.10e-16 |
|
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: 84.97 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDpdypsqrllWMaqd 1703
Cdd:cd17631 11 RTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN---------FR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 aqlsllLTHEELKarwphcpcpllclDTLQERYASLPCEDLqeacspaqlAYVIYTSGSTGRPKGVQISHGALLSFLLSL 1783
Cdd:cd17631 79 ------LTPPEVA-------------YILADSGAKVLFDDL---------ALLMYTSGTTGRPKGAMLTHRNLLWNAVNA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 1784 QSLLSLSPHDRWLAITSIsFDIAGLELYLP--LLAGAQIQLasqEQASDPRQLASLLAQLPISILQATPTTWQLLLE 1858
Cdd:cd17631 131 LAALDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVI---LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQ 203
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
526-1007 |
1.30e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 85.62 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 526 LAHYLHAQGIRPHDVVAIS------------AQRCAALVLAIL-----------GILKAGSTVLILDPS----YPParll 578
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAalnsdlylewllAVACAGGIVAPLnyrwsfeeaksAMLLVRPVMLVTDETcsswYEE---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 579 eyVQRAHARGW-LRIEGATDCQELdeWCRANSYCNLVLARNFALSGILSQYASSapayrvgPNDIACLTFTSGSTGRPKG 657
Cdd:PLN02860 121 --LQNDRLPSLmWQVFLESPSSSV--FIFLNSFLTTEMLKQRALGTTELDYAWA-------PDDAVLICFTSGTTGRPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 658 VLQRHGPL-THFLPwmrdRFAFT---QTDRYSLLSGLAHDPLQREIFTPLCVGAT-ICIPDqehmGDPGWLAQWMQGQEI 732
Cdd:PLN02860 190 VTISHSALiVQSLA----KIAIVgygEDDVYLHTAPLCHIGGLSSALAMLMVGAChVLLPK----FDAKAALQAIKQHNV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 733 TIASFTPALLQLLTQgMGEDDLPSARIPSLRYAFVVGDALTRRHVARLYAVAPHITCVNLYGSTETQRAVSYFVL--PTA 810
Cdd:PLN02860 262 TSMITVPAMMADLIS-LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLhdPTL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 811 SSTESPASVTALLDKEVIPL------GKGMPGAQILIlneagNLAGIGELGEIYVRSPHLAFGYLDDP-----DQTNERF 879
Cdd:PLN02860 341 ESPKQTLQTVNQTKSSSVHQpqgvcvGKPAPHVELKI-----GLDESSRVGRILTRGPHVMLGYWGQNsetasVLSNDGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 880 LvnpfthqehdrlyRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAY 959
Cdd:PLN02860 416 L-------------DTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVAC 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 960 I-----------THHNEQVKPVLSN--LRAFV-TQRLPAFMVPAHFVFMSR-LPLNANGKVDR 1007
Cdd:PLN02860 483 VrlrdgwiwsdnEKENAKKNLTLSSetLRHHCrEKNLSRFKIPKLFVQWRKpFPLTTTGKIRR 545
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
515-945 |
1.72e-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: 84.83 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGStvlILDPSYPPA--RLLEYVQRaHARGWLRI 592
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGH---ISVPLYPTLnpDTIRYVLE-HSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 EGatdcqELDEW-----------CRANSYCNLVLARNFALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQR 661
Cdd:cd05932 84 VG-----KLDDWkamapgvpeglISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFLPWMRDRFAFTQTDRysLLS--GLAHDPLQREIF-TPLCVGATICIPDQEHMgdpgwLAQWMQGQEITIASFT 738
Cdd:cd05932 159 FGSFAWAAQAGIEHIGTEENDR--MLSylPLAHVTERVFVEgGSLYGGVLVAFAESLDT-----FVEDVQRARPTLFFSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 739 PALLQLLTQGMgEDDLPSARIPSLRYAFVVGdALTRRHVARlyavAPHITCVNLYGS---------TETQRAVSYFVLPT 809
Cdd:cd05932 232 PRLWTKFQQGV-QDKIPQQKLNLLLKIPVVN-SLVKRKVLK----GLGLDQCRLAGCgsapvppalLEWYRSLGLNILEA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 810 ASSTESPA--SVTALLDKEVIPLGKGMPGAQIlilneagnlaGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthq 887
Cdd:cd05932 306 YGMTENFAysHLNYPGRDKIGTVGNAGPGVEV----------RISEDGEILVRSPALMMGYYKDPEATAEAF-------- 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 888 EHDRLYRTGDLGRYLPDGNAEFAGR-NDLQVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:cd05932 368 TADGFLRTGDKGELDADGNLTITGRvKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
513-1010 |
2.60e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 84.54 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQ-GIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEY----------- 580
Cdd:PRK08751 50 TITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQlidsgasvlvv 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 581 -------VQRAHARGWLRIEGATDCQELDEWCRAnSYCNLV------LARNFALSGILSQYAS-------SAPAYRVGPN 640
Cdd:PRK08751 130 idnfgttVQQVIADTPVKQVITTGLGDMLGFPKA-ALVNFVvkyvkkLVPEYRINGAIRFREAlalgrkhSMPTLQIEPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLqrhgpLTHflpwmRDRFAFTQTDRYSLLSGLAHDPLQREIFTPLCV--------------- 705
Cdd:PRK08751 209 DIAFLQYTGGTTGVAKGAM-----LTH-----RNLVANMQQAHQWLAGTGKLEEGCEVVITALPLyhifaltanglvfmk 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 706 --GATICIPDQEHMgdPGWLAQwMQGQEITIASFTPALLQLLTQGMGEDDLPsarIPSLRYAFVVGDALtRRHVARLYAV 783
Cdd:PRK08751 279 igGCNHLISNPRDM--PGFVKE-LKKTRFTAFTGVNTLFNGLLNTPGFDQID---FSSLKMTLGGGMAV-QRSVAERWKQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 784 APHITCVNLYGSTETqravsyfvlptassteSPASVTALLDKEVI--PLGKGMPGAQILILNEAGNLAGIGELGEIYVRS 861
Cdd:PRK08751 352 VTGLTLVEAYGLTET----------------SPAACINPLTLKEYngSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 862 PHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVAD 941
Cdd:PRK08751 416 PQVMKGYWKRPEETAKVM--------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 942 AAVIireDTPDNK--QIVAYIThhneqVK--PVLS--NLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK08751 488 VAAV---GVPDEKsgEIVKVVI-----VKkdPALTaeDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
495-912 |
5.95e-16 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 83.64 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 495 AQQAHLRPENIAIIDEIN-----TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILD 569
Cdd:cd05921 2 AHWARQAPDRTWLAEREGnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 570 PSYPparLL--EYVQRAHARGWLR-----------IEGATDCQELDEWCRANSYcNLVLARN-FALSGILSQ--YASSAP 633
Cdd:cd05921 82 PAYS---LMsqDLAKLKHLFELLKpglvfaqdaapFARALAAIFPLGTPLVVSR-NAVAGRGaISFAELAATppTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 634 AY-RVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGL--AHDPLQREIFTPLCV-GATI 709
Cdd:cd05921 158 AFaAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLpwNHTFGGNHNFNLVLYnGGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 710 CIPDQEHMgdPGWLAQWMQG-QEI-TIASFT-PALLQLLTQGMGEDDLPSAR-IPSLRYAFVVGDALTRRHVARLYAVA- 784
Cdd:cd05921 238 YIDDGKPM--PGGFEETLRNlREIsPTVYFNvPAGWEMLVAALEKDEALRRRfFKRLKLMFYAGAGLSQDVWDRLQALAv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 785 ----PHITCVNLYGSTETQravsyfvlPTASSTESPASVTALldkevipLGKGMPGAQILILNEAGNLagigelgEIYVR 860
Cdd:cd05921 316 atvgERIPMMAGLGATETA--------PTATFTHWPTERSGL-------IGLPAPGTELKLVPSGGKY-------EVRVK 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 861 SPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYL----PDGNAEFAGR 912
Cdd:cd05921 374 GPNVTPGYWRQPELTAQAF--------DEEGFYCLGDAAKLAdpddPAKGLVFDGR 421
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
928-1004 |
6.52e-16 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 74.12 E-value: 6.52e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 928 EIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEqVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGK 1004
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG-VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
468-1010 |
7.81e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 83.35 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 468 STRASSVLP-DPGAPISAHwegtihdLFAQQAHlrPENIAIIDEIN--TVSYGELEARSNQLAHYLHAQ-GIRPHDVVAI 543
Cdd:PLN02574 27 SKHPPVPLPsDPNLDAVSF-------IFSHHNH--NGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVmGVRQGDVVLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 544 SAQRCAALVLAILGILKAGSTVLILDPSYPPARL---------------LEYVQRAHARGwLRIEGATDCQELDEWCRAN 608
Cdd:PLN02574 98 LLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIkkrvvdcsvglaftsPENVEKLSPLG-VPVIGVPENYDFDSKRIEF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 609 SycnlvlarnfALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTH----FLPWMRDRFAFTQTDRY 684
Cdd:PLN02574 177 P----------KFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAmvelFVRFEASQYEYPGSDNV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 685 SL-------LSGLAhdplqreIFTP--LCVGATICIPDQEHMGDpgwLAQWMQGQEITIASFTPALLQLLT---QGMGED 752
Cdd:PLN02574 247 YLaalpmfhIYGLS-------LFVVglLSLGSTIVVMRRFDASD---MVKVIDRFKVTHFPVVPPILMALTkkaKGVCGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 753 DLPSARIPSLRYAfvvgdALTRRHVARLYAVAPHITCVNLYGSTETqravsyfvlpTASSTESPASVTAlldKEVIPLGK 832
Cdd:PLN02574 317 VLKSLKQVSCGAA-----PLSGKFIQDFVQTLPHVDFIQGYGMTES----------TAVGTRGFNTEKL---SKYSSVGL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 833 GMPGAQILILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAG 911
Cdd:PLN02574 379 LAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI--------DKDGWLRTGDIAYFDEDGYLYIVD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 912 RNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQvkpVLS--NLRAFVTQRLPAFMVPA 989
Cdd:PLN02574 451 RLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS---TLSqeAVINYVAKQVAPYKKVR 527
|
570 580
....*....|....*....|.
gi 1574832895 990 HFVFMSRLPLNANGKVDRKAL 1010
Cdd:PLN02574 528 KVVFVQSIPKSPAGKILRREL 548
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
634-1010 |
1.17e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.86 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 634 AYRVGP---NDIACLTFTSGSTGRPKGVLQRHGPL------TH-FL----PWM----RDRFAFTQTDRYSLLSGlahdpl 695
Cdd:PRK07824 26 ALRVGEpidDDVALVVATSGTTGTPKGAMLTAAALtasadaTHdRLggpgQWLlalpAHHIAGLQVLVRSVIAG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 696 qreiFTPLCVgaticipDQEHMGDPGWLAQWMQ--GQEITIASFTPAllQLLtQGMGEddlpSARIPSLRY--AFVVGDA 771
Cdd:PRK07824 100 ----SEPVEL-------DVSAGFDPTALPRAVAelGGGRRYTSLVPM--QLA-KALDD----PAATAALAEldAVLVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 772 LTRRHVARlYAVAPHITCVNLYGSTETQRAVSYfvlptasstespasvtallDkeviplGKGMPGAQILILNeagnlagi 851
Cdd:PRK07824 162 PAPAPVLD-AAAAAGINVVRTYGMSETSGGCVY-------------------D------GVPLDGVRVRVED-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 852 gelGEIYVRSPHLAFGY--LDDPDqtnerflvnPFThqEHDrLYRTGDLGRyLPDGNAEFAGRNDLQVKIRGYRIELEEI 929
Cdd:PRK07824 208 ---GRIALGGPTLAKGYrnPVDPD---------PFA--EPG-WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 930 EAILVEHPMVADAAVIireDTPDNK--QIVAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:PRK07824 272 EAALATHPAVADCAVF---GLPDDRlgQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDR 348
|
...
gi 1574832895 1008 KAL 1010
Cdd:PRK07824 349 RAL 351
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
6-362 |
1.89e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.29 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 6 QRLAALSPEKRALLKQQlgkQGSRFNTFPLSFAQQRLWLLDQlnPGNASYNIAAAIRFAGPLRVDLLEKCIHLLVRRHES 85
Cdd:PRK12467 2157 QSLAAVAQEGDGTVSID---QGPVTGDLPLLPIQQMFFADDI--PERHHWNQSVLLEPREALDAELLEAALQALLVHHDA 2231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 86 LRTTFAMLNGE-------PIQVIRPnLTLQIPLIDLTSLpeaereaslqHAINNEAHIPFDLKTGPLVRLALLRKSPLEH 158
Cdd:PRK12467 2232 LRLGFVQEDGGwsamhraPEQERRP-LLWQVVVADKEEL----------EALCEQAQRSLDLEEGPLLRAVLATLPDGSQ 2300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 159 ILLLNTHHIISDGWSLGVFLHELSLCYSAALAGNSPTLPAPSLQYADYAAWQRNWLKGENLTNLLDYWRKQLADMPplLE 238
Cdd:PRK12467 2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGAS--TE 2378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 239 LPMDHPRPAVQTSHGAVVSLLLPSEISTAL----KALSQHEGVTLFMTTLALfqiLLQRYTGRRDIVIGTPIANR----N 310
Cdd:PRK12467 2379 LPCDHPQGGLQRRHAASVTTHLDSEWTRRLlqeaPAAYRTQVNDLLLTALAR---VIARWTGQASTLIQLEGHGRedlfD 2455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 311 RTDIEHVFGFFVNTLVLRIDVASELNfrTLLQRVKEMtLEAYAHQDIPFDAL 362
Cdd:PRK12467 2456 EIDLTRTVGWFTSLYPVKLSPTASLA--TSIKTIKEQ-LRAVPNKGLGFGVL 2504
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
513-945 |
3.12e-15 |
|
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: 80.87 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLIldpsypparlleyvqrahaRGwlri 592
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV-------------------RG---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 eGATDCQELdEWCRANSYCNLVLARNfalsgilsqyassapayrvGPNDIACLTFTSGSTGRPKGVLQRHGPLTHflpWM 672
Cdd:cd17640 62 -SDSSVEEL-LYILNHSESVALVVEN-------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLH---QI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 673 RDRFAFTQT---DRYSLLSGLAHdPLQR--EIFTPLCVGATIC--IPdqeHMGDPgwLAQWmqgQEITIASfTPALLQLL 745
Cdd:cd17640 118 RSLSDIVPPqpgDRFLSILPIWH-SYERsaEYFIFACGCSQAYtsIR---TLKDD--LKRV---KPHYIVS-VPRLWESL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 746 TQGMGEDDLPSARIPS-LRYAFVVGD----------ALTRrHVARLY-AVAPHItcVNLYGSTETqravsyfvlptasst 813
Cdd:cd17640 188 YSGIQKQVSKSSPIKQfLFLFFLSGGifkfgisgggALPP-HVDTFFeAIGIEV--LNGYGLTET--------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 814 eSPASVTALLDKEVI-PLGKGMPGAQILILNEAGN-LAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDR 891
Cdd:cd17640 250 -SPVVSARRLKCNVRgSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL--------DSDG 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 892 LYRTGDLGRYLPDGNAEFAGR-NDLQVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:cd17640 321 WFNTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1624-1860 |
3.22e-15 |
|
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: 80.58 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLLLTHEElkarwphcpcpllcldtlqeryaslpcedlqeacspaQLAYVIYTSGSTGRPKGVQISH-GALLSFLLS 1782
Cdd:cd05919 81 CEARLVVTSAD-------------------------------------DIAYLLYSSGTTGPPKGVMHAHrDPLLFADAM 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1783 LQSLLSLSPHDRWLAITSISFDIA-GLELYLPLLAGAQIQLASqeQASDPRQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:cd05919 124 AREALGLTPGDRVFSSAKMFFGYGlGNSLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSC 200
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
809-1096 |
4.31e-15 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 78.25 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 809 TASSTESPASVTALLDKEVIPLGKgmPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLddpdQTNERFLVNPFTHQE 888
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAI--VQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIR----LLAAAARAPFIPVPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 889 HDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVK 968
Cdd:COG3433 75 PAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 969 PVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPeAADEATLSLATPQSPIQEELCLLWCELLGLK--- 1045
Cdd:COG3433 155 GLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPAL-AAAEALLAAASPAPALETALTEEELRADVAEllg 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1046 ----KVGITQNFFELGGHSLLATQLLARInEKFNSTLSLRSLFEAPTIEGIASLI 1096
Cdd:COG3433 234 vdpeEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALL 287
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
510-944 |
4.47e-15 |
|
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: 80.86 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 510 EINTVSYGELEARSNQLAHYL-HAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARG 588
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 589 WLRIEG---ATDCQELDEWCRANSYCNLVLARNFALSGILSQYAS----SAPAYRVGPNDIACLTFTSGSTGRPKGVLQR 661
Cdd:cd05905 91 ALTVEAclkGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 662 HGPLTHFlpwMRDRFAFTQTDRYSLL---------SGLAHDPLQrEIFTplcvGATICIPDQEHMGDPGWLaqWMQGQEI 732
Cdd:cd05905 171 HSSLLAH---CRALKEACELYESRPLvtvldfksgLGLWHGCLL-SVYS----GHHTILIPPELMKTNPLL--WLQTLSQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 733 TIASFTPALLQLLTQGMgeDDLPS------ARIP---SLRYAFVVGD-----ALTRRHVARLYAVAPHITCVnlygSTET 798
Cdd:cd05905 241 YKVRDAYVKLRTLHWCL--KDLSStlaslkNRDVnlsSLRMCMVPCEnrpriSSCDSFLKLFQTLGLSPRAV----STEF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 799 QRAVSYFvlPTASSTESPASVTALLDK-----EVIPL--------------GKGMPGAQILILNEAG-NLAGIGELGEIY 858
Cdd:cd05905 315 GTRVNPF--ICWQGTSGPEPSRVYLDMralrhGVVRLderdkpnslplqdsGKVLPGAQVAIVNPETkGLCKDGEIGEIW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 859 VRSPHLAFGY--LDDP-DQTNERFLVNPFTHQEHDRLY-RTGDLG--RYLPDGNAEFAGRNDLQVK--------IRGYRI 924
Cdd:cd05905 393 VNSPANASGYflLDGEtNDTFKVFPSTRLSTGITNNSYaRTGLLGflRPTKCTDLNVEEHDLLFVVgsidetleVRGLRH 472
|
490 500
....*....|....*....|.
gi 1574832895 925 ELEEIEA-ILVEHPMVADAAV 944
Cdd:cd05905 473 HPSDIEAtVMRVHPYRGRCAV 493
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
512-968 |
5.61e-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: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 512 NTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARgwlr 591
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 592 iegatdcqeldewcransycnLVLARNfalsgilsqyassapayrvgPNDIACLTFTSGSTGRPKGVLqrhgpLTHFLPW 671
Cdd:cd05914 82 ---------------------AIFVSD--------------------EDDVALINYTSGTTGNSKGVM-----LTYRNIV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 672 MRDRFAF-----TQTDRYSLLSGLAHD-PLQREIFTPLCVGATICIPDQEhmgdPGWLAQWMQGQEITIASFTPALLQLL 745
Cdd:cd05914 116 SNVDGVKevvllGKGDKILSILPLHHIyPLTFTLLLPLLNGAHVVFLDKI----PSAKIIALAFAQVTPTLGVPVPLVIE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 746 TQGMgEDDLPSARIPSLRYA----------------------------FVVGDALTRRHVAR-LYAVAphITCVNLYGST 796
Cdd:cd05914 192 KIFK-MDIIPKLTLKKFKFKlakkinnrkirklafkkvheafggnikeFVIGGAKINPDVEEfLRTIG--FPYTIGYGMT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 797 ETQRAVSYfvlpTASSTESPASVtalldkeviplGKGMPGAQILILNEAGNlagiGELGEIYVRSPHLAFGYLDDPDQTN 876
Cdd:cd05914 269 ETAPIISY----SPPNRIRLGSA-----------GKVIDGVEVRIDSPDPA----TGEGEIIVRGPNVMKGYYKNPEATA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 877 ERFLVNPFthqehdrlYRTGDLGRYLPDGNAEFAGR-NDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREdtpDNKQ 955
Cdd:cd05914 330 EAFDKDGW--------FHTGDLGKIDAEGYLYIRGRkKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQE---KKLV 398
|
490
....*....|...
gi 1574832895 956 IVAYITHHNEQVK 968
Cdd:cd05914 399 ALAYIDPDFLDVK 411
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1752-1875 |
5.76e-15 |
|
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: 78.48 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1752 QLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLAsqeQASDP 1831
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL---PKFDP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1574832895 1832 RQLASLLAQLPISILQATPTTWQLLLETGWSGKAGL----TLLSGAKP 1875
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLsslrALVSGGAP 125
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
513-1010 |
6.92e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 80.19 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYL-HAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLR 591
Cdd:PRK05677 49 TLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 592 IEGATDCQE-------------------LDEWCRA--NSYCNLV--------LARNFALSGILSQYA--SSAPAyRVGPN 640
Cdd:PRK05677 129 LANMAHLAEkvlpktgvkhvivtevadmLPPLKRLliNAVVKHVkkmvpayhLPQAVKFNDALAKGAgqPVTEA-NPQAD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 641 DIACLTFTSGSTGRPKGVLqrhgpLTHflpwmRDRFA-FTQTDrySLLSGLAHDPLQREI----------FTPLCV---- 705
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAM-----LTH-----RNLVAnMLQCR--ALMGSNLNEGCEILIaplplyhiyaFTFHCMamml 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 706 --GATICIPDQEHMgdPGW---LAQWMQGQEITIASFTPALLQlltqgmgEDDLPSARIPSLRYAFVVGDALTRRHVARL 780
Cdd:PRK05677 276 igNHNILISNPRDL--PAMvkeLGKWKFSGFVGLNTLFVALCN-------NEAFRKLDFSALKLTLSGGMALQLATAERW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 781 YAVAPHITCVNlYGSTETqravsyfvlptassteSP-ASVTALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYV 859
Cdd:PRK05677 347 KEVTGCAICEG-YGMTET----------------SPvVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 860 RSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMV 939
Cdd:PRK05677 410 KGPQVMKGYWQRPEATDEIL--------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 940 ADAAVIIREDTPDNKQIVAYIThhneqVKP----VLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK05677 482 LQCAAIGVPDEKSGEAIKVFVV-----VKPgetlTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
632-1019 |
9.86e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 79.34 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 632 APAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFTP-LCVGATIC 710
Cdd:PRK07867 144 PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 711 I----------PDQEHMGdpgwlaqwmqgqeITIASFTPALLQLLtqgMGEDDLPSARIPSLRYAFvvGDALTRRHVARl 780
Cdd:PRK07867 224 LrrkfsasgflPDVRRYG-------------ATYANYVGKPLSYV---LATPERPDDADNPLRIVY--GNEGAPGDIAR- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 781 YAVAPHITCVNLYGSTETQRAVSYFVLPTASSTESPASVTALLDKEViplGKGMPGAQILILNEAGNLAGIGELgeIYVR 860
Cdd:PRK07867 285 FARRFGCVVVDGFGSTEGGVAITRTPDTPPGALGPLPPGVAIVDPDT---GTECPPAEDADGRLLNADEAIGEL--VNTA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 861 SPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVA 940
Cdd:PRK07867 360 GPGGFEGYYNDPEADAERM---------RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 941 DAAVIIREDTPDNKQIVAYIthhneqvkpVLSNLRAFVTQRLPAF----------MVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK07867 431 EVAVYAVPDPVVGDQVMAAL---------VLAPGAKFDPDAFAEFlaaqpdlgpkQWPSYVRVCAELPRTATFKVLKRQL 501
|
....*....
gi 1574832895 1011 PApEAADEA 1019
Cdd:PRK07867 502 SA-EGVDCA 509
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1634-1860 |
1.93e-14 |
|
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: 77.93 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHE 1713
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1714 ELKARwphcpcpllcldtlqeryaslpcedlqeaCSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHD 1793
Cdd:cd05969 81 ELYER-----------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 1794 R-WLA-----ITSISFDIAGlelylPLLAGAQIqlASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETG 1860
Cdd:cd05969 132 IyWCTadpgwVTGTVYGIWA-----PWLNGVTN--VVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEG 197
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1631-1773 |
3.28e-14 |
|
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: 77.64 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1631 STTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLL 1710
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1711 THEELKAR----------------------WPHCPCPLLClDTLQERYASLPcEDLQEacSPAQLAYVIYTSGSTGRPKG 1768
Cdd:cd05911 88 TDPDGLEKvkeaakelgpkdkiivlddkpdGVLSIEDLLS-PTLGEEDEDLP-PPLKD--GKDDTAAILYSSGTTGLPKG 163
|
....*
gi 1574832895 1769 VQISH 1773
Cdd:cd05911 164 VCLSH 168
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1633-1775 |
3.56e-14 |
|
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: 77.66 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGiGPGCLVGL--------------CLHRspslllcllailktGAAYVPLDPDYPSQ--- 1695
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLlappgldfvaaflgCLYA--------------GAIAVPLPPPTPGRhae 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1696 RLLWMAQDAQLSLLLTHEELKA---RWPHCPC-----PLLCLDTLQERYASLPCEDlqeACSPAQLAYVIYTSGSTGRPK 1767
Cdd:cd05931 89 RLAAILADAGPRVVLTTAAALAavrAFAASRPaagtpRLLVVDLLPDTSAADWPPP---SPDPDDIAYLQYTSGSTGTPK 165
|
....*...
gi 1574832895 1768 GVQISHGA 1775
Cdd:cd05931 166 GVVVTHRN 173
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
637-936 |
5.34e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 77.16 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 637 VGPNDIACLTFTSGSTGRPKGVlqrhgPLTH------------------------FLPWMRdRFAFTQTDRYSLLSGL-- 690
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGV-----PLTHanllanqraclkffspkeddvmmsFLPPFH-AYGFNSCTLFPLLSGVpv 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 691 --AHDPLQreiftplcvgaticipdqehmgdPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDlpsARIPSLRYAFVV 768
Cdd:PRK06334 254 vfAYNPLY-----------------------PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQE---SCLPSLRFVVIG 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 769 GDALT---RRHVARLYavaPHITCVNLYGSTETQRAVsyfvlpTASSTESPASVTALldkeviplgkGMP--GAQILILN 843
Cdd:PRK06334 308 GDAFKdslYQEALKTF---PHIQLRQGYGTTECSPVI------TINTVNSPKHESCV----------GMPirGMDVLIVS 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 844 EAGNL-AGIGELGEIYVRSPHLAFGYL-DDPDQTnerflvnpFTHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRG 921
Cdd:PRK06334 369 EETKVpVSSGETGLVLTRGTSLFSGYLgEDFGQG--------FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGA 440
|
330
....*....|....*
gi 1574832895 922 YRIELEEIEAILVEH 936
Cdd:PRK06334 441 EMVSLEALESILMEG 455
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1625-1859 |
5.50e-14 |
|
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: 76.56 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAH-LLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANrLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLLLtheelkarwphcpcpllcldtlqeryaslpcedlqeacspaQLAYVIYTSGSTGRPKGVQISHGALLSFLLSL 1783
Cdd:cd05941 83 SEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 1784 QSLLSLSPHDRWLAITSIsFDIAGLELYL--PLLAGAQIQLASQeqaSDPRQLASLLAQLPISILQATPTTWQLLLET 1859
Cdd:cd05941 122 VDAWRWTEDDVLLHVLPL-HHVHGLVNALlcPLFAGASVEFLPK---FDPKEVAISRLMPSITVFMGVPTIYTRLLQY 195
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
509-905 |
5.79e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 76.96 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 509 DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARg 588
Cdd:PRK07768 25 DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 589 wLRIEGATDCQELDEWcransycnLVLARNFALSGI----LSQYASSAPAYRV--GPNDIACLTFTSGSTGRPKGVLQRH 662
Cdd:PRK07768 104 -IGMIGAKAVVVGEPF--------LAAAPVLEEKGIrvltVADLLAADPIDPVetGEDDLALMQLTSGSTGSPKAVQITH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 663 GPLTHFLPWMRDRFAFT-QTDRysLLSGLA--HD-PLQREIFTPLCVGAT-ICIPDQEHMGDPgwlAQWMQ-----GQEI 732
Cdd:PRK07768 175 GNLYANAEAMFVAAEFDvETDV--MVSWLPlfHDmGMVGFLTVPMYFGAElVKVTPMDFLRDP---LLWAEliskyRGTM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 733 TIA-SFTPALL-QLLTQGM--GEDDLpsariPSLRYAFVVGDALTRRHVARLYAV-APH------ITCVnlYGSTETQRA 801
Cdd:PRK07768 250 TAApNFAYALLaRRLRRQAkpGAFDL-----SSLRFALNGAEPIDPADVEDLLDAgARFglrpeaILPA--YGMAEATLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 802 VSYFVLPTASSTESPAS-----------VTALLDKEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLd 870
Cdd:PRK07768 323 VSFSPCGAGLVVDEVDAdllaalrravpATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL- 401
|
410 420 430
....*....|....*....|....*....|....*
gi 1574832895 871 DPDqtnerflvNPFTHQEHDRLYRTGDLGrYLPDG 905
Cdd:PRK07768 402 TMD--------GFIPAQDADGWLDTGDLG-YLTEE 427
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1633-1859 |
1.55e-13 |
|
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: 75.11 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTH 1712
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1713 EELKarwphcpcpllcldtlQERYASLPcedlqeacspAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPH 1792
Cdd:cd05903 81 ERFR----------------QFDPAAMP----------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 1793 DRWLAITSISFDIAGLE-LYLPLLAGAQIQLasqEQASDPRQLASLLAQLPISILQATPTTWQLLLET 1859
Cdd:cd05903 135 DVFLVASPMAHQTGFVYgFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
450-1010 |
2.06e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 75.40 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 450 LASQVSERDEMISRyslvSTRASSVLPDpgapisahwEGTIHDLFAQQAHLRPENIAIIDEIN--TVSYGELEARSNQLA 527
Cdd:PLN02330 3 MEIQKQEDNEHIFR----SRYPSVPVPD---------KLTLPDFVLQDAELYADKVAFVEAVTgkAVTYGEVVRDTRRFA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 528 HYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARG-------WLRIEG-ATDCQ 599
Cdd:PLN02330 70 KALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLivtndtnYGKVKGlGLPVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 600 ELDEWCRANS--YCNLVLArnfalsgilSQYASSAPAYR-VGPNDIACLTFTSGSTGRPKGVLqrhgpLTHflpwmRDRF 676
Cdd:PLN02330 150 VLGEEKIEGAvnWKELLEA---------ADRAGDTSDNEeILQTDLCALPFSSGTTGISKGVM-----LTH-----RNLV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 677 AFTQTDRYSLLSGLAHDPLQREIFTPLCV-GAT-ICIPDQEHMGDPGWLAQW--------MQGQEITIASFTPALLQLLT 746
Cdd:PLN02330 211 ANLCSSLFSVGPEMIGQVVTLGLIPFFHIyGITgICCATLRNKGKVVVMSRFelrtflnaLITQEVSFAPIVPPIILNLV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 747 QG--MGEDDLPSARIPSLRYAfvvGDALTRRHVARLYAVAPHITCVNLYGSTETqravSYFVLptasSTESPASVTALLD 824
Cdd:PLN02330 291 KNpiVEEFDLSKLKLQAIMTA---AAPLAPELLTAFEAKFPGVQVQEAYGLTEH----SCITL----THGDPEKGHGIAK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 825 KEVIplGKGMPGAQILILN-EAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHqehdrlyrTGDLGRYLP 903
Cdd:PLN02330 360 KNSV--GFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLH--------TGDIGYIDD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 904 DGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIireDTPDNK--QIVAYITHHNEQVKPVLSNLRAFVTQR 981
Cdd:PLN02330 430 DGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVV---PLPDEEagEIPAACVVINPKAKESEEDILNFVAAN 506
|
570 580
....*....|....*....|....*....
gi 1574832895 982 LPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PLN02330 507 VAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1610-1769 |
2.10e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 75.31 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERsslqPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:PRK07798 9 FEAVADAVPDR----VALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLLTH-------EELKARWPHcpcpllcLDTL---------QERYASLPCEDLQEACSPAQL 1753
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALVYErefaprvAEVLPRLPK-------LRTLvvvedgsgnDLLPGAVDYEDALAAGSPERD 157
|
170 180
....*....|....*....|....
gi 1574832895 1754 A--------YVIYTSGSTGRPKGV 1769
Cdd:PRK07798 158 FgerspddlYLLYTGGTTGMPKGV 181
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1632-1854 |
1.03e-12 |
|
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: 72.63 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1632 TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLt 1711
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1712 heelkarwphcpcpllcldtlqeryaslpCEDlqeacsPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSP 1791
Cdd:cd05907 83 -----------------------------VED------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 1792 HDR---WLAITSISFDIAGleLYLPLLAGAQIQLasqeqASDPRQLASLLAQLPISILQATPTTWQ 1854
Cdd:cd05907 128 GDRhlsFLPLAHVFERRAG--LYVPLLAGARIYF-----ASSAETLLDDLSEVRPTVFLAVPRVWE 186
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1618-1775 |
1.23e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.60 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1618 CERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPsqrl 1697
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP---- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1698 lwmaqDAQLSLLLTHEELKARWPHCPCP-LLCLDTLQERYASLPCEDlqeACSPAQLAYVIYTSGSTGRPKGVQISHGA 1775
Cdd:PRK09029 89 -----QPLLEELLPSLTLDFALVLEGENtFSALTSLHLQLVEGAHAV---AWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1612-1875 |
1.70e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 72.33 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1612 HLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPD 1691
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1692 YPSQRLLWMAQDAQLSLLLTH--------EELKARWP-------HCPCPLLC-LDTLQERYASLPCEDlqeACSPAQLAY 1755
Cdd:PRK06188 96 GSLDDHAYVLEDAGISTLIVDpapfveraLALLARVPslkhvltLGPVPDGVdLLAAAAKFGPAPLVA---AALPPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1756 VIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFdiAGLELYLP-LLAGAQIQLAsqeQASDPRQL 1834
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH--AGGAFFLPtLLRGGTVIVL---AKFDPAEV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1574832895 1835 ASLLAQLPISILQATPTTWQLLLETGWSGKAGL----TLLSGAKP 1875
Cdd:PRK06188 248 LRAIEEQRITATFLVPTMIYALLDHPDLRTRDLssleTVYYGASP 292
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1606-1774 |
2.51e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 72.21 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1606 PSCGLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGA-- 1683
Cdd:PRK08279 35 SKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1684 --------------------------------AYVPLDPDYPSQRLLWMAQDAQLSLLLTHEELKArwphcpcpllCLDT 1731
Cdd:PRK08279 115 allntqqrgavlahslnlvdakhlivgeelveAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAA----------AAAG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1574832895 1732 lqeryASLPCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:PRK08279 185 -----APTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHM 222
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
620-1012 |
3.66e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 71.21 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 620 ALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREI 699
Cdd:PRK13388 130 AYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 700 FTP-LCVGATICIPDqeHMGDPGWLAQWmqgQEITIASFT---PALLQLLTQGMGEDDlpsARIPsLRYAFvvGD----- 770
Cdd:PRK13388 210 WAPaVASGAAVALPA--KFSASGFLDDV---RRYGATYFNyvgKPLAYILATPERPDD---ADNP-LRVAF--GNeaspr 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 771 ---ALTRRHVARLYavaphitcvNLYGSTETqrAVSYFVLPTAsstesPASVtalldkevipLGKGMPGAQIL------- 840
Cdd:PRK13388 279 diaEFSRRFGCQVE---------DGYGSSEG--AVIVVREPGT-----PPGS----------IGRGAPGVAIYnpetlte 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 841 ----ILNEAGNLAGIGE-LGEIYVRSPHLAF-GYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRND 914
Cdd:PRK13388 333 cavaRFDAHGALLNADEaIGELVNTAGAGFFeGYYNNPEATAERM---------RHGMYWSGDLAYRDADGWIYFAGRTA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 915 LQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYIthhneqvkpVLSNLRAFVTQRLPAFMV------- 987
Cdd:PRK13388 404 DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAAL---------VLRDGATFDPDAFAAFLAaqpdlgt 474
|
410 420
....*....|....*....|....*...
gi 1574832895 988 ---PAHFVFMSRLPLNANGKVDRKALPA 1012
Cdd:PRK13388 475 kawPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1624-1857 |
4.27e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 71.09 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:PRK07656 21 KEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILAR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLLLTH-------EELKARWPHCPCPLLClDTLQERYASLPCEDLQEACSPAQLAY------------VIYTSGSTG 1764
Cdd:PRK07656 101 GDAKALFVLglflgvdYSATTRLPALEHVVIC-ETEEDDPHTEKMKTFTDFLAAGDPAErapevdpddvadILFTSGTTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1765 RPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSIsFDIAGLELYL--PLLAGAQIQLASQeqaSDPRQLASLLAQLP 1842
Cdd:PRK07656 180 RPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLPV---FDPDEVFRLIETER 255
|
250
....*....|....*
gi 1574832895 1843 ISILQATPTTWQLLL 1857
Cdd:PRK07656 256 ITVLPGPPTMYNSLL 270
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1624-1856 |
6.38e-12 |
|
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: 70.62 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRllwmaQD 1703
Cdd:cd17647 11 PSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR-----QN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLlltheelkARwphcPCPLLCLdtlqeryaslpcEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSL 1783
Cdd:cd17647 86 IYLGV--------AK----PRGLIVI------------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 1784 QSLLSLSPHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEQASDPRQLASLLAQLPISILQATPTTWQLL 1856
Cdd:cd17647 142 AKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLL 214
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
854-1010 |
6.56e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 70.82 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 854 LGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLyRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAIL 933
Cdd:PLN03102 392 MGEIVIKGSSIMKGYLKNPKATSEAF--------KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 934 VEHPMVADAAVIIREDTPDNKQIVAYI------THHNEQVKPVLS---NLRAFVTQRLPAFMVPAHFVFMSRLPLNANGK 1004
Cdd:PLN03102 463 YKYPKVLETAVVAMPHPTWGETPCAFVvlekgeTTKEDRVDKLVTrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGK 542
|
....*.
gi 1574832895 1005 VDRKAL 1010
Cdd:PLN03102 543 ILKPKL 548
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
890-1016 |
8.21e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 69.68 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 890 DRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDtPDNKQIVA--YITHHneQV 967
Cdd:PRK08308 290 DKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKD-PVAGERVKakVISHE--EI 366
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1574832895 968 KPVlsNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALPAPEAA 1016
Cdd:PRK08308 367 DPV--QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVT 413
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1635-1773 |
1.64e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 68.86 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1635 TYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLThee 1714
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1715 lkarwphcpcpllcldtlqeryaslpcedlqeacspaQLAYVIYTSGSTGRPKGVQISH 1773
Cdd:cd05934 82 -------------------------------------DPASILYTSGTTGPPKGVVITH 103
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
637-1010 |
2.65e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.18 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 637 VGPNDIACLTFTSGSTGRPKGVLqrhgpLTHF-----LPWMRDRFAFTQTDRysLLSGLahdP------LQREIFTPLCV 705
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVM-----LSHHnilsnIEQISDVFNLRNDDV--ILSSL---PffhsfgLTVTLWLPLLE 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 706 G-ATICIPDQEhmgDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPSAripSLRYAfVVGDALTRRHVARLYAVA 784
Cdd:PRK08633 849 GiKVVYHPDPT---DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFA---SLRLV-VAGAEKLKPEVADAFEEK 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 785 PHITCVNLYGSTETQravsyfvlPTASstespASVTALLDKEVIPL--------GKGMPGAQILILN-EAGNLAGIGELG 855
Cdd:PRK08633 922 FGIRILEGYGATETS--------PVAS-----VNLPDVLAADFKRQtgskegsvGMPLPGVAVRIVDpETFEELPPGEDG 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 856 EIYVRSPHLAFGYLDDPDQTNErflvnPFTHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGY-----RIELEEIE 930
Cdd:PRK08633 989 LILIGGPQVMKGYLGDPEKTAE-----VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEmvplgAVEEELAK 1063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 931 AILVEHPMVADAAViiredtPDNK---QIVAYITHHNEQVkpvlSNLRAFVTQ-RLPAFMVPAHFVFMSRLPLNANGKVD 1006
Cdd:PRK08633 1064 ALGGEEVVFAVTAV------PDEKkgeKLVVLHTCGAEDV----EELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
....
gi 1574832895 1007 RKAL 1010
Cdd:PRK08633 1134 LKGL 1137
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
640-1012 |
3.43e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 68.44 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 640 NDIACLTFTSGSTGRPKGVlQRH--GPLTHFLPWMRDRFA-------FTQTDrysllSGLA--HDPLqreIFTPLCVG-A 707
Cdd:PRK10524 233 NEPSYILYTSGTTGKPKGV-QRDtgGYAVALATSMDTIFGgkagetfFCASD-----IGWVvgHSYI---VYAPLLAGmA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 708 TICIPDQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQgMGEDDLPSARIPSLRYAFVVGDALTRrHVARLYAVAPHI 787
Cdd:PRK10524 304 TIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKK-QDPALLRKHDLSSLRALFLAGEPLDE-PTASWISEALGV 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 788 TCVNLYGSTET-------QRAVSyfvlPTASSTESPasvtalldkeviplGKGMPGAQILILNEA-GNLAGIGELGEIYV 859
Cdd:PRK10524 382 PVIDNYWQTETgwpilaiARGVE----DRPTRLGSP--------------GVPMYGYNVKLLNEVtGEPCGPNEKGVLVI 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 860 RSPhLAFGYL-----DDpdqtnERFLVNPFTHQEHdRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILV 934
Cdd:PRK10524 444 EGP-LPPGCMqtvwgDD-----DRFVKTYWSLFGR-QVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESIS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 935 EHPMVADAAVIIREDTPDNKQIVAYI-------THHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:PRK10524 517 SHPAVAEVAVVGVKDALKGQVAVAFVvpkdsdsLADREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
....*
gi 1574832895 1008 KALPA 1012
Cdd:PRK10524 597 RAIQA 601
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1620-1769 |
3.53e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.18 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1620 RSSLQPALHAGST--TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRL 1697
Cdd:PRK13391 9 TTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1698 LWMAQDAQLSLLLT---HEELKARWP-HCPCPLLCL----DTLQERYASLpcEDLQEACSPAQLA------YVIYTSGST 1763
Cdd:PRK13391 89 AYIVDDSGARALITsaaKLDVARALLkQCPGVRHRLvldgDGELEGFVGY--AEAVAGLPATPIAdeslgtDMLYSSGTT 166
|
....*.
gi 1574832895 1764 GRPKGV 1769
Cdd:PRK13391 167 GRPKGI 172
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1629-1773 |
4.44e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 67.79 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1629 AGST-TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLS 1707
Cdd:PRK08008 32 GGVVrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1708 LLLTHEE-------LKARWPHCPCPLLCLDT----------LQERYASLPCE-DLQEACSPAQLAYVIYTSGSTGRPKGV 1769
Cdd:PRK08008 112 LLVTSAQfypmyrqIQQEDATPLRHICLTRValpaddgvssFTQLKAQQPATlCYAPPLSTDDTAEILFTSGTTSRPKGV 191
|
....
gi 1574832895 1770 QISH 1773
Cdd:PRK08008 192 VITH 195
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1624-1858 |
4.67e-11 |
|
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: 67.72 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTT--LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMA 1701
Cdd:cd05926 3 APALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1702 QDAQLSLLLT-----HEELKARwPHCPCPLLCL------DTLQERYASLP-CEDLQEACS------PAQLAYVIYTSGST 1763
Cdd:cd05926 83 ADLGSKLVLTpkgelGPASRAA-SKLGLAILELaldvgvLIRAPSAESLSnLLADKKNAKsegvplPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1764 GRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSIsFDIAGL--ELYLPLLAGAQIQLASQEQASDprqLASLLAQL 1841
Cdd:cd05926 162 GRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHGLvaSLLSTLAAGGSVVLPPRFSAST---FWPDVRDY 237
|
250
....*....|....*..
gi 1574832895 1842 PISILQATPTTWQLLLE 1858
Cdd:cd05926 238 NATWYTAVPTIHQILLN 254
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1620-1858 |
5.61e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 67.29 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1620 RSSLQP---ALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQR 1696
Cdd:PRK03640 11 RAFLTPdrtAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1697 LLWMAQDAQLSLLLTHEELKARwpHCPCPLLCLDTLQEryasLPCED--LQEACSPAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAK--LIPGISVKFAELMN----GPKEEaeIQEEFDLDEVATIMYTSGTTGKPKGVIQTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1775 ALLSFLLSLQSLLSLSPHDRWLAITSIsFDIAGLELYL-PLLAGAQIQLasqEQASDPRQLASLLAQLPISILQATPTTW 1853
Cdd:PRK03640 165 NHWWSAVGSALNLGLTEDDCWLAAVPI-FHISGLSILMrSVIYGMRVVL---VEKFDAEKINKLLQTGGVTIISVVSTML 240
|
....*
gi 1574832895 1854 QLLLE 1858
Cdd:PRK03640 241 QRLLE 245
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
854-1012 |
6.20e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.56 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 854 LGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAIL 933
Cdd:PLN02479 402 MGEIVMRGNMVMKGYLKNPKANEEAF---------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 934 VEHPMVADAAVIIREDTPDNKQIVAYIT------HHNEQVkpVLSNLRAFVTQRLPAFMVPAHFVFmSRLPLNANGKVDR 1007
Cdd:PLN02479 473 YTHPAVLEASVVARPDERWGESPCAFVTlkpgvdKSDEAA--LAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQK 549
|
....*
gi 1574832895 1008 KALPA 1012
Cdd:PLN02479 550 HVLRA 554
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1625-1775 |
9.52e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 66.88 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDpdypsqrllWMAQDA 1704
Cdd:PRK08316 28 TALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN---------FMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTH----------------EELKARWPHCPCPLLCLDTLQERYAS-LPCEDLQEACSPA---------QLAYVIY 1758
Cdd:PRK08316 99 ELAYILDHsgaraflvdpalaptaEAALALLPVDTLILSLVLGGREAPGGwLDFADWAEAGSVAepdveladdDLAQILY 178
|
170
....*....|....*..
gi 1574832895 1759 TSGSTGRPKGVQISHGA 1775
Cdd:PRK08316 179 TSGTESLPKGAMLTHRA 195
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
513-1026 |
1.19e-10 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 66.84 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYV----------Q 582
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIvdckpkvvitC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 583 RAHARG--WLRIEGATDCQeLDEWCRANSYCNLVLA-----------------RNFALSGILSQYASSAPAYRVGPNDIA 643
Cdd:PLN02654 200 NAVKRGpkTINLKDIVDAA-LDESAKNGVSVGICLTyenqlamkredtkwqegRDVWWQDVVPNYPTKCEVEWVDAEDPL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 644 CLTFTSGSTGRPKGVLQRHGP-LTHFLPWMRDRFAFTQTDRY------SLLSGLAHdplqrEIFTPLCVGATICIPD-QE 715
Cdd:PLN02654 279 FLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYwctadcGWITGHSY-----VTYGPMLNGATVLVFEgAP 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 716 HMGDPGWLAQWMQGQEITIASFTPALLQLLtqgMGEDDLPSARIP--SLRYAFVVGDALTRRHVARLYAVAPHITC--VN 791
Cdd:PLN02654 354 NYPDSGRCWDIVDKYKVTIFYTAPTLVRSL---MRDGDEYVTRHSrkSLRVLGSVGEPINPSAWRWFFNVVGDSRCpiSD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 792 LYGSTETQravSYFVLPTASS-TESPASVTalldkeviplgkgMP--GAQILILNEAGNLAGiGEL-GEIYVRS--PHlA 865
Cdd:PLN02654 431 TWWQTETG---GFMITPLPGAwPQKPGSAT-------------FPffGVQPVIVDEKGKEIE-GECsGYLCVKKswPG-A 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 866 FGYLDDPDQTNERFLVNPFTHqehdrLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:PLN02654 493 FRTLYGDHERYETTYFKPFAG-----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVV 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 946 IREDTPDNKQIVAYIT-----HHNEQVKpvlSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP--APEAADE 1018
Cdd:PLN02654 568 GIEHEVKGQGIYAFVTlvegvPYSEELR---KSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRkiASRQLDE 644
|
570
....*....|
gi 1574832895 1019 A--TLSLATP 1026
Cdd:PLN02654 645 LgdTSTLADP 654
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1632-1769 |
1.24e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 66.47 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1632 TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLT 1711
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 1712 HE-------ELKARWPHcPCPLLCLDTLQ-ERYASLpcEDLQEACSPAQLAYVI------YTSGSTGRPKGV 1769
Cdd:PRK08276 90 SAaladtaaELAAELPA-GVPLLLVVAGPvPGFRSY--EEALAAQPDTPIADETagadmlYSSGTTGRPKGI 158
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
513-988 |
1.27e-10 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 66.22 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGStvlildpsypPARLLEYVQRAhargwlri 592
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA----------VAALINYNLRG-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 EGATDCQELdewcransycnlvlarnfalsgilsqyaSSAPAYRVgpnDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWM 672
Cdd:cd05940 65 ESLAHCLNV----------------------------SSAKHLVV---DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 673 RDRFAFTQTDR-YSLLSgLAHDP-LQREIFTPLCVGATICIPDQEHMGDpgwlaQW--MQGQEITIASFTPALLQ-LLTQ 747
Cdd:cd05940 114 AGSGGALPSDVlYTCLP-LYHSTaLIVGWSACLASGATLVIRKKFSASN-----FWddIRKYQATIFQYIGELCRyLLNQ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 748 GMGEDDlpsaRIPSLRYAF-------VVGDALTRRHVARLYavaphitcvNLYGSTETQRA-VSYFVLPTASSTESPASV 819
Cdd:cd05940 188 PPKPTE----RKHKVRMIFgnglrpdIWEEFKERFGVPRIA---------EFYAATEGNSGfINFFGKPGAIGRNPSLLR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 820 TALLDKEViplgKGMPGAQILILNEAGNL--AGIGELGE-IYVRSPHLAF-GYLdDPDQTNERFLVNPFthQEHDRLYRT 895
Cdd:cd05940 255 KVAPLALV----KYDLESGEPIRDAEGRCikVPRGEPGLlISRINPLEPFdGYT-DPAATEKKILRDVF--KKGDAWFNT 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 896 GDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAV--IIREDTPDNKQIVAYITHHNEQVKpvLSN 973
Cdd:cd05940 328 GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQPNEEFD--LSA 405
|
490
....*....|....*
gi 1574832895 974 LRAFVTQRLPAFMVP 988
Cdd:cd05940 406 LAAHLEKNLPGYARP 420
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1610-1774 |
1.47e-10 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 66.05 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSlQPALHAGS-TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPL 1688
Cdd:PRK07514 5 LFDALRAAFADRD-APFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1689 DPDYPSQRLLWMAQDAQLSLLL----THEELKARWPHCPCP-LLCLD-----TLQERYASLPCEDLQEACSPAQLAYVIY 1758
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVcdpaNFAWLSKIAAAAGAPhVETLDadgtgSLLEAAAAAPDDFETVPRGADDLAAILY 163
|
170
....*....|....*.
gi 1574832895 1759 TSGSTGRPKGVQISHG 1774
Cdd:PRK07514 164 TSGTTGRSKGAMLSHG 179
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1046-1096 |
4.26e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 57.94 E-value: 4.26e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 1046 KVGITQNFF-ELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIASLI 1096
Cdd:COG0236 24 EITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
615-1004 |
4.64e-10 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 64.60 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 615 LARNFALSGILSQYASSAPAY-RVGPNDIACLTFTSGSTGRPKGVLQRHGPLT------HFLPW-MR--DRFAFTQTDRY 684
Cdd:cd05943 223 IAKALTLEDFLATGAAGELEFePLPFDHPLYILYSSGTTGLPKCIVHGAGGTLlqhlkeHILHCdLRpgDRLFYYTTCGW 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 685 ----SLLSGLAhdplqreiftplcVGATICIPDqehmGDPG---WLAQWMQGQEITIASF--TPALLQLLTQGmgedDLP 755
Cdd:cd05943 303 mmwnWLVSGLA-------------VGATIVLYD----GSPFypdTNALWDLADEEGITVFgtSAKYLDALEKA----GLK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 756 SAR---IPSLRYAFVVGDALTRRHVARLY-AVAPHITCVNLYGSTETqraVSYFVL--PTASSTESPASVTALldkevip 829
Cdd:cd05943 362 PAEthdLSSLRTILSTGSPLKPESFDYVYdHIKPDVLLASISGGTDI---ISCFVGgnPLLPVYRGEIQCRGL------- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 830 lgkgmpGAQILILNEAGNlAGIGELGEIYVRSPHLA--FGYLDDPDqtNERFLVNPFTHqeHDRLYRTGDLGRYLPDGNA 907
Cdd:cd05943 432 ------GMAVEAFDEEGK-PVWGEKGELVCTKPFPSmpVGFWNDPD--GSRYRAAYFAK--YPGVWAHGDWIEITPRGGV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 908 EFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQV--KPVLSNLRAFVTQRLPAF 985
Cdd:cd05943 501 VILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVEldDELRKRIRSTIRSALSPR 580
|
410
....*....|....*....
gi 1574832895 986 MVPAHFVFMSRLPLNANGK 1004
Cdd:cd05943 581 HVPAKIIAVPDIPRTLSGK 599
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1633-1775 |
4.76e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 64.53 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPL----DPDYPSQRLlwmaQDAQLSL 1708
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRL----EDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1709 LLTHEEL-----KARWPHCPCPLLC--LDTLQERYASLPcEDLQEA--------CSPAQLAYVIYTSGSTGRPKGVQISH 1773
Cdd:PRK04319 149 LITTPALlerkpADDLPSLKHVLLVgeDVEEGPGTLDFN-ALMEQAsdefdiewTDREDGAILHYTSGSTGKPKGVLHVH 227
|
..
gi 1574832895 1774 GA 1775
Cdd:PRK04319 228 NA 229
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
485-1010 |
4.84e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 64.39 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 485 HWEGTIHDLF--AQQAHLRPENI--AIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILK 560
Cdd:PRK06018 7 DWPLLCHRIIdhAARIHGNREVVtrSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 561 AGSTVLILDPSYPPARLLEYVQRAHARGWL----------RIEGATDCQEL------DEWCRANSYCNLVlarnfALSGI 624
Cdd:PRK06018 87 IGAICHTVNPRLFPEQIAWIINHAEDRVVItdltfvpileKIADKLPSVERyvvltdAAHMPQTTLKNAV-----AYEEW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 625 LSQyASSAPAYRVGPNDIAC-LTFTSGSTGRPKGVLQRH--GPLTHFLPWMRDRFAFTQTDRYSLLSGLAHDPLQREIFT 701
Cdd:PRK06018 162 IAE-ADGDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHrsNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 702 PLCVGATICIPDQEHmgDPGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLpsaRIPSLRYAFVVGDALTRRHVARL- 780
Cdd:PRK06018 241 APSMGTKLVMPGAKL--DGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGL---KLPHLKMVVCGGSAMPRSMIKAFe 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 781 -YAVAPhitcVNLYGSTETQRAVSYFVLPTASSTespASVTALLDkevIPLGKGMP--GAQILILNEAGN-LAGIGE-LG 855
Cdd:PRK06018 316 dMGVEV----RHAWGMTEMSPLGTLAALKPPFSK---LPGDARLD---VLQKQGYPpfGVEMKITDDAGKeLPWDGKtFG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 856 EIYVRSPHLAFGY-------LDDpdqtnerflvnpfthqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEE 928
Cdd:PRK06018 386 RLKVRGPAVAAAYyrvdgeiLDD------------------DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSID 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 929 IEAILVEHPMVADAAVI-IREDTPDNKQIVayITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDR 1007
Cdd:PRK06018 448 LENLAVGHPKVAEAAVIgVYHPKWDERPLL--IVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILK 525
|
...
gi 1574832895 1008 KAL 1010
Cdd:PRK06018 526 TAL 528
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1047-1090 |
5.73e-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: 56.80 E-value: 5.73e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1574832895 1047 VGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIE 1090
Cdd:pfam00550 18 IDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
639-1007 |
6.84e-10 |
|
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: 64.05 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGAT-ICIPDQEH 716
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDmGLIAFHLAPLIAGMNqYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 717 MGDPG-WLAQwMQGQEITIAS---FTPALL--QLLTQGMGEDDLPSARIpSLRYAFVVGDALTRRHVARLYAVAPHITCV 790
Cdd:cd05908 185 IRRPIlWLKK-ASEHKATIVSspnFGYKYFlkTLKPEKANDWDLSSIRM-ILNGAEPIDYELCHEFLDHMSKYGLKRNAI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 791 -NLYGSTETQRAVSY------FVLPTAS----STESPASVTALLDKE---VIPLGKGMPGAQILILNEAGNLAGIGELGE 856
Cdd:cd05908 263 lPVYGLAEASVGASLpkaqspFKTITLGrrhvTHGEPEPEVDKKDSEcltFVEVGKPIDETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 857 IYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGrYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEH 936
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVF--------TDDGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEEL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 937 PMVADAAVII---REDTPDNKQIVAYITHHN--EQVKPVLSNLRAFVTQR--------LPafmvpahfvfMSRLPLNANG 1003
Cdd:cd05908 414 EGVELGRVVAcgvNNSNTRNEEIFCFIEHRKseDDFYPLGKKIKKHLNKRggwqinevLP----------IRRIPKTTSG 483
|
....
gi 1574832895 1004 KVDR 1007
Cdd:cd05908 484 KVKR 487
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
639-944 |
6.89e-10 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 64.16 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLTH----FLPWMRDRFAFTQTDRY-SLLSgLAHdplqreIFTPLCVGATICI-- 711
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEILNKINPTDVYiSYLP-LAH------IFERVVEALFLYHga 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 --------------------PD----------------QEHMGDPGWLAQWMqgqeitiasFTPAL---LQLLTQGMGE- 751
Cdd:cd05927 186 kigfysgdirlllddikalkPTvfpgvprvlnriydkiFNKVQAKGPLKRKL---------FNFALnykLAELRSGVVRa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 752 ----DDLPSARIPSL---RYAF-VVGDALTRRHVARLYAVAPHITCVNLYGSTETqravsyfvlpTAsstesPASVTALL 823
Cdd:cd05927 257 spfwDKLVFNKIKQAlggNVRLmLTGSAPLSPEVLEFLRVALGCPVLEGYGQTEC----------TA-----GATLTLPG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 824 DKEVIPLGKGMPGAQIlilneagNLAGIGEL----------GEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHqehdrly 893
Cdd:cd05927 322 DTSVGHVGGPLPCAEV-------KLVDVPEMnydakdpnprGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLH------- 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 894 rTGDLGRYLPDGnaefagrndlQVKI-----------RGYRIELEEIEAILVEHPMVADAAV 944
Cdd:cd05927 388 -TGDIGEWLPNG----------TLKIidrkknifklsQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1617-1851 |
7.51e-10 |
|
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: 64.05 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1617 QCERSSL-----QPAL-HAG----STTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYV 1686
Cdd:cd05968 65 QLLDKWLadtrtRPALrWEGedgtSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1687 PLDPDYPSQRLLWMAQDAQLSLLLTH-------------EELKARWPHCPCpllCLDTLQERYASLPCE---------DL 1744
Cdd:cd05968 145 PIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQCPT---VEKVVVVRHLGNDFTpakgrdlsyDE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1745 QEACSPAQLA--------YVIYTSGSTGRPKG-VQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLPLL 1815
Cdd:cd05968 222 EKETAGDGAErtesedplMIIYTSGTTGKPKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLI 301
|
250 260 270
....*....|....*....|....*....|....*....
gi 1574832895 1816 AGAQIQLasQEQASD---PRQLASLLAQLPISILQATPT 1851
Cdd:cd05968 302 LGATMVL--YDGAPDhpkADRLWRMVEDHEITHLGLSPT 338
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
637-952 |
7.95e-10 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 63.24 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 637 VGPNDIACLTFTSGSTGRPKGVlqrhgPLT-HFLPWMRDRFA-------FTQTDR------YSLLSG--LAHDPLQReif 700
Cdd:COG1541 80 VPLEEIVRIHASSGTTGKPTVV-----GYTrKDLDRWAELFArslraagVRPGDRvqnafgYGLFTGglGLHYGAER--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 701 tplcVGATIcIPdqehMGdPGWLA---QWMQGQEITIASFTPALLQLLTQGMGEDDLPSARIpSLRYAFVVGDALT---R 774
Cdd:COG1541 152 ----LGATV-IP----AG-GGNTErqlRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDL-SLKKGIFGGEPWSeemR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 775 RHVARLYavapHITCVNLYGSTETQRAVSYfvlptasstESPAsvtalldkeviplGKGMpgaqilILNEAGNLAgigel 854
Cdd:COG1541 221 KEIEERW----GIKAYDIYGLTEVGPGVAY---------ECEA-------------QDGL------HIWEDHFLV----- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 855 gEIYvrsphlafgyldDPDqTNERF-------LVnpFTHQEHDRL----YRTGDLGRYLPD------GNAEFA---GRND 914
Cdd:COG1541 264 -EII------------DPE-TGEPVpegeegeLV--VTTLTKEAMplirYRTGDLTRLLPEpcpcgrTHPRIGrilGRAD 327
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1574832895 915 LQVKIRGYRIELEEIEAILVEHPMVADAAVII--REDTPD 952
Cdd:COG1541 328 DMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVvdREGGLD 367
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1613-1774 |
1.29e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 63.24 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1613 LIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDY 1692
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1693 PSQRLLWMAQDAQLSLLLTHEELKARWPHCPCPLLCLDTL-------------QERYASLPCEDLQEAC---SPAQLAYV 1756
Cdd:PRK06155 106 RGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVwlldapasvsvpaGWSTAPLPPLDAPAPAaavQPGDTAAI 185
|
170
....*....|....*...
gi 1574832895 1757 IYTSGSTGRPKGVQISHG 1774
Cdd:PRK06155 186 LYTSGTTGPSKGVCCPHA 203
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
478-912 |
1.57e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.97 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 478 PGAPISAHWEgTIHDLFAQQAHLRPENIAII-----DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAI-SAQRCAAL 551
Cdd:PRK08180 30 SAEPLGDYPR-RLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMIlSGNSIEHA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 552 VLAiLGILKAGSTVLILDPSY-----PPARLleyvqrAHARGWLRiEGATDCQELDEWCRANSYCNL-----VLARN--- 618
Cdd:PRK08180 109 LLA-LAAMYAGVPYAPVSPAYslvsqDFGKL------RHVLELLT-PGLVFADDGAAFARALAAVVPadvevVAVRGavp 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 619 ----FALSGILSQYASSA--PAY-RVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLS--- 688
Cdd:PRK08180 181 graaTPFAALLATPPTAAvdAAHaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDwlp 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 689 -----------GLAhdplqreiftpLCVGATICIPDQEHMgdPGWLAQWMQG-QEI--TIASFTPALLQLLTQGMGEDDL 754
Cdd:PRK08180 261 wnhtfggnhnlGIV-----------LYNGGTLYIDDGKPT--PGGFDETLRNlREIspTVYFNVPKGWEMLVPALERDAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 755 PSARIPS-LRYAFVVGDALtRRHV-ARLYAVA-----PHITCVNLYGSTETQravsyfvlPTASSTESPASVTALldkev 827
Cdd:PRK08180 328 LRRRFFSrLKLLFYAGAAL-SQDVwDRLDRVAeatcgERIRMMTGLGMTETA--------PSATFTTGPLSRAGN----- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 828 ipLGKGMPGAQILILNEAGNLagigelgEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNA 907
Cdd:PRK08180 394 --IGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAF--------DEEGYYRSGDAVRFVDPADP 456
|
....*....
gi 1574832895 908 E----FAGR 912
Cdd:PRK08180 457 ErglmFDGR 465
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1630-1856 |
1.79e-09 |
|
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: 62.46 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1630 GSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLL 1709
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1710 LTHEElkarwphcpcpllcldtlqeryaslpcEDLqeacspaqlAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSL 1789
Cdd:cd05914 84 FVSDE---------------------------DDV---------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLL 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1790 SPHDRWLAITSISfDIAGL--ELYLPLLAGAQIQLAsqEQASDPRQLASLLAQlpISILQATPTTWQLL 1856
Cdd:cd05914 128 GKGDKILSILPLH-HIYPLtfTLLLPLLNGAHVVFL--DKIPSAKIIALAFAQ--VTPTLGVPVPLVIE 191
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1643-1861 |
1.99e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 62.46 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1643 ANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAA----YVPLDPDYPSQRLLWMAQDAQLSLLLTHE----E 1714
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAgaadR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1715 LKARWPHCPCPLLCLDT--LQERYASLPCEDLqeacSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPH 1792
Cdd:cd05922 83 LRDALPASPDPGTVLDAdgIRAARASAPAHEV----SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1793 DRWLAITSISFDiAGLELYLP-LLAGAQIQLAsqEQASDPRQLASLLAQLPISILQATPTTWQLLLETGW 1861
Cdd:cd05922 159 DRALTVLPLSYD-YGLSVLNThLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGF 225
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
636-945 |
2.04e-09 |
|
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: 62.76 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 636 RVGPNDIACLTFTSGSTGRPKGVLQRHGPLThflpW--------MRDRFAFTQTDrySLLS--GLAHDPLQR-EIFTPLC 704
Cdd:cd05933 146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNIT----WtakaasqhMDLRPATVGQE--SVVSylPLSHIAAQIlDIWLPIK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 VGATICIPDQE-----------------HMGDPGWLAQWMQGQEITIASFTPALLQLLTQGMG----------EDDLPSA 757
Cdd:cd05933 220 VGGQVYFAQPDalkgtlvktlrevrptaFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGvgletnlklmGGESPSP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 758 RIPSLRYAFV---VGDALTRRHVARLY-AVAP------------HITCVNLYGSTETQravsyfvlptassteSPASVTA 821
Cdd:cd05933 300 LFYRLAKKLVfkkVRKALGLDRCQKFFtGAAPisretlefflslNIPIMELYGMSETS---------------GPHTISN 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 822 LLDKEVIPLGKGMPGAQILILNEAGNlaGIGElgeIYVRSPHLAFGYLDDPDQTNErflvnpfTHQEHDRLyRTGDLGRY 901
Cdd:cd05933 365 PQAYRLLSCGKALPGCKTKIHNPDAD--GIGE---ICFWGRHVFMGYLNMEDKTEE-------AIDEDGWL-HSGDLGKL 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1574832895 902 LPDGNAEFAGRNDLQVKIRG------YRIEleeiEAILVEHPMVADAAVI 945
Cdd:cd05933 432 DEDGFLYITGRIKELIITAGgenvppVPIE----DAVKKELPIISNAMLI 477
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1631-1860 |
2.05e-09 |
|
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: 62.59 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1631 STTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLL 1710
Cdd:cd17634 82 SRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1711 THEEL--------------KARWPHCPCP--LLCLDTLQERY-----ASLPCEDLQEACSPAQLA---------YVIYTS 1760
Cdd:cd17634 162 TADGGvragrsvplkknvdDALNPNVTSVehVIVLKRTGSDIdwqegRDLWWRDLIAKASPEHQPeamnaedplFILYTS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1761 GSTGRPKGVQISHGALLSFLLSLQSLLS-LSPHDRWLAITSISFDIAGLEL-YLPLLAGAQIQL-ASQEQASDPRQLASL 1837
Cdd:cd17634 242 GTTGKPKGVLHTTGGYLVYAATTMKYVFdYGPGDIYWCTADVGWVTGHSYLlYGPLACGATTLLyEGVPNWPTPARMWQV 321
|
250 260
....*....|....*....|...
gi 1574832895 1838 LAQLPISILQATPTTWQLLLETG 1860
Cdd:cd17634 322 VDKHGVNILYTAPTAIRALMAAG 344
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1624-1774 |
2.59e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 62.37 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:PRK06178 49 RPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELND 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLLLT-------------------------HEELKARwPHCPCP-------LLCLDT--LQERYASLPCEDLQEACS 1749
Cdd:PRK06178 129 AGAEVLLAldqlapvveqvraetslrhvivtslADVLPAE-PTLPLPdslraprLAAAGAidLLPALRACTAPVPLPPPA 207
|
170 180
....*....|....*....|....*
gi 1574832895 1750 PAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:PRK06178 208 LDALAALNYTGGTTGMPKGCEHTQR 232
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1620-1774 |
2.61e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 62.21 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1620 RSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLW 1699
Cdd:PRK06145 14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1700 MAQDAQLSLLLTHEELKARwPHCPCPLLCLDTLQERYAS------LPCEDlQEACSPAQLAYVIYTSGSTGRPKGVQISH 1773
Cdd:PRK06145 94 ILGDAGAKLLLVDEEFDAI-VALETPKIVIDAAAQADSRrlaqggLEIPP-QAAVAPTDLVRLMYTSGTTDRPKGVMHSY 171
|
.
gi 1574832895 1774 G 1774
Cdd:PRK06145 172 G 172
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
808-1011 |
3.06e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.55 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 808 PTASSTESPASVTALLDKEV----IPLGKGMPGAQILILNeagnlagiGELGEIYVRSPHLAFGYLddPDqtnerflvnp 883
Cdd:PRK07445 259 PTYGMTETASQIATLKPDDFlagnNSSGQVLPHAQITIPA--------NQTGNITIQAQSLALGYY--PQ---------- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 884 ftHQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIireDTPDN---KQIVA-Y 959
Cdd:PRK07445 319 --ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVL---GLPDPhwgEVVTAiY 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574832895 960 ITHHNEqvkPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKALP 1011
Cdd:PRK07445 394 VPKDPS---ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
512-945 |
3.08e-09 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 62.06 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 512 NTVSYGELEARSNQLAHYLHAQGIRPHDVVAI-------------SAQRCAALVLAILG----------ILKAGSTVLI- 567
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAIlgdnrpewvwaelAAQAIGALSLGIYQdsmaeevaylLNYTGARVVIa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 568 -----LDPSYPPAR---LLEYV-------QRAHARGWLRiegatDCQELDEWCRA------NSYCNLVLARNfalsgils 626
Cdd:cd17641 90 edeeqVDKLLEIADripSVRYViycdprgMRKYDDPRLI-----SFEDVVALGRAldrrdpGLYEREVAAGK-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 627 qyassapayrvgPNDIACLTFTSGSTGRPKGVLQRHGPLTHF---------------------LPW-MRDRFAFTQtdry 684
Cdd:cd17641 157 ------------GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHcaaylaadplgpgdeyvsvlpLPWiGEQMYSVGQ---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 685 SLLSGLA-HDPLQ--------REI-----FTPLCVGATICIPDQEHMGDPGWLAQWM------QGQEITIASF---TPAL 741
Cdd:cd17641 221 ALVCGFIvNFPEEpetmmedlREIgptfvLLPPRVWEGIAADVRARMMDATPFKRFMfelgmkLGLRALDRGKrgrPVSL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 742 LQLLTQGMGE--------DDLPSARipsLRYAFVVGDALTRrHVARLYavapHITCVNL---YGSTETqrAVSYFVLPTA 810
Cdd:cd17641 301 WLRLASWLADallfrplrDRLGFSR---LRSAATGGAALGP-DTFRFF----HAIGVPLkqlYGQTEL--AGAYTVHRDG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 811 SSteSPASVtalldkeviplGKGMPGAQILILNEagnlagigelGEIYVRSPHLAFGYLDDPDQTNERFLVNPFTHqehd 890
Cdd:cd17641 371 DV--DPDTV-----------GVPFPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLH---- 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 891 rlyrTGDLGRYLPDGNAEFAGR-NDLQVKIRGYRIELEEIEAILVEHPMVADAAVI 945
Cdd:cd17641 424 ----TGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVL 475
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1634-1830 |
7.43e-09 |
|
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: 60.19 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHE 1713
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1714 ELkarwphcpcpllcldtlqeryaslpcEDLqeacspaqlAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHD 1793
Cdd:cd05935 82 EL--------------------------DDL---------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1574832895 1794 RWLAITSIsFDIAGLE--LYLPLLAGAQIQLAS---QEQASD 1830
Cdd:cd05935 127 VILACLPL-FHVTGFVgsLNTAVYVGGTYVLMArwdRETALE 167
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1634-1877 |
8.08e-09 |
|
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: 60.04 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHE 1713
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1714 ElkarwphcpcpllcldtlqeryaslpcedlqeacspaQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHD 1793
Cdd:cd05972 81 E-------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1794 RWLAITS------ISFDIAGlelylPLLAGAQIqLASQEQASDPRQLASLLAQLPISILQATPTTWQLLLETGwsgkagl 1867
Cdd:cd05972 124 IHWNIADpgwakgAWSSFFG-----PWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQD------- 190
|
250
....*....|
gi 1574832895 1868 tLLSGAKPSL 1877
Cdd:cd05972 191 -LSSYKFSHL 199
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
509-960 |
1.04e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 60.31 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 509 DEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVlildpsypparlleyvqraharg 588
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPI----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 589 wlriegatdcqeldewcrANSYCNLVLArnfALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLT-- 666
Cdd:cd17639 58 ------------------VTVYATLGED---ALIHSLNETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVag 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 667 ------HFLPWMRDrfaftqTDRY-SLLSgLAHdplqreIF----TPLCV--GATIC----------IPDQEHmGD---- 719
Cdd:cd17639 117 iaglgdRVPELLGP------DDRYlAYLP-LAH------IFelaaENVCLyrGGTIGygsprtltdkSKRGCK-GDltef 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 720 -PgwlaqwmqgqeiTIASFTPALLQLLTQGMgEDDLPSAriPSL-RYAFVVGDALTRRHVARLYAvaphiTCV------- 790
Cdd:cd17639 183 kP------------TLMVGVPAIWDTIRKGV-LAKLNPM--GGLkRTLFWTAYQSKLKALKEGPG-----TPLldelvfk 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 791 --------NLYG--------STETQRAVSYFVLPTASS---TESPASVTALL--DKEVIPLGKGMPGAQILILN--EAGN 847
Cdd:cd17639 243 kvraalggRLRYmlsggaplSADTQEFLNIVLCPVIQGyglTETCAGGTVQDpgDLETGRVGPPLPCCEIKLVDweEGGY 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 848 LAGIGE-LGEIYVRSPHLAFGYLDDPDQTNERFLvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGR-NDLqVKIR-GYRI 924
Cdd:cd17639 323 STDKPPpRGEILIRGPNVFKGYYKNPEKTKEAFD--------GDGWFHTGDIGEFHPDGTLKIIDRkKDL-VKLQnGEYI 393
|
490 500 510
....*....|....*....|....*....|....*.
gi 1574832895 925 ELEEIEAILVEHPMVADAAVIIredTPDNKQIVAYI 960
Cdd:cd17639 394 ALEKLESIYRSNPLVNNICVYA---DPDKSYPVAIV 426
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1633-1858 |
3.67e-08 |
|
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: 58.13 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDypsqrllwmaqdaqlsllLTH 1712
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR------------------LTP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1713 EELkarwphcpcpllcldTLQERYASLPCEDLqeacspaqlAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPH 1792
Cdd:cd05912 63 NEL---------------AFQLKDSDVKLDDI---------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 1793 DRWLAITSIsFDIAGLELYL-PLLAGAQIQLasqEQASDPRQLASLLAQLPISILQATPTTWQLLLE 1858
Cdd:cd05912 119 DNWLCALPL-FHISGLSILMrSVIYGMTVYL---VDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE 181
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
498-1010 |
4.97e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 58.03 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 498 AHLRPENIAIIDEINTVSYGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAG--------------- 562
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGavlntlntrldaasi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 563 --------STVLILDPSYPP--ARLLEYVQRAHArgwLRIEGATDCQELDEWCRANSYCNLVlarnfalsgilsqyASSA 632
Cdd:PRK08162 108 afmlrhgeAKVLIVDTEFAEvaREALALLPGPKP---LVIDVDDPEYPGGRFIGALDYEAFL--------------ASGD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 633 PAYR-VGPND----IAcLTFTSGSTGRPKGVLQRHgplthflpwmrdRFAFTQTDRYSLLSGLAHDPLQreIFT-PL--C 704
Cdd:PRK08162 171 PDFAwTLPADewdaIA-LNYTSGTTGNPKGVVYHH------------RGAYLNALSNILAWGMPKHPVY--LWTlPMfhC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 VGAtiCIPdqehmgdpgWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLPSARI---------PSLRYAFvvgdaltRR 775
Cdd:PRK08162 236 NGW--CFP---------WTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIvlsalinapAEWRAGI-------DH 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 776 HVARLYAVAP--------------HITCVnlYGSTETqravsYfvlptassteSPASVTALLDK-EVIPLG-----KGMP 835
Cdd:PRK08162 298 PVHAMVAGAAppaaviakmeeigfDLTHV--YGLTET-----Y----------GPATVCAWQPEwDALPLDeraqlKARQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 836 GAQILILNEAGNL--------AGIGE-LGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGn 906
Cdd:PRK08162 361 GVRYPLQEGVTVLdpdtmqpvPADGEtIGEIMFRGNIVMKGYLKNPKATEEAF---------AGGWFHTGDLAVLHPDG- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 907 aefagrndlQVKIR----------GYRIELEEIEAILVEHPMVADAAVIIRED-----TPdnkqiVAYIThhneqVKPVL 971
Cdd:PRK08162 431 ---------YIKIKdrskdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDpkwgeVP-----CAFVE-----LKDGA 491
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1574832895 972 S----NLRAFVTQRLPAFMVPAHFVFmSRLPLNANGKVDRKAL 1010
Cdd:PRK08162 492 SateeEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVL 533
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1632-1856 |
5.59e-08 |
|
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: 57.75 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1632 TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWmaqdaqlslLLT 1711
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLY---------ILN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1712 HEElkarwphcpCPLLCLDTlqeryaslpcedlqeacSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSP 1791
Cdd:cd17640 75 HSE---------SVALVVEN-----------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQP 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 1792 HDRWLAITSI--SFDIAgLELYLPLLAGAQIqlasqeqASDPRQLASLLAQLPISILQATPTTWQLL 1856
Cdd:cd17640 129 GDRFLSILPIwhSYERS-AEYFIFACGCSQA-------YTSIRTLKDDLKRVKPHYIVSVPRLWESL 187
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
621-1016 |
6.23e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.05 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 621 LSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDR----------------- 683
Cdd:PRK06814 774 IKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKvfnalpvfhsfgltggl 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 684 -YSLLSG----LAHDPLQREIFTPLC--VGATICIpdqehmGDPGWLAQWmqgqeitiasftpallqlltqgmgeddlps 756
Cdd:PRK06814 854 vLPLLSGvkvfLYPSPLHYRIIPELIydTNATILF------GTDTFLNGY------------------------------ 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 757 ARIP------SLRYAFVVGDAL---TRRHVARLYAVapHItcVNLYGSTETQRAVSyFVLPTASStesPASVtalldkev 827
Cdd:PRK06814 898 ARYAhpydfrSLRYVFAGAEKVkeeTRQTWMEKFGI--RI--LEGYGVTETAPVIA-LNTPMHNK---AGTV-------- 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 828 iplGKGMPGaqilILNEAGNLAGIGELGEIYVRSPHLAFGYLDdpdqtnerfLVNPFTHQE-HDRLYRTGDLGRYLPDGN 906
Cdd:PRK06814 962 ---GRLLPG----IEYRLEPVPGIDEGGRLFVRGPNVMLGYLR---------AENPGVLEPpADGWYDTGDIVTIDEEGF 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 907 AEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVaYITHHNEQVKPVLsnLRAFVTQRLPAFM 986
Cdd:PRK06814 1026 ITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERII-LLTTASDATRAAF--LAHAKAAGASELM 1102
|
410 420 430
....*....|....*....|....*....|....*...
gi 1574832895 987 VPAHFVFMSRLPLNANGKVD--------RKALPAPEAA 1016
Cdd:PRK06814 1103 VPAEIITIDEIPLLGTGKIDyvavtklaEEAAAKPEAA 1140
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
516-960 |
1.06e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.94 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 516 YGELEARSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGstvLILDPSYPPARL---LEYVQraHARGWLRI 592
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAG---LVPVPLPLPMGFggrESYIA--QLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 593 EGATDC---QELDEWCRAnsycnLVLARNFALSGILSQY----ASSAPAYRVGPNDIACLTFTSGSTGRPKGVLQRHGPL 665
Cdd:PRK09192 127 AQPAAIitpDELLPWVNE-----ATHGNPLLHVLSHAWFkalpEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 666 THFLPWM-RDRFAFTQTDR-YSLLSgLAHD-PLQREIFTPLCVGATI-CIPDQEHMGDP-GWLaQWMQGQEITIaSFTPA 740
Cdd:PRK09192 202 MANLRAIsHDGLKVRPGDRcVSWLP-FYHDmGLVGFLLTPVATQLSVdYLPTRDFARRPlQWL-DLISRNRGTI-SYSPP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 741 L-LQLLTQGMGEDDLPSARIPSLRYAFVVGDaLTRRHVarLYAVAPHITCVNL--------YGSTETQRAVSYFVLPTAS 811
Cdd:PRK09192 279 FgYELCARRVNSKDLAELDLSCWRVAGIGAD-MIRPDV--LHQFAEAFAPAGFddkafmpsYGLAEATLAVSFSPLGSGI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 812 STE---------SPASVTALLD----KEVIPLGKGMPGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNEr 878
Cdd:PRK09192 356 VVEevdrdrleyQGKAVAPGAEtrrvRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDV- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 879 flvnpfthQEHDRLYRTGDLGrYLPDGNAEFAGR-NDLqVKIRGYRIELEEIEAILVEHPMV--ADAAVIIREdTPDNKQ 955
Cdd:PRK09192 435 --------LAADGWLDTGDLG-YLLDGYLYITGRaKDL-IIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIA-QENGEK 503
|
....*
gi 1574832895 956 IVAYI 960
Cdd:PRK09192 504 IVLLV 508
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
513-672 |
1.21e-07 |
|
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: 56.92 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLHAQ-GIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHARGWLr 591
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 592 ieGATDCQE-LDEWC---RANSYCNLVLARNFALSGI--LSQYASSA-----PAY---RVGPNDIACLTFTSGSTGRPKG 657
Cdd:cd05938 84 --VAPELQEaVEEVLpalRADGVSVWYLSHTSNTEGVisLLDKVDAAsdepvPASlraHVTIKSPALYIYTSGTTGLPKA 161
|
170
....*....|....*
gi 1574832895 658 VLqrhgpLTHFLPWM 672
Cdd:cd05938 162 AR-----ISHLRVLQ 171
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
835-1010 |
1.29e-07 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 56.60 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 835 PGAQILILNEAGNLAGIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRND 914
Cdd:PRK08974 385 PSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI---------KDGWLATGDIAVMDEEGFLRIVDRKK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 915 LQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPvlSNLRAFVTQRLPAFMVPAHFVFM 994
Cdd:PRK08974 456 DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTE--EELITHCRRHLTGYKVPKLVEFR 533
|
170
....*....|....*.
gi 1574832895 995 SRLPLNANGKVDRKAL 1010
Cdd:PRK08974 534 DELPKSNVGKILRREL 549
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1606-1774 |
1.51e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 56.51 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1606 PSCGLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLA-HLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAA 1684
Cdd:PRK08314 8 PETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAgYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1685 YVPLDPDYPSQRLLWMAQDAQLSLLLTHEELKAR--------------------------------WPHCPCPLLCL--- 1729
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdylpaepeiavpaWLRAEPPLQALapg 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 1730 ------DTLQERYASLPCEdlqeaCSPAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:PRK08314 168 gvvawkEALAAGLAPPPHT-----AGPDDLAVLPYTSGTTGVPKGCMHTHR 213
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1624-1872 |
2.40e-07 |
|
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: 55.56 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAH-LLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQ 1702
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1703 DAQLSLLLTHEELKARwphcpcpllcldtlqeryaslpcEDLqeaCSPAqlayviYTSGSTGRPKGVQISHGALLSFLLS 1782
Cdd:cd05958 81 KARITVALCAHALTAS-----------------------DDI---CILA------FTSGTTGAPKATMHFHRDPLASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1783 -LQSLLSLSPHDRWLAITSISFDIA-GLELYLPLLAGAQIQLASQEQASDprqLASLLAQLPISILQATPTTWQLLLEtg 1860
Cdd:cd05958 129 yAVNVLRLREDDRFVGSPPLAFTFGlGGVLLFPFGVGASGVLLEEATPDL---LLSAIARYKPTVLFTAPTAYRAMLA-- 203
|
250
....*....|..
gi 1574832895 1861 wSGKAGLTLLSG 1872
Cdd:cd05958 204 -HPDAAGPDLSS 214
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1635-1772 |
2.45e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 55.58 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1635 TYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHEE 1714
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1715 LKArwphCPCPLLCLDTLQeryASLPCEDLQEACS--PAQLAYVIYTSGSTGRPKGVQIS 1772
Cdd:PRK09088 104 VAA----GRTDVEDLAAFI---ASADALEPADTPSipPERVSLILFTSGTSGQPKGVMLS 156
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
515-1010 |
2.63e-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: 55.51 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 515 SYGELEA-------RSNQLAHYLHAQGIRPHDVVAISAQRCAALVLAILGILKAGSTVLILDPSYPPARLLEYVQRAHAR 587
Cdd:cd05915 19 TGEVHRTtyaevyqRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 588 GWLriegaTDCQELDEwcrANSYCNLV--LARNFALSGILSQY----ASSAPAYR----VGPNDIACLTFTSGSTGRPKG 657
Cdd:cd05915 99 VLL-----FDPNLLPL---VEAIRGELktVQHFVVMDEKAPEGylayEEALGEEAdpvrVPERAACGMAYTTGTTGLPKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 658 VLQRHgplthflpwmrdRFAFTQTDRYSLLSGLAHDPLQreiftplcvgATICIPDQEHMGdpGWLAQWmqgqeiTIASF 737
Cdd:cd05915 171 VVYSH------------RALVLHSLAASLVDGTALSEKD----------VVLPVVPMFHVN--AWCLPY------AATLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 738 TPALLQLltQGMGEDDlpsaripslryafVVGDALTRRHVARLYAVAPhitCVNLYGSTETQRAVSY-FVLPTASSTESP 816
Cdd:cd05915 221 GAKQVLP--GPRLDPA-------------SLVELFDGEGVTFTAGVPT---VWLALADYLESTGHRLkTLRRLVVGGSAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 817 ASVTALLDK-------------EVIPLGKG---MPGAQILILNEAGNLA---GIGELGE--------------------- 856
Cdd:cd05915 283 PRSLIARFErmgvevrqgygltETSPVVVQnfvKSHLESLSEEEKLTLKaktGLPIPLVrlrvadeegrpvpkdgkalge 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 857 IYVRSPHLAFGYLDDPDQTNERFLVNPFthqehdrlYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEH 936
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDGF--------FRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGH 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 937 PMVADAAVIIREDTPDNKQIVAYITHHNEQVKPvlSNLRAFVTQRLPAF-MVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:cd05915 435 PKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTP--EELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1609-1858 |
2.72e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 55.64 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1609 GLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQH-GIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVP 1687
Cdd:PRK06839 3 GIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1688 LDPDYPSQRLLWMAQDAQLSLLL-------THEELKARwpHCPCPLLCLDTLQERYASLPcEDLQEACSPAQLaYVIYTS 1760
Cdd:PRK06839 83 LNIRLTENELIFQLKDSGTTVLFvektfqnMALSMQKV--SYVQRVISITSLKEIEDRKI-DNFVEKNESASF-IICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1761 GSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSIsFDIAGLELY-LP-LLAGAQIQLASQeqaSDPRQLASLL 1838
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFaFPtLFAGGVIIVPRK---FEPTKALSMI 234
|
250 260
....*....|....*....|
gi 1574832895 1839 AQLPISILQATPTTWQLLLE 1858
Cdd:PRK06839 235 EKHKVTVVMGVPTIHQALIN 254
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1625-1775 |
3.19e-07 |
|
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: 55.38 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDpdypsQRLlwmaqDA 1704
Cdd:cd12118 21 TSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN-----TRL-----DA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574832895 1705 Q-LSLLLTHEELKarwphcpcpLLCLDTLQERYASL----PCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISH-GA 1775
Cdd:cd12118 91 EeIAFILRHSEAK---------VLFVDREFEYEDLLaegdPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHrGA 158
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1626-1770 |
3.27e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 55.47 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1626 ALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQ 1705
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1706 LSLLLTHEEL-KARWPHCP--CPLLCLDT---LQERY-----------------ASLPCEDLQEACSPAQLAYVIYTSGS 1762
Cdd:PRK12406 84 ARVLIAHADLlHGLASALPagVTVLSVPTppeIAAAYrispalltppagaidweGWLAQQEPYDGPPVPQPQSMIYTSGT 163
|
....*...
gi 1574832895 1763 TGRPKGVQ 1770
Cdd:PRK12406 164 TGHPKGVR 171
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
639-1017 |
4.68e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.10 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGATICI-PDQEH 716
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSfGLTVGLFTPLLTGAEVFLyPSPLH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 717 MgdpGWLAQWMQGQEITIASFTPALLQLLTQGMGEDDLpsARipsLRYAfVVGDALTRRHVARLYAVAPHITCVNLYGST 796
Cdd:PRK08043 444 Y---RIVPELVYDRNCTVLFGTSTFLGNYARFANPYDF--AR---LRYV-VAGAEKLQESTKQLWQDKFGLRILEGYGVT 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 797 ETQRAVSYFVlPTASsteSPASVtalldkeviplGKGMPGAQILILneagNLAGIGELGEIYVRSPHLAFGYL--DDPDQ 874
Cdd:PRK08043 515 ECAPVVSINV-PMAA---KPGTV-----------GRILPGMDARLL----SVPGIEQGGRLQLKGPNIMNGYLrvEKPGV 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 875 tnerfLVNPFTHQEHDRL----YRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIREDT 950
Cdd:PRK08043 576 -----LEVPTAENARGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDA 650
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 951 PDNKQIVAYIThHNEQVKPVLsnLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVD----RKALPAPEAAD 1017
Cdd:PRK08043 651 SKGEALVLFTT-DSELTREKL--QQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDfvtlKSMVDEPEQHD 718
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1632-1773 |
6.78e-07 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 54.37 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1632 TTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLT 1711
Cdd:PRK06087 48 ASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1712 --------HE----ELKARWPHCPcPLLCLDTLQERYASLP----CED---LQEACSPA--QLAYVIYTSGSTGRPKGVQ 1770
Cdd:PRK06087 128 ptlfkqtrPVdlilPLQNQLPQLQ-QIVGVDKLAPATSSLSlsqiIADyepLTTAITTHgdELAAVLFTSGTEGLPKGVM 206
|
...
gi 1574832895 1771 ISH 1773
Cdd:PRK06087 207 LTH 209
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1633-1774 |
7.62e-07 |
|
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: 53.90 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAyvpldpdypsqrllwMAqdaqlsLLLTH 1712
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV---------------AA------LINYN 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 1713 EELKarwphcpcPLL-CLDTLQERYASlpcedlqeacspAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:cd05940 62 LRGE--------SLAhCLNVSSAKHLV------------VDAALYIYTSGTTGLPKAAIISHR 104
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
893-1010 |
7.86e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 54.38 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 893 YRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVIIRedtPDN---KQIVAYIT-HHNEQVK 968
Cdd:PRK00174 485 YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGR---PDDikgQGIYAFVTlKGGEEPS 561
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1574832895 969 PVLSN-LRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK00174 562 DELRKeLRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRIL 604
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1624-1888 |
1.17e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 53.63 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:PRK07786 33 APALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1704 AQLSLLLTHEELK--ARWPHCPCPLLCL----------------DTLQERYASLPCEDLQEAcSPAqlaYVIYTSGSTGR 1765
Cdd:PRK07786 113 CGAHVVVTEAALApvATAVRDIVPLLSTvvvaggssddsvlgyeDLLAEAGPAHAPVDIPND-SPA---LIMYTSGTTGR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1766 PKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSISFDIAGLELYLP-LLAGAQIQLASQeQASDPRQLASLLAQLPIS 1844
Cdd:PRK07786 189 PKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPL-GAFDPGQLLDVLEAEKVT 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1845 ILQATPTTWQLLL-ETGWSGKA-GLTLLS-GAKP---SLLISLAACCPVA 1888
Cdd:PRK07786 268 GIFLVPAQWQAVCaEQQARPRDlALRVLSwGAAPasdTLLRQMAATFPEA 317
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1631-1774 |
1.35e-06 |
|
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: 53.33 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1631 STTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLL 1710
Cdd:cd05966 82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1711 THEE---------LKAR----WPHCPCPLLCL---------DTLQERyaSLPCEDLQE----ACSPAQLA-----YVIYT 1759
Cdd:cd05966 162 TADGgyrggkvipLKEIvdeaLEKCPSVEKVLvvkrtggevPMTEGR--DLWWHDLMAkqspECEPEWMDsedplFILYT 239
|
170
....*....|....*
gi 1574832895 1760 SGSTGRPKGVQISHG 1774
Cdd:cd05966 240 SGSTGKPKGVVHTTG 254
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1599-1774 |
1.69e-06 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 52.97 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1599 SSPLPAAPSCGLHHLIEAQCERSSLQPAL--HAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLL 1676
Cdd:PRK05852 7 AAPMASDFGPRIADLVEVAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1677 AILKTGAAYVPLDPDYP--SQRLLWMAQDAQLSLLLTHEELKARWPHCPCPLLCL----DTLQERYASLPCEDLQEACSP 1750
Cdd:PRK05852 87 AASRADLVVVPLDPALPiaEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVnvggDSGPSGGTLSVHLDAATEPTP 166
|
170 180 190
....*....|....*....|....*....|...
gi 1574832895 1751 AQL---------AYVIYTSGSTGRPKGVQISHG 1774
Cdd:PRK05852 167 ATStpeglrpddAMIMFTGGTTGLPKMVPWTHA 199
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1633-1774 |
1.78e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.98 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTH 1712
Cdd:PRK09274 41 ELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1713 EelKA-------RWPhCPC--PLLC-----------LDTL--QERYASLPCEDLQeacsPAQLAYVIYTSGSTGRPKGVQ 1770
Cdd:PRK09274 121 P--KAhlarrlfGWG-KPSvrRLVTvggrllwggttLATLlrDGAAAPFPMADLA----PDDMAAILFTSGSTGTPKGVV 193
|
....
gi 1574832895 1771 ISHG 1774
Cdd:PRK09274 194 YTHG 197
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
516-1007 |
1.79e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 516 YGELEARSNQLAHYLHAQGirPHDVVAISAQRCAALVLAILGILKAGSTVLILdPSypPARlleyvqrahargwlrieGA 595
Cdd:PRK05851 34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVSIL-PG--PVR-----------------GA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 596 tdcqELDEWCRAN----------------SYCNLVLARNFALS-GILSQYAS---SAPAYRVGPNDIACLTFTSGSTGRP 655
Cdd:PRK05851 92 ----DDGRWADATltrfagigvrtvlshgSHLERLRAVDSSVTvHDLATAAHtnrSASLTPPDSGGPAVLQGTAGSTGTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 656 KGVLQRHGPLTHFLPWMRDRFAFTQ-TDRysllsGLAHDPLQREI-FTPLCVGATicipdqehMGDPGWLA--------- 724
Cdd:PRK05851 168 RTAILSPGAVLSNLRGLNARVGLDAaTDV-----GCSWLPLYHDMgLAFLLTAAL--------AGAPLWLApttafsasp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 725 -QWMQGQEITIASFTPA------LLqlltqGMGEDDLPSARIPSLRYAFVVG-----DALTR--RHVARL----YAVAPH 786
Cdd:PRK05851 235 fRWLSWLSDSRATLTAApnfaynLI-----GKYARRVSDVDLGALRVALNGGepvdcDGFERfaTAMAPFgfdaGAAAPS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 787 itcvnlYGSTETQRAVSyfvlptassteSPASVTALLDKEVIP-----------LGKGMPGAQILILNEAGNlAGIG--E 853
Cdd:PRK05851 310 ------YGLAESTCAVT-----------VPVPGIGLRVDEVTTddgsgarrhavLGNPIPGMEVRISPGDGA-AGVAgrE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 854 LGEIYVRSPHLAFGYLDDPdqtnerflvnPFthqEHDRLYRTGDLGrYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAIL 933
Cdd:PRK05851 372 IGEIEIRGASMMSGYLGQA----------PI---DPDDWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVA 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 934 VEHPMVADAAVI---IREDTPDNKQIVAYithhnEQVKPVLSNLRAFVTQRLPAF--MVPAHFVFMS--RLPLNANGKVD 1006
Cdd:PRK05851 438 AQVRGVREGAVVavgTGEGSARPGLVIAA-----EFRGPDEAGARSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKLR 512
|
.
gi 1574832895 1007 R 1007
Cdd:PRK05851 513 R 513
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1632-1851 |
1.79e-06 |
|
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: 52.72 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1632 TTLTYRQLNQQANQLAHLLRQHGIgPGCLVGLCLhrSPSLLLCLLAILKTGAAYVPLDPDYPS--QRLLWMAQDAQLSLL 1709
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTK-EGENVGVML--PPSAGGALANFALALSGKVPVMLNYTAglRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1710 LTHEEL--KARWPHC-----PCPLLCLDTLQER-------------YASLPCEDLQEACSPAQ---LAYVIYTSGSTGRP 1766
Cdd:cd05909 83 LTSKQFieKLKLHHLfdveyDARIVYLEDLRAKiskadkckaflagKFPPKWLLRIFGVAPVQpddPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1767 KGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSI--SFDIAGlELYLPLLAGAQIQLASqeQASDPRQLASLLAQLPIS 1844
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTG-CLWLPLLSGIKVVFHP--NPLDYKKIPELIYDKKAT 239
|
....*..
gi 1574832895 1845 ILQATPT 1851
Cdd:cd05909 240 ILLGTPT 246
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1635-1773 |
2.99e-06 |
|
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: 52.05 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1635 TYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLdpdypsqrllwmaqdaqlSLLLTHEE 1714
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL------------------FALFGPEA 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1715 LKARwphcpcpllcldtLQERYASLPCEDLqeacsPAQLAYVIYTSGSTGRPKGVQISH 1773
Cdd:cd05971 70 LEYR-------------LSNSGASALVTDG-----SDDPALIIYTSGTTGPPKGALHAH 110
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1633-1887 |
5.00e-06 |
|
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: 51.31 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTh 1712
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1713 eELKARWPhcpcpllcldtlqeryaslpcedlqeacspaqlAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPH 1792
Cdd:cd05910 81 -IPKADEP---------------------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1793 DRWLAitsiSFDIAGleLYLPLLAGAQI---QLASQEQASDPRQLASLLAQLPISILQATPTTWQLLleTGWSGKAGLTL 1869
Cdd:cd05910 127 EVDLA----TFPLFA--LFGPALGLTSVipdMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERV--ARYCAQHGITL 198
|
250
....*....|....*...
gi 1574832895 1870 lsgakPSLLISLAACCPV 1887
Cdd:cd05910 199 -----PSLRRVLSAGAPV 211
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
640-1010 |
5.98e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 51.32 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 640 NDIACLTFTSGSTGRPKGVLQRHGPLthFLPWMR----DRFAFTQTDRYSLLSGLAHDPLQREIFTPLCVGATICIPDqe 715
Cdd:PRK05620 181 TTAAAICYSTGTTGAPKGVVYSHRSL--YLQSLSlrttDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPG-- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 716 HMGDPGWLAQWMQGQEITIASFTPAL-LQLLTQGMGEddlPSARIpSLRYAFVVGDALTRRhVARLYAVAPHITCVNLYG 794
Cdd:PRK05620 257 PDLSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKN---PPERM-SLQEIYVGGSAVPPI-LIKAWEERYGVDVVHVWG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 795 STETqravsyfvLPTASSTESPASVT-ALLDKEVIPLGKGMPGAQILILNEAGNLAGIGE-LGEIYVRSPHLAFGYLDDP 872
Cdd:PRK05620 332 MTET--------SPVGTVARPPSGVSgEARWAYRVSQGRFPASLEYRIVNDGQVMESTDRnEGEIQVRGNWVTASYYHSP 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 873 DQTN----ERFLVNP-------FTHqehDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVAD 941
Cdd:PRK05620 404 TEEGggaaSTFRGEDvedandrFTA---DGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574832895 942 AAVIireDTPDNKQI-----VAYITHHNEQVKPVLSNLRAFVTQRLPAFMVPAHFVFMSRLPLNANGKVDRKAL 1010
Cdd:PRK05620 481 CAVI---GYPDDKWGerplaVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
855-995 |
6.28e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 51.27 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 855 GEIYVRSPHLAFGYLDDPDQTNERFLVNpfthqEHD-RLYRTGDLGRYLPDGNAEFAGRNDLQVKIR-GYRIELEEIEAI 932
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKTDEVYKVD-----ERGmRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 933 LVEHPMV------AD-------AAVIIREDTPDN---KQIVAY-----ITHHNEQVKPVLSNL-RAFVTQRLPAFMVPAH 990
Cdd:PLN02387 578 LSVSPYVdnimvhADpfhsycvALVVPSQQALEKwakKAGIDYsnfaeLCEKEEAVKEVQQSLsKAAKAARLEKFEIPAK 657
|
....*
gi 1574832895 991 FVFMS 995
Cdd:PLN02387 658 IKLLP 662
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1632-1884 |
7.11e-06 |
|
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: 51.09 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1632 TTLTYRQLNQQANQLAHLLRQHGIGPGCLVG-LCL--HR-------SPSlllcllailkTGAAYVPLDPDYPSQRLLWMA 1701
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVAtLAWntHRhlelyyaVPG----------MGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1702 QDAQLSLLLTH-------EELKARWPHCPCPLLCLDTLQERYASLPC----EDLQEACSPA--------QLAYVI-YTSG 1761
Cdd:cd12119 94 NHAEDRVVFVDrdflpllEAIAPRLPTVEHVVVMTDDAAMPEPAGVGvlayEELLAAESPEydwpdfdeNTAAAIcYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1762 STGRPKGVQISHGALlsfllslqsllslsphdrWL----AITSISFDIAGLELYLPL----------------LAGAQIQ 1821
Cdd:cd12119 174 TTGNPKGVVYSHRSL------------------VLhamaALLTDGLGLSESDVVLPVvpmfhvnawglpyaaaMVGAKLV 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574832895 1822 LASqeQASDPRQLASLLAQLPISILQATPTTWQLLLEtgWSGKAGLTLLSGAKpsLLISLAAC 1884
Cdd:cd12119 236 LPG--PYLDPASLAELIEREGVTFAAGVPTVWQGLLD--HLEANGRDLSSLRR--VVIGGSAV 292
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1633-1773 |
9.04e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 50.70 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVG-LCL-HRspSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLL 1710
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLALGVRAGDGVAvLARnHR--GFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 1711 THEELKARWPHCPCPLLCL-------DTLQERYASLPC-EDLQEACSPAQL-------AYVIYTSGSTGRPKGVQISH 1773
Cdd:PRK07788 152 YDDEFTDLLSALPPDLGRLrawggnpDDDEPSGSTDETlDDLIAGSSTAPLpkppkpgGIVILTSGTTGTPKGAPRPE 229
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1610-1767 |
1.10e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 50.37 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSlqPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPG--CLVGLclhrsPSLL---LCLLAILKTGAA 1684
Cdd:PRK10946 27 LTDILTRHAASDA--IAVICGERQFSYRELNQASDNLACSLRRQGIKPGdtALVQL-----GNVAefyITFFALLKLGVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1685 yvPLDPDYPSQR--LLWMAQDAQLSLLLT------------HEELKARWPHCPCPLLCLDTLQERYASL---PCEDLQEA 1747
Cdd:PRK10946 100 --PVNALFSHQRseLNAYASQIEPALLIAdrqhalfsdddfLNTLVAEHSSLRVVLLLNDDGEHSLDDAinhPAEDFTAT 177
|
170 180
....*....|....*....|.
gi 1574832895 1748 CSPA-QLAYVIYTSGSTGRPK 1767
Cdd:PRK10946 178 PSPAdEVAFFQLSGGSTGTPK 198
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
630-1010 |
1.21e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 50.51 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 630 SSAPAYrvgpndiacLTFTSGSTGRPKGVLQRHGP----LTHFLPWMRDRFAFTQTDRYSLLSGLA-HDPLqreiFTPLC 704
Cdd:PTZ00237 253 SSHPLY---------ILYTSGTTGNSKAVVRSNGPhlvgLKYYWRSIIEKDIPTVVFSHSSIGWVSfHGFL----YGSLS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 705 VGATIC-----IPDQEHMGDPGWLAqwMQGQEITIASFTPALLQLLTQgmgeDDlPSARIPSLRY------AFVVGDALT 773
Cdd:PTZ00237 320 LGNTFVmfeggIIKNKHIEDDLWNT--IEKHKVTHTLTLPKTIRYLIK----TD-PEATIIRSKYdlsnlkEIWCGGEVI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 774 RRHVARLYAVAPHITCVNLYGSTETqrAVSYFVlpTASSTESPASVTalldkeviplgkGMPGAQI--LILNEAGNLAGI 851
Cdd:PTZ00237 393 EESIPEYIENKLKIKSSRGYGQTEI--GITYLY--CYGHINIPYNAT------------GVPSIFIkpSILSEDGKELNV 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 852 GELGEIYVRSPhLAFGYLDDPDQTNERF--LVNPFTHqehdrLYRTGDLGryLPDGNAEFA--GRNDLQVKIRGYRIELE 927
Cdd:PTZ00237 457 NEIGEVAFKLP-MPPSFATTFYKNDEKFkqLFSKFPG-----YYNSGDLG--FKDENGYYTivSRSDDQIKISGNKVQLN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 928 EIEAILVEHPMVADAAVIIREDTPDNKQIVAYITHHNEQVKPVLS------NLRAFVTQRLPAFMVPAHFVFMSRLPLNA 1001
Cdd:PTZ00237 529 TIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDlnklknEINNIITQDIESLAVLRKIIIVNQLPKTK 608
|
....*....
gi 1574832895 1002 NGKVDRKAL 1010
Cdd:PTZ00237 609 TGKIPRQII 617
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1610-1767 |
1.37e-05 |
|
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: 50.14 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLd 1689
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 pdYPSQR---LLWMAQDAQLSLLLT------------HEELKARWPHC--------PCPLLCLDTLQERyaslPCEDLQE 1746
Cdd:COG1021 106 --LPAHRraeISHFAEQSEAVAYIIpdrhrgfdyralARELQAEVPSLrhvlvvgdAGEFTSLDALLAA----PADLSEP 179
|
170 180
....*....|....*....|.
gi 1574832895 1747 ACSPAQLAYVIYTSGSTGRPK 1767
Cdd:COG1021 180 RPDPDDVAFFQLSGGTTGLPK 200
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1626-1859 |
1.39e-05 |
|
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: 50.20 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1626 ALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPdypsqRLlwmaQDAQ 1705
Cdd:cd05923 21 ADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINP-----RL----KAAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1706 LSLLLTHEELKARWpHCPCPL---------LCLDTLQER-------YASLPCEDlqEACSPAQLAYVIYTSGSTGRPKGV 1769
Cdd:cd05923 92 LAELIERGEMTAAV-IAVDAQvmdaifqsgVRVLALSDLvglgepeSAGPLIED--PPREPEQPAFVFYTSGTTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1770 QISHGALLSFLLSLQSLLSLS--PHDRWLAITSISFDIAGLELYLPLLAGAQIQLASQEqaSDPRQLASLLAQLPISILQ 1847
Cdd:cd05923 169 VIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEE--FDPADALKLIEQERVTSLF 246
|
250
....*....|..
gi 1574832895 1848 ATPTTWQLLLET 1859
Cdd:cd05923 247 ATPTHLDALAAA 258
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1630-1853 |
1.43e-05 |
|
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: 49.97 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1630 GSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD--PDYPSQRllwmAQDAQLS 1707
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYDEPN----ARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1708 ---------LLLTH-------EELKARWPHCPCPLLCLDTLQERYASLPCEdlqeACSPAQLAYVIYTSGSTGRPKGVQI 1771
Cdd:cd05906 112 hiwqllgspVVLTDaelvaefAGLETLSGLPGIRVLSIEELLDTAADHDLP----QSRPDDLALLMLTSGSTGFPKAVPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1772 SHGALLSFLLSLQSLLSLSPHDR---WLAitsisFD-IAGL-ELYL-PLLAGA-QIQLASQEQASDPRQLASLLAQLPIS 1844
Cdd:cd05906 188 THRNILARSAGKIQHNGLTPQDVflnWVP-----LDhVGGLvELHLrAVYLGCqQVHVPTEEILADPLRWLDLIDRYRVT 262
|
....*....
gi 1574832895 1845 IlqatptTW 1853
Cdd:cd05906 263 I------TW 265
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1752-1873 |
1.47e-05 |
|
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: 49.25 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1752 QLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLaITSISFDIAGLE-LYLPLLAGAQIQLASQEQAsd 1830
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGGLAiLVRSLLAGAELVLLERNQA-- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1574832895 1831 prqLASLLAQLPISILQATPTTWQLLLE----TGWSGKAGLTLLSGA 1873
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPTQLQRLLDsgqgPAALKSLRAVLLGGA 121
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
513-988 |
1.78e-05 |
|
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: 49.74 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 513 TVSYGELEARSNQLAHYLH-AQGIRPHDVVAISAQRCAALVLAILGILKAGSTvlildpsypPArLLEYVqrahargwLR 591
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PA-FINYN--------LS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 592 IEGATDCQELdewcranSYCNLVLarnfalsgilsqyassapayrVGPNDIACLTFTSGSTGRPKGVlqrhgplthFLPW 671
Cdd:cd05937 67 GDPLIHCLKL-------SGSRFVI---------------------VDPDDPAILIYTSGTTGLPKAA---------AISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 672 MRDR---------FAFTQTDR-YS---LLSGLAHdplqreiFTPLCV----GATICIpdqehmgDPGWLAQ--WMQ--GQ 730
Cdd:cd05937 110 RRTLvtsnllshdLNLKNGDRtYTcmpLYHGTAA-------FLGACNclmsGGTLAL-------SRKFSASqfWKDvrDS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 731 EITIASFTPALLQLLTQGMGEddlPSARIPSLRYAFVVG------DALTRRhvarlYAVaPHITcvNLYGSTE-----TQ 799
Cdd:cd05937 176 GATIIQYVGELCRYLLSTPPS---PYDRDHKVRVAWGNGlrpdiwERFRER-----FNV-PEIG--EFYAATEgvfalTN 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 800 RAVSYFvlpTASSTESPASVTAL-LDKEVIPLGKGMPGAQILILNEAG--NLAGIGELGEIYVRSPH----LAFGYLDDP 872
Cdd:cd05937 245 HNVGDF---GAGAIGHHGLIRRWkFENQVVLVKMDPETDDPIRDPKTGfcVRAPVGEPGEMLGRVPFknreAFQGYLHNE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 873 DQTNERFLVNPFthQEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKIRGYRIELEEIEAILVEHPMVADAAVI-IREDTP 951
Cdd:cd05937 322 DATESKLVRDVF--RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYgVKVPGH 399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1574832895 952 DNKQIVAYITHHNEQVKPV---LSNLRAFVTQRLPAFMVP 988
Cdd:cd05937 400 DGRAGCAAITLEESSAVPTeftKSLLASLARKNLPSYAVP 439
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1625-1769 |
2.37e-05 |
|
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: 49.29 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDA 1704
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1705 QLSLLLTHEELKAR--------WPHCPCPLLCLDTLQERYASLPCEDLQE--------ACSPAQLAYVIYTSGSTGRPKG 1768
Cdd:cd05959 101 RARVVVVSGELAPVlaaaltksEHTLVVLIVSGGAGPEAGALLLAELVAAeaeqlkpaATHADDPAFWLYSSGSTGRPKG 180
|
.
gi 1574832895 1769 V 1769
Cdd:cd05959 181 V 181
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1602-1774 |
2.70e-05 |
|
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: 49.16 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1602 LPAAPSCGLHHLIEAQCERSslQPALHAGST--TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAIL 1679
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPS--RPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1680 KTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHEELKARWPHCPCPLLCLDTLQERyASLPCEDLQEACSPAQLAYVI-- 1757
Cdd:cd05904 79 SLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFD-SLSFSDLLFEADEAEPPVVVIkq 157
|
170 180
....*....|....*....|....
gi 1574832895 1758 -------YTSGSTGRPKGVQISHG 1774
Cdd:cd05904 158 ddvaallYSSGTTGRSKGVMLTHR 181
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1634-1773 |
3.07e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 49.00 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHE 1713
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1714 ELK-------------------------ARWPHC----------PCPLLCLDTLQERYASLPCEDLQEACSPAQLAYVI- 1757
Cdd:PRK12583 126 AFKtsdyhamlqellpglaegqpgalacERLPELrgvvslapapPPGFLAWHELQARGETVSREALAERQASLDRDDPIn 205
|
170
....*....|....*...
gi 1574832895 1758 --YTSGSTGRPKGVQISH 1773
Cdd:PRK12583 206 iqYTSGTTGFPKGATLSH 223
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1630-1773 |
3.25e-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: 48.83 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1630 GSTTLTYRQLNQQANQLAHLLRQH-GIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSL 1708
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1709 LLTHEELKA--------------RW----PHCPCPLL--CLDTLQERYASLPCEDLQEACSPAQLAYVIYTSGSTGRPKG 1768
Cdd:cd05938 82 LVVAPELQEaveevlpalradgvSVwylsHTSNTEGVisLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKA 161
|
....*
gi 1574832895 1769 VQISH 1773
Cdd:cd05938 162 ARISH 166
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1634-1814 |
4.35e-05 |
|
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: 48.62 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLdpdYPSqrllwmAQDAQLSLLLTHE 1713
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPT------LNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1714 ELKA------------------RWPHCPCPLLC-------LDTLQERYASLPCEDLQEacsPAQLAYVIYTSGSTGRPKG 1768
Cdd:cd05932 78 ESKAlfvgklddwkamapgvpeGLISISLPPPSaancqyqWDDLIAQHPPLEERPTRF---PEQLATLIYTSGTTGQPKG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1574832895 1769 VQISHGALLSFLLSLQSLLSLSPHDRWLAitsisfdiaglelYLPL 1814
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIGTEENDRMLS-------------YLPL 187
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1634-1869 |
6.14e-05 |
|
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: 47.90 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPL----DPDYPSQRLlwMAQDAQlsLL 1709
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGPKAIEHRL--RTSGAR--LV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1710 LTHEELKARwphcpcplLCLDTLQEryaslpcedlqeacspaqlayvIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSL 1789
Cdd:cd05973 77 VTDAANRHK--------LDSDPFVM----------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1790 SPHDRWLAITS------ISFDIAGlelylPLLAGAQIQLasQEQASDPRQLASLLAQLPISILQATPTTWQLLLETGWSG 1863
Cdd:cd05973 127 RPEDSFWNAADpgwaygLYYAITG-----PLALGHPTIL--LEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEV 199
|
....*.
gi 1574832895 1864 KAGLTL 1869
Cdd:cd05973 200 PARPKG 205
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1634-1858 |
6.46e-05 |
|
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: 47.56 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLdpdypsqrllwmaqdaqlSLLLTHE 1713
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------------TTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1714 ELKarwphcpcpllclDTLQERYASLPCEDLQEACSPAQLAYviYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHD 1793
Cdd:cd05974 63 DLR-------------DRVDRGGAVYAAVDENTHADDPMLLY--FTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 1794 RWLAITSISF-DIAGLELYLPLLAGAQIQLASQEQAsDPRQLASLLAQLPISILQATPTTWQLLLE 1858
Cdd:cd05974 128 VHWNISSPGWaKHAWSCFFAPWNAGATVFLFNYARF-DAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
639-968 |
7.43e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 47.89 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 639 PNDIACLTFTSGSTGRPKGVLQRHGPLTHFLPWM---RDRF--AFTQTDRYSLLSGLAH--DPLQREIFtpLCVGATIci 711
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQFedKMTHDDVYLSFLPLAHilDRMIEEYF--FRKGASV-- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 712 pdQEHMGDPGWLAQWMQGQEITIASFTPALLQLLTQGMG---EDDLPSARIP----------------SLRYAFVVGDAL 772
Cdd:PLN02430 295 --GYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQkalQELNPRRRLIfnalykyklawmnrgySHKKASPMADFL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 773 TRRHV-ARLYAVAPHITCVNLYGSTETQ---RAVS-YFVLPTASSTESPASVTALLDKEVIPLGK-GMPGA-QILILNEA 845
Cdd:PLN02430 373 AFRKVkAKLGGRLRLLISGGAPLSTEIEeflRVTScAFVVQGYGLTETLGPTTLGFPDEMCMLGTvGAPAVyNELRLEEV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 846 GNLA----GIGELGEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqeHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKI-R 920
Cdd:PLN02430 453 PEMGydplGEPPRGEICVRGKCLFSGYYKNPELTEEVM---------KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQ 523
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1574832895 921 GYRIELEEIEAILVEHPMVADaaVIIREDTpDNKQIVAYITHHNEQVK 968
Cdd:PLN02430 524 GEYVALEYLENVYGQNPIVED--IWVYGDS-FKSMLVAVVVPNEENTN 568
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1608-1858 |
9.25e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 47.34 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1608 CGLHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVglcLHRSPSLLLCLLAIL---KTGAA 1684
Cdd:PRK07470 7 MNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRI---LVHSRNCNQMFESMFaafRLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1685 YVP----LDPDypsqRLLWMAQDAQLSLLLTH----EELKARWPHCPCPLLCLD----TLQERYASLPCEDLQEACSPAQ 1752
Cdd:PRK07470 84 WVPtnfrQTPD----EVAYLAEASGARAMICHadfpEHAAAVRAASPDLTHVVAiggaRAGLDYEALVARHLGARVANAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1753 LAY-----VIYTSGSTGRPKGVQISHG--ALLSFLLSLQSLLSLSPHDRWLAITSISFDiAGLELYLPLLAGAQIQLASQ 1825
Cdd:PRK07470 160 VDHddpcwFFFTSGTTGRPKAAVLTHGqmAFVITNHLADLMPGTTEQDASLVVAPLSHG-AGIHQLCQVARGAATVLLPS 238
|
250 260 270
....*....|....*....|....*....|...
gi 1574832895 1826 EQAsDPRQLASLLAQLPISILQATPTTWQLLLE 1858
Cdd:PRK07470 239 ERF-DPAEVWALVERHRVTNLFTVPTILKMLVE 270
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
510-1009 |
1.05e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 47.42 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 510 EINTVSYGELEARSNQLAHYLHaQGIRPHDVVAISAQRCAALVLAILGILKAGS-TVLILDPSYPparllEYVQRAHARg 588
Cdd:PRK07769 52 VARDLTWSQFGARNRAVGARLQ-QVTKPGDRVAILAPQNLDYLIAFFGALYAGRiAVPLFDPAEP-----GHVGRLHAV- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 589 wlriegATDCQ--------ELDEWCRaNSYCNLVLA---RNFALSGILSQYASSAPAYRVGPNDIACLTFTSGSTGRPKG 657
Cdd:PRK07769 125 ------LDDCTpsailtttDSAEGVR-KFFRARPAKerpRVIAVDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 658 VLQRHGPLTHFLPWMRDRFAFTQTDRYSLLSGLAHD-PLQREIFTPLCVGA-TICIPdQEHMGDPG-WLAQWMQGQEITI 734
Cdd:PRK07769 198 VQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDmGLITVLLPALLGHYiTFMSP-AAFVRRPGrWIRELARKPGGTG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 735 ASFTpALLQLLTQGMGEDDLPSARIPSLRYAFVVG-----DALTRRHVARLY-AVAPhitcvnlYGSTETQRAVSY---- 804
Cdd:PRK07769 277 GTFS-AAPNFAFEHAAARGLPKDGEPPLDLSNVKGllngsEPVSPASMRKFNeAFAP-------YGLPPTAIKPSYgmae 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 805 ---FVLPTASSTEspASV-----TALLDKEVIPLGKGMPGA--------------QILILNEAGNLAGIGELGEIYVRSP 862
Cdd:PRK07769 349 atlFVSTTPMDEE--PTViyvdrDELNAGRFVEVPADAPNAvaqvsagkvgvsewAVIVDPETASELPDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 863 HLAFGYLDDPDQTNERF---LVNPFTHQ------EHDRLYRTGDLGRYLpDGNAEFAGR-NDLqVKIRG---YRIELEE- 928
Cdd:PRK07769 427 NIGTGYWGKPEETAATFqniLKSRLSEShaegapDDALWVRTGDYGVYF-DGELYITGRvKDL-VIIDGrnhYPQDLEYt 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 929 ------------IEAILV---EHPMVA--DAAVIIREDTPDNKQ---IVAYIT--HHNEQVKPVLSNLRAFVTQR--LPA 984
Cdd:PRK07769 505 aqeatkalrtgyVAAFSVpanQLPQVVfdDSHAGLKFDPEDTSEqlvIVAERApgAHKLDPQPIADDIRAAIAVRhgVTV 584
|
570 580
....*....|....*....|....*...
gi 1574832895 985 ---FMVPAhfvfmSRLPLNANGKVDRKA 1009
Cdd:PRK07769 585 rdvLLVPA-----GSIPRTSSGKIARRA 607
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1634-1769 |
1.44e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.91 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTHE 1713
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574832895 1714 ELKARWPHCPCPLLCLDTlqERYASLPCEDLQEACSPAQLayVIYTSGSTGRPKGV 1769
Cdd:PRK13383 141 EFAERIAGADDAVAVIDP--ATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGV 192
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1634-1775 |
1.45e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 46.92 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1634 LTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD-PDYPSQRLLW------MAQDAQL 1706
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLASAQP 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574832895 1707 SLLLTHEELK---------ARWPHCPCPLLcLDTLQERYASLPcedlqeACSPAQLAYVIYTSGSTGRPKGVQISHGA 1775
Cdd:PRK09192 130 AAIITPDELLpwvneathgNPLLHVLSHAW-FKALPEADVALP------RPTPDDIAYLQYSSGSTRFPRGVIITHRA 200
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1047-1093 |
1.49e-04 |
|
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: 42.24 E-value: 1.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1574832895 1047 VGITQNFFELGGHSLLATQLLARINEKFNSTLSLRSLFEAPTIEGIA 1093
Cdd:smart00823 33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1749-1774 |
1.83e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 46.65 E-value: 1.83e-04
10 20
....*....|....*....|....*.
gi 1574832895 1749 SPAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHG 273
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1624-1773 |
1.83e-04 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 46.56 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1624 QPALHAgSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQD 1703
Cdd:PRK06060 22 RPAFYA-ADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 1704 AQLSLLLTHEELKARWPhcPCPLL-CLDTLQERYASLPCEdlQEACSPAQLAYVIYTSGSTGRPKGVQISH 1773
Cdd:PRK06060 101 TEPALVVTSDALRDRFQ--PSRVAeAAELMSEAARVAPGG--YEPMGGDALAYATYTSGTTGPPKAAIHRH 167
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1736-1774 |
1.92e-04 |
|
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: 46.44 E-value: 1.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 1736 YASLPCEDLQEA----------CS--PAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:cd17639 61 YATLGEDALIHSlnetecsaifTDgkPDDLACIMYTSGSTGNPKGVMLTHG 111
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1625-1774 |
2.05e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.21 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGSTTLTYRQLNQQANQLAHLLRQHgIGPG--CLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPdypSQRLLWMAQ 1702
Cdd:PRK07867 20 RGLYFEDSFTSWREHIRGSAARAAALRAR-LDPTrpPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNP---TRRGAALAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1703 DAQLS---LLLTHEELKARWPHCPCPLLCLDTLQERYASL--PCEDLQ---EACSPAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:PRK07867 96 DIAHAdcqLVLTESAHAELLDGLDPGVRVINVDSPAWADElaAHRDAEppfRVADPDDLFMLIFTSGTSGDPKAVRCTHR 175
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1750-1775 |
2.21e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 46.05 E-value: 2.21e-04
10 20
....*....|....*....|....*.
gi 1574832895 1750 PAQLAYVIYTSGSTGRPKGVQISHGA 1775
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGN 138
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1610-1774 |
2.35e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 46.15 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:PRK05605 34 LVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRL-------------LW---------MAQDAQLSLLLT---------HEELKARWP-----------HCPCP-L 1726
Cdd:PRK05605 114 PLYTAHELehpfedhgarvaiVWdkvaptverLRRTTPLETIVSvnmiaamplLQRLALRLPipalrkaraalTGPAPgT 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1574832895 1727 LCLDTLQEryASLPCEDLQEAC---SPAQLAYVIYTSGSTGRPKGVQISHG 1774
Cdd:PRK05605 194 VPWETLVD--AAIGGDGSDVSHprpTPDDVALILYTSGTTGKPKGAQLTHR 242
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1633-1769 |
2.94e-04 |
|
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: 45.91 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLR-QHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRL-------------L 1698
Cdd:cd17632 67 TITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLapilaeteprllaV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1699 WMAQ-DAQLSLLLT------------HEELKA----------RWPHCPCPLLCLDTLQERYASL-PCEDLQEACSPAQLA 1754
Cdd:cd17632 147 SAEHlDLAVEAVLEggtpprlvvfdhRPEVDAhraalesareRLAAVGIPVTTLTLIAVRGRDLpPAPLFRPEPDDDPLA 226
|
170
....*....|....*
gi 1574832895 1755 YVIYTSGSTGRPKGV 1769
Cdd:cd17632 227 LLIYTSGSTGTPKGA 241
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1731-1770 |
4.01e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 45.32 E-value: 4.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1574832895 1731 TLQERY--ASLPCEDLqEACSPAqlaYVIYTSGSTGRPKGVQ 1770
Cdd:PRK10524 215 TLRAQHlgARVPVEWL-ESNEPS---YILYTSGTTGKPKGVQ 252
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1625-1773 |
4.34e-04 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 45.36 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1625 PALHAGST--TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQ 1702
Cdd:PLN02246 40 PCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1703 DAQLSLLLTH----EELKARWPHCPCPLLCLDTLQERYasLPCEDLQEAC---------SPAQLAYVIYTSGSTGRPKGV 1769
Cdd:PLN02246 120 ASGAKLIITQscyvDKLKGLAEDDGVTVVTIDDPPEGC--LHFSELTQADenelpeveiSPDDVVALPYSSGTTGLPKGV 197
|
....
gi 1574832895 1770 QISH 1773
Cdd:PLN02246 198 MLTH 201
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1749-1851 |
5.05e-04 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 45.30 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1749 SPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSI--SFDIAGlELYLPLLAGaqIQLASQE 1826
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV-TLWLPLLEG--IKVVYHP 856
|
90 100
....*....|....*....|....*
gi 1574832895 1827 QASDPRQLASLLAQLPISILQATPT 1851
Cdd:PRK08633 857 DPTDALGIAKLVAKHRATILLGTPT 881
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1623-1775 |
6.49e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 44.60 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1623 LQPALHAGSTTLTYRQLNQQANQLAHllRQHGIGPgclVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQ 1702
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAGAATAVAE--RVAGARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1703 DAQLSLLL--THEELKARwPHCPCpllcldTLQERYASLPCEDlqeacSPAQLAYVIYTSGSTGRPKGVQISHGA 1775
Cdd:PRK07787 90 DSGAQAWLgpAPDDPAGL-PHVPV------RLHARSWHRYPEP-----DPDAPALIVYTSGTTGPPKGVVLSRRA 152
|
|
| ArgR-Cyc_NRPS-like |
cd20480 |
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ... |
1339-1481 |
7.86e-04 |
|
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-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. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. 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). In addition to Cyc-domains there are various other 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. 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: 380470 [Multi-domain] Cd Length: 406 Bit Score: 44.03 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1339 RYWHGQLATAPALLDLPTD-HPRPPIQTFVgARHQLHLPAELLEQLMVLSHQQQVTLYMTLLAAFLLLLYRYSGQEDLVV 1417
Cdd:cd20480 182 AFWNEQILQLPSSANLPTVcEPEKLRETGI-TRRTLTLSSDKWQQLVTISKQHNVTPELTLASIFSAVLSLWGNQKDMML 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1418 GTPIAgrQRRELEGVIGLFANTLVLrtDLSG-DPSFLELLQRVREVTLQAYSQQDMPFEKLVAEL 1481
Cdd:cd20480 261 RFDLN--KKNDVAGVIGQFTQPLLV--GLSGfGQSFLSLVKENQKHFEQAYPFRQIPIFDLVRQL 321
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1610-1773 |
9.35e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 44.25 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1610 LHHLIEAQCERSSLQPALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLD 1689
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1690 PDYPSQRLLWMAQDAQLSLLL---------THEELKARWPHC---------PCPLLCLDTLQERYASLPCEDLQEA---- 1747
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILcldlvfprvTNVQSATKIEHVivtriadflPFPKNLLYPFVQKKQSNLVVKVSESetih 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1574832895 1748 ----------------CSPAQ-LAYVIYTSGSTGRPKGVQISH 1773
Cdd:PRK06710 186 lwnsvekevntgvevpCDPENdLALLQYTGGTTGFPKGVMLTH 228
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1635-1773 |
1.07e-03 |
|
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: 44.02 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1635 TYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLT--- 1711
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiae 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574832895 1712 ---HEELKARWPHCPCPLL---CLDTLQERYASLP--CEDLQEACSPAQ---------LAYVIYTSGSTGRPKGVQISH 1773
Cdd:cd05970 129 dniPEEIEKAAPECPSKPKlvwVGDPVPEGWIDFRklIKNASPDFERPTansypcgedILLVYFSSGTTGMPKMVEHDF 207
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1756-1888 |
1.08e-03 |
|
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: 43.64 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1756 VIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDRWLAITSIsFDIAGLE--LYLPLLAGAQIqlaSQEQASDPRQ 1833
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF-FHTFGYKagIVACLLTGATV---VPVAVFDVDA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1574832895 1834 LASLLAQLPISILQATPTTWQLLLETGWSGKAGLTLLSGAkpsllISLAACCPVA 1888
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAA-----VTGAATVPVE 130
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1726-1775 |
1.19e-03 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 44.02 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1726 LLCLDTLQERYASLPCEDLQEAcsPAQLAYVIYTSGSTGRPKGVQISHGA 1775
Cdd:PLN02860 149 FLTTEMLKQRALGTTELDYAWA--PDDAVLICFTSGTTGRPKGVTISHSA 196
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1633-1770 |
1.50e-03 |
|
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: 43.39 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLLWMAQDAQLSLLLTH 1712
Cdd:TIGR02188 88 KITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1713 EE---------LKA----RWPHCPCPL---LCLDTLQERYAS------LPCEDLQE----ACSPAQLA-----YVIYTSG 1761
Cdd:TIGR02188 168 DEglrggkvipLKAivdeALEKCPVSVehvLVVRRTGNPVVPwvegrdVWWHDLMAkasaYCEPEPMDsedplFILYTSG 247
|
....*....
gi 1574832895 1762 STGRPKGVQ 1770
Cdd:TIGR02188 248 STGKPKGVL 256
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1626-1773 |
2.31e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 42.77 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1626 ALHAGSTTL------------TYRQLNQQANQLAHLLRQHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDPD-Y 1692
Cdd:PRK07008 20 ARHAGDTEIvsrrvegdihryTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1693 PSQrLLWM---AQDAQLSLLLTHEEL-KARWPHCP------------------CPLLCLDTLQE----RYAsLPCEDLQE 1746
Cdd:PRK07008 100 PEQ-IAYIvnhAEDRYVLFDLTFLPLvDALAPQCPnvkgwvamtdaahlpagsTPLLCYETLVGaqdgDYD-WPRFDENQ 177
|
170 180
....*....|....*....|....*..
gi 1574832895 1747 ACSpaqlayVIYTSGSTGRPKGVQISH 1773
Cdd:PRK07008 178 ASS------LCYTSGTTGNPKGALYSH 198
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
855-944 |
2.37e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.78 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 855 GEIYVRSPHLAFGYLDDPDQTNERFlvnpfthqEHDRLYRTGDLGRYLPDGNAEFAGRNDLQVKI-RGYRIELEEIEAIL 933
Cdd:PLN02736 459 GEICVRGPIIFKGYYKDEVQTREVI--------DEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIENVY 530
|
90
....*....|.
gi 1574832895 934 VEHPMVADAAV 944
Cdd:PLN02736 531 AKCKFVAQCFV 541
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1749-1852 |
4.28e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 41.96 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1749 SPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSPHDR-------WLAITSISFDIagLELYLPLLAGAQIQ 1821
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLPLSHIAAQI--LDIWLPIKVGGQVY 225
|
90 100 110
....*....|....*....|....*....|.
gi 1574832895 1822 LAsqeqasdprQLASLLAQLPISILQATPTT 1852
Cdd:cd05933 226 FA---------QPDALKGTLVKTLREVRPTA 247
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1633-1795 |
4.53e-03 |
|
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: 41.65 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1633 TLTYRQLNQQANQLAHLLR-QHGIGPGCLVGLCLHRSPSLLLCLLAILKTGAAYVPLDpdypsqrllWMAQDAQLslllT 1711
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPL----I 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1712 HeelkarwphcpcpllCLDTlqeryaslpCEDLQEACSPAQLAYVIYTSGSTGRPKGVQISHGALLSFLLSLQSLLSLSP 1791
Cdd:cd05937 72 H---------------CLKL---------SGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKN 127
|
....
gi 1574832895 1792 HDRW 1795
Cdd:cd05937 128 GDRT 131
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
852-947 |
5.38e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 41.65 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 852 GELGEIYVRSPHLAFGYLDDPDQTNERF---LVNPFTHQEH-------DRLYRTGDLGRYLpDGNAEFAGRNDLQVKIRG 921
Cdd:PRK12476 427 GEVGEIWLHGDNIGRGYWGRPEETERTFgakLQSRLAEGSHadgaaddGTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
|
90 100
....*....|....*....|....*.
gi 1574832895 922 YRIELEEIEAilvehpMVADAAVIIR 947
Cdd:PRK12476 506 RNHYPQDIEA------TVAEASPMVR 525
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1622-1773 |
5.52e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 41.69 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1622 SLQP---ALHAGSTTLTYRQLNQQANQLAHLLRQHGIGPGClVGLCLHRSPSLLLCLLAILKTGAAYVPLDPDYPSQRLL 1698
Cdd:PRK07638 12 SLQPnkiAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 1699 WMAQDAQLSLLLTHEELKARWPHCPCPLLCLDT---LQERYAS--LPCEDLQEACspaqlAYVIYTSGSTGRPKGVQISH 1773
Cdd:PRK07638 91 ERLAISNADMIVTERYKLNDLPDEEGRVIEIDEwkrMIEKYLPtyAPIENVQNAP-----FYMGFTSGSTGKPKAFLRAQ 165
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
464-542 |
9.16e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 40.93 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574832895 464 YSLVSTRASSVLPDPGAPISAHW--EGTIHdlFAQQA--HLRPENIAII-----DEINTVSYGELEARSNQLAHYLHAQG 534
Cdd:PRK03584 58 FGVIGSTPYTVVLAGRRMPGARWfpGARLN--YAENLlrHRRDDRPAIIfrgedGPRRELSWAELRRQVAALAAALRALG 135
|
....*...
gi 1574832895 535 IRPHDVVA 542
Cdd:PRK03584 136 VGPGDRVA 143
|
|
| |
