|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-2547 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1955.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 5 PEIQDIY---PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVL 81
Cdd:PRK12467 41 PQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDE-EGFRQVID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 82 KERQSRLQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFL 161
Cdd:PRK12467 120 ASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 162 AIYKAL--GKE-QLPDFePVHpFSKYI----KWLMRQDRKEAEAFWKTRLIDVKQTASLP------KTSSSSKGKLEqma 228
Cdd:PRK12467 200 QLYSAYsqGREpSLPAL-PIQ-YADYAiwqrSWLEAGERERQLAYWQEQLGGEHTVLELPtdrprpAVPSYRGARLR--- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 229 FTLSKEQTEGLRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRpsDLEDVEKMVGLFINTIPVRVKSGPE- 307
Cdd:PRK12467 275 VDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR--NRVETERLIGFFVNTQVLKAEVDPQa 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 308 SFLTLVSHLQQESLKAEAYSYYPLYDI----QAQSMLKHE-----LFDHIVVFE--------NIPAQR--EIESLNQADA 368
Cdd:PRK12467 353 SFLELLQQVKRTALGAQAHQDLPFEQLvealQPERSLSHSplfqvMFNHQNTATggrdregaQLPGLTveELSWARHTAQ 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 369 FDFTVDDFDMDEvtnygcsikiipgsSLYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKM 448
Cdd:PRK12467 433 FDLALDTYESAQ--------------GLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARE 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 449 LYEFNqTEPAAPLAPTLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVI 528
Cdd:PRK12467 499 LVRWN-APATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVV 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 529 AVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGPGLSV-----SGFSGETLEVNLSSLRTEPAENEPVcaHTDG 603
Cdd:PRK12467 578 GLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAqlpvpAGLRSLCLDEPADLLCGYSGHNPEV--ALDP 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 604 GSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKD 683
Cdd:PRK12467 656 DNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARD 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 684 PALMTEAFTNEGVTTAHFIPAMANSFLDqvemeteEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTE 763
Cdd:PRK12467 736 AEAFAALMADQGVTVLKIVPSHLQALLQ-------ASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTE 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 764 ATVDAAFFRYDHEkDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPF-YR 842
Cdd:PRK12467 809 TTVGVSTYELSDE-ERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgAD 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 843 GERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYI------EGQ 916
Cdd:PRK12467 888 GGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLvpaavaDGA 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 917 DQKTARTE----LGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALPAPDGAAERRVYTAPRTITEMKLAKLWEEVLKYGP 992
Cdd:PRK12467 968 EHQATRDElkaqLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVER 1047
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 993 AGTRDHFFEQGGHSLKATALVSRIAKAFGVQVPLKEIFAKPTLEELAAVIQELDESPHAAIEPAEIQDTYPVSSAQKRMY 1072
Cdd:PRK12467 1048 VGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQW 1127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1073 VLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDDVPFQLME---LAAAED-- 1147
Cdd:PRK12467 1128 FLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ-EDGRTRQVIHPVGSLTLEEpllLAADKDea 1206
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1148 ----FV-----RPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYA------SRTLHPLRIQYK 1212
Cdd:PRK12467 1207 qlkvYVeaearQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAaysqgqSLQLPALPIQYA 1286
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1213 DYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLL 1292
Cdd:PRK12467 1287 DYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLL 1366
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1293 AAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEELVD 1372
Cdd:PRK12467 1367 ASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVE 1446
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1373 RLDVVRDMSRNPLFDVMFALQ-NMERESLTLHDLHLTTIAHDaHKVSKFDMTLYAAeEDQETIRFDVEFNTDIYQKQTIK 1451
Cdd:PRK12467 1447 ALQPERSLSHSPLFQVMFNHQrDDHQAQAQLPGLSVESLSWE-SQTAQFDLTLDTY-ESSEGLQASLTYATDLFEASTIE 1524
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1452 KWLSYYIHILHHVIEHQNIHLGDIHVLDEHETSSFIHTFNQTKQDYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRE 1531
Cdd:PRK12467 1525 RLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGE 1604
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1532 LNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLL-QS---DR 1607
Cdd:PRK12467 1605 LNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLtQShlqAR 1684
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1608 LESHMAGKRLFIEDIQ-LEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILL 1684
Cdd:PRK12467 1685 LPLPDGLRSLVLDQEDdWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYqlSAADVVLQ 1764
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1685 TASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLS--RLILGGE 1762
Cdd:PRK12467 1765 FTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSlrRVVCGGE 1844
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1763 ALSPNHVNRVRNTAPDLALWNGYGPTENT---TFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVG 1839
Cdd:PRK12467 1845 ALEVEALRPWLERLPDTGLFNLYGPTETAvdvTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLG 1924
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1840 GDGLARGYFGRPELTKEKFVPNPF-TPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKE 1918
Cdd:PRK12467 1925 GVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVRE 2004
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1919 AAVIVRTGPSGhKELLAYM-SLQAEMNIEKVRSL---------LSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPE 1988
Cdd:PRK12467 2005 AVVIAQDGANG-KQLVAYVvPTDPGLVDDDEAQValrailknhLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD 2083
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1989 TTAINTAYAPPRNQLEERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARLGRFDLKITAGDLFRHPTIKEAAPLI 2068
Cdd:PRK12467 2084 ASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVA 2163
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2069 RKTER--NIDQRPIEGEVPWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQL 2146
Cdd:PRK12467 2164 QEGDGtvSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGW 2243
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2147 QQFNRGIHGE----LYSLNIRDLsktAQWEKLIEDEvadlQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSW 2221
Cdd:PRK12467 2244 SAMHRAPEQErrplLWQVVVADK---EELEALCEQA----QRSLDLEEGPLLRAVLATLPDGSQrLLLVIHHLVVDGVSW 2316
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2222 RILLEDLSAAYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRTVEKEKAALLPCEKPHSAADNiRKTES 2301
Cdd:PRK12467 2317 RILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQR-RHAAS 2395
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2302 FT--LSEEDTHVLIHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRDHTLPELDISRTVGWFTTIYPVLId 2379
Cdd:PRK12467 2396 VTthLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKL- 2474
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2380 lhhAAEGELGLAVKTVKDTLGRIPDKGMGYGILKYLTSSENK-TIQFGKAPEIGFNYLGQFN---DTERQQKFSFSGLAS 2455
Cdd:PRK12467 2475 ---SPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARqTLQALPVPRITFNYLGQFDgsfDAEKQALFVPSGEFS 2551
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2456 GKDITPTWQREQTLEMSAMVRQNQLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHCAHKQETEKTVSDFSSQSLTAE 2535
Cdd:PRK12467 2552 GAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQE 2631
|
2650
....*....|..
gi 2040046167 2536 DLDDIASFVEEL 2547
Cdd:PRK12467 2632 QLDRLPVAVGDI 2643
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-2547 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1898.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2 VQQPEIQDIYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGsLDTERFQKSLDALIERYDIFRTAFIHKN-VAKPRQVV 80
Cdd:PRK12316 1548 LPAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDgLEQPLQVI 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 81 lkERQSRLQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEF 160
Cdd:PRK12316 1627 --HKQVELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEV 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 161 LAIYKAlgkeQLPDfEPVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVKQTASLPKTSSSSKGKLEQMAF--TLSKEQTEG 238
Cdd:PRK12316 1705 LQRYAG----QPVA-APGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHqqLLDPAQTRA 1779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 239 LRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPE-SFLTLVSHLQ 317
Cdd:PRK12316 1780 LAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDqSVADWLQEVQ 1859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 318 QESLKAEAYSYYPLYDIQAQSMLKHE-LFDHIVVFENIPAQreiESLNQADAFDFTVDDFDMDEVTNYGCSIKIIPGSSL 396
Cdd:PRK12316 1860 ALNLALREHEHTPLYDIQRWAGQGGEaLFDSLLVFENYPVA---EALKQGAPAGLVFGRVSNHEQTNYPLTLAVTLGETL 1936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 397 YIRINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKMLYEFNQTEPAAPLAPTLHSFFTRRAALS 476
Cdd:PRK12316 1937 SLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARA 2016
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:PRK12316 2017 PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML 2096
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTGPGLSVSGFSGETLEvNLSSLRTEPAENEPVCA---HTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFL 633
Cdd:PRK12316 2097 EDSGAALLLTQRHLLERLPLPAGVA-RLPLDRDAEWADYPDTApavQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHC 2175
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 634 SGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQG-WekDPALMTEAFTNEGVTTAHFIPAMansfLDQ 712
Cdd:PRK12316 2176 QAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDElW--DPEQLYDEMERHGVTILDFPPVY----LQQ 2249
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 713 VEMETEEKRTSLAktLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVPG 792
Cdd:PRK12316 2250 LAEHAERDGRPPA--VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGN 2327
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 793 ARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPF-YRGERMYQTGDLARWLPDGTVEWLGRMDGQV 871
Cdd:PRK12316 2328 RRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQV 2407
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 872 KIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTA-----RTELGKRLPAYMMPSSFIEMREWPV 946
Cdd:PRK12316 2408 KIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDllaelRAWLAARLPAYMVPAHWVVLERLPL 2487
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 947 TPSGKLDRKALPAPDGAAERRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALVSRIAKAFGVQVPL 1026
Cdd:PRK12316 2488 NPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPL 2567
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1027 KEIFAKPTLEELAAVIQELDESPHAAIEPAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFR 1106
Cdd:PRK12316 2568 RILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFD 2647
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1107 QLIRRHESLRTSFETGADG-----------EPVQRIHDDVPFQLMELAAAEDFVRPFRLQEAPLFRAALVKEAEESHLLL 1175
Cdd:PRK12316 2648 ALVLRHETLRTRFVEVGEQtrqvilpnmslRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLV 2727
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1176 VDMHHIISDGVSVGTLIREFSELYA------SRTLHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPA 1249
Cdd:PRK12316 2728 ITQHHIVSDGWSMQVMVDELVQAYAgarrgeQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPL 2807
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1250 DNARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMF 1329
Cdd:PRK12316 2808 DRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFF 2887
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1330 VNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHLTT 1409
Cdd:PRK12316 2888 VNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIES 2967
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1410 IAHDAHKvSKFDMTLyAAEEDQETIRFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDEHETSSFIHT 1489
Cdd:PRK12316 2968 FAWDGAA-TQFDLAL-DTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEA 3045
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1490 FNQTKQDYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGIL 1569
Cdd:PRK12316 3046 WNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLL 3125
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1570 GILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLL-QSDRLESHMAGKRLFIEDIQLEaGISANNPEQQGGPDSLAYIMYT 1648
Cdd:PRK12316 3126 AILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLsQSHLRLPLAQGVQVLDLDRGDE-NYAEANPAIRTMPENLAYVIYT 3204
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1649 SGSTGTPKGVMVEQRGVVRL--VKNSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQ 1726
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSNHlcWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELIN 3284
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1727 QNGITTLWLT-SSLFNQLSEQNERTFSDLSRLILGGEALSPNHVNRVrntAPDLALWNGYGPTENTTFSTCFRIEHEYKH 1805
Cdd:PRK12316 3285 SEGVDVLHAYpSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV---FAGLPLYNLYGPTEATITVTHWQCVEEGKD 3361
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1806 SIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTID 1885
Cdd:PRK12316 3362 AVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIE 3441
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1886 YIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGpsghKELLAYMSLQAEMNI--EKVRSLLSQQLPGFMIPA 1963
Cdd:PRK12316 3442 YIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPA 3517
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1964 HLVELAALPLTQNGKLDRRALPEPETTAINTAYAPPRNQLEERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARL 2043
Cdd:PRK12316 3518 HLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA 3597
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2044 GRFDLKITAGDLFRHPTIKEAAPLIR-KTERNIDQRPIEGEVPWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLR 2122
Cdd:PRK12316 3598 RQAGIRFTPKDLFQHQTIQGLARVARvGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALE 3677
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2123 TALQHLVIHHDALRMTIIDDGGQLQQFNRGIHGELYSLNIRDLSKTAQWEKLIEdevaDLQRSIHLQTGPLLKAGLFNTM 2202
Cdd:PRK12316 3678 AALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGE----EAQRSLDLADGPLLRALLATLA 3753
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2203 SGTY-LFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRTVEKEKA 2281
Cdd:PRK12316 3754 DGSQrLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVS 3833
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2282 ALLPCEKPHSAADNIRKTESFT-LSEEDTHVLIHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRDHTLPE 2360
Cdd:PRK12316 3834 SELPCDHPQGALQNRHAASVQTrLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFAD 3913
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2361 LDISRTVGWFTTIYPVLIdlhhAAEGELGLAVKTVKDTLGRIPDKGMGYGILKYLTSSENKTIQFG-KAPEIGFNYLGQF 2439
Cdd:PRK12316 3914 IDLSRTVGWFTSLFPVRL----SPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGlPVPRITFNYLGQF 3989
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2440 NDTERQQK--FSFSGLASGKDITPTWQREQTLEMSAMVRQNQLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHCAHK 2517
Cdd:PRK12316 3990 DGSFDEEMalFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDA 4069
|
2570 2580 2590
....*....|....*....|....*....|
gi 2040046167 2518 QETEKTVSDFSSQSLTAEDLDDIASFVEEL 2547
Cdd:PRK12316 4070 ERHGVTPSDFPLAGLDQARLDALPLPLGEI 4099
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
12-2538 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1691.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQSRLQFV 91
Cdd:PRK05691 677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERD-GVALQRIDAQGEFALQRI 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 92 DISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKEQ 171
Cdd:PRK05691 756 DLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 172 LPDFEPVH-PFSKYIKWlMRQ--DRKEAE---AFWKTRLIDVKQTASLPKT---SSSSKGKLEQMAFTLSKEQTEGLRKL 242
Cdd:PRK05691 836 TAELAPLPlGYADYGAW-QRQwlAQGEAArqlAYWKAQLGDEQPVLELATDhprSARQAHSAARYSLRVDASLSEALRGL 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 243 ALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSdlEDVEKMVGLFINTIPVRVK-SGPESFLTLVSHLQQESL 321
Cdd:PRK05691 915 AQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR--LETQGLVGFFINTQVLRAQlDGRLPFTALLAQVRQATL 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 322 KAEAYSYYPLYDI-----QAQsmlKHELFDhiVVFENipAQREIESLNQ-----ADAFDFTVDD--FDM---DEVTNYGc 386
Cdd:PRK05691 993 GAQAHQDLPFEQLvealpQAR---EQGLFQ--VMFNH--QQRDLSALRRlpgllAEELPWHSREakFDLqlhSEEDRNG- 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 387 sikiipgsslYIRINFDIG--LYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKmLYEFNQTePAAPLAPT 464
Cdd:PRK05691 1065 ----------RLTLSFDYAaeLFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQA-PCAPAQAW 1132
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLVTGPGL-----SVSGFSGetleVNLSSLRTEPAENEPVCAHTDGGSLAYVIYTSGSTGTP 619
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLlerlpQAEGVSA----IALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQP 1288
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 620 KGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTA 699
Cdd:PRK05691 1289 KGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTL 1368
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 700 HFIPAMANSFLDqvemeteEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEkDR 779
Cdd:PRK05691 1369 HFVPPLLQLFID-------EPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAE-DG 1440
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 780 ERMrlPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPF-YRGERMYQTGDLARWLPD 858
Cdd:PRK05691 1441 ERS--PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNAD 1518
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 859 GTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTARTE-----LGKRLPAYM 933
Cdd:PRK05691 1519 GALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAErlkaaLAAELPEYM 1598
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 934 MPSSFIEMREWPVTPSGKLDRKALPAPDGaaERRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALV 1013
Cdd:PRK05691 1599 VPAQLIRLDQMPLGPSGKLDRRALPEPVW--QQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIV 1676
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1014 SRIAKAFGVQVPLKEIFAKPTLEELAAVIQELDES----PHAAIEPAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAA 1089
Cdd:PRK05691 1677 SRTRQACDVELPLRALFEASELGAFAEQVARIQAAgernSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGM 1756
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1090 LKLTGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDDVPFQ-----------------LMELAAAEDFvRPF 1152
Cdd:PRK05691 1757 ARLSGVLDVDRFEAALQALILRHETLRTTFPS-VDGVPVQQVAEDSGLRmdwqdfsalpadarqqrLQQLADSEAH-QPF 1834
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1153 RLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYAS------RTLHPLRIQYKDYAVWQQAFKQGEA 1226
Cdd:PRK05691 1835 DLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAflddreSPLEPLPVQYLDYSVWQRQWLESGE 1914
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1227 YNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQE 1306
Cdd:PRK05691 1915 RQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQR 1994
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1307 DIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEELVDRLDVVRDMSRNPLF 1386
Cdd:PRK05691 1995 DLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLF 2074
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1387 DVMFALQNME-RESLTLHDLHLTTIAHDAhKVSKFDMTLYAAEEDQetiRFD--VEFNTDIYQKQTIKKWLSYYIHILHH 1463
Cdd:PRK05691 2075 QVMCNVQRWEfQQSRQLAGMTVEYLVNDA-RATKFDLNLEVTDLDG---RLGccLTYSRDLFDEPRIARMAEHWQNLLEA 2150
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1464 VIEHQNIHLGDIHVLDEHETSSFIHTFNQTKQDYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAAL 1543
Cdd:PRK05691 2151 LLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARAL 2230
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1544 RANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLqSDRLESHMAGK------RL 1617
Cdd:PRK05691 2231 RERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL-SDRALFEALGElpagvaRW 2309
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1618 FIEDIQ-LEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVR----LVKNSDMAfsPEDRILLTASLGFDA 1692
Cdd:PRK05691 2310 CLEDDAaALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMhcqaVIERFGMR--ADDCELHFYSINFDA 2387
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1693 MTFEVFGPLLNGACLYISDKETYlDSDRLKTFIQQNGITTLWLTSSLFNQLSE----QNErtFSDLSRLILGGEALSPNH 1768
Cdd:PRK05691 2388 ASERLLVPLLCGARVVLRAQGQW-GAEEICQLIREQQVSILGFTPSYGSQLAQwlagQGE--QLPVRMCITGGEALTGEH 2464
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1769 VNRVRNTAPDLALWNGYGPTENTTFS-TCFRIEH--EYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLAR 1845
Cdd:PRK05691 2465 LQRIRQAFAPQLFFNAYGPTETVVMPlACLAPEQleEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQ 2544
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1846 GYFGRPELTKEKFVPNPFTP-GERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVR 1924
Cdd:PRK05691 2545 GYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL 2624
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1925 TGPSGhKELLAYMS---------LQAEMNiEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTAINTA 1995
Cdd:PRK05691 2625 DTPSG-KQLAGYLVsavagqddeAQAALR-EALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQA 2702
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1996 YAPPRNQLEERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARLGRFDLKITAGDLFRHPTIKEAAPLIRKTER-N 2074
Cdd:PRK05691 2703 YQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAaQ 2782
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2075 IDQRPIEGEVPWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQFNRGIH 2154
Cdd:PRK05691 2783 AEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVT 2862
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2155 GE--LYSLNIRDLSKTAQwekliedEVADLQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLEDLSAA 2231
Cdd:PRK05691 2863 AQelLWQVTVADFAECAA-------LFADAQRSLDLQQGPLLRALLVDGPQGQQrLLLAIHHLVVDGVSWRVLLEDLQAL 2935
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2232 YSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRTVEKEKAALLPCEKPHSAADNIR-KTESFTLSEEDTH 2310
Cdd:PRK05691 2936 YRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHaQTVSVRLDAERTR 3015
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2311 VLIHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRDHTLPELDISRTVGWFTTIYPVLIDLHHAAEGELGL 2390
Cdd:PRK05691 3016 QLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAPGDDAARGE 3095
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2391 AVKTVKDTLGRIPDKGMGYGILKYL-TSSENKTIQFGKAPEIGFNYLGQFNdterqQKFSFSGLASGKDITPTWQRE--- 2466
Cdd:PRK05691 3096 SIKAIKEQLRAVPHKGLGYGVLRYLaDAAVREAMAALPQAPITFNYLGQFD-----QSFASDALFRPLDEPAGPAHDpda 3170
|
2570 2580 2590 2600 2610 2620 2630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 2467 ---QTLEMSAMVRQNQLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHCAHKQETEKTVSDFSSQSLTAEDLD 2538
Cdd:PRK05691 3171 plpNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLD 3245
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1051-2538 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1229.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1051 AAIEPAEIQdtyPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADgEPVQR 1130
Cdd:PRK12316 42 AGVSSAERD---RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGAD-DSLAQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1131 IHDDVPFQL------------MELAAAEDFVR----PFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIRE 1194
Cdd:PRK12316 118 VPLDRPLEVefedcsglpeaeQEARLRDEAQReslqPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1195 FSELY------ASRTLHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSL 1268
Cdd:PRK12316 198 FSRFYsayatgAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1269 DADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDF 1348
Cdd:PRK12316 278 DPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1349 LREVRETALEAYEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNM---ERESLTLHDLHLTTIAHDAhKVSKFDMTLY 1425
Cdd:PRK12316 358 LAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLvadIEALDTVAGLEFGQLEWKS-RTTQFDLTLD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1426 AAEEDqETIRFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDEHETSSFIHTFNQTKQDYPKHETISR 1505
Cdd:PRK12316 437 TYEKG-GRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHR 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1506 LFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDM 1585
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1586 PTERLEWMLSDSNAVMLLQSDRLESHM---AG-KRLFIEDIQLE-AGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMV 1660
Cdd:PRK12316 596 PAERLAYMLEDSGVQLLLSQSHLGRKLplaAGvQVLDLDRPAAWlEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGN 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1661 EQRGVVRLVKNSDMAFSPE--DRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSS 1738
Cdd:PRK12316 676 RHRALSNRLCWMQQAYGLGvgDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1739 LFNQ-LSEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANST 1817
Cdd:PRK12316 756 MLQAfLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLA 835
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1818 AYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIR 1897
Cdd:PRK12316 836 CYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR 915
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1898 GYRIELGEIEAALRQIDGVKEAAVIVRTGpsghKELLAYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHLVELAALPLTQ 1975
Cdd:PRK12316 916 GLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGYVVLESEGGDwrEALKAHLAASLPEYMVPAQWLALERLPLTP 991
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1976 NGKLDRRALPEPETTAINTAYAPPRNQLEERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARLGRFDLKITAGDL 2055
Cdd:PRK12316 992 NGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDL 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2056 FRHPTIKEAAPLIR-KTERNIDQRPIEGEVPWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDA 2134
Cdd:PRK12316 1072 FQHQTIRSLALVAKaGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDA 1151
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2135 LRMTIID-DGGQLQQFNRGIHGElySLNIRDLSKTAQWEKLIEDEvadlQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIH 2212
Cdd:PRK12316 1152 LRLRFREeDGGWQQAYAAPQAGE--VLWQRQAASEEELLALCEEA----QRSLDLEQGPLLRALLVDMADGSQrLLLVIH 1225
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2213 HLVVDGVSWRILLEDLSAAYSQAAAgqpvQLPRKTDSYQYFANRLAEYAESSkvIREQSYWRTVEKEKAALLPCEKPHSA 2292
Cdd:PRK12316 1226 HLVVDGVSWRILLEDLQRAYADLDA----DLPARTSSYQAWARRLHEHAGAR--AEELDYWQAQLEDAPHELPCENPDGA 1299
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2293 ADN-IRKTESFTLSEEDTHVLIHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRDHTLPELDISRTVGWFT 2371
Cdd:PRK12316 1300 LENrHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWFT 1379
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2372 TIYPVliDLHHAAegELGLAVKTVKDTLGRIPDKGMGYGILKYLTSSE-NKTIQFGKAPEIGFNYLGQFNDT-ERQQKFS 2449
Cdd:PRK12316 1380 SLFPV--RLTPAA--DLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEaAARLAALPQPRITFNYLGQFDRQfDEAALFV 1455
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2450 FSGLASGKDITPTWQREQTLEMSAMVRQNQLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHCAHKQETEKTVSDFSS 2529
Cdd:PRK12316 1456 PATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPL 1535
|
....*....
gi 2040046167 2530 QSLTAEDLD 2538
Cdd:PRK12316 1536 AGLSQAQLD 1544
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1045-2274 |
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: 1099.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1045 LDESPHAAIEPAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGAD 1124
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1125 GEPVQRIHDDVPFQLM---------------ELAAAEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVG 1189
Cdd:COG1020 81 RPVQVIQPVVAAPLPVvvllvdlealaeaaaEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1190 TLIREFSELYASRT------LHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDH 1263
Cdd:COG1020 161 LLLAELLRLYLAAYagaplpLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1264 VSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENK 1343
Cdd:COG1020 241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1344 CFSDFLREVRETALEAYEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHLTTIaHDAHKVSKFDMT 1423
Cdd:COG1020 321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPL-ELDSGTAKFDLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1424 LYAAEEDqETIRFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDEHETSSFIHTFNQTKQDYPKHETI 1503
Cdd:COG1020 400 LTVVETG-DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1504 SRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTE 1583
Cdd:COG1020 479 HELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1584 DMPTERLEWMLSDSNAVMLLQSDRLESHMAG---KRLFIEDIQLEAGiSANNPEQQGGPDSLAYIMYTSGSTGTPKGVMV 1660
Cdd:COG1020 559 AYPAERLAYMLEDAGARLVLTQSALAARLPElgvPVLALDALALAAE-PATNPPVPVTPDDLAYVIYTSGSTGRPKGVMV 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1661 EQRGVVRLV--KNSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSS 1738
Cdd:COG1020 638 EHRALVNLLawMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPS 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1739 LFNQLSEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKH--SIPIGRPIANS 1816
Cdd:COG1020 718 LLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADggSVPIGRPIANT 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1817 TAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFT-PGERMYRTGDLARWLKDGTIDYIGRMDDQVK 1895
Cdd:COG1020 798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1896 IRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHLVELAALPL 1973
Cdd:COG1020 878 IRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAaaALLRLALALLLPPYMVPAAVVLLLPLPL 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1974 TQNGKLDRRALPEPETTAINTAYAPPRNQLEERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARLGRFDLKITAG 2053
Cdd:COG1020 958 TGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLL 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2054 DLFRHPTIKEAAPLIRKTERNIDQRPIEGEV--PWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIH 2131
Cdd:COG1020 1038 LLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAplPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2132 HDALRMTIIDDGGQLQQFNRGIHGELYSLNIRDLSKTAQWEKLIEDEVADLQRSIHLQTGPLLKAGLFNTMSGTYLFLTI 2211
Cdd:COG1020 1118 LLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 2212 HHLVVDGVSWRILLEDLSAAYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWR 2274
Cdd:COG1020 1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALL 1260
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
461-2347 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 951.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 461 LAPTLHSFFTRRAALSPNLPAVRF------SGGILTYRELDQYTNQLAIRLKKKGVAKESVVgVLADRSPEMVIAVLAVL 534
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 535 KAGGAYVPLDPdyPE-------ERLRYMLADSGARLLVTGPGLSVSGFSGETLEVN-------LSSLRTEPAEN--EPvc 598
Cdd:PRK05691 86 YAGVIAVPAYP--PEsarrhhqERLLSIIADAEPRLLLTVADLRDSLLQMEELAAAnapellcVDTLDPALAEAwqEP-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 599 aHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQF--PLTEDDVIV----LKSSFSFDASIWQLFWWMIPGAS 672
Cdd:PRK05691 162 -ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVswlpLYHDMGLIGGLLQPIFSGVPCVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 673 M---YLL--PQGWekdpalmTEAFTNEGVTTAHFiPAMANSFLDQVEMETEEKRTSLAKtLKRVFAGGEALAPQTAARFA 747
Cdd:PRK05691 241 MspaYFLerPLRW-------LEAISEYGGTISGG-PDFAYRLCSERVSESALERLDLSR-WRVAYSGSEPIRQDSLERFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 748 RSLP-----ETAVIHGYGPTEAT----------------VDAAFFRYDH-EKDRERMRLPIGKPVPGARLYILDSEK-AV 804
Cdd:PRK05691 312 EKFAacgfdPDSFFASYGLAEATlfvsggrrgqgipaleLDAEALARNRaEPGTGSVLMSCGRSQPGHAVLIVDPQSlEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 805 QPIGVAGELYIAGAGVARGYLNRPELTEERFLDdpfYRGERMYQTGDLArWLPDGTVEWLGRMDGQVKIRGYRIEPGEVE 884
Cdd:PRK05691 392 LGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 885 AAL-RQIDGVRE---AAVVARTEGEE-TELYAYIEGQDQK-TARTELGKRL-----PAYMMPSSFIEMRE---WPVTPSG 950
Cdd:PRK05691 468 KTVeREVEVVRKgrvAAFAVNHQGEEgIGIAAEISRSVQKiLPPQALIKSIrqavaEACQEAPSVVLLLNpgaLPKTSSG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 951 KLDRKA---------------LPAPDGAAERRVYTAPRTITEMkLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALVSR 1015
Cdd:PRK05691 548 KLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQAR-IAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVAR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1016 IAKAFGVQVPLKEIFAKPTLEELAAVIQEL--DESPH-AAIEPAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKL 1092
Cdd:PRK05691 627 LRDELGIDLNLRQLFEAPTLAAFSAAVARQlaGGGAAqAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHL 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1093 TGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDDVPFQLM-----ELAAAEDFVR-----------PFRLQE 1156
Cdd:PRK05691 707 RGELDEAALRASFQRLVERHESLRTRFYE-RDGVALQRIDAQGEFALQridlsDLPEAEREARaaqireeearqPFDLEK 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1157 APLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASR------TLHPLRIQYKDYAVWQ-QAFKQGEAyNR 1229
Cdd:PRK05691 786 GPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWQrQWLAQGEA-AR 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1230 QEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDII 1309
Cdd:PRK05691 865 QLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIR 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1310 IGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEELVDRLDVVRDMSrnpLFDVM 1389
Cdd:PRK05691 945 IGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG---LFQVM 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1390 F-----------ALQNMERESLTLHDLHlttiahdahkvSKFDMTLYAAEEDQETIRFDVEFNTDIYQKQTIKKWLSYYI 1458
Cdd:PRK05691 1022 FnhqqrdlsalrRLPGLLAEELPWHSRE-----------AKFDLQLHSEEDRNGRLTLSFDYAAELFDAATIERLAEHFL 1090
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1459 HILHHVIEHQNIHLGDIHVLDEHETSSfIHTFNQTKQDyPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANR 1538
Cdd:PRK05691 1091 ALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCA-PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANR 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1539 IAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQS----DRLESHMAG 1614
Cdd:PRK05691 1169 LAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQshllERLPQAEGV 1248
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1615 KRLFIEDIQLEagisaNNPEQQGG----PDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK--NSDMAFSPEDRILLTASL 1688
Cdd:PRK05691 1249 SAIALDSLHLD-----SWPSQAPGlhlhGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQwmQATYALDDSDVLMQKAPI 1323
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1689 GFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERT-FSDLSRLILGGEALSPN 1767
Cdd:PRK05691 1324 SFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAaCTSLRRLFSGGEALPAE 1403
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1768 HVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGY 1847
Cdd:PRK05691 1404 LRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGY 1483
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1848 FGRPELTKEKFVPNPF-TPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTG 1926
Cdd:PRK05691 1484 LGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREG 1563
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1927 PSGhKELLAYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTAinTAYAPPRNQLE 2004
Cdd:PRK05691 1564 AAG-AQLVGYYTGEAGQEAeaERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ--REHVEPRTELQ 1640
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2005 ERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARL-GRFDLKITAGDLFRHPTIKEAAPLIRKT----ERNIdQRP 2079
Cdd:PRK05691 1641 QQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTrQACDVELPLRALFEASELGAFAEQVARIqaagERNS-QGA 1719
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2080 IE-----GEVPWTPVQR--WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTI-IDDGGQLQQFNR 2151
Cdd:PRK05691 1720 IArvdrsQPVPLSYSQQrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFpSVDGVPVQQVAE 1799
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2152 GIHGELYSLNIRDLSKTAQWEKLieDEVADLQ--RSIHLQTGPLLKAGLFNTMSGT-YLFLTIHHLVVDGVSWRILLEDL 2228
Cdd:PRK05691 1800 DSGLRMDWQDFSALPADARQQRL--QQLADSEahQPFDLERGPLLRACLVKAAEREhYFVLTLHHIVTEGWAMDIFAREL 1877
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2229 SAAYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRT-VEKEKAAL-LPCEKPHSAADNIR-KTESFTLS 2305
Cdd:PRK05691 1878 GALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAqLGNEHPLLeLPADRPRPPVQSHRgELYRFDLS 1957
|
2010 2020 2030 2040
....*....|....*....|....*....|....*....|....*
gi 2040046167 2306 EEdthvLIHKVN--NAYNTDTQDILLTAA-SLALCDWMGERKLRI 2347
Cdd:PRK05691 1958 PE----LAARVRafNAQRGLTLFMTMTATlAALLYRYSGQRDLRI 1998
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1014-2297 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 933.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1014 SRIAKAFgVQVPLKEifAKPTLEELAAVIQELDESPHAAIepAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLT 1093
Cdd:PRK12467 7 LRIARRF-ITLPLEK--RRLYLEKMQEEGVSFANLPIPQV--RSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1094 GPLDRARLDEVFRQLIRRHESLRTSFeTGADGEPVQRIHDDVPF-----------------QLMELAAAEdFVRPFRLQE 1156
Cdd:PRK12467 82 GELDVSALRRAFDALVARHESLRTRF-VQDEEGFRQVIDASLSLtiplddlaneqgraresQIEAYINEE-VARPFDLAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1157 APLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASR------TLHPLRIQYKDYAVWQQAFKQGEAYNRQ 1230
Cdd:PRK12467 160 GPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1231 EAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIII 1310
Cdd:PRK12467 240 LAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1311 GSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEELVDRLDVVRDMSRNPLFDVMF 1390
Cdd:PRK12467 320 GVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1391 ALQNM-----ERESLTLHDLHLTTIAHDAHKvSKFDMTLYAAEEDQEtIRFDVEFNTDIYQKQTIKKWLSYYIHILHHVI 1465
Cdd:PRK12467 400 NHQNTatggrDREGAQLPGLTVEELSWARHT-AQFDLALDTYESAQG-LWAAFTYATDLFEATTIERLATHWRNLLEAIV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1466 EHQNIHLGDIHVLDEHETSSFIHTFNQTKQDYPKHeTISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRA 1545
Cdd:PRK12467 478 AEPRRRLGELPLLDAEERARELVRWNAPATEYAPD-CVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1546 NGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDRLESHM---AGKR--LFIE 1620
Cdd:PRK12467 557 AGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLpvpAGLRslCLDE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1621 DIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILLTASLGFDAMTFEVF 1698
Cdd:PRK12467 637 PADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLqlAADDSMLMVSTFAFDLGVTELF 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1699 GPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSeQNERTFSDLSR--LILGGEALSPNHVNRVRNTA 1776
Cdd:PRK12467 717 GALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALL-QASRVALPRPQraLVCGGEALQVDLLARVRALG 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1777 PDLALWNGYGPTENTTFSTCFRIEHEYKHS--IPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELT 1854
Cdd:PRK12467 796 PGARLINHYGPTETTVGVSTYELSDEERDFgnVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALT 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1855 KEKFVPNPF-TPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGpSGHKEL 1933
Cdd:PRK12467 876 AERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPG-DAGLQL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1934 LAYM--------SLQAEMNIEkVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTAINTAYAPPRNQLEE 2005
Cdd:PRK12467 955 VAYLvpaavadgAEHQATRDE-LKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEK 1033
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2006 RLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARL-GRFDLKITAGDLFRHPTI----KEAAPLIRKTERNIDQRPI 2080
Cdd:PRK12467 1034 RLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVrQRLGIQVPLRTLFEHQTLagfaQAVAAQQQGAQPALPDVDR 1113
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2081 EGEVPWTPVQ--RWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQFnrgIHGEL- 2157
Cdd:PRK12467 1114 DQPLPLSYAQerQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQV---IHPVGs 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2158 YSLNIRDLSKTAQWEKLIEDEV-ADLQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLEDLSAAYSQA 2235
Cdd:PRK12467 1191 LTLEEPLLLAADKDEAQLKVYVeAEARQPFDLEQGPLLRVGLLRLAADEHvLVLTLHHIVSDGWSMQVLVDELVALYAAY 1270
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 2236 AAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRT-VEKEKAAL-LPCEKPHSAADNIR 2297
Cdd:PRK12467 1271 SQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAqLGGEQPVLeLPTDRPRPAVQSHR 1334
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
8-1300 |
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: 914.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 8 QDIYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHkNVAKPRQVVLKERQSR 87
Cdd:COG1020 15 AAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRT-RAGRPVQVIQPVVAAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 88 LQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKAL 167
Cdd:COG1020 94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 168 -----GKEQLPDFEPVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVKQTASLP-----KTSSSSKGKLEqmAFTLSKEQTE 237
Cdd:COG1020 174 yagapLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPtdrprPAVQSYRGARV--SFRLPAELTA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 238 GLRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPsdLEDVEKMVGLFINTIPVRVK-SGPESFLTLVSHL 316
Cdd:COG1020 252 ALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDlSGDPSFAELLARV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 317 QQESLKAEAYSYYPLYDIQ-----AQSMLKHELFDHIVVFENIPAQreieslnQADAFDFTVDDFDMD-EVTNYGCSIKI 390
Cdd:COG1020 330 RETLLAAYAHQDLPFERLVeelqpERDLSRNPLFQVMFVLQNAPAD-------ELELPGLTLEPLELDsGTAKFDLTLTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 391 IP-GSSLYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKMLYEFNQTEPAAPLAPTLHSFF 469
Cdd:COG1020 403 VEtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 470 TRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPE 549
Cdd:COG1020 483 EAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 550 ERLRYMLADSGARLLVTGPGL--SVSGFSGETLEVNLSSLRTEPAENEPVCAHTDggSLAYVIYTSGSTGTPKGVAVEHR 627
Cdd:COG1020 563 ERLAYMLEDAGARLVLTQSALaaRLPELGVPVLALDALALAAEPATNPPVPVTPD--DLAYVIYTSGSTGRPKGVMVEHR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 628 QAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMAN 707
Cdd:COG1020 641 ALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 708 SFLDQVemeteekrTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEkDRERMRLPIG 787
Cdd:COG1020 721 ALLDAA--------PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPP-DADGGSVPIG 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 788 KPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYR-GERMYQTGDLARWLPDGTVEWLGR 866
Cdd:COG1020 792 RPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpGARLYRTGDLARWLPDGNLEFLGR 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 867 MDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEG-EETELYAYIEGQDQKTA-----RTELGKRLPAYMMPSSFIE 940
Cdd:COG1020 872 ADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApGDKRLVAYVVPEAGAAAaaallRLALALLLPPYMVPAAVVL 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 941 MREWPVTPSGKLDRKALPAPDGAAERRVYTAPRTITEMKLAKLWEEVLKyGPAGTRDHFFEQGGHSLKATALVSRIAKAF 1020
Cdd:COG1020 952 LLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLV-VVVGDDDFFFFGGGLGLLLLLALARAARLL 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1021 GVQVPLKEIFAKPTLEELAAVIQELDESPHAAIEPAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRAR 1100
Cdd:COG1020 1031 LLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1101 LDEVFRQLIRRHESLRTSFETGADGEPVQRIHDDVPF-------------QLMELAAAEDFVRPFRLQEAPLFRAALVKE 1167
Cdd:COG1020 1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAAlalaallalllaaAAAAAELLAAAALLLLLALLLLALLLLLLL 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1168 AEESHLLLVDMHHIISDGVSVGTLIREFSELYASRT------LHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGE 1241
Cdd:COG1020 1191 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAaaaallALALLLALLALAALLALAALAALAAALLALALALLALA 1270
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1242 LPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLA 1300
Cdd:COG1020 1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
6-1354 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 852.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 6 EIQDIYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGsLDTERFQKSLDALIERYDIFRTAFIHK-NVAKPRQVVlkER 84
Cdd:PRK12467 2642 DIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDgELEEPLQVV--YK 2718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 85 QSRLQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIY 164
Cdd:PRK12467 2719 QARLPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY 2798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 165 kalGKEQLPdfEPVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVKQT----ASLPKTSSSSKGKLEQMAFTLSKEQTEGLR 240
Cdd:PRK12467 2799 ---FGQPPP--AREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPtrlaRALYPAPAEAVAGHGAHYLHLDATQTRQLI 2873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 241 KLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPE-SFLTLVSHLQQE 319
Cdd:PRK12467 2874 EFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEqTVSDWLQQVQAQ 2953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 320 SLKAEAYSYYPLYDIQAQSMLKHE-LFDHIVVFENIPAQreiESLNQADAFDFTVDDFDMDEVTNYGCSIKIIPGSSLYI 398
Cdd:PRK12467 2954 NLALREFEHTPLADIQRWAGQGGEaLFDSILVFENYPIS---EALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTLEL 3030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 399 RINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKMLYEFNQTEPAAPLAPTLHSFFTRRAALSPN 478
Cdd:PRK12467 3031 EFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPE 3110
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 479 LPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLAD 558
Cdd:PRK12467 3111 APALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIED 3190
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 559 SGARLLVTGPGL-----SVSGfsGETLEVNLSSLRTEPAENePVcAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFL 633
Cdd:PRK12467 3191 SGVKLLLTQAHLleqlpAPAG--DTALTLDRLDLNGYSENN-PS-TRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHL 3266
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 634 SGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPqGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDqv 713
Cdd:PRK12467 3267 CWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAYLQQFAE-- 3343
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 714 emetEEKRTSLAkTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVPGA 793
Cdd:PRK12467 3344 ----DAGGADCA-SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGR 3418
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 794 RLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFY-RGERMYQTGDLARWLPDGTVEWLGRMDGQVK 872
Cdd:PRK12467 3419 SIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVK 3498
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 873 IRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAY----IEGQDQK-TARTELGKRLPAYMMPSSFIEMREWPVT 947
Cdd:PRK12467 3499 IRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYvvpaDPQGDWReTLRDHLAASLPDYMVPAQLLVLAAMPLG 3578
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 948 PSGKLDRKALPAPDgAAERRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALVSRIAKAFGVQVPLK 1027
Cdd:PRK12467 3579 PNGKVDRKALPDPD-AKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLR 3657
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1028 EIFAKPTLEELAAVIQELDesphAAIEPAeiqdtypvssaqkrmyvlqqledggvgynmpaalkltgpLDRARLDEVFRQ 1107
Cdd:PRK12467 3658 DLMSAPTIAELAGYSPLGD----VPVNLL---------------------------------------LDLNRLETGFPA 3694
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1108 LIRRHESLRTSFetgaDGEPVQRIHDdvpfqlmelaaaedfvrpfrlqeaplfraalvkeaEESHLLLVDMHHIISDGvs 1187
Cdd:PRK12467 3695 LFCRHEGLGTVF----DYEPLAVILE-----------------------------------GDRHVLGLTCRHLLDDG-- 3733
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1188 vgtlirefselYASRTLHPLRIQYKDYAVWQQAfkQGEAYnrqEAYWlkQLDGELpvlelpadnarpavrsfagdhvsfs 1267
Cdd:PRK12467 3734 -----------WQDTSLQAMAVQYADYILWQQA--KGPYG---LLGW--SLGGTL------------------------- 3770
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1268 ldadtssglykiardngctlymvllaaySTLLARLSGQEdiiigspiagrahKDLESVIGMFVNTLAIRTRPVENKCFSD 1347
Cdd:PRK12467 3771 ----------------------------ARLVAELLERE-------------GESEAFLGLFDNTLPLPDEFVPQAEFLE 3809
|
....*..
gi 2040046167 1348 FLREVRE 1354
Cdd:PRK12467 3810 LLRQLGE 3816
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-1050 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 838.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 6 EIQDIYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGsLDTERFQKSLDALIERYDIFRTAFIHKN-VAKPRQVVLKER 84
Cdd:PRK12316 4098 EIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGeLGRPLQVVHKQV 4176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 85 QsrLQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIY 164
Cdd:PRK12316 4177 S--LPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 165 KALGKEQlpdfePVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVKQTASLPKTSSSSKGK----LEQMAFTLSKEQTEGLR 240
Cdd:PRK12316 4255 SGRPPAQ-----PGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRsangYGEHVRELDATATARLR 4329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 241 KLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPE-SFLTLVSHLQQE 319
Cdd:PRK12316 4330 EFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQqSVVEWLQQVQRQ 4409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 320 SLKAEAYSYYPLYDIQAQSMLKHE-LFDHIVVFENIPAQreiESLNQADAFDFTVDDFDMDEVTNYGCSIKIIPGSSLYI 398
Cdd:PRK12316 4410 NLALREHEHTPLYEIQRWAGQGGEaLFDSLLVFENYPVS---EALQQGAPGGLRFGEVTNHEQTNYPLTLAVGLGETLSL 4486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 399 RINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKMLYEFNQTEPAAPLAPTLHSFFTRRAALSPN 478
Cdd:PRK12316 4487 QFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPD 4566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 479 LPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLAD 558
Cdd:PRK12316 4567 AVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMED 4646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 559 SGARLLVTGPGLSvsgfSGETLEVNLSSLRTEPA-------ENEPVCAhTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAA 631
Cdd:PRK12316 4647 SGAALLLTQSHLL----QRLPIPDGLASLALDRDedwegfpAHDPAVR-LHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN 4721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 632 FLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEkDPALMTEAFTNEGVTTAHFIPAMANSFLD 711
Cdd:PRK12316 4722 HLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAE 4800
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 712 QVEMETEEKRtslaktLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVP 791
Cdd:PRK12316 4801 HAERDGEPPS------LRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLG 4874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 792 GARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPF-YRGERMYQTGDLARWLPDGTVEWLGRMDGQ 870
Cdd:PRK12316 4875 NRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQ 4954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 871 VKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTA-------------RTELGKRLPAYMMPSS 937
Cdd:PRK12316 4955 VKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALAdadeaqaelrdelKAALRERLPEYMVPAH 5034
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 938 FIEMREWPVTPSGKLDRKALPAPDGAAERRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALVSRIA 1017
Cdd:PRK12316 5035 LVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQ 5114
|
1050 1060 1070
....*....|....*....|....*....|...
gi 2040046167 1018 KAFGVQVPLKEIFAKPTLEELAAVIQELDESPH 1050
Cdd:PRK12316 5115 LELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-1354 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 756.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFiHKNVAKPRQVVLKERQSRLQFV 91
Cdd:PRK12316 51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF-PRGADDSLAQVPLDRPLEVEFE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 92 DISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKEQ 171
Cdd:PRK12316 130 DCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 172 LPDFEPVhP--FSKYI----KWLMRQDRKEAEAFWKTRLIDVKQTASLPK-----TSSSSKGKLEQmaFTLSKEQTEGLR 240
Cdd:PRK12316 210 EPGLPAL-PiqYADYAlwqrSWLEAGEQERQLEYWRAQLGEEHPVLELPTdhprpAVPSYRGSRYE--FSIDPALAEALR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 241 KLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRpsDLEDVEKMVGLFINTIPVRVK-SGPESFLTLVSHLQQE 319
Cdd:PRK12316 287 GTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANR--NRAEVEGLIGFFVNTQVLRSVfDGRTRVATLLAGVKDT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 320 SLKAEAYSYYP---LYD-IQAQSMLKHE-LFDhiVVFENIPAQREIESLNQADAFDFTVDDFDmDEVTNYGCSIKII-PG 393
Cdd:PRK12316 365 VLGAQAHQDLPferLVEaLKVERSLSHSpLFQ--VMYNHQPLVADIEALDTVAGLEFGQLEWK-SRTTQFDLTLDTYeKG 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 394 SSLYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKMLYEFNQTEPAAPLAPTLHSFFTRRA 473
Cdd:PRK12316 442 GRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQV 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 474 ALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLR 553
Cdd:PRK12316 522 ERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLA 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 554 YMLADSGARLLVT----GPGLSVS-GFSGETLEVNLSSLRTEPAENEPVCAHTDggSLAYVIYTSGSTGTPKGVAVEHRQ 628
Cdd:PRK12316 602 YMLEDSGVQLLLSqshlGRKLPLAaGVQVLDLDRPAAWLEGYSEENPGTELNPE--NLAYVIYTSGSTGKPKGAGNRHRA 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANS 708
Cdd:PRK12316 680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLdqvemetEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRErmrLPIGK 788
Cdd:PRK12316 760 FL-------QDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDS---VPIGR 829
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 789 PVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMD 868
Cdd:PRK12316 830 PIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRID 909
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 869 GQVKIRGYRIEPGEVEAALRQIDGVREAAVVARtegEETELYAYIEGQDQKTARTE-----LGKRLPAYMMPSSFIEMRE 943
Cdd:PRK12316 910 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQLVGYVVLESEGGDWREalkahLAASLPEYMVPAQWLALER 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 944 WPVTPSGKLDRKALPAPDGAAERRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALVSRiAKAFGVQ 1023
Cdd:PRK12316 987 LPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSR-ARQAGIQ 1065
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1024 VPLKEIFAKPTLEELAAVIQeldESPHAAIEPAEIQDTYPVSSAQKRMYvlQQLEDGGVGYNMPAALKLTGPLDRARLDE 1103
Cdd:PRK12316 1066 LSPRDLFQHQTIRSLALVAK---AGQATAADQGPASGEVALAPVQRWFF--EQAIPQRQHWNQSLLLQARQPLDPDRLGR 1140
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1104 VFRQLIRRHESLRTSFEtGADGEPVQRIHDDVPFQLM---------ELAA-AEDFVRPFRLQEAPLFRAALVKEAEESHL 1173
Cdd:PRK12316 1141 ALERLVAHHDALRLRFR-EEDGGWQQAYAAPQAGEVLwqrqaaseeELLAlCEEAQRSLDLEQGPLLRALLVDMADGSQR 1219
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1174 LLVDMHHIISDGVSVGTLIREFSELYASRT--LHPLRIQYKDYAVWQQAFKQGEAynRQEAYWLKQLDGELPvlELPADN 1251
Cdd:PRK12316 1220 LLLVIHHLVVDGVSWRILLEDLQRAYADLDadLPARTSSYQAWARRLHEHAGARA--EELDYWQAQLEDAPH--ELPCEN 1295
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1252 ARPAVRSFAGDHVSFSLDADTSSGLYKIA----RDNGCTLymvLLAAYSTLLARLSGQEDIIIGSPIAGRAHK----DLE 1323
Cdd:PRK12316 1296 PDGALENRHERKLELRLDAERTRQLLQEApaayRTQVNDL---LLTALARVTCRWSGQASVLVQLEGHGREDLfediDLS 1372
|
1370 1380 1390
....*....|....*....|....*....|.
gi 2040046167 1324 SVIGMFVNTLAIRTRPVENkcFSDFLREVRE 1354
Cdd:PRK12316 1373 RTVGWFTSLFPVRLTPAAD--LGESIKAIKE 1401
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1031-2063 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 749.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1031 AKPTLEELAAVIQE-LDESPHAaiePAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGpLDRARLDEVFRQLI 1109
Cdd:PRK12316 4074 VTPSDFPLAGLDQArLDALPLP---LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAAL 4149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1110 RRHESLRTSF-ETGADGEPVQRIHDDV--PF-------------QLMELAAAEDfVRPFRLQEAPLFRAALVKEAEESHL 1173
Cdd:PRK12316 4150 DRHDVLRSGFvWQGELGRPLQVVHKQVslPFaeldwrgradlqaALDALAAAER-ERGFDLQRAPLLRLVLVRTAEGRHH 4228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1174 LLVDMHHIISDGVSVGTLIREFSELYASRTLHPLRIQYKDYAVWQQafKQGEAYNrqEAYWLKQLDGELPVLELPADNAR 1253
Cdd:PRK12316 4229 LIYTNHHILMDGWSNSQLLGEVLERYSGRPPAQPGGRYRDYIAWLQ--RQDAAAS--EAFWREQLAALDEPTRLAQAIAR 4304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1254 PAVRSFAG--DHVSfSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAH--KDLESVIGMF 1329
Cdd:PRK12316 4305 ADLRSANGygEHVR-ELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAelPGIEGQIGLF 4383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1330 VNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEELvdrlDVVRDMSRNPLFDVMFALQN------MEResLTLH 1403
Cdd:PRK12316 4384 INTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEI----QRWAGQGGEALFDSLLVFENypvseaLQQ--GAPG 4457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1404 DLHLTTIAHdaHKVSKFDMTLYAAEEDQETIRFDveFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDEHET 1483
Cdd:PRK12316 4458 GLRFGEVTN--HEQTNYPLTLAVGLGETLSLQFS--YDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQ 4533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1484 SSFIHTFNQTKQDYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPE 1563
Cdd:PRK12316 4534 QRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAE 4613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1564 LAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQ----SDRLESHMAGKRLFIEDIQLEAGISANNPEQQGGP 1639
Cdd:PRK12316 4614 MMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTqshlLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHP 4693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1640 DSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKEtYLD 1717
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYelTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDS-LWD 4772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1718 SDRLKTFIQQNGITTLWLTSSLFNQLSEQNERT--FSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFST 1795
Cdd:PRK12316 4773 PERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDgePPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVL 4852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1796 CFRI---EHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF-TPGERMYR 1871
Cdd:PRK12316 4853 LWKArdgDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYR 4932
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1872 TGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGhKELLAYM-----------SLQ 1940
Cdd:PRK12316 4933 TGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVvpqdpaladadEAQ 5011
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1941 AEMNiEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTAINTAYAPPRNQLEERLAVIWQEVLGVEKV 2020
Cdd:PRK12316 5012 AELR-DELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERV 5090
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 2040046167 2021 GIEDSFFELGGDSIKALQVSARL-GRFDLKITAGDLFRHPTIKE 2063
Cdd:PRK12316 5091 GLDDNFFELGGHSLLAIQVTSRIqLELGLELPLRELFQTPTLAA 5134
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1505-1984 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 710.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1505 RLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTED 1584
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1585 MPTERLEWMLSDSNAVMLLQSDRLESHMAGKRLFIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRG 1664
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1665 VVRLVKNSD-MAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQL 1743
Cdd:cd12117 161 VVRLVKNTNyVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1744 SEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKH--SIPIGRPIANSTAYIV 1821
Cdd:cd12117 241 ADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVagSIPIGRPIANTRVYVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1822 NSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRI 1901
Cdd:cd12117 321 DEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1902 ELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
...
gi 2040046167 1982 RAL 1984
Cdd:cd12117 481 RAL 483
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1038-2145 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 703.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1038 LAAVIQE-LDESPHAaiePAEIQDTYPVSSAQKRMyVLQQLEDGGVG-YNMPAALKLTGpLDRARLDEVFRQLIRRHESL 1115
Cdd:PRK12467 2625 LAGLSQEqLDRLPVA---VGDIEDIYPLSPMQQGM-LFHTLYEGGAGdYINQMRVDVEG-LDVERFRTAWQAVIDRHEIL 2699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1116 RTSF-ETGADGEPVQRIHD--DVPFQ-------------LMELAAAeDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMH 1179
Cdd:PRK12467 2700 RSGFlWDGELEEPLQVVYKqaRLPFSrldwrdradleqaLDALAAA-DRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNH 2778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1180 HIISDGVSVGTLIREFSELYASRTLHPLRIQYKDYAVWQQAfkqgEAYNRQEAYWLKQL-DGELPVLELPADNARPA-VR 1257
Cdd:PRK12467 2779 HILMDGWSGSQLLGEVLQRYFGQPPPAREGRYRDYIAWLQA----QDAEASEAFWKEQLaALEEPTRLARALYPAPAeAV 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1258 SFAGDHvSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAH--KDLESVIGMFVNTLAI 1335
Cdd:PRK12467 2855 AGHGAH-YLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAqlRGAEQQLGLFINTLPV 2933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1336 RTRPVENKCFSDFLREVRETALEAYEHQDYPF-----------EELVDRLDVVRDmsrnplFDVMFALQNMERESLTLHD 1404
Cdd:PRK12467 2934 IASPRAEQTVSDWLQQVQAQNLALREFEHTPLadiqrwagqggEALFDSILVFEN------YPISEALKQGAPSGLRFGA 3007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1405 LHlttiahdAHKVSKFDMTLYAAEEDQETIRFDveFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDEHETS 1484
Cdd:PRK12467 3008 VS-------SREQTNYPLTLAVGLGDTLELEFS--YDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERR 3078
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1485 SFIHTFNQTKQDYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPEL 1564
Cdd:PRK12467 3079 QVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEM 3158
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1565 AVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDRLESHM----AGKRLFIEDIQLEaGISANNPEQQGGPD 1640
Cdd:PRK12467 3159 IVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpapaGDTALTLDRLDLN-GYSENNPSTRVMGE 3237
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1641 SLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYlDS 1718
Cdd:PRK12467 3238 NLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYelDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DP 3316
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 DRLKTFIQQNGITTLWLTSSLFNQLSEQNE-RTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENT---TFS 1794
Cdd:PRK12467 3317 EELWQAIHAHRISIACFPPAYLQQFAEDAGgADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVvtvTLW 3396
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1795 TCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF-TPGERMYRTG 1873
Cdd:PRK12467 3397 KCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsGSGGRLYRTG 3476
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1874 DLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGhKELLAYMSLQAEMN--IEKVRSL 1951
Cdd:PRK12467 3477 DLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGdwRETLRDH 3555
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1952 LSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTaINTAYAPPRNQLEERLAVIWQEVLGVEKVGIEDSFFELGG 2031
Cdd:PRK12467 3556 LAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK-GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGG 3634
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2032 DSIKALQVSARLGR-FDLKITAGDLFRHPTIKEAAPliRKTERNIDQRPIegevpwTPVQRwflaqhieERQHFNQSVML 2110
Cdd:PRK12467 3635 DSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAELAG--YSPLGDVPVNLL------LDLNR--------LETGFPALFCR 3698
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|...
gi 2040046167 2111 HSSEG--FQEQPLRTALQH------LVIHHdalrmtIIDDGGQ 2145
Cdd:PRK12467 3699 HEGLGtvFDYEPLAVILEGdrhvlgLTCRH------LLDDGWQ 3735
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1515-1984 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 631.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLqsdrleshmagkrlfiediqleagisannpeqqGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDM 1674
Cdd:cd05930 81 EDSGAKLVL---------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1675 AF--SPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQL-SEQNERTF 1751
Cdd:cd05930 128 AYplTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLlQELELAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1752 SDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRI--EHEYKHSIPIGRPIANSTAYIVNSRGRLQP 1829
Cdd:cd05930 208 PSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLRPVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1830 MGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAA 1909
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 1910 LRQIDGVKEAAVIVRTGPSGHKELLAYMSLQA--EMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05930 368 LLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-1048 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 631.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 6 EIQDIYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLKERQ 85
Cdd:PRK05691 3253 EIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGR 3332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 86 SRLQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYK 165
Cdd:PRK05691 3333 TPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYT 3412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 166 ALGKEQLPDFEPVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVKQTASLP-------KTSSSSKGKLEQMAFT-LSKEQTE 237
Cdd:PRK05691 3413 ALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPIPsdrpflrEHAGDSGGMVVGDCYTrLDAADGA 3492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 238 GLRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSgPE-----SFLTL 312
Cdd:PRK05691 3493 RLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQL-PAagqrcSVRQW 3571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 313 VSHLQQESLKAEAYSYYPLYDIQAQSMLK--HELFDHIVVFENIPAqrEIESLNQADAFDFTVDDFDMDevTNYGCSIKI 390
Cdd:PRK05691 3572 LQGLLDSNMELREYEYLPLVAIQECSELPkgQPLFDSLFVFENAPV--EVSVLDRAQSLNASSDSGRTH--TNFPLTAVC 3647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 391 IPGSSLYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKMLYEFNQTEPAAPLAPTLHSFFT 470
Cdd:PRK05691 3648 YPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFE 3727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 471 RRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEE 550
Cdd:PRK05691 3728 AQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQ 3807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 551 RLRYMLADSGARLLVTGPGLSVSGFS--GETLEVNLSSLRT-EPAENEPVCAHTDG-----GSLAYVIYTSGSTGTPKGV 622
Cdd:PRK05691 3808 RLQRIIELSRTPVLVCSAACREQARAllDELGCANRPRLLVwEEVQAGEVASHNPGiysgpDNLAYVIYTSGSTGLPKGV 3887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 623 AVEHRqaaAFLSGMQRQFP---LTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTA 699
Cdd:PRK05691 3888 MVEQR---GMLNNQLSKVPylaLSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVL 3964
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 700 HFIPAMANSFLdqvemetEEKRTSLAkTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDR 779
Cdd:PRK05691 3965 ESVPSLIQGML-------AEDRQALD-GLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTR 4036
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 780 ERMrLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPF-YRGERMYQTGDLARWLPD 858
Cdd:PRK05691 4037 GSY-LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSD 4115
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 859 GTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTARTELGKR--------LP 930
Cdd:PRK05691 4116 GVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGALLERikqrlraeLP 4195
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 931 AYMMPSSFIEMREWPVTPSGKLDRKALPAPD-GAAERRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKA 1009
Cdd:PRK05691 4196 DYMVPLHWLWLDRLPLNANGKLDRKALPALDiGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLA 4275
|
1050 1060 1070
....*....|....*....|....*....|....*....
gi 2040046167 1010 TALVSRIAKAFGVQVPLKEIFAKPTLEELAAVIQELDES 1048
Cdd:PRK05691 4276 TQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGS 4314
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
477-957 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 627.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTGPGlsvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGM 636
Cdd:cd05930 81 EDSGAKLVLTDPD-----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 637 QRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEME 716
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 717 TeekrtslAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERmRLPIGKPVPGARLY 796
Cdd:cd05930 206 A-------LPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDG-RVPIGRPIPNTRVY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 797 ILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGY 876
Cdd:cd05930 278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 877 RIEPGEVEAALRQIDGVREAAVVARTEG-EETELYAYIEGQDQKTA-----RTELGKRLPAYMMPSSFIEMREWPVTPSG 950
Cdd:cd05930 358 RIELGEIEAALLAHPGVREAAVVAREDGdGEKRLVAYVVPDEGGELdeeelRAHLAERLPDYMVPSAFVVLDALPLTPNG 437
|
....*..
gi 2040046167 951 KLDRKAL 957
Cdd:cd05930 438 KVDRKAL 444
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1063-2068 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 605.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1063 PVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGaDGEPVQRIHDDVPFQLME- 1141
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQWVDPALTFPLPEi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1142 ---------LAAAE-----DFVRPFRL-QEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASR---- 1202
Cdd:PRK10252 88 idlrtqpdpHAAAQalmqaDLQQDLRVdSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWlrge 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1203 -----TLHPLRIQYKDYavwqQAFKQGEAYNRQEAYWLKQLDGELPVLELPAdnARPAVRSFAGDHVSFSLDADTSSGLY 1277
Cdd:PRK10252 168 ptpasPFTPFADVVEEY----QRYRASEAWQRDAAFWAEQRRQLPPPASLSP--APLPGRSASADILRLKLEFTDGAFRQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1278 KIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETAL 1357
Cdd:PRK10252 242 LAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1358 EAYEHQDYPFEELVdrldvvRDMSR----NPLFDVMFALQNMErESLTLHDLHLTTIAHDAHKVSkfDMTLYAAEEDQET 1433
Cdd:PRK10252 322 KMRRHQRYDAEQIV------RDSGRaagdEPLFGPVLNIKVFD-YQLDFPGVQAQTHTLATGPVN--DLELALFPDEHGG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1434 IRFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDEHETSSfIHTFNQTKQDYPKhETISRLFEYQAAK 1513
Cdd:PRK10252 393 LSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIPE-TTLSALVAQQAAK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1514 TPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWM 1593
Cdd:PRK10252 471 TPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1594 LSDSNAVMLLQSDRLESHMAGKR-LFIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVV-RLVKN 1671
Cdd:PRK10252 551 LEDARPSLLITTADQLPRFADVPdLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnRLLWM 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1672 SD-MAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLF----NQL-SE 1745
Cdd:PRK10252 631 QNhYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLaafvASLtPE 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1746 QNERTFSDLSRLILGGEALSPNHVNRV--RNTAPdlaLWNGYGPTE---NTTFSTCFRIEHEYK--HSIPIGRPIANSTA 1818
Cdd:PRK10252 711 GARQSCASLRQVFCSGEALPADLCREWqqLTGAP---LHNLYGPTEaavDVSWYPAFGEELAAVrgSSVPIGYPVWNTGL 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1819 YIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRG 1898
Cdd:PRK10252 788 RILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRG 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1899 YRIELGEIEAALRQIDGVKEA---AVIVRTGPS---GHKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAA 1970
Cdd:PRK10252 868 QRIELGEIDRAMQALPDVEQAvthACVINQAAAtggDARQLVGYLVSQsgLPLDTSALQAQLRERLPPHMVPVVLLQLDQ 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1971 LPLTQNGKLDRRALPEPETTAiNTAYAPPRNQLEERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARLGR-FDLK 2049
Cdd:PRK10252 948 LPLSANGKLDRKALPLPELKA-QVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRqFARQ 1026
|
1050
....*....|....*....
gi 2040046167 2050 ITAGDLFRHPTIKEAAPLI 2068
Cdd:PRK10252 1027 VTPGQVMVASTVAKLATLL 1045
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
12-1053 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 601.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKE-RQSRLQF 90
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDN-GEVWQWVDPAlTFPLPEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 91 VDISHLDETAKETFVDQfeHDDKKKGFDL-QTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGK 169
Cdd:PRK10252 88 IDLRTQPDPHAAAQALM--QADLQQDLRVdSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 170 EQLPDFEPVHPFS----KYIKWLMRQDRKEAEAFWKTRLIDVKQTASL-----PKTSSSS-----KGKLEQMAFTlskeq 235
Cdd:PRK10252 166 GEPTPASPFTPFAdvveEYQRYRASEAWQRDAAFWAEQRRQLPPPASLspaplPGRSASAdilrlKLEFTDGAFR----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 236 teglRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGR-PSDLEDVEKMVglfINTIPVRVKSGPESFL-TLV 313
Cdd:PRK10252 241 ----QLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlGSAALTATGPV---LNVLPLRVHIAAQETLpELA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 314 SHLQQESLKAEAYSYYPLYDIQAQSML---KHELFDHIV---VFENIPAQREIESLNQADAFDfTVDDFDMdevtnyGCS 387
Cdd:PRK10252 314 TRLAAQLKKMRRHQRYDAEQIVRDSGRaagDEPLFGPVLnikVFDYQLDFPGVQAQTHTLATG-PVNDLEL------ALF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 388 IKIIPGSSLYIRINFDigLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKmLYEFNQTEPAAPLApTLHS 467
Cdd:PRK10252 387 PDEHGGLSIEILANPQ--RYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIPET-TLSA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 468 FFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDY 547
Cdd:PRK10252 463 LVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGY 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 548 PEERLRYMLADSGARLLVTGPGLS---VSGFSGETLEVNLSSLRTEPA-ENEPVCAHTdggslAYVIYTSGSTGTPKGVA 623
Cdd:PRK10252 543 PDDRLKMMLEDARPSLLITTADQLprfADVPDLTSLCYNAPLAPQGAApLQLSQPHHT-----AYIIFTSGSTGRPKGVM 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 624 VEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIP 703
Cdd:PRK10252 618 VGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVP 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 704 AMANSFLDQVemeTEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLpeTAVIHG-YGPTEATVDAAF---FRYDHEKDR 779
Cdd:PRK10252 698 SMLAAFVASL---TPEGARQSCASLRQVFCSGEALPADLCREWQQLT--GAPLHNlYGPTEAAVDVSWypaFGEELAAVR 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 780 ERmRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDG 859
Cdd:PRK10252 773 GS-SVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDG 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 860 TVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVAR-------TEGEETELYAYI-----EGQDQKTARTELGK 927
Cdd:PRK10252 852 AVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaaTGGDARQLVGYLvsqsgLPLDTSALQAQLRE 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 928 RLPAYMMPSSFIEMREWPVTPSGKLDRKALPAPDGAAeRRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSL 1007
Cdd:PRK10252 932 RLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKA-QVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSL 1010
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 2040046167 1008 KATALVSRIAKAFGVQVPLKEIFAKPTLEELAAViqeLDESPHAAI 1053
Cdd:PRK10252 1011 LAMKLAAQLSRQFARQVTPGQVMVASTVAKLATL---LDAEEDESR 1053
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
466-957 |
0e+00 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 593.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 466 HSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDP 545
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 546 DYPEERLRYMLADSGARLLVTGPGLSVSGFSGETLEVNLSSLRTEPAENEPVcAHTDGGSLAYVIYTSGSTGTPKGVAVE 625
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPL-VPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 626 HRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAM 705
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 706 ANSFLdqvemetEEKRTSLAKTLKRVFAGGEALAPQTAARFARsLPETAVIHGYGPTEATVDAAFFRYDHEKDRERmrLP 785
Cdd:cd17646 240 LRVFL-------AEPAAGSCASLRRVFCSGEALPPELAARFLA-LPGAELHNLYGPTEAAIDVTHWPVRGPAETPS--VP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 786 IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLG 865
Cdd:cd17646 310 IGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 866 RMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEG-EETELYAYI------EGQDQKTARTELGKRLPAYMMPSSF 938
Cdd:cd17646 390 RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPaGAARLVGYVvpaagaAGPDTAALRAHLAERLPEYMVPAAF 469
|
490
....*....|....*....
gi 2040046167 939 IEMREWPVTPSGKLDRKAL 957
Cdd:cd17646 470 VVLDALPLTANGKLDRAAL 488
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1061-1467 |
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: 578.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1061 TYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDDVPFQL- 1139
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVE-VDGEPVQVILPPLPLPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1140 ---------------MELAAAEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRT- 1203
Cdd:cd19531 80 vvdlsglpeaereaeAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1204 -----LHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYK 1278
Cdd:cd19531 160 grpspLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1279 IARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALE 1358
Cdd:cd19531 240 LARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1359 AYEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHLTTIAHDaHKVSKFDMTLYAAEEDQEtIRFDV 1438
Cdd:cd19531 320 AYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVD-SGTAKFDLTLSLTETDGG-LRGSL 397
|
410 420
....*....|....*....|....*....
gi 2040046167 1439 EFNTDIYQKQTIKKWLSYYIHILHHVIEH 1467
Cdd:cd19531 398 EYNTDLFDAATIERMAGHFQTLLEAIVAD 426
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1505-1988 |
0e+00 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 577.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1505 RLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTED 1584
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1585 MPTERLEWMLSDSNAVMLLQSDRLES--HMAGKRLFIEDIQLEAGISAN-NPEQQggPDSLAYIMYTSGSTGTPKGVMVE 1661
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPpiAFIGLIDLLDEDTIYHEESENlEPVSK--SDDLAYVIYTSGSTGKPKGVMIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1662 QRGVVRLVKNSD--MAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSL 1739
Cdd:cd17655 159 HRGVVNLVEWANkvIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1740 FNQLSEQNERTFSDLSRLILGGEALSPNHVNRV---RNTAPDLalWNGYGPTENTTFSTCFRIEHEY--KHSIPIGRPIA 1814
Cdd:cd17655 239 LKLLDAADDSEGLSLKHLIVGGEALSTELAKKIielFGTNPTI--TNAYGPTETTVDASIYQYEPETdqQVSVPIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1815 NSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQV 1894
Cdd:cd17655 317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1895 KIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLT 1974
Cdd:cd17655 397 KIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
490
....*....|....
gi 2040046167 1975 QNGKLDRRALPEPE 1988
Cdd:cd17655 477 PNGKVDRKALPEPD 490
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
469-957 |
1.35e-176 |
|
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: 550.65 E-value: 1.35e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 469 FTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:cd12117 3 FEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVTGPGLSVSGFSGETLEVNLSSLRTEPAENEPVCAhtDGGSLAYVIYTSGSTGTPKGVAVEHRQ 628
Cdd:cd12117 83 AERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPV--SPDDLAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGmQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANS 708
Cdd:cd12117 161 VVRLVKN-TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLDQVEmeteekrTSLAkTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERmRLPIGK 788
Cdd:cd12117 240 LADEDP-------ECFA-GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAG-SIPIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 789 PVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMD 868
Cdd:cd12117 311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 869 GQVKIRGYRIEPGEVEAALRQIDGVREAAVVART-EGEETELYAYIEGQDQKTA---RTELGKRLPAYMMPSSFIEMREW 944
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREdAGGDKRLVAYVVAEGALDAaelRAFLRERLPAYMVPAAFVVLDEL 470
|
490
....*....|...
gi 2040046167 945 PVTPSGKLDRKAL 957
Cdd:cd12117 471 PLTANGKVDRRAL 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
469-961 |
2.91e-176 |
|
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: 550.39 E-value: 2.91e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 469 FTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVT-GPGLSVSGFSGETLEVNLSSLRTEPAEN-EPVCAHTDggsLAYVIYTSGSTGTPKGVAVEH 626
Cdd:cd17655 83 EERIQYILEDSGADILLTqSHLQPPIAFIGLIDLLDEDTIYHEESENlEPVSKSDD---LAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 627 RQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMA 706
Cdd:cd17655 160 RGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 707 NsfldqvemETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETA-VIHGYGPTEATVDAAFFRYDHEKDRErMRLP 785
Cdd:cd17655 240 K--------LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTETTVDASIYQYEPETDQQ-VSVP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 786 IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLG 865
Cdd:cd17655 311 IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 866 RMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVART-EGEETELYAYIEGQ---DQKTARTELGKRLPAYMMPSSFIEM 941
Cdd:cd17655 391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKdEQGQNYLCAYIVSEkelPVAQLREFLARELPDYMIPSYFIKL 470
|
490 500
....*....|....*....|
gi 2040046167 942 REWPVTPSGKLDRKALPAPD 961
Cdd:cd17655 471 DEIPLTPNGKVDRKALPEPD 490
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
10-430 |
1.95e-175 |
|
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: 544.88 E-value: 1.95e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 10 IYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLKERQSRLQ 89
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 90 FVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGK 169
Cdd:cd19543 81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 170 EQLPDFEPVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVKQTASLPK---TSSSSKGKLEQMAFTLSKEQTEGLRKLALQA 246
Cdd:cd19543 161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKelpADADGSYEPGEVSFELSAELTARLQELARQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 247 GATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGP-ESFLTLVSHLQQESLKAEA 325
Cdd:cd19543 241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPdQTVLELLKDLQAQQLELRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 326 YSYYPLYDIQAQSMLKHELFDHIVVFENIPAQREIESLNQADAFDFTvdDFDMDEVTNYGCSIKIIPGSSLYIRINFDIG 405
Cdd:cd19543 321 HEYVPLYEIQAWSEGKQALFDHLLVFENYPVDESLEEEQDEDGLRIT--DVSAEEQTNYPLTVVAIPGEELTIKLSYDAE 398
|
410 420
....*....|....*....|....*
gi 2040046167 406 LYDPAMMKKIELYLRHIIGSVIADP 430
Cdd:cd19543 399 VFDEATIERLLGHLRRVLEQVAANP 423
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-1339 |
2.63e-175 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 605.24 E-value: 2.63e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 3 QQPEIQDI-----YPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPR 77
Cdd:PRK05691 1716 SQGAIARVdrsqpVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVD-GVPV 1794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 78 QVVLKERQSRLQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVM 157
Cdd:PRK05691 1795 QQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFA 1874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 158 KEFLAIYKALGKEQLPDFEPVhPFsKYI-------KWLMRQDRKEAEAFWKTRLIDVKQTASLPKTS-----SSSKGKLE 225
Cdd:PRK05691 1875 RELGALYEAFLDDRESPLEPL-PV-QYLdysvwqrQWLESGERQRQLDYWKAQLGNEHPLLELPADRprppvQSHRGELY 1952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 226 QmaFTLSKEQTEGLRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISG--RPsdleDVEKMVGLFINTIPVRVK 303
Cdd:PRK05691 1953 R--FDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANriRP----ESEGLIGAFLNTQVLRCQ 2026
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 304 -SGPESFLTLVSHLQQESLKAEAYSYYPlydiqaqsmlkhelFDHIV----------------VFENIpaQR-------- 358
Cdd:PRK05691 2027 lDGQMSVSELLEQVRQTVIEGQSHQDLP--------------FDHLVealqpprsaaynplfqVMCNV--QRwefqqsrq 2090
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 359 ----EIESL-NQADA--FDFTVDDFDMDEvtNYGCSikiipgsslyirINFDIGLYDPAMMKKIELYLRHIIGSVIADPN 431
Cdd:PRK05691 2091 lagmTVEYLvNDARAtkFDLNLEVTDLDG--RLGCC------------LTYSRDLFDEPRIARMAEHWQNLLEALLGDPQ 2156
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 432 QQIAQIALLGEETAKKMLYEFNQTEPAAPLAPTLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVA 511
Cdd:PRK05691 2157 QRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVG 2236
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 512 KESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGPGLSV------SGFSGETLEVNLS 585
Cdd:PRK05691 2237 PQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEalgelpAGVARWCLEDDAA 2316
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 586 SLRTEPAENEPVCAHTDggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFW 665
Cdd:PRK05691 2317 ALAAYSDAPLPFLSLPQ--HQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLV 2394
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 666 WMIPGASMYLLPQG-W--EKDPALMTEaftnEGVTTAHFIPAMANSFLDQVEMETEEKRTSLAKTlkrvfaGGEALAPQT 742
Cdd:PRK05691 2395 PLLCGARVVLRAQGqWgaEEICQLIRE----QQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCIT------GGEALTGEH 2464
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 743 AARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVpGARL-YILDSEKAVQPIGVAGELYIAGAGVA 821
Cdd:PRK05691 2465 LQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVV-GARVaYILDADLALVPQGATGELYVGGAGLA 2543
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 822 RGYLNRPELTEERFLDDPF-YRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA 900
Cdd:PRK05691 2544 QGYHDRPGLTAERFVADPFaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA 2623
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 901 RTEGEETELYAYI---------EGQDQ--KTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALPAPDGAAERRVY 969
Cdd:PRK05691 2624 LDTPSGKQLAGYLvsavagqddEAQAAlrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAY 2703
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 970 TAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALVSRiAKAFGVQVPLKEIFAKPTLEELAAVIQeldESP 1049
Cdd:PRK05691 2704 QAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVAT---HSE 2779
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1050 HAAIEPAEIQDTYPVSSAQKRMYVLQQLEDGgvGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFeTGADGE--- 1126
Cdd:PRK05691 2780 AAQAEQGPLQGASGLTPIQHWFFDSPVPQPQ--HWNQALLLEPRQALDPALLEQALQALVEHHDALRLRF-SQADGRwqa 2856
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1127 -----PVQRIHDDVPFQLMELAAA--EDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELY 1199
Cdd:PRK05691 2857 eyravTAQELLWQVTVADFAECAAlfADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALY 2936
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1200 asRTLHPLRIQ--------YKDYAVWQQAFKQGEAYNRQEAYWLKQLDGelPVLELPADNARPAVRSFAGDHVSFSLDAD 1271
Cdd:PRK05691 2937 --RQLSAGAEPalpaktsaFRDWAARLQAYAGSESLREELGWWQAQLGG--PRAELPCDRPQGGNLNRHAQTVSVRLDAE 3012
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1272 TSSGLYKIARDNGCT-LYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHK----DLESVIGMFVNTLAIRTRP 1339
Cdd:PRK05691 3013 RTRQLLQQAPAAYRTqVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTP 3085
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
490-898 |
9.80e-167 |
|
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: 519.90 E-value: 9.80e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKK-KGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP 568
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 GLSvSGFSGETLEVNLSSLRTEPAEN-----EPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLT 643
Cdd:TIGR01733 81 ALA-SRLAGLVLPVILLDPLELAALDdapapPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 644 EDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEG-VTTAHFIPAMANSFLDQVEmeteekrt 722
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALP-------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 723 SLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVPGARLYILDSEK 802
Cdd:TIGR01733 232 PALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 803 AVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFY--RGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEP 880
Cdd:TIGR01733 312 RPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIEL 391
|
410
....*....|....*...
gi 2040046167 881 GEVEAALRQIDGVREAAV 898
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1038-2069 |
9.33e-166 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 575.19 E-value: 9.33e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1038 LAAVIQE-LDESPhaaIEPAEIQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLR 1116
Cdd:PRK05691 3236 LAQLTQAqLDALP---VPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALR 3312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1117 TSFETGADGEPVQRIHD--DVPFQLMELAAAEDFVRPFRLQ--------------EAPLFRAALVKEAEESHLLLVDMHH 1180
Cdd:PRK05691 3313 ASFSWNAGETMLQVIHKpgRTPIDYLDWRGLPEDGQEQRLQalhkqereagfdllNQPPFHLRLIRVDEARYWFMMSNHH 3392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1181 IISDGVSVGTLIREFSELYAS----RTLH-PLRIQYKDYAVWQQafKQGEAYNRQeaYWLKQLDGELPVLELPADnaRPA 1255
Cdd:PRK05691 3393 ILIDAWCRSLLMNDFFEIYTAlgegREAQlPVPPRYRDYIGWLQ--RQDLAQARQ--WWQDNLRGFERPTPIPSD--RPF 3466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1256 VRSFAGDHVSF-------SLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGR--AHKDLESVI 1326
Cdd:PRK05691 3467 LREHAGDSGGMvvgdcytRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTV 3546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1327 GMFVNTLAIRTR---PVENKCFSDFLREVRETALEAYEHQDYPfeeLVDRLDVVRDMSRNPLFDVMFALQNMERESLTL- 1402
Cdd:PRK05691 3547 GLFINSIALRVQlpaAGQRCSVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENAPVEVSVLd 3623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1403 HDLHLTTIAHDAHKVSKFDMTL--YAAEEDQETIRFDVEFntdiYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDE 1480
Cdd:PRK05691 3624 RAQSLNASSDSGRTHTNFPLTAvcYPGDDLGLHLSYDQRY----FDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGE 3699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1481 HETSSFIHTFNQTKQDYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSR 1560
Cdd:PRK05691 3700 QERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAER 3779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1561 TPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQS-----------DRLESHMAGKRLFIEDIQlEAGIS 1629
Cdd:PRK05691 3780 GLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSaacreqarallDELGCANRPRLLVWEEVQ-AGEVA 3858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1630 ANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVV--RLVKNSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACL 1707
Cdd:PRK05691 3859 SHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLnnQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARV 3938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1708 YISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGP 1787
Cdd:PRK05691 3939 EIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGP 4018
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1788 TENTTFSTCFRIEHEYKHS--IPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF-T 1864
Cdd:PRK05691 4019 AECSDDVAFFRVDLASTRGsyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgA 4098
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1865 PGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGhKELLAYM------S 1938
Cdd:PRK05691 4099 PGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLvphqtvL 4177
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1939 LQAEMnIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTAI-NTAYAPPRNQLEERLAVIWQEVLGV 2017
Cdd:PRK05691 4178 AQGAL-LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLqSQAYLAPRNELEQTLATIWADVLKV 4256
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 2018 EKVGIEDSFFELGGDSIKALQVSARLGR-FDLKITAGDLFRHPTIKEAAPLIR 2069
Cdd:PRK05691 4257 ERVGVHDNFFELGGHSLLATQIASRVQKaLQRNVPLRAMFECSTVEELAEYIE 4309
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1506-1984 |
3.46e-164 |
|
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: 516.06 E-value: 3.46e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1506 LFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDM 1585
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1586 PTERLEWMLSDSNAVMLLQSDRLESHM-AGKRLFIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRG 1664
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLpAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1665 VV-RLV-KNSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQ 1742
Cdd:cd17646 163 IVnRLLwMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 -LSEQNERTFSDLSRLILGGEALSPNHVNRVRnTAPDLALWNGYGPTENTTFSTCFRIE-HEYKHSIPIGRPIANSTAYI 1820
Cdd:cd17646 243 fLAEPAAGSCASLRRVFCSGEALPPELAARFL-ALPGAELHNLYGPTEAAIDVTHWPVRgPAETPSVPIGRPVPNTRLYV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1821 VNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYR 1900
Cdd:cd17646 322 LDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1901 IELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQA---EMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNG 1977
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaaGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANG 481
|
....*..
gi 2040046167 1978 KLDRRAL 1984
Cdd:cd17646 482 KLDRAAL 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1507-1985 |
4.95e-163 |
|
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: 513.04 E-value: 4.95e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1507 FEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMP 1586
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1587 TERLEWMLSDSNAVMLLQSDRLESHMAGKRLFI--EDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRG 1664
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVtlLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1665 VVRLVKNSDMAFS--PEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQ 1742
Cdd:cd17651 161 LANLVAWQARASSlgPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 LSEQ---NERTFSDLSRLILGGEALSPNHVNRVRNTA-PDLALWNGYGPTEnTTFSTCFRIEHEYKH---SIPIGRPIAN 1815
Cdd:cd17651 241 LAEHgrpLGVRLAALRYLLTGGEQLVLTEDLREFCAGlPGLRLHNHYGPTE-THVVTALSLPGDPAAwpaPPPIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1816 STAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVK 1895
Cdd:cd17651 320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1896 IRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHLVELAALPL 1973
Cdd:cd17651 400 IRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVdaAELRAALATHLPEYMVPSAFVLLDALPL 479
|
490
....*....|..
gi 2040046167 1974 TQNGKLDRRALP 1985
Cdd:cd17651 480 TPNGKLDRRALP 491
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2083-2514 |
1.21e-162 |
|
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: 509.10 E-value: 1.21e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2083 EVPWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQFNRGIHGELYSLNI 2162
Cdd:cd19534 1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2163 RDLSKTAQWEKlIEDEVADLQRSIHLQTGPLLKAGLFN-TMSGTYLFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQPV 2241
Cdd:cd19534 81 VDLSSLAQAAA-IEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2242 QLPRKTdSYQYFANRLAEYAESSKVIREQSYWRTVEKEKAALLPCEKPHSAADniRKTESFTLSEEDTHVLIHKVNNAYN 2321
Cdd:cd19534 160 PLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTYGD--ARTVSFTLDEEETEALLQEANAAYR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2322 TDTQDILLTAASLALCDWMGERKLRIAMEGHGRDHTLPELDISRTVGWFTTIYPVLIDLhhAAEGELGLAVKTVKDTLGR 2401
Cdd:cd19534 237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDL--EASEDLGDTLKRVKEQLRR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2402 IPDKGMGYGILKYLTSSENKTIQFGKAPEIGFNYLGQFNDTERQQKFSFSGL-ASGKDITPTWQREQTLEMSAMVRQNQL 2480
Cdd:cd19534 315 IPNKGIGYGILRYLTPEGTKRLAFHPQPEISFNYLGQFDQGERDDALFVSAVgGGGSDIGPDTPRFALLDINAVVEGGQL 394
|
410 420 430
....*....|....*....|....*....|....
gi 2040046167 2481 HFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHC 2514
Cdd:cd19534 395 VITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
469-958 |
2.64e-162 |
|
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: 511.12 E-value: 2.64e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 469 FTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVTGPGLSvSGFSGEtlEVNLSSLRTEPAENEPVCAH---TDGGSLAYVIYTSGSTGTPKGVAVE 625
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALA-GELAVE--LVAVTLLDQPGAAAGADAEPdpaLDADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 626 HRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAM 705
Cdd:cd17651 158 HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 706 ANSFLDQVemeTEEKRTSLAktLKRVFAGGEALAPQTA-ARFARSLPETAVIHGYGPTEATVdAAFFRYDHEKDRERMRL 784
Cdd:cd17651 238 LRALAEHG---RPLGVRLAA--LRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHV-VTALSLPGDPAAWPAPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 785 PIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWL 864
Cdd:cd17651 312 PIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 865 GRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGE-ETELYAYIEGQDQKTA-----RTELGKRLPAYMMPSSF 938
Cdd:cd17651 392 GRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPgEKRLVAYVVGDPEAPVdaaelRAALATHLPEYMVPSAF 471
|
490 500
....*....|....*....|
gi 2040046167 939 IEMREWPVTPSGKLDRKALP 958
Cdd:cd17651 472 VLLDALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1528-1921 |
3.03e-161 |
|
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: 504.49 E-value: 3.03e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1528 TYRELNQRANRIAAALRAN-GVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSD 1606
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 RLESHMAG---KRLFIEDIQLEAGISANNPEQ---QGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVknSDMA----F 1676
Cdd:TIGR01733 81 ALASRLAGlvlPVILLDPLELAALDDAPAPPPpdaPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL--AWLArrygL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1677 SPEDRILLTASLGFDAMTFEVFGPLLNGACLY-ISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLS 1755
Cdd:TIGR01733 159 DPDDRVLQFASLSFDASVEEIFGALLAGATLVvPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1756 RLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHE---YKHSIPIGRPIANSTAYIVNSRGRLQPMGV 1832
Cdd:TIGR01733 239 LVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDdapRESPVPIGRPLANTRLYVLDDDLRPVPVGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1833 IGELCVGGDGLARGYFGRPELTKEKFVPNPFTP--GERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAAL 1910
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
|
410
....*....|.
gi 2040046167 1911 RQIDGVKEAAV 1921
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1515-1985 |
6.10e-158 |
|
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: 496.89 E-value: 6.10e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLqsdrleSHmagkrlfiediqleagisannpeqqgGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDM 1674
Cdd:cd17649 81 EDSGAGLLL------TH--------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1675 AF--SPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFS 1752
Cdd:cd17649 129 RYglTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1753 D----LSRLILGGEALSPNHVNRVRNTApdLALWNGYGPTENTTFSTCFRIEHEYKH---SIPIGRPIANSTAYIVNSRG 1825
Cdd:cd17649 209 GrppsLRLYIFGGEALSPELLRRWLKAP--VRLFNAYGPTEATVTPLVWKCEAGAARagaSMPIGRPLGGRSAYILDADL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1826 RLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF-TPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELG 1904
Cdd:cd17649 287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1905 EIEAALRQIDGVKEAAVIVRTGPSGHKeLLAYMSLQAEMNI----EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLD 1980
Cdd:cd17649 367 EIEAALLEHPGVREAAVVALDGAGGKQ-LVAYVVLRAAAAQpelrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
....*
gi 2040046167 1981 RRALP 1985
Cdd:cd17649 446 RKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1515-1984 |
6.78e-156 |
|
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: 491.81 E-value: 6.78e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLQSDRLESHMAGKRLFIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK--NS 1672
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHsmRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1673 DMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQL---SEQNER 1749
Cdd:cd12116 161 RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLldaGWQGRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1750 TFsdlsRLILGGEALSPNHVNRVrnTAPDLALWNGYGPTENTTFSTCFRIEHEYKHsIPIGRPIANSTAYIVNSRGRLQP 1829
Cdd:cd12116 241 GL----TALCGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAARVTAAAGP-IPIGRPLANTQVYVLDAALRPVP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1830 MGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF-TPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEA 1908
Cdd:cd12116 314 PGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 1909 ALRQIDGVKEAAVIVRTGPsGHKELLAYMSLQAEM--NIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd12116 394 ALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAapDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
477-958 |
1.22e-153 |
|
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: 484.56 E-value: 1.22e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTgpglsvsgfsgetlevnlsslrtepaenepvcahTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGM 636
Cdd:cd17649 81 EDSGAGLLLT----------------------------------HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 637 QRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEME 716
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 717 TEEKRTSLaktlkRVFA-GGEALAPQTAARfARSLPETaVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVPGARL 795
Cdd:cd17649 207 GDGRPPSL-----RLYIfGGEALSPELLRR-WLKAPVR-LFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 796 YILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYR-GERMYQTGDLARWLPDGTVEWLGRMDGQVKIR 874
Cdd:cd17649 280 YILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 875 GYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTA-------RTELGKRLPAYMMPSSFIEMREWPVT 947
Cdd:cd17649 360 GFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQpelraqlRTALRASLPDYMVPAHLVFLARLPLT 439
|
490
....*....|.
gi 2040046167 948 PSGKLDRKALP 958
Cdd:cd17649 440 PNGKLDRKALP 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1515-1985 |
3.73e-153 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 482.52 E-value: 3.73e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLQSdrleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDM 1674
Cdd:cd17652 81 ADARPALLLTT---------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1675 AFS--PEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNertFS 1752
Cdd:cd17652 128 AFDvgPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD---LP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1753 DLSRLILGGEALSPNHVNRvrnTAPDLALWNGYGPTENTTFST---CFRIEHEykhsIPIGRPIANSTAYIVNSRGRLQP 1829
Cdd:cd17652 205 DLRTLVVAGEACPAELVDR---WAPGRRMINAYGPTETTVCATmagPLPGGGV----PPIGRPVPGTRVYVLDARLRPVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1830 MGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF-TPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEA 1908
Cdd:cd17652 278 PGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1909 ALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAE--MNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALP 1985
Cdd:cd17652 358 ALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1515-1984 |
7.89e-153 |
|
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: 482.19 E-value: 7.89e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLqsdrleshmagkrlfiediqleagisannpeqqGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK--NS 1672
Cdd:cd17643 81 ADSGPSLLL---------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAatQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1673 DMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFS 1752
Cdd:cd17643 128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1753 DLSRL---ILGGEALSPN----HVNRVRNTAPDLAlwNGYGPTENTTFSTCFRIEHEY---KHSIPIGRPIANSTAYIVN 1822
Cdd:cd17643 208 DPLALryvIFGGEALEAAmlrpWAGRFGLDRPQLV--NMYGITETTVHVTFRPLDAADlpaAAASPIGRPLPGLRVYVLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1823 SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFT-PGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRI 1901
Cdd:cd17643 286 ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1902 ELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEM--NIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAaaDIAELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
....*
gi 2040046167 1980 DRRAL 1984
Cdd:cd17643 446 DRAAL 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
477-957 |
8.35e-151 |
|
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: 476.41 E-value: 8.35e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTgpglsvsgfsgetlevnlsslrtepaenepvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGM 636
Cdd:cd17643 81 ADSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 637 QRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAmanSFLDQVEME 716
Cdd:cd17643 126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPS---AFYQLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 717 TEEKRTSLAktLKRVFAGGEALAPQTAARFAR--SLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVPGAR 794
Cdd:cd17643 203 DRDGRDPLA--LRYVIFGGEALEAAMLRPWAGrfGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 795 LYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYR-GERMYQTGDLARWLPDGTVEWLGRMDGQVKI 873
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 874 RGYRIEPGEVEAALRQIDGVREAAVVARTEGE-ETELYAYIEGQDQKTA-----RTELGKRLPAYMMPSSFIEMREWPVT 947
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVIVREDEPgDTRLVAYVVADDGAAAdiaelRALLKELLPDYMVPARYVPLDALPLT 440
|
490
....*....|
gi 2040046167 948 PSGKLDRKAL 957
Cdd:cd17643 441 VNGKLDRAAL 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
477-957 |
2.60e-150 |
|
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: 476.01 E-value: 2.60e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTGPGLsVSGFSGETLEVNLSSLRTePAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGM 636
Cdd:cd12116 81 EDAEPALVLTDDAL-PDRLPAGLPVLLLALAAA-AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 637 QRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDqvemE 716
Cdd:cd12116 159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD----A 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 717 TEEKRTSLaktlkRVFAGGEALAPQTAARFARslPETAVIHGYGPTEATVDAAFFRYDHEKDrermRLPIGKPVPGARLY 796
Cdd:cd12116 235 GWQGRAGL-----TALCGGEALPPDLAARLLS--RVGSLWNLYGPTETTIWSTAARVTAAAG----PIPIGRPLANTQVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 797 ILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYR-GERMYQTGDLARWLPDGTVEWLGRMDGQVKIRG 875
Cdd:cd12116 304 VLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 876 YRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTARTE-----LGKRLPAYMMPSSFIEMREWPVTPSG 950
Cdd:cd12116 384 HRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAalrahLRATLPAYMVPSAFVRLDALPLTANG 463
|
....*..
gi 2040046167 951 KLDRKAL 957
Cdd:cd12116 464 KLDRKAL 470
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
477-958 |
2.40e-149 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 471.74 E-value: 2.40e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTGPGlsvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGM 636
Cdd:cd17652 81 ADARPALLLTTPD-----------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 637 QRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSfldqveME 716
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA------LP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 717 TEEkrtslAKTLKRVFAGGEALAPQTAARFArslPETAVIHGYGPTEATVDAAFfrydHEKDRERMRLPIGKPVPGARLY 796
Cdd:cd17652 200 PDD-----LPDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCATM----AGPLPGGGVPPIGRPVPGTRVY 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 797 ILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPF-YRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRG 875
Cdd:cd17652 268 VLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 876 YRIEPGEVEAALRQIDGVREAAVVARTEGEETE-LYAYIEGQDQKTA-----RTELGKRLPAYMMPSSFIEMREWPVTPS 949
Cdd:cd17652 348 FRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKrLVAYVVPAPGAAPtaaelRAHLAERLPGYMVPAAFVVLDALPLTPN 427
|
....*....
gi 2040046167 950 GKLDRKALP 958
Cdd:cd17652 428 GKLDRRALP 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1506-1984 |
1.45e-148 |
|
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: 469.88 E-value: 1.45e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1506 LFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDM 1585
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1586 PTERLEWMLSDSNAVMLLQsdrleshmagkrlfiediqleagisannpeqqgGPDSLAYIMYTSGSTGTPKGVMVEQRGV 1665
Cdd:cd12115 84 PPERLRFILEDAQARLVLT---------------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRNA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1666 VRLVKNSDMAFSPEDR--ILLTASLGFDAMTFEVFGPLLNGACLYISDKETYL-DSDRLKtfiqqnGITTLWLTSSLFNQ 1742
Cdd:cd12115 131 AAFLQWAAAAFSAEELagVLASTSICFDLSVFELFGPLATGGKVVLADNVLALpDLPAAA------EVTLINTVPSAAAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 LSEQNERTFSdLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVN 1822
Cdd:cd12115 205 LLRHDALPAS-VRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYVLD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1823 SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIE 1902
Cdd:cd12115 284 RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1903 LGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEM--NIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLD 1980
Cdd:cd12115 364 LGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAagLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKID 443
|
....
gi 2040046167 1981 RRAL 1984
Cdd:cd12115 444 RSAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1502-1985 |
5.07e-148 |
|
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: 469.22 E-value: 5.07e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV 1581
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 TEDMPTERLEWMLSDSNAVMLLQSdrleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVE 1661
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQ---------------------------------PENLAYVIYTSGSTGKPKGVMIE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1662 QRGVVRLVKNSDMAF--SPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSL 1739
Cdd:cd17644 128 HQSLVNLSHGLIKEYgiTSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1740 FNQLSEQNERTFSD----LSRLILGGEALSPNHVNR-VRNTAPDLALWNGYGPTENTTFSTCFRI---EHEYKHSIPIGR 1811
Cdd:cd17644 208 WHLLVLELLLSTIDlpssLRLVIVGGEAVQPELVRQwQKNVGNFIQLINVYGPTEATIAATVCRLtqlTERNITSVPIGR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1812 PIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF--TPGERMYRTGDLARWLKDGTIDYIGR 1889
Cdd:cd17644 288 PIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1890 MDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEM--NIEKVRSLLSQQLPGFMIPAHLVE 1967
Cdd:cd17644 368 IDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEEspSTVELRQFLKAKLPDYMIPSAFVV 447
|
490
....*....|....*...
gi 2040046167 1968 LAALPLTQNGKLDRRALP 1985
Cdd:cd17644 448 LEELPLTPNGKIDRRALP 465
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1058-1483 |
7.36e-148 |
|
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: 468.35 E-value: 7.36e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1058 IQDTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRIHDDVPF 1137
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1138 QLMEL-----------AAAEDFVR-----PFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYAS 1201
Cdd:pfam00668 81 ELEIIdisdlseseeeEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1202 ----RTLHPLRIQ-YKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGL 1276
Cdd:pfam00668 161 llkgEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1277 YKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETA 1356
Cdd:pfam00668 241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1357 LEAYEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNM--ERESLTLHDLHLTTIAHD--AHKVSKFDMTLyAAEEDQE 1432
Cdd:pfam00668 321 LSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgQDSQEEEFQLSELDLSVSsvIEEEAKYDLSL-TASERGG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 1433 TIRFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHLGDIHVLDEHET 1483
Cdd:pfam00668 400 GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEK 450
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
477-957 |
1.52e-144 |
|
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: 458.47 E-value: 1.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTGPGlsvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGM 636
Cdd:cd17650 81 EDSGAKLLLTQPE-----------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 637 QRQFPLTEDDVIVLK-SSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEM 715
Cdd:cd17650 126 RREYELDSFPVRLLQmASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 716 ETEekRTSLAKTLKRVFAGGEALAPQTAArfARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVPGARL 795
Cdd:cd17650 206 NGL--DLSAMRLLIVGSDGCKAQDFKTLA--ARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 796 YILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRG 875
Cdd:cd17650 282 YVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 876 YRIEPGEVEAALRQIDGVREAAVVARTE-GEETELYAYI---EGQDQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGK 951
Cdd:cd17650 362 FRIELGEIESQLARHPAIDEAVVAVREDkGGEARLCAYVvaaATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441
|
....*.
gi 2040046167 952 LDRKAL 957
Cdd:cd17650 442 VDRRAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
464-958 |
1.67e-142 |
|
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: 453.43 E-value: 1.67e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL 543
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGARLLVTGPglsvsgfsgetlevnlsslrtepaENepvcahtdggsLAYVIYTSGSTGTPKGVA 623
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQP------------------------EN-----------LAYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 624 VEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIP 703
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 704 AMANSFLDQVEMETeekrTSLAKTLKRVFAGGEALAPQTAARFARSL-PETAVIHGYGPTEATVDAAFFRYDHEKDRERM 782
Cdd:cd17644 206 AYWHLLVLELLLST----IDLPSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEATIAATVCRLTQLTERNIT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 783 RLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYR--GERMYQTGDLARWLPDGT 860
Cdd:cd17644 282 SVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 861 VEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVAR-TEGEETELYAYIEGQDQKTARTE-----LGKRLPAYMM 934
Cdd:cd17644 362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVReDQPGNKRLVAYIVPHYEESPSTVelrqfLKAKLPDYMI 441
|
490 500
....*....|....*....|....
gi 2040046167 935 PSSFIEMREWPVTPSGKLDRKALP 958
Cdd:cd17644 442 PSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1505-1985 |
1.92e-142 |
|
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: 452.01 E-value: 1.92e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1505 RLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTED 1584
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1585 MPTERLEWMLSDSNAVMLLQSdrleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRG 1664
Cdd:cd17645 82 YPGERIAYMLADSSAKILLTN---------------------------------PDDLAYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1665 VVRLVKNSDMAFS--PEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSL--- 1739
Cdd:cd17645 129 LVNLCEWHRPYFGvtPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAaeq 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1740 FNQLSEQNERTfsdlsrLILGGEALspnhvNRVRNTApdLALWNGYGPTENTTFSTCFRIEHEYKhSIPIGRPIANSTAY 1819
Cdd:cd17645 209 FMQLDNQSLRV------LLTGGDKL-----KKIERKG--YKLVNNYGPTENTVVATSFEIDKPYA-NIPIGKPIDNTRVY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1820 IVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGY 1899
Cdd:cd17645 275 ILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1900 RIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKV 434
|
....*.
gi 2040046167 1980 DRRALP 1985
Cdd:cd17645 435 DRKALP 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1514-1985 |
4.10e-142 |
|
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: 452.70 E-value: 4.10e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1514 TPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWM 1593
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1594 LSDSNAVMLLQSDRLESHMA--GKRLFIEDiQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK- 1670
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSfnKSTILLED-PSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1671 -NSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNE- 1748
Cdd:cd17656 160 eREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREf 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1749 --RTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTC-FRIEHEYKHSIPIGRPIANSTAYIVNSRG 1825
Cdd:cd17656 240 inRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYtINPEAEIPELPPIGKPISNTWIYILDQEQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1826 RLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGE 1905
Cdd:cd17656 320 QLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1906 IEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALP 1985
Cdd:cd17656 400 IEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1515-1984 |
2.77e-137 |
|
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: 437.67 E-value: 2.77e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLQSdrleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDM 1674
Cdd:cd17650 81 EDSGAKLLLTQ---------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1675 -----AFSPedRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSE---Q 1746
Cdd:cd17650 128 eyeldSFPV--RLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyvyR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1747 NERTFSDLSRLILGGEALSPN-HVNRVRNTAPDLALWNGYGPTENTTFSTCF---RIEHEYKHSIPIGRPIANSTAYIVN 1822
Cdd:cd17650 206 NGLDLSAMRLLIVGSDGCKAQdFKTLAARFGQGMRIINSYGVTEATIDSTYYeegRDPLGDSANVPIGRPLPNTAMYVLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1823 SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIE 1902
Cdd:cd17650 286 ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1903 LGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRR 1982
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
..
gi 2040046167 1983 AL 1984
Cdd:cd17650 446 AL 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
465-957 |
1.04e-136 |
|
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: 435.98 E-value: 1.04e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLVTGPGlsvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAV 624
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD-----------------------------------DLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 625 EHRQAAAFLSGMQRQFPlTEDDVIVLKS-SFSFDASIWQLFWWMIPGASMYLLpqgwekDPALMTEAF-TNEGVTTAHFI 702
Cdd:cd12115 126 EHRNAAAFLQWAAAAFS-AEELAGVLAStSICFDLSVFELFGPLATGGKVVLA------DNVLALPDLpAAAEVTLINTV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 703 PAMANSFLDQvemeteekrTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRErm 782
Cdd:cd12115 199 PSAAAELLRH---------DALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGE-- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 783 rLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVE 862
Cdd:cd12115 268 -VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 863 WLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVAR-TEGEETELYAYIEGQDQKTARTE-----LGKRLPAYMMPS 936
Cdd:cd12115 347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIgDAAGERRLVAYIVAEPGAAGLVEdlrrhLGTRLPAYMVPS 426
|
490 500
....*....|....*....|.
gi 2040046167 937 SFIEMREWPVTPSGKLDRKAL 957
Cdd:cd12115 427 RFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
477-957 |
3.49e-134 |
|
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: 429.77 E-value: 3.49e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVT-GPGLSVSGFSGETLEVNLSSLRTEPAENEPVCAHTDggsLAYVIYTSGSTGTPKGVAVEHRQAAAFLSG 635
Cdd:cd12114 81 ADAGARLVLTdGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDD---LAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 636 MQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEM 715
Cdd:cd12114 158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 716 ETEEKRTslaktLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDhEKDRERMRLPIGKPVPGARL 795
Cdd:cd12114 238 AQALLPS-----LRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPID-EVPPDWRSIPYGRPLANQRY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 796 YILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPfyRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRG 875
Cdd:cd12114 312 RVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 876 YRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTARTE------LGKRLPAYMMPSSFIEMREWPVTPS 949
Cdd:cd12114 390 YRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPdalrafLAQTLPAYMIPSRVIALEALPLTAN 469
|
....*...
gi 2040046167 950 GKLDRKAL 957
Cdd:cd12114 470 GKVDRAAL 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
466-958 |
5.88e-134 |
|
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: 427.74 E-value: 5.88e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 466 HSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDP 545
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 546 DYPEERLRYMLADSGARLLVTGPGlsvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAVE 625
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPD-----------------------------------DLAYVIYTSGSTGLPKGVMIE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 626 HRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAM 705
Cdd:cd17645 126 HHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 706 ANSFLdqvEMETEEKRTslaktlkrVFAGGEALApqtaaRFARSlpETAVIHGYGPTEATVDAAFFrydhEKDRERMRLP 785
Cdd:cd17645 206 AEQFM---QLDNQSLRV--------LLTGGDKLK-----KIERK--GYKLVNNYGPTENTVVATSF----EIDKPYANIP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 786 IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLG 865
Cdd:cd17645 264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 866 RMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGE-ETELYAYI---EGQDQKTARTELGKRLPAYMMPSSFIEM 941
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADgRKYLVAYVtapEEIPHEELREWLKNDLPDYMIPTYFVHL 423
|
490
....*....|....*..
gi 2040046167 942 REWPVTPSGKLDRKALP 958
Cdd:cd17645 424 KALPLTANGKVDRKALP 440
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1506-1984 |
1.03e-132 |
|
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: 425.80 E-value: 1.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1506 LFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDM 1585
Cdd:cd05918 4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1586 PTERLEWMLSDSNAVMLLQSDrleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGV 1665
Cdd:cd05918 84 PLQRLQEILQDTGAKVVLTSS--------------------------------PSDAAYVIFTSGSTGKPKGVVIEHRAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1666 VRLVK--NSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYI-SDKETyldSDRLKTFIQQNGITTLWLTSSLFNQ 1742
Cdd:cd05918 132 STSALahGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIpSEEDR---LNDLAGFINRLRVTWAFLTPSVARL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 LSEQnerTFSDLSRLILGGEALSPNHVNRvrnTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSIpIGRPIAnSTAYIVN 1822
Cdd:cd05918 209 LDPE---DVPSLRTLVLGGEALTQSDVDT---WADRVRLINAYGPAECTIAATVSPVVPSTDPRN-IGRPLG-ATCWVVD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1823 --SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNP-------FTPGERMYRTGDLARWLKDGTIDYIGRMDDQ 1893
Cdd:cd05918 281 pdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1894 VKIRGYRIELGEIEAALRQIDGVKE---AAVIVRTGPSGHKELLAYMSLQAEM-------------------NIEKVRSL 1951
Cdd:cd05918 361 VKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGSSsgsgdgdslflepsdefraLVAELRSK 440
|
490 500 510
....*....|....*....|....*....|...
gi 2040046167 1952 LSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05918 441 LRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
7-449 |
1.24e-132 |
|
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: 424.44 E-value: 1.24e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 7 IQDIYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLKERQS 86
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 87 RLQFVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKA 166
Cdd:pfam00668 81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 167 LGKEQLPDFEPVHPFSKYIKW----LMRQDRKEAEAFWKTRLIDVKQTASLPKTSSSSKG---KLEQMAFTLSKEQTEGL 239
Cdd:pfam00668 161 LLKGEPLPLPPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADrsfKGDRLSFTLDEDTEELL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 240 RKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSdlEDVEKMVGLFINTIPVRVK-SGPESFLTLVSHLQQ 318
Cdd:pfam00668 241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDpKGGKTFSELIKRVQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 319 ESLKAEAYSYYPLYDIQAQS-----MLKHELFDHIVVFENIPAQREIESLNQADAFDFTVDDFdMDEVTNYGCSIKIIP- 392
Cdd:pfam00668 319 DLLSAEPHQGYPFGDLVNDLrlprdLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSV-IEEEAKYDLSLTASEr 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 393 GSSLYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQQIAQIALLGEETAKKML 449
Cdd:pfam00668 398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1515-1984 |
7.63e-131 |
|
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: 420.52 E-value: 7.63e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNA-VMLLQSDRLESHMAGKRLFIEDIQLEAGiSANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK--N 1671
Cdd:cd12114 81 ADAGArLVLTDGPDAQLDVAVFDVLILDLDALAA-PAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILdiN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1672 SDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITtLWLT-SSLFNQL---SEQN 1747
Cdd:cd12114 160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVT-LWNSvPALLEMLldvLEAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1748 ERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIE--HEYKHSIPIGRPIANSTAYIVNSRG 1825
Cdd:cd12114 239 QALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDevPPDWRSIPYGRPLANQRYRVLDPRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1826 RLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPftPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGE 1905
Cdd:cd12114 319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1906 IEAALRQIDGVKEAAVIVRTGPSGhKELLAYMSLQAEMNI---EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRR 1982
Cdd:cd12114 397 IEAALQAHPGVARAVVVVLGDPGG-KRLAAFVVPDNDGTPiapDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
..
gi 2040046167 1983 AL 1984
Cdd:cd12114 476 AL 477
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1063-1467 |
1.03e-127 |
|
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: 409.51 E-value: 1.03e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1063 PVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFeTGADGEPVQRIHD----DVPFQ 1138
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVF-PEDDGGPYQVVLPaaeaRPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1139 LMELAAAE------DFV-RPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRTLH------ 1205
Cdd:cd19540 82 VVDVTEDElaarlaEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGrapdwa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1206 PLRIQYKDYAVWQQAFKQGEA-----YNRQEAYWLKQLDGeLP-VLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKI 1279
Cdd:cd19540 162 PLPVQYADYALWQRELLGDEDdpdslAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1280 ARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEA 1359
Cdd:cd19540 241 AREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1360 YEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHLTTIAHDAHkVSKFDMTLYAAEEDQET-----I 1434
Cdd:cd19540 321 FAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTG-VAKFDLSFTLTERRDADgapagL 399
|
410 420 430
....*....|....*....|....*....|...
gi 2040046167 1435 RFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEH 1467
Cdd:cd19540 400 TGELEYATDLFDRSTAERLADRFVRVLEAVVAD 432
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
476-958 |
2.44e-126 |
|
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: 407.63 E-value: 2.44e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 476 SPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYM 555
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 556 LADSGARLLVTGPGLSVS-GFSGETLEVNLSSLRTEPAENEPVCAHTDggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLS 634
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKlSFNKSTILLEDPSISQEDTSNIDYINNSD--DLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 635 GMQRQF-PLTEDDVIVLkSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAhFIPAmanSFLDQV 713
Cdd:cd17656 159 FEREKTnINFSDKVLQF-ATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPV---AFLKFI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 714 EMETEEKrTSLAKTLKRVFAGGEALapQTAARFARSLPETAV-IHG-YGPTEATVDAAFfRYDHEKDRERMRlPIGKPVP 791
Cdd:cd17656 234 FSEREFI-NRFPTCVKHIITAGEQL--VITNEFKEMLHEHNVhLHNhYGPSETHVVTTY-TINPEAEIPELP-PIGKPIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 792 GARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQV 871
Cdd:cd17656 309 NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 872 KIRGYRIEPGEVEAALRQIDGVREAAVVARTEGE-ETELYAYIEGQDQKTA---RTELGKRLPAYMMPSSFIEMREWPVT 947
Cdd:cd17656 389 KIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKgEKYLCAYFVMEQELNIsqlREYLAKQLPEYMIPSFFVPLDQLPLT 468
|
490
....*....|.
gi 2040046167 948 PSGKLDRKALP 958
Cdd:cd17656 469 PNGKVDRKALP 479
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1505-1984 |
1.88e-125 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 402.84 E-value: 1.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1505 RLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTED 1584
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1585 MPTERLEWMLSDSNAVMLLQSDRleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRG 1664
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTDS-------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1665 VVRLVK--NSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLdSDRLKTfiqqngITTLWLTSSLfnq 1742
Cdd:cd17653 130 VLNYVSqpPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPF-AHVART------VDALMSTPSI--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 LSEQNERTFSDLSRLILGGEALSPNHVNRvrnTAPDLALWNGYGPTENTTFSTCFRIEHEykHSIPIGRPIANSTAYIVN 1822
Cdd:cd17653 200 LSTLSPQDFPNLKTIFLGGEAVPPSLLDR---WSPGRRLYNAYGPTECTISSTMTELLPG--QPVTIGKPIPNSTCYILD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1823 SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIE 1902
Cdd:cd17653 275 ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRIN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1903 LGEIEAALRQIDG-VKEAAVIVRTGpsghkELLAYMSlQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:cd17653 355 LEEIEEVVLQSQPeVTQAAAIVVNG-----RLVAFVT-PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDR 428
|
...
gi 2040046167 1982 RAL 1984
Cdd:cd17653 429 KAL 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
473-957 |
1.31e-123 |
|
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: 398.54 E-value: 1.31e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERL 552
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 553 RYMLADSGARLLVTgpglsvsgfsgetlevnlsslrtepaenepvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAF 632
Cdd:cd05945 81 REILDAAKPALLIA-----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 633 LSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPamanSFLDQ 712
Cdd:cd05945 126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTP----SFAAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 713 VEMETEEKRTSLAkTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGKPVPG 792
Cdd:cd05945 202 CLLSPTFTPESLP-SLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 793 ARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPfyrGERMYQTGDLARWLPDGTVEWLGRMDGQVK 872
Cdd:cd05945 281 AKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 873 IRGYRIEPGEVEAALRQIDGVREAAVVARTEGE-ETELYAYIEG------QDQKTARTELGKRLPAYMMPSSFIEMREWP 945
Cdd:cd05945 358 LNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEkVTELIAFVVPkpgaeaGLTKAIKAELAERLPPYMIPRRFVYLDELP 437
|
490
....*....|..
gi 2040046167 946 VTPSGKLDRKAL 957
Cdd:cd05945 438 LNANGKIDRKAL 449
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
465-957 |
9.41e-122 |
|
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: 394.22 E-value: 9.41e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLVTgpglsvsgfsgetlevnlsslrtepaenepvcahTDGGSLAYVIYTSGSTGTPKGVAV 624
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLT----------------------------------SSPSDAAYVIFTSGSTGKPKGVVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 625 EHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQgWEKDPALmTEAFTNEGVTTAHFIPA 704
Cdd:cd05918 127 EHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSE-EDRLNDL-AGFINRLRVTWAFLTPS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 705 MANSF-LDQVEmeteekrtslakTLKRVFAGGEALAPQTAARFArslPETAVIHGYGPTEATVDAAFFRYDHEKDRERmr 783
Cdd:cd05918 205 VARLLdPEDVP------------SLRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAECTIAATVSPVVPSTDPRN-- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 784 lpIGKPVpGARLYILDSEKAVQ--PIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFY-------RGERMYQTGDLAR 854
Cdd:cd05918 268 --IGRPL-GATCWVVDPDNHDRlvPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWlkqegsgRGRRLYRTGDLVR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 855 WLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA----RTEGEETELYAYIEGQDQ------------ 918
Cdd:cd05918 345 YNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpKDGSSSPQLVAFVVLDGSssgsgdgdslfl 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2040046167 919 ----------KTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05918 425 epsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1511-1984 |
4.14e-115 |
|
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: 373.89 E-value: 4.14e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERL 1590
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 EWMLSDSNAVMLLQSdrleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK 1670
Cdd:cd05945 81 REILDAAKPALLIAD---------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1671 --NSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTlW----------LTSS 1738
Cdd:cd05945 128 wmLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITV-WvstpsfaamcLLSP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1739 LFNQLSEQNERTFsdlsrlILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIE----HEYKhSIPIGRPIA 1814
Cdd:cd05945 207 TFTPESLPSLRHF------LFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTpevlDGYD-RLPIGYAKP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1815 NSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPftpGERMYRTGDLARWLKDGTIDYIGRMDDQV 1894
Cdd:cd05945 280 GAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1895 KIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEK---VRSLLSQQLPGFMIPAHLVELAAL 1971
Cdd:cd05945 357 KLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLtkaIKAELAERLPPYMIPRRFVYLDEL 436
|
490
....*....|...
gi 2040046167 1972 PLTQNGKLDRRAL 1984
Cdd:cd05945 437 PLNANGKIDRKAL 449
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
477-958 |
4.76e-115 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 374.04 E-value: 4.76e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAK-ESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYM 555
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 556 LADSGARLLVTGPglsvsgfsgetlevnlsslrtepaenepvcahTDggsLAYVIYTSGSTGTPKGVAVEHRQAAAFLSG 635
Cdd:cd17648 81 LEDTGARVVITNS--------------------------------TD---LAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 636 MQRQFPL--TEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPamanSFLDQV 713
Cdd:cd17648 126 LSERYFGrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTP----SVLQQY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 714 EMEteeKRTSLaktlKRVFAGGEALapqTAARFA--RSLPETAVIHGYGPTEATVDA--AFFRYDHEKDRErmrlpIGKP 789
Cdd:cd17648 202 DLA---RLPHL----KRVDAAGEEF---TAPVFEklRSRFAGLIINAYGPTETTVTNhkRFFPGDQRFDKS-----LGRP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 790 VPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFY--------RGERMYQTGDLARWLPDGTV 861
Cdd:cd17648 267 VRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargRNARLYKTGDLVRWLPSGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 862 EWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVAR------TEGEETELYAYI----EGQDQKTARTELGKRLPA 931
Cdd:cd17648 347 EYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedasqaQSRIQKYLVGYYlpepGHVPESDLLSFLRAKLPR 426
|
490 500
....*....|....*....|....*..
gi 2040046167 932 YMMPSSFIEMREWPVTPSGKLDRKALP 958
Cdd:cd17648 427 YMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1515-1985 |
1.98e-114 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 372.12 E-value: 1.98e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVG-SESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWM 1593
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1594 LSDSNAvmllqsdrleshmagkRLFIEDiqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVR----LV 1669
Cdd:cd17648 81 LEDTGA----------------RVVITN-----------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNlrtsLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1670 KNSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSlfnQLSEQNER 1749
Cdd:cd17648 128 ERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPS---VLQQYDLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1750 TFSDLSRLILGGEALSPNHVNRVRNTAPDLALwNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQP 1829
Cdd:cd17648 205 RLPHLKRVDAAGEEFTAPVFEKLRSRFAGLII-NAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1830 MGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF-TPGE-------RMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRI 1901
Cdd:cd17648 284 VGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqTEQErargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1902 ELGEIEAALRQIDGVKEAAVIVRTGPS-----GHKELLAYMSLQAEMNIEK-VRSLLSQQLPGFMIPAHLVELAALPLTQ 1975
Cdd:cd17648 364 EPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIPVTI 443
|
490
....*....|
gi 2040046167 1976 NGKLDRRALP 1985
Cdd:cd17648 444 NGKLDVRALP 453
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
465-959 |
2.13e-113 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 369.14 E-value: 2.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLVTgpglsvsgfsgetlevnlsslrtepaenepvcahtdggslAYVIYTSGSTGTPKGVAV 624
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 625 EHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDAS-IWQLFWWMIPGASMYLLPqgwEKDPALMTEAFTNEGVTTAHFIP 703
Cdd:COG0318 121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 704 AMANSFLDQVEMETEekRTSlakTLKRVFAGGEALAPQTAARFARSLpETAVIHGYGPTEATVDAAFFRYDHekdRERMR 783
Cdd:COG0318 198 TMLARLLRHPEFARY--DLS---SLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDP---GERRP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 784 LPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFlDDPFYRgermyqTGDLARWLPDGTVEW 863
Cdd:COG0318 269 GSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLR------TGDLGRLDEDGYLYI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 864 LGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEetELYAYIEGQDQKTA-----RTELGKRLPAYMMP 935
Cdd:COG0318 342 VGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDekwGE--RVVAFVVLRPGAELdaeelRAFLRERLARYKVP 419
|
490 500
....*....|....*....|....
gi 2040046167 936 SSFIEMREWPVTPSGKLDRKALPA 959
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRALRE 443
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
469-957 |
9.76e-113 |
|
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: 366.25 E-value: 9.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 469 FTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:cd17653 3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVTGPGlsvsgfsgetlevnlsslrtepaenepvcahtdGGSLAYVIYTSGSTGTPKGVAVEHRQ 628
Cdd:cd17653 83 SARIQAILRTSGATLLLTTDS---------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLlpqgweKDPAlMTEAFTNEGVTTAHFIPamanS 708
Cdd:cd17653 130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPS-DPFAHVARTVDALMSTP----S 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLDQVemeteeKRTSLaKTLKRVFAGGEALAPQTAARFArslPETAVIHGYGPTEATVDAAFFRYdhekdRERMRLPIGK 788
Cdd:cd17653 199 ILSTL------SPQDF-PNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTECTISSTMTEL-----LPGQPVTIGK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 789 PVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMD 868
Cdd:cd17653 264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRED 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 869 GQVKIRGYRIEPGEVEAALRQIDG-VREAAVVArtegEETELYAYI--EGQDQKTARTELGKRLPAYMMPSSFIEMREWP 945
Cdd:cd17653 344 NQVKVRGFRINLEEIEEVVLQSQPeVTQAAAIV----VNGRLVAFVtpETVDVDGLRSELAKHLPSYAVPDRIIALDSFP 419
|
490
....*....|..
gi 2040046167 946 VTPSGKLDRKAL 957
Cdd:cd17653 420 LTANGKVDRKAL 431
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1507-1897 |
1.09e-112 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 365.48 E-value: 1.09e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1507 FEYQAAKTPHAPAV-IYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDM 1585
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1586 PTERLEWMLSDSNAVMLLQSDRLESHM------------------AGKRLFIEDIQLEAGISANNPEQ--QGGPDSLAYI 1645
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEEllealgklevvklvlvldRDPVLKEEPLPEEAKPADVPPPPppPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1646 MYTSGSTGTPKGVMVEQRGVVRLVKNSDM------AFSPEDRILLTASLGFDA-MTFEVFGPLLNGACLYISDKETYLDS 1718
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprgfGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 DRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRNTAPDlALWNGYGPTENTTFST 1795
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLrlvLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1796 CFRIEHEYKHSIP-IGRPIANSTAYIVN-SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPnpftpgERMYRTG 1873
Cdd:pfam00501 320 TPLPLDEDLRSLGsVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
|
410 420
....*....|....*....|....
gi 2040046167 1874 DLARWLKDGTIDYIGRMDDQVKIR 1897
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
469-874 |
1.13e-112 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 365.48 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 469 FTRRAALSPNLPAVRFSGGI-LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDY 547
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 548 PEERLRYMLADSGARLLVTGPGLSVSGF----------SGETLEVNLSSLRTEPAENEPVCAH--------TDGGSLAYV 609
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELlealgklevvKLVLVLDRDPVLKEEPLPEEAKPADvpppppppPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 610 IYTSGSTGTPKGVAVEHRQAAAFLSGM----QRQFPLTEDDVIVLKSSFSFDAS-IWQLFWWMIPGASMYLLPQGWEKDP 684
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 685 ALMTEAFTNEGVTTAHFIPAMANSFLDQvemetEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPEtAVIHGYGPTEA 764
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEA-----GAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 765 TVDAAFFRYDHekDRERMRLPIGKPVPGARLYILD-SEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRg 843
Cdd:pfam00501 315 TGVVTTPLPLD--EDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYR- 391
|
410 420 430
....*....|....*....|....*....|.
gi 2040046167 844 ermyqTGDLARWLPDGTVEWLGRMDGQVKIR 874
Cdd:pfam00501 392 -----TGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1063-1468 |
2.02e-111 |
|
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: 362.74 E-value: 2.02e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1063 PVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDD----VPFQ 1138
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPE-EDGVPYQLILEEdeatPKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1139 LMELAAAE------DFVR-PFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRT------LH 1205
Cdd:cd19538 82 IKEVDEEEleseinEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCkgeapeLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1206 PLRIQYKDYAVWQQAFKQGEAYN-----RQEAYWLKQLDGeLPV-LELPADNARPAVRSFAGDHVSFSLDADTSSGLYKI 1279
Cdd:cd19538 162 PLPVQYADYALWQQELLGDESDPdsliaRQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1280 ARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEA 1359
Cdd:cd19538 241 AKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1360 YEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHlTTIAHDAHKVSKFDMTL-----YAAEEDQeTI 1434
Cdd:cd19538 321 YEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLE-AKLELRTVGSAKFDLTFelreqYNDGTPN-GI 398
|
410 420 430
....*....|....*....|....*....|....
gi 2040046167 1435 RFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEHQ 1468
Cdd:cd19538 399 EGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1503-1986 |
7.51e-108 |
|
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: 352.96 E-value: 7.51e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1503 ISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVT 1582
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1583 EDMPTERLEWMLSDSNAVMLLqsdrleshmagkrlfiediqleagisannpeqqggpdsLAYIMYTSGSTGTPKGVMVEQ 1662
Cdd:COG0318 81 PRLTAEELAYILEDSGARALV--------------------------------------TALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1663 RGVVRLVKNS--DMAFSPEDRILLTASLGFD-AMTFEVFGPLLNGACLYISDKetyLDSDRLKTFIQQNGITTLWLTSSL 1739
Cdd:COG0318 123 RNLLANAAAIaaALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPTM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1740 FNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRNTApDLALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANS 1816
Cdd:COG0318 200 LARLLRHPEFARYDLSSLrlvVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1817 TAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKI 1896
Cdd:COG0318 279 EVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1897 RGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLT 1974
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpgAELDAEELRAFLRERLARYKVPRRVEFVDELPRT 431
|
490
....*....|..
gi 2040046167 1975 QNGKLDRRALPE 1986
Cdd:COG0318 432 ASGKIDRRALRE 443
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1063-1461 |
2.03e-94 |
|
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: 313.55 E-value: 2.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1063 PVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRI---------HD 1133
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEIlppgpapleVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1134 DVPFQLMELAAA-EDFVR-----PFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRT---- 1203
Cdd:cd19539 83 DLSDPDSDRERRlEELLReresrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1204 --LHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGeLPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIAR 1281
Cdd:cd19539 163 apLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1282 DNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYE 1361
Cdd:cd19539 242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1362 HQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHLTTIAHDAHKVSKFDMTLYAAEEDqETIRFDVEFN 1441
Cdd:cd19539 322 HQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEG-TGLRGSLGYA 400
|
410 420
....*....|....*....|
gi 2040046167 1442 TDIYQKQTIKKWLSYYIHIL 1461
Cdd:cd19539 401 TSLFDEETIQGFLADYLQVL 420
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
473-957 |
1.67e-88 |
|
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: 298.98 E-value: 1.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERL 552
Cdd:TIGR01734 10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 553 RYMLADSGARLLVTGPGLSVSGFSGETLEVNLsslrTEPAENE--PVC--AHTDGGSLAYVIYTSGSTGTPKGVAVEHRQ 628
Cdd:TIGR01734 90 EMIIEAAGPELVIHTAELSIDAVGTQIITLSA----LEQAETSggPVSfdHAVKGDDNYYIIYTSGSTGNPKGVQISHDN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPamanS 708
Cdd:TIGR01734 166 LVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTP----S 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLDQVEME---TEEKRTSLAktlkRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLP 785
Cdd:TIGR01734 242 FVDMCLLDpnfNQENYPHLT----HFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQYPRLP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 786 IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLddpFYRGERMYQTGDLARwLPDGTVEWLG 865
Cdd:TIGR01734 318 IGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFYQG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 866 RMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEE--TELYAYIEGQDQKTAR---------TELGKRLPAYMM 934
Cdd:TIGR01734 394 RLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHkvEYLIAAIVPETEDFEKefqltkaikKELKKSLPAYMI 473
|
490 500
....*....|....*....|...
gi 2040046167 935 PSSFIEMREWPVTPSGKLDRKAL 957
Cdd:TIGR01734 474 PRKFIYRDQLPLTANGKIDRKAL 496
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
477-957 |
1.18e-87 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 296.81 E-value: 1.18e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:PRK04813 16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTGPGLSVSGFSGETLevNLSSLRTEPAENEPV--CAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLS 634
Cdd:PRK04813 96 EVAKPSLIIATEELPLEILGIPVI--TLDELKDIFATGNPYdfDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 635 GMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFT----NEGVTTAHFIPA--MANS 708
Cdd:PRK04813 174 WMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPqlpiNVWVSTPSFADMclLDPS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FldqvemeTEEKRTSlaktLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATV--------DAAFFRYDhekdre 780
Cdd:PRK04813 254 F-------NEEHLPN----LTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVavtsieitDEMLDQYK------ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 781 rmRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDdpfYRGERMYQTGDLARwLPDGT 860
Cdd:PRK04813 317 --RLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDGL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 861 VEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA-RTEGEETELYAYI---EGQDQKTA------RTELGKRLP 930
Cdd:PRK04813 391 LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPyNKDHKVQYLIAYVvpkEEDFEREFeltkaiKKELKERLM 470
|
490 500
....*....|....*....|....*..
gi 2040046167 931 AYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK04813 471 EYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
2080-2533 |
1.33e-86 |
|
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: 291.93 E-value: 1.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2080 IEGEVPWTPVQ--RWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTII-DDGGQLQQFNRGI-HG 2155
Cdd:pfam00668 1 VQDEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEErPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2156 ELYSLNIRDLSKTAQwEKLIEDEV-ADLQRSIHLQTGPLLKAGLFN-TMSGTYLFLTIHHLVVDGVSWRILLEDLSAAYS 2233
Cdd:pfam00668 81 ELEIIDISDLSESEE-EEAIEAFIqRDLQSPFDLEKGPLFRAGLFRiAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2234 QAAAGQPVQLPRKTDsYQYFANRLAEYAESSKVIREQSYWRTVEKEKAAL--LPCEKPHSAADNIR-KTESFTLSEEDTH 2310
Cdd:pfam00668 160 QLLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVlqLPKDYARPADRSFKgDRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2311 vLIHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRdhtlPELDISRTVGWFTTIYPVLIDLHHAAegELGL 2390
Cdd:pfam00668 239 -LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR----PSPDIERMVGMFVNTLPLRIDPKGGK--TFSE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2391 AVKTVKDTLGRI-PDKGMGYGILKY---LTSSENKTIQFGkaPEIGF-NYLGQFNDTErqqKFSFSGLASGKDITPTWQR 2465
Cdd:pfam00668 312 LIKRVQEDLLSAePHQGYPFGDLVNdlrLPRDLSRHPLFD--PMFSFqNYLGQDSQEE---EFQLSELDLSVSSVIEEEA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 2466 EQTLEMSAMVRQNQLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHCAHKQETEKTVSDFSSQSLT 2533
Cdd:pfam00668 387 KYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1234-2089 |
1.95e-86 |
|
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: 313.54 E-value: 1.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1234 WLKQLDGeLPVLELPADNARPAVRSFAGDHVSFSLDADTSsglykiARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSp 1313
Cdd:TIGR03443 2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1314 iagRAHKDLESVIgmfvntlaIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEELVDRLDVVRDMSRNP-LFDVMFal 1392
Cdd:TIGR03443 74 ---SSNKSGRPFV--------LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAF-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1393 QNMERESLTLHDLHLTTiahdahkvskfDMTLYAAEEDQEtIRFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEHQNIHL 1472
Cdd:TIGR03443 141 QDAPDNQQTTYSTGSTT-----------DLTVFLTPSSPE-LELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1473 GDIHVLDEHETSSF---------------IH-TFNQTKQDYPKHETIsrlFEYQAAKTPHAPaviydRQTLTYRELNQRA 1536
Cdd:TIGR03443 209 GKVSLITPSQKSLLpdptkdldwsgfrgaIHdIFADNAEKHPDRTCV---VETPSFLDPSSK-----TRSFTYKQINEAS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1537 NRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGA---------------YL------------------PVTE 1583
Cdd:TIGR03443 281 NILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATfsvidpaypparqtiYLsvakpraliviekagtldQLVR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1584 DMPTERLEwMLSDSNAVMLLQSDRLEshmaGKRLFIEDIQLEAGISANNPEQQG---GPDSLAYIMYTSGSTGTPKGV-- 1658
Cdd:TIGR03443 361 DYIDKELE-LRTEIPALALQDDGSLV----GGSLEGGETDVLAPYQALKDTPTGvvvGPDSNPTLSFTSGSEGIPKGVlg 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1659 -----------MVEQRGVvrlvknsdmafSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQ 1727
Cdd:TIGR03443 436 rhfslayyfpwMAKRFGL-----------SENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAK 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1728 NGITTLWLTSSLFNQLSEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIE------- 1800
Cdd:TIGR03443 505 YGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPsrssdst 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1801 --HEYKHSIPIGRPIANSTAYIVNSRGRLQPMGV--IGELCVGGDGLARGYFGRPELTKEKFVPNPFT------------ 1864
Cdd:TIGR03443 585 flKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdpshwidldken 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1865 ----------PGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELL 1934
Cdd:TIGR03443 665 nkperefwlgPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLV 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1935 AYM----------SLQAEMN------------------IEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:TIGR03443 745 SYIvpqdksdeleEFKSEVDdeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPF 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1987 PETTAINTAYAPPR--------NQLEERLAVIWQEVL--GVEKVGIEDSFFELGGDSIKALQVSARLGR-FDLKITAGDL 2055
Cdd:TIGR03443 825 PDTAQLAAVAKNRSasaadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKkLNVELPLGLI 904
|
970 980 990
....*....|....*....|....*....|....*..
gi 2040046167 2056 FRHPTIKEAA---PLIRKTERNIDQRPIEGEVPWTPV 2089
Cdd:TIGR03443 905 FKSPTIKGFAkevDRLKKGEELADEGDSEIEEEETVL 941
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
10-430 |
1.50e-84 |
|
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: 284.73 E-value: 1.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 10 IYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLKERQSRLQ 89
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 90 FVDISHLDEtaKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRA-HEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKAL- 167
Cdd:cd19536 81 ELDLTPLEE--QLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDeRERFLLVISDHHSILDGWSLYLLVKEILAVYNQLl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 168 --GKEQLPdfePVHPFSKYIKWLMRQDRKEA-EAFWKTRLIDVKqTASLPKTSSSSKGKLEQMAFTL-SKEQTEGLRKLA 243
Cdd:cd19536 159 eyKPLSLP---PAQPYRDFVAHERASIQQAAsERYWREYLAGAT-LATLPALSEAVGGGPEQDSELLvSVPLPVRSRSLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 244 LQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPESFLTLVSHLQQESLKA 323
Cdd:cd19536 235 KRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEETVEDLLKRAQEQELES 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 324 EAYSYYPLYDIQAQSMlKHELFDHIVVFENIPAQREIESLNQADAFDftVDDFDMDEVTNYGCSIKIIP-GSSLYIRINF 402
Cdd:cd19536 315 LSHEQVPLADIQRCSE-GEPLFDSIVNFRHFDLDFGLPEWGSDEGMR--RGLLFSEFKSNYDVNLSVLPkQDRLELKLAY 391
|
410 420
....*....|....*....|....*...
gi 2040046167 403 DIGLYDPAMMKKIELYLRHIIGSVIADP 430
Cdd:cd19536 392 NSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1062-1467 |
9.23e-78 |
|
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: 265.43 E-value: 9.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1062 YPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFeTGADGEPVQ------------ 1129
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQvvldktvrfrie 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1130 ----RIHDDVPFQLMELAAAeDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELY-----A 1200
Cdd:cd19066 81 iidlRNLADPEARLLELIDQ-IQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYdaaerQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1201 SRTLHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIA 1280
Cdd:cd19066 160 KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1281 RDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAY 1360
Cdd:cd19066 240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1361 EHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHLTTIAHDAHKVSKFDMTLYAAEEDQETIRFDVEF 1440
Cdd:cd19066 320 EHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDPDGDLLLRLEY 399
|
410 420
....*....|....*....|....*..
gi 2040046167 1441 NTDIYQKQTIKKWLSYYIHILHHVIEH 1467
Cdd:cd19066 400 SRGVYDERTIDRFAERYMTALRQLIEN 426
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
199-1045 |
1.47e-77 |
|
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: 285.42 E-value: 1.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 199 FWKTRLIDvkQTASL-----PKTSSSSKGKlEQMAFTLSKEqteglrKLALQAGATLNTVFQALWGIILQKINRCDDAVF 273
Cdd:TIGR03443 1 RWSERLDN--PTLSVlphdyLRPANNRLVE-ATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 274 GSvisgrpsdleDVEKMVGLFINTIPVrvkSGPESFLTLVSHLQQESLKAEAYSYYPLYDIQAQSMLKHELFDHIVVFEn 353
Cdd:TIGR03443 72 GT----------SSNKSGRPFVLRLNI---TPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFR- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 354 ipaqreiesLNQADAFDFTVDDFDMDEVTNYgcSIKIIPGSS-LYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADPNQ 432
Cdd:TIGR03443 138 ---------LAFQDAPDNQQTTYSTGSTTDL--TVFLTPSSPeLELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 433 QIAQIALLgEETAKKMLyefnqTEPAAPL-----APTLHSFFTRRAALSPNLPAVRFSGGIL---------TYRELDQYT 498
Cdd:TIGR03443 207 PIGKVSLI-TPSQKSLL-----PDPTKDLdwsgfRGAIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEAS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 499 NQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLV----TGP-GLSVS 573
Cdd:TIGR03443 281 NILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIviekAGTlDQLVR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 574 GFSGETLEvnlssLRTEPaenePVCAHTDGGSLA--------------YVIY-------------------TSGSTGTPK 620
Cdd:TIGR03443 361 DYIDKELE-----LRTEI----PALALQDDGSLVggsleggetdvlapYQALkdtptgvvvgpdsnptlsfTSGSEGIPK 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 621 GVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAH 700
Cdd:TIGR03443 432 GVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTH 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 701 FIPAMANSFLDQVemeteekrTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFF----RYDHE 776
Cdd:TIGR03443 512 LTPAMGQLLSAQA--------TTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFeipsRSSDS 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 777 KDRERMR--LPIGKPVPGARLYILDSEKAVQPIGVA--GELYIAGAGVARGYLNRPELTEERFLDD-------------- 838
Cdd:TIGR03443 584 TFLKNLKdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNwfvdpshwidldke 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 839 ------PFYRG--ERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVRE-AAVVARTEGEETEL 909
Cdd:TIGR03443 664 nnkperEFWLGprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEPTL 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 910 YAYI-------------------EGQDQ------------KTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALP 958
Cdd:TIGR03443 744 VSYIvpqdksdeleefksevddeESSDPvvkglikyrkliKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALP 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 959 APD------GAAERRVYTAPR--TITEMKLAKLWEEVLKYGPA--GTRDHFFEQGGHSLKATALVSRIAKAFGVQVPLKE 1028
Cdd:TIGR03443 824 FPDtaqlaaVAKNRSASAADEefTETEREIRDLWLELLPNRPAtiSPDDSFFDLGGHSILATRMIFELRKKLNVELPLGL 903
|
970
....*....|....*..
gi 2040046167 1029 IFAKPTLEELAAVIQEL 1045
Cdd:TIGR03443 904 IFKSPTIKGFAKEVDRL 920
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1503-1986 |
3.42e-77 |
|
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: 266.24 E-value: 3.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1503 ISRLFEYqAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVT 1582
Cdd:TIGR01734 3 IEAIQAF-AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1583 EDMPTERLEWMLSDSNAVMLLQSDRLESHMAGKRLFIEDIQLEAGISANNPEQQ---GGPDSLaYIMYTSGSTGTPKGVM 1659
Cdd:TIGR01734 82 TSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDhavKGDDNY-YIIYTSGSTGNPKGVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1660 VEQRGVVRLVK--NSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTlWLTS 1737
Cdd:TIGR01734 161 ISHDNLVSFTNwmLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNV-WVST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1738 SLFNQ---LSEQ-NERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHE----YKhSIPI 1809
Cdd:TIGR01734 240 PSFVDmclLDPNfNQENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEildqYP-RLPI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1810 GRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVpnpFTPGERMYRTGDLARwLKDGTIDYIGR 1889
Cdd:TIGR01734 319 GFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQLFYQGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1890 MDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSgHK--ELLAYMSLQ-----AEMNIEK-VRSLLSQQLPGFMI 1961
Cdd:TIGR01734 395 LDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKD-HKveYLIAAIVPEtedfeKEFQLTKaIKKELKKSLPAYMI 473
|
490 500
....*....|....*....|....*
gi 2040046167 1962 PAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:TIGR01734 474 PRKFIYRDQLPLTANGKIDRKALAE 498
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1503-1984 |
9.90e-76 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 262.14 E-value: 9.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1503 ISRLFEYqAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVT 1582
Cdd:PRK04813 5 IETIEEF-AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1583 EDMPTERLEWMLSDSNAVMLLQSDRLESHMAGKRLFIEDiQLEAGISANNP---EQQGGPDSLAYIMYTSGSTGTPKGVM 1659
Cdd:PRK04813 84 VSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLD-ELKDIFATGNPydfDHAVKGDDNYYIIFTSGTTGKPKGVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1660 VEQRGVVRLVK--NSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTlWLTS 1737
Cdd:PRK04813 163 ISHDNLVSFTNwmLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINV-WVST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1738 SLFNQL----SEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHE----YKhSIPI 1809
Cdd:PRK04813 242 PSFADMclldPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEmldqYK-RLPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1810 GRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFvpnpFT-PGERMYRTGDLARwLKDGTIDYIG 1888
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTfDGQPAYHTGDAGY-LEDGLLFYQG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1889 RMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIvrtgPS--GHK--ELLAYMSL-----QAEMNIEK-VRSLLSQQLPG 1958
Cdd:PRK04813 396 RIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV----PYnkDHKvqYLIAYVVPkeedfEREFELTKaIKKELKERLME 471
|
490 500
....*....|....*....|....*.
gi 2040046167 1959 FMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK04813 472 YMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1064-1288 |
9.81e-75 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 249.19 E-value: 9.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1064 VSSAQKRMYVLqqlEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDDVPFQL---- 1139
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVE-EDGEPVQRIDPDADLPLevvd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1140 ------------MELAAAEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYA------S 1201
Cdd:COG4908 77 lsalpepereaeLEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAallegeP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1202 RTLHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIAR 1281
Cdd:COG4908 157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236
|
....*..
gi 2040046167 1282 DNGCTLY 1288
Cdd:COG4908 237 AHGATVN 243
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1061-1462 |
3.60e-73 |
|
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: 251.61 E-value: 3.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1061 TYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSF-ETGADGEPVQRIHDDVPFQL 1139
Cdd:cd19532 1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLASSPLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1140 --MELAAAEDFVR--------PFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRTLHPLRI 1209
Cdd:cd19532 81 ehVQISDEAEVEEeferlknhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1210 QYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGE---LPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCT 1286
Cdd:cd19532 161 QYLDFAARQRQDYESGALDEDLAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1287 LYMVLLAAYSTLLARLSGQEDIIIGspI--AGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQD 1364
Cdd:cd19532 241 PFHFYLAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1365 YPFEELVDRLDVVRDMSRNPLFDVMFALQNMERESLTLHDLHLT-TIAHDAHkvSKFDMTLYAAEEDQETIRFDVEFNTD 1443
Cdd:cd19532 319 VPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEgEEFEDAR--TPYDLSLDIIDNPDGDCLLTLKVQSS 396
|
410
....*....|....*....
gi 2040046167 1444 IYQKQTIKKWLSYYIHILH 1462
Cdd:cd19532 397 LYSEEDAELLLDSYVNLLE 415
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1642-1980 |
8.56e-71 |
|
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: 241.81 E-value: 8.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1642 LAYIMYTSGSTGTPKGVMVEQRGVVRLVKN--SDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSD 1719
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAlaASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1720 RLktfIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRNtAPDLALWNGYGPTENTTFSTC 1796
Cdd:cd04433 82 EL---IEREKVTILLGVPTLLARLLKAPESAGYDLSSLralVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1797 FRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFvpnpftpGERMYRTGDLA 1876
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1877 RWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSL--QAEMNIEKVRSLLSQ 1954
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLrpGADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 2040046167 1955 QLPGFMIPAHLVELAALPLTQNGKLD 1980
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1061-1467 |
2.63e-70 |
|
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: 243.76 E-value: 2.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1061 TYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDDVPF--- 1137
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEE-EDGVPFQKIEPSKPLsfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1138 --QLMELAAAE--DFVR-----PFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYAS------- 1201
Cdd:cd20484 80 eeDISSLKESEiiAYLRekakePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQAllqgkqp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1202 RTLHPLRIqYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLYKIAR 1281
Cdd:cd20484 160 TLASSPAS-YYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1282 DNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYE 1361
Cdd:cd20484 239 SQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1362 HQDYPFEELVDRLDVVRDMSRNPLFDVMFALQNMeRESLTLHD--------LHLTTIaHDAHKVSKFDMTLYAAEEDQET 1433
Cdd:cd20484 319 HAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNF-LQSTSLQQflaeyqdvLSIEFV-EGIHQEGEYELVLEVYEQEDRF 396
|
410 420 430
....*....|....*....|....*....|....
gi 2040046167 1434 IrFDVEFNTDIYQKQTIKKWLSYYIHILHHVIEH 1467
Cdd:cd20484 397 T-LNIKYNPDLFDASTIERMMEHYVKLAEELIAN 429
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
606-953 |
3.54e-69 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 237.18 E-value: 3.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 LAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGwekDPA 685
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 686 LMTEAFTNEGVTTAHFIPAMANSFLDQvemeTEEKRTSLAkTLKRVFAGGEALAPQTAARFARsLPETAVIHGYGPTEAT 765
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKA----PESAGYDLS-SLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 766 VDAAFFRYDhekDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEErFLDDPFYRger 845
Cdd:cd04433 153 GTVATGPPD---DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAA-VDEDGWYR--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 846 myqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETE-LYAYIE-----GQDQK 919
Cdd:cd04433 226 ---TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGErVVAVVVlrpgaDLDAE 302
|
330 340 350
....*....|....*....|....*....|....
gi 2040046167 920 TARTELGKRLPAYMMPSSFIEMREWPVTPSGKLD 953
Cdd:cd04433 303 ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1062-1467 |
5.04e-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: 5.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1062 YPVSSAQKRMYvLQQLEDGGVG-YNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRIHDDVPF--- 1137
Cdd:cd19543 2 YPLSPMQEGML-FHSLLDPGSGaYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLpwr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1138 -----------QLMELA--AAEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYAS--- 1201
Cdd:cd19543 81 eldlshlseaeQEAELEalAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAAlge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1202 ---RTLHPLRiQYKDYAVWQQAFKQGEAynrqEAYWLKQLDG--ELPVleLPADNARPAVRSFAGDHVSFSLDADTSSGL 1276
Cdd:cd19543 161 gqpPSLPPVR-PYRDYIAWLQRQDKEAA----EAYWREYLAGfeEPTP--LPKELPADADGSYEPGEVSFELSAELTARL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1277 YKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAH--KDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRE 1354
Cdd:cd19543 234 QELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAelPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1355 TALEAYEHQDYPFEELvdrldVVRDMSRNPLFDVMFALQN----------MERESLTLHDLHLTTIAHdahkvskFDMTL 1424
Cdd:cd19543 314 QQLELREHEYVPLYEI-----QAWSEGKQALFDHLLVFENypvdesleeeQDEDGLRITDVSAEEQTN-------YPLTV 381
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2040046167 1425 YAAEEDQETIRFdvEFNTDIYQKQTIKKWLSYYIHILHHVIEH 1467
Cdd:cd19543 382 VAIPGEELTIKL--SYDAEVFDEATIERLLGHLRRVLEQVAAN 422
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
465-957 |
3.05e-65 |
|
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: 230.53 E-value: 3.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLVTgpglsvsgfsGETLEVNLSSLRTEPAENEPvcahtDGGSLAYVIYTSGSTGTPKGVAV 624
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIV----------AVSFTDLLAAGAPLGERVAL-----TPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 625 EHRQAAAFLSGMQR--QFPLTEDDVIV----LKSSFSFDASIwQLFWWMipGASMYLLPQgweKDPALMTEAFTNEGVTT 698
Cdd:cd05936 146 THRNLVANALQIKAwlEDLLEGDDVVLaalpLFHVFGLTVAL-LLPLAL--GATIVLIPR---FRPIGVLKEIRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 699 AHFIPAMANSFLDQvemetEEKRTSLAKTLKRVFAGGEALAPQTAARFARsLPETAVIHGYGPTEATVDAAFfrydHEKD 778
Cdd:cd05936 220 FPGVPTMYIALLNA-----PEFKKRDFSSLRLCISGGAPLPVEVAERFEE-LTGVPIVEGYGLTETSPVVAV----NPLD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 779 RERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPD 858
Cdd:cd05936 290 GPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLR-------TGDIGYMDED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 859 GTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA---RTEGEETElyAYIEGQDQKTARTE-----LGKRLP 930
Cdd:cd05936 363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGvpdPYSGEAVK--AFVVLKEGASLTEEeiiafCREQLA 440
|
490 500
....*....|....*....|....*..
gi 2040046167 931 AYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05936 441 GYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1502-1984 |
3.46e-65 |
|
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: 231.98 E-value: 3.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV 1581
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 TEDMPTERLEWMLSDSNAVMLLQS----DRLESHMAGKRLFI---------EDIQLEAGISANN-----------PEQQG 1637
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSserlDLLHPALPGCHDLRtliivgdpaHASEGHPGEEPASwpkllalgdadPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 GPDSLAYIMYTSGSTGTPKGVMVEQRGVV-------RLVKNsdmafSPEDRILLTASLGFDAMTFEVFGPLLNGACLYIS 1710
Cdd:TIGR03098 161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVagaqsvaTYLEN-----RPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1711 DketYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQN--ERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPT 1788
Cdd:TIGR03098 236 D---YLLPRDVLKALEKHGITGLAAVPPLWAQLAQLDwpESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1789 EntTF-STCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPG- 1866
Cdd:TIGR03098 313 E--AFrSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGe 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1867 ----ERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGP-SGHKELLAYM-SLQ 1940
Cdd:TIGR03098 391 lhlpELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPtLGQAIVLVVTpPGG 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2040046167 1941 AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:TIGR03098 471 EELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
10-415 |
4.28e-65 |
|
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: 228.35 E-value: 4.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 10 IYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLKERQSRLQ 89
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 90 FVDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGK 169
Cdd:cd19547 81 LLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 170 EQLPDFEPVHPFSKYIKWLMRQDRK--EAEAFWKTRLIDVKqtaslPKTSSSSKGKLEQMAFTLSKEQTEGLRKLALQA- 246
Cdd:cd19547 161 GREPQLSPCRPYRDYVRWIRARTAQseESERFWREYLRDLT-----PSPFSTAPADREGEFDTVVHEFPEQLTRLVNEAa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 247 ---GATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPESFLT-LVSHLQQESLK 322
Cdd:cd19547 236 rgyGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTgLLETIHRDLAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 323 AEAYSYYPLYDIQA----QSMLKHELFDHIVVFENIPaqreiESLNQADAFDFTVDDFDMDEVTNYGCSIKIIPGSSLYI 398
Cdd:cd19547 316 TAAHGHVPLAQIKSwasgERLSGGRVFDNLVAFENYP-----EDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAF 390
|
410
....*....|....*..
gi 2040046167 399 RINFDIGLYDPAMMKKI 415
Cdd:cd19547 391 HFNYDTTHFTRAQVDRF 407
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1506-1984 |
4.25e-64 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 230.00 E-value: 4.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1506 LFEYQAAKTPHAPAVIY-----DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLP 1580
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1581 VTEDMPTERLEWMLSDSNAVMLLQSDrlESHMAGKRLFIEDIQLEAGISANNPEQ-----------------------QG 1637
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITAD--GGLRGGKVIDLKEKVDEALEELPSLEHvivvgrtgadvpmegdldwdellAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 GPDSL----------AYIMYTSGSTGTPKGVMVEQRGV-VRLVKNSDMAF--SPEDRILLTASLGFdaMTFE---VFGPL 1701
Cdd:COG0365 172 ASAEFepeptdaddpLFILYTSGTTGKPKGVVHTHGGYlVHAATTAKYVLdlKPGDVFWCTADIGW--ATGHsyiVYGPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1702 LNGACLYISD-KETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFS--DLSRL-ILG--GEALSPNHVNRVRNT 1775
Cdd:COG0365 250 LNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkyDLSSLrLLGsaGEPLNPEVWEWWYEA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1776 --APdlaLWNGYGPTE-NTTFSTCFRIEHEYKHSIpiGRPIANSTAYIVNSRGRLQPMGVIGELCVGGD--GLARGYFGR 1850
Cdd:COG0365 330 vgVP---IVDGWGQTEtGGIFISNLPGLPVKPGSM--GKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWND 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1851 PELTKEKFvpnpFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGH 1930
Cdd:COG0365 405 PERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRG 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1931 KELLAYMSLQAEMN-----IEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:COG0365 481 QVVKAFVVLKPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1063-1466 |
5.35e-64 |
|
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: 225.60 E-value: 5.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1063 PVSSAQKRMYVLQQ-LEDGGVgYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSF-ETGADGEpvQRIHDDVPFQL- 1139
Cdd:cd20483 3 PMSTFQRRLWFLHNfLEDKTF-LNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYfEGDDFGE--QQVLDDPSFHLi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1140 -MEL-------AAAEDFVR-----PFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELY----ASR 1202
Cdd:cd20483 80 vIDLseaadpeAALDQLVRnlrrqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1203 ---TLHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLE-LP-ADNARPAVRSFAGDHVSFSLDADTSSGLY 1277
Cdd:cd20483 160 dlaTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKlLPfAKAERPPVKDYERSTVEATLDKELLARMK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1278 KIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETAL 1357
Cdd:cd20483 240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1358 EAYEHQDYPFEELVDRLDVVRDMSRNPLFDVMFALQnMERESLTLH--DLHLTTIAHDAHKvSKFDMTLYAAEEDQETIR 1435
Cdd:cd20483 320 EAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-VHGKFPEYDtgDFKFTDYDHYDIP-TACDIALEAEEDPDGGLD 397
|
410 420 430
....*....|....*....|....*....|.
gi 2040046167 1436 FDVEFNTDIYQKQTIKKWLSYYIHILHHVIE 1466
Cdd:cd20483 398 LRLEFSTTLYDSADMERFLDNFVTFLTSVIR 428
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1515-1984 |
1.63e-63 |
|
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: 224.66 E-value: 1.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYD----RQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERL 1590
Cdd:cd17654 1 PDRPALIIDqttsDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 EWMLSDSNAVMLLQSDRLEShmagKRLFIEDIQLEAGISAnnpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK 1670
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELDN----APLSFTPEHRHFNIRT--------DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1671 NSDMAF--SPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFI-QQNGITTLWLTSSLFNQLSEQN 1747
Cdd:cd17654 149 HFRSLFniTSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1748 ERTF-----SDLSRLILGGEALSPNHVNRV-RNTAPDLALWNGYGPTENTTFSTCFRIEHEyKHSIPIGRPIANSTAYIV 1821
Cdd:cd17654 229 IKSTvlsatSSLRVLALGGEPFPSLVILSSwRGKGNRTRIFNIYGITEVSCWALAYKVPEE-DSPVQLGSPLLGTVIEVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1822 NSRGRLQPmgviGELCVGGdgLARGYFGRPELTkekfvpnpfTPGERMYRTGDLARwLKDGTIDYIGRMDDQVKIRGYRI 1901
Cdd:cd17654 308 DQNGSEGT----GQVFLGG--LNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1902 ELGEIEAALRQIDGVKEAAVIVrtgpSGHKELLAYMSLQAEMNIEKvRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:cd17654 372 NLDLIQQVIESCLGVESCAVTL----SDQQRLIAFIVGESSSSRIH-KELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDK 446
|
...
gi 2040046167 1982 RAL 1984
Cdd:cd17654 447 SEL 449
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
464-959 |
2.46e-62 |
|
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: 223.51 E-value: 2.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL 543
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGARLLVTG--------PGLSVSGFSGETLEVN-LSSLRTEPAENEPVC---AHTDGG------- 604
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSserldllhPALPGCHDLRTLIIVGdPAHASEGHPGEEPASwpkLLALGDadpphpv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 605 ---SLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASM----YLLP 677
Cdd:TIGR03098 161 idsDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhdYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 678 QGwekdpalMTEAFTNEGVTTAHFIPAMansfldQVEMETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIH 757
Cdd:TIGR03098 241 RD-------VLKALEKHGITGLAAVPPL------WAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 758 GYGPTEAtvdaafFRYDHEKDRERMRLP--IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERF 835
Cdd:TIGR03098 308 MYGLTEA------FRSTYLPPEEVDRRPdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 836 LDDP-----FYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEET 907
Cdd:TIGR03098 382 RPLPpfpgeLHLPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDptlGQAI 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 908 ELYAYIEGQ---DQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALPA 959
Cdd:TIGR03098 462 VLVVTPPGGeelDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
11-430 |
6.43e-62 |
|
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: 219.20 E-value: 6.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 11 YPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAkPRQVVLKER-QSRLQ 89
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGR-YEQVVLDKTvRFRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 90 FVDISHLDEtaKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGK 169
Cdd:cd19066 81 IIDLRNLAD--PEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 170 EQLPDFEPVHPFSKYIKWLMRQDRKEAE----AFWKTRLIDVKQTASLPK---TSSSSKGKLEQMAFTLSKEQTEGLRKL 242
Cdd:cd19066 159 QKPTLPPPVGSYADYAAWLEKQLESEAAqadlAYWTSYLHGLPPPLPLPKakrPSQVASYEVLTLEFFLRSEETKRLREV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 243 ALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDleDVEKMVGLFINTIPVRVK-SGPESFLTLVSHLQQESL 321
Cdd:cd19066 239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDtSPDATFPELLKRTKEQSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 322 KAEAYS--YYPLYDIQAQSML---KHELFDHIVVFENIPAQREIESLNQADAFDFTVddfdmDEVTNYGCSIKIIPGSS- 395
Cdd:cd19066 317 EAIEHQrvPFIELVRHLGVVPeapKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTS-----SEGTVFDLDLEASEDPDg 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 2040046167 396 -LYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADP 430
Cdd:cd19066 392 dLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
10-430 |
1.33e-61 |
|
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: 217.56 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 10 IYPLSFMQEGMLFHSLldQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKP-RQVVLKErqSRL 88
Cdd:cd19542 1 IYPCTPMQEGMLLSQL--RSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQVVLKS--LDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 89 QFVDISHLDETAKEtfVDQFEHDDKkkgfDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKalg 168
Cdd:cd19542 77 PIEEVETDEDSLDA--LTRDLLDDP----TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 169 kEQLPDfePVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVkqTASLPKTSSSSKGKLEQMAFTLSKEQTegLRKLALQAGA 248
Cdd:cd19542 148 -GQLLP--PAPPFSDYISYLQSQSQEESLQYWRKYLQGA--SPCAFPSLSPKRPAERSLSSTRRSLAK--LEAFCASLGV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 249 TLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPE-SFLTLVSHLQQESLKAEAYS 327
Cdd:cd19542 221 TLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDwTVLDLLRQLQQQYLRSLPHQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 328 YYPLYDIQAQSMLKH--ELFDHIVVFENIPAQREIESlnqADAFDFTVDDFDMDevTNYGCSIKIIP-GSSLYIRINFDI 404
Cdd:cd19542 301 HLSLREIQRALGLWPsgTLFNTLVSYQNFEASPESEL---SGSSVFELSAAEDP--TEYPVAVEVEPsGDSLKVSLAYST 375
|
410 420
....*....|....*....|....*.
gi 2040046167 405 GLYDPAMMKKIELYLRHIIGSVIADP 430
Cdd:cd19542 376 SVLSEEQAEELLEQFDDILEALLANP 401
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1525-1987 |
2.71e-61 |
|
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: 220.47 E-value: 2.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLq 1604
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 sdrleshmagkrlFIEDiqleAGISAnnpeqqgGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRI 1682
Cdd:cd17647 98 -------------VIRA----AGVVV-------GPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFnlSENDKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1683 LLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLILGGE 1762
Cdd:cd17647 154 TMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1763 ALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIE---------HEYKHSIPIGRPIANSTAYIVNSRGRLQPMGV- 1832
Cdd:cd17647 234 ILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPsrssdptflKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIg 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1833 -IGELCVGGDGLARGYFGRPELTKEKFVPNPFT----------------------PGERMYRTGDLARWLKDGTIDYIGR 1889
Cdd:cd17647 314 eVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlgPRDRLYRTGDLGRYLPNGDCECCGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1890 MDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMN------------------------- 1944
Cdd:cd17647 394 ADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPddesfaqedvpkevstdpivkglig 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2040046167 1945 ----IEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEP 1987
Cdd:cd17647 474 yrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
490-960 |
5.56e-61 |
|
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: 219.70 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVT--G 567
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVirA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 568 PGLSVSGFSGETLEvnlsslrtepaenepvcahtdggslayviYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDV 647
Cdd:cd17647 102 AGVVVGPDSNPTLS-----------------------------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 648 IVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVemeteekrTSLAKT 727
Cdd:cd17647 153 FTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQA--------TTPFPK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 728 LKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFF----RYDHEKDRERMR--LPIGKPVPGARLYILDSE 801
Cdd:cd17647 225 LHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFevpsRSSDPTFLKNLKdvMPAGRGMLNVQLLVVNRN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 802 KAVQ--PIGVAGELYIAGAGVARGYLNRPELTEERFLDD--------------------PFYRG--ERMYQTGDLARWLP 857
Cdd:cd17647 305 DRTQicGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGprDRLYRTGDLGRYLP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 858 DGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVRE-AAVVARTEGEETELYAYIEGQDQKTA--------------- 921
Cdd:cd17647 385 NGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnITLVRRDKDEEPTLVSYIVPRFDKPDdesfaqedvpkevst 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 922 -----------------RTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALPAP 960
Cdd:cd17647 465 dpivkgligyrklikdiREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
489-952 |
7.94e-60 |
|
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: 215.15 E-value: 7.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP 568
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 G--------------------LSVSGFSGETLEVNLSSLRTEPAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQ 628
Cdd:cd05911 91 DglekvkeaakelgpkdkiivLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGMQRQFPLTE--DDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGwekDPALMTEAFTNEGVTTAHFIPAMA 706
Cdd:cd05911 171 LIANLSQVQTFLYGNDgsNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKF---DSELFLDLIEKYKITFLYLVPPIA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 707 NSFLdqvemeteeKRTSLAK----TLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVdAAFFRYDHEKDRERm 782
Cdd:cd05911 248 AALA---------KSPLLDKydlsSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGG-ILTVNPDGDDKPGS- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 783 rlpIGKPVPGARLYILDSE-KAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTV 861
Cdd:cd05911 317 ---VGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLH------TGDIGYFDEDGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 862 EWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL-YAYIEGQDQKTArTElgKRLPAYMMPS---- 936
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELpRAYVVRKPGEKL-TE--KEVKDYVAKKvasy 464
|
490 500
....*....|....*....|...
gi 2040046167 937 -------SFIEmrEWPVTPSGKL 952
Cdd:cd05911 465 kqlrggvVFVD--EIPKSASGKI 485
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
477-957 |
8.40e-58 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 208.09 E-value: 8.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRF----SGGILTY----RELDQYTNQLairlKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:cd17654 1 PDRPALIIdqttSDTTVSYadlaEKISNLSNFL----RKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVTGpGLSVSGFSGETLEVNLSSLRTepaenepvcahtdGGSLAYVIYTSGSTGTPKGVAVEHRQ 628
Cdd:cd17654 77 EQRSLTVMKKCHVSYLLQN-KELDNAPLSFTPEHRHFNIRT-------------DECLAYVIHTSGTTGTPKIVAVPHKC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEA-FTNEGVTTAHFIPAMAN 707
Cdd:cd17654 143 ILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADIlFKRHRITVLQATPTLFR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 708 SFLDQVEMETEEKRTSlakTLKRVFAGGEALAPQTAARFAR-SLPETAVIHGYGPTEATVDAAFFRYdhekDRERMRLPI 786
Cdd:cd17654 223 RFGSQSIKSTVLSATS---SLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITEVSCWALAYKV----PEEDSPVQL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 787 GKPVPGARLYILDSEKAVQPIGVAGELyIAGAGVARGYLNRPELTeerflddpfyrgerMYQTGDLARwLPDGTVEWLGR 866
Cdd:cd17654 296 GSPLLGTVIEVRDQNGSEGTGQVFLGG-LNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 867 MDGQVKIRGYRIEPGEVEAALRQIDGVrEAAVVARTEGEetELYAYIEGQD-----QKTARTELgkrLPAYMMPSSFIEM 941
Cdd:cd17654 360 KDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQQ--RLIAFIVGESsssriHKELQLTL---LSSHAIPDTFVQI 433
|
490
....*....|....*.
gi 2040046167 942 REWPVTPSGKLDRKAL 957
Cdd:cd17654 434 DKLPLTSHGKVDKSEL 449
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
471-954 |
9.05e-58 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 207.46 E-value: 9.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 471 RRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEE 550
Cdd:cd17631 3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 551 RLRYMLADSGARLLVtgpglsvsgfsgetlevnlsslrtepaenepvcahtdgGSLAYVIYTSGSTGTPKGVAVEHRQ-- 628
Cdd:cd17631 83 EVAYILADSGAKVLF--------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNll 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGMQrqFPLTEDDV-IVLKSSFSfdasIWQLFWWMIP----GASMYLLPqgwEKDPALMTEAFTNEGVTTAHFIP 703
Cdd:cd17631 125 WNAVNALAA--LDLGPDDVlLVVAPLFH----IGGLGVFTLPtllrGGTVVILR---KFDPETVLDLIERHRVTSFFLVP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 704 AMANSFLDQVEMEteekRTSLAkTLKRVFAGGEALAPQTAARFARSlpETAVIHGYGPTEATVDAAFFRYDHEkdRERMR 783
Cdd:cd17631 196 TMIQALLQHPRFA----TTDLS-SLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSPEDH--RRKLG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 784 lPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPDGTVEW 863
Cdd:cd17631 267 -SAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFH-------TGDLGRLDEDGYLYI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 864 LGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVAR------------------TEGEETELYAYiegqdqktarteL 925
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVpdekwgeavvavvvprpgAELDEDELIAH------------C 406
|
490 500
....*....|....*....|....*....
gi 2040046167 926 GKRLPAYMMPSSFIEMREWPVTPSGKLDR 954
Cdd:cd17631 407 RERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1061-1467 |
1.89e-57 |
|
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: 206.07 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1061 TYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETgADGEPVQRIHDDVPFQL- 1139
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTE-EEGEPYQWIDPYTPVPIr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1140 ----------MELAAA---EDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELY------- 1199
Cdd:cd19533 80 hidlsgdpdpEGAAQQwmqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallkgr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1200 --ASRTLHPLRiqykDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLELpADNARPAVRSFAGDHVSFSLDadTSSGLY 1277
Cdd:cd19533 160 paPPAPFGSFL----DLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSL-ARRAPGRSLAFLRRTAELPPE--LTRTLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1278 KIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETAL 1357
Cdd:cd19533 233 EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1358 EAYEHQDYPFEELvdRLDVVRDMSRNPLFDVMFALQNMEREsLTLHDLHLTTIAHDAHKVSKFDMTLYaAEEDQETIRFD 1437
Cdd:cd19533 313 SLLRHQRYRYEDL--RRDLGLTGELHPLFGPTVNYMPFDYG-LDFGGVVGLTHNLSSGPTNDLSIFVY-DRDDESGLRID 388
|
410 420 430
....*....|....*....|....*....|
gi 2040046167 1438 VEFNTDIYQKQTIKKWLSYYIHILHHVIEH 1467
Cdd:cd19533 389 FDANPALYSGEDLARHQERLLRLLEEAAAD 418
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1511-1981 |
1.92e-57 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 206.69 E-value: 1.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERL 1590
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 EWMLSDSNAVMLLqsdrleshmagkrlfiediqleagisannpeqqggpDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK 1670
Cdd:cd17631 85 AYILADSGAKVLF------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1671 NSDMAF--SPEDRILLTASL-GFDAMTFEVFGPLLNGACLYISDKetyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQN 1747
Cdd:cd17631 129 NALAALdlGPDDVLLVVAPLfHIGGLGVFTLPTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPTMIQALLQHP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1748 ERTFSDLSRL--ILGGEALSPNHVNRvRNTAPDLALWNGYGPTEnTTFSTCF-RIEHEYKHSIPIGRPIANSTAYIVNSR 1824
Cdd:cd17631 206 RFATTDLSSLraVIYGGAPMPERLLR-ALQARGVKFVQGYGMTE-TSPGVTFlSPEDHRRKLGSAGRPVFFVEVRIVDPD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1825 GRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELG 1904
Cdd:cd17631 284 GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1905 EIEAALRQIDGVKEAAVI----VRTGPSGHkellAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGK 1978
Cdd:cd17631 357 EVEDVLYEHPAVAEVAVIgvpdEKWGEAVV----AVVVPRpgAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGK 432
|
...
gi 2040046167 1979 LDR 1981
Cdd:cd17631 433 ILK 435
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
2387-2540 |
5.50e-57 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 194.80 E-value: 5.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2387 ELGLAVKTVKDTLGRIPDKGMGYGILKYLTSSENKTiQFGKAPEIGFNYLGQFNDTERQQKFSFSGLASGKDITPTWQRE 2466
Cdd:TIGR01720 1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKL-AASPQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 2467 QTLEMSAMVRQNQLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHCAHKQETEKTVSDFSSQSLTAEDLDDI 2540
Cdd:TIGR01720 80 YALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1503-1984 |
7.51e-57 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 205.87 E-value: 7.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1503 ISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVT 1582
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1583 EDMPTERLEWMLSDSNAVMLLQSDRLESHMAGKRLFIEDIQLEagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQ 1662
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALT-------------PEDVAVLQYTSGTTGVPKGAMLTH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1663 RGVVRLVKNSDMAFSP---EDRILLTAsLGFdamtFEVFG-------PLLNGACLYISdkETYLDSDRLKTfIQQNGITT 1732
Cdd:cd05936 148 RNLVANALQIKAWLEDlleGDDVVLAA-LPL----FHVFGltvalllPLALGATIVLI--PRFRPIGVLKE-IRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1733 LWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRnTAPDLALWNGYGPTEnTTFSTCFRIEHEYKHSIPI 1809
Cdd:cd05936 220 FPGVPTMYIALLNAPEFKKRDFSSLrlcISGGAPLPVEVAERFE-ELTGVPIVEGYGLTE-TSPVVAVNPLDGPRKPGSI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1810 GRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGR 1889
Cdd:cd05936 298 GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVDR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1890 MDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSGhKELLAYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHLV 1966
Cdd:cd05936 371 KKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSG-EAVKAFVVLKEGASLteEEIIAFCREQLAGYKVPRQVE 449
|
490
....*....|....*...
gi 2040046167 1967 ELAALPLTQNGKLDRRAL 1984
Cdd:cd05936 450 FRDELPKSAVGKILRREL 467
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
466-957 |
2.94e-55 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 203.80 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 466 HSFFTRRAALSPNLPAVRFSG-----GILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAY 540
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 541 VPLDPDYPEERLRYMLADSGARLLVTGPGLSVSGFSGETLEV------NLSSLRT-----------------------EP 591
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKvdealeELPSLEHvivvgrtgadvpmegdldwdellAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 592 AENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSG-MQRQFPLTEDDVIvlkssFSFdASI-WQ--LFWWM 667
Cdd:COG0365 172 ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGDVF-----WCT-ADIgWAtgHSYIV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 668 IP----GASMYLLPQGWE-KDPALMTEAFTNEGVTTAHFIPAMANSFLDqvEMETEEKRTSLaKTLKRVFAGGEALAPQT 742
Cdd:COG0365 246 YGpllnGATVVLYEGRPDfPDPGRLWELIEKYGVTVFFTAPTAIRALMK--AGDEPLKKYDL-SSLRLLGSAGEPLNPEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 743 AARFARSL--PetaVIHGYGPTEAT-VDAAFFRYDHEKdrermrlP--IGKPVPGARLYILDSEKAVQPIGVAGELYIAG 817
Cdd:COG0365 323 WEWWYEAVgvP---IVDGWGQTETGgIFISNLPGLPVK-------PgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 818 A--GVARGYLNRPELTEERFLDDpfYRGerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVRE 895
Cdd:COG0365 393 PwpGMFRGYWNDPERYRETYFGR--FPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAE 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 896 AAVVART-EGEETELYAYI---EGQD-----QKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:COG0365 469 AAVVGVPdEIRGQVVKAFVvlkPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1495-1987 |
3.40e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 202.72 E-value: 3.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1495 QDYPKheTISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKA 1574
Cdd:PRK06187 2 QDYPL--TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1575 GGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDRLESHMAG---------KRLFIED-------------IQLEAGISANN 1632
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAilpqlptvrTVIVEGDgpaaplapevgeyEELLAAASDTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1633 PEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVV--RLVKNSDMAFSPEDRILLTASLgFDAMTFEV-FGPLLNGACLYI 1709
Cdd:PRK06187 160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1710 SDKetyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNR--VRNTAPdlaLWNG 1784
Cdd:PRK06187 239 PRR---FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLrlvIYGGAALPPALLREfkEKFGID---LVQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1785 YGPTENTTFSTCFRIEHEYKHSIPI----GRPIANSTAYIVNSRGRLQPM--GVIGELCVGGDGLARGYFGRPELTKEKF 1858
Cdd:PRK06187 313 YGMTETSPVVSVLPPEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1859 VPNpftpgerMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI----VRTGpsghKELL 1934
Cdd:PRK06187 393 DGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgvpdEKWG----ERPV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1935 AYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEP 1987
Cdd:PRK06187 462 AVVVLKPGATLdaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1060-1388 |
5.32e-55 |
|
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: 199.63 E-value: 5.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1060 DTYPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFeTGADGEPVQRIHDD----- 1134
Cdd:cd19546 3 DEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF-PGDGGDVHQRILDAdaarp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1135 ----VPFQLMELAA--AEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASR------ 1202
Cdd:cd19546 82 elpvVPATEEELPAllADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrap 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1203 TLHPLRIQYKDYAVWQQAFKQGE-----AYNRQEAYWLKQLDGELPVLELPADNARPAVRSFAGDHVSFSLDADTSSGLY 1277
Cdd:cd19546 162 ERAPLPLQFADYALWERELLAGEddrdsLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1278 KIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHK-DLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETA 1356
Cdd:cd19546 242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321
|
330 340 350
....*....|....*....|....*....|..
gi 2040046167 1357 LEAYEHQDYPFEELVDRLDVVRDMSRNPLFDV 1388
Cdd:cd19546 322 REARRHQDVPFERLAELLALPPSADRHPVFQV 353
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
464-957 |
1.90e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 200.41 E-value: 1.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL 543
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGARLLVTGPGLS-----------------VSGFSGETLEVNLSS-----LRTEPAENEPVcaHT 601
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEFVpllaailpqlptvrtviVEGDGPAAPLAPEVGeyeelLAAASDTFDFP--DI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 602 DGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVlkssfsfdaSIWQLFW---WMIPGASMYL--- 675
Cdd:PRK06187 165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYL---------VIVPMFHvhaWGLPYLALMAgak 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 676 --LPQgwEKDPALMTEAFTNEGVTTAHFIPAMANsFLDQVEMETEEKRTSlaktLKRVFAGGEALAPQTAARFARSLPET 753
Cdd:PRK06187 236 qvIPR--RFDPENLLDLIETERVTFFFAVPTIWQ-MLLKAPRAYFVDFSS----LRLVIYGGAALPPALLREFKEKFGID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 754 aVIHGYGPTEATVDAAFFRY-DHEKDRERMRLPIGKPVPGARLYILDSEKAVQP--IGVAGELYIAGAGVARGYLNRPEL 830
Cdd:PRK06187 309 -LVQGYGMTETSPVVSVLPPeDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 831 TEERFLDDpFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA---RTEGEET 907
Cdd:PRK06187 388 TAETIDGG-WLH------TGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGvpdEKWGERP 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 908 elYAYIEGQDQKTA-----RTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK06187 461 --VAVVVLKPGATLdakelRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1502-1986 |
3.33e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 196.66 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV 1581
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 TEDMPTERLEWMLSDSNAVMLLQSDRL--ESHMAGKRL-------FIEDIQLEAG----------ISANNPEQQG---GP 1639
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFlgVDYSATTRLpalehvvICETEEDDPHtekmktftdfLAAGDPAERApevDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1640 DSLAYIMYTSGSTGTPKGVMVEQRGVVRLVknSDMA----FSPEDRILltASLGFdamtFEVFG-------PLLNGACLY 1708
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGAMLTHRQLLSNA--ADWAeylgLTEGDRYL--AANPF----FHVFGykagvnaPLMRGATIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1709 ISDKetyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRNTAPDLALWNGY 1785
Cdd:PRK07656 238 PLPV---FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLrlaVTGAASMPVALLERFESELGVDIVLTGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1786 GPTENTTFSTCFRIEHEYKhSIP--IGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF 1863
Cdd:PRK07656 315 GLSEASGVTTFNRLDDDRK-TVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1864 tpgermYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI----VRTGPSGHkellAYMSL 1939
Cdd:PRK07656 394 ------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgvpdERLGEVGK----AYVVL 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2040046167 1940 Q--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK07656 464 KpgAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1525-1979 |
9.38e-53 |
|
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: 194.35 E-value: 9.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNA-VMLL 1603
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPkVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1604 QSDRLE-------------------SHMAGKRLFIEDIQLEAGISANN-PEQQG-GPDSLAYIMYTSGSTGTPKGVMVEQ 1662
Cdd:cd05911 89 DPDGLEkvkeaakelgpkdkiivldDKPDGVLSIEDLLSPTLGEEDEDlPPPLKdGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1663 RgvvRLVKNSDMA-------FSPEDRILltASLGFDAMT--FEVFGPLLNGACLYISDK---ETYLDSdrlktfIQQNGI 1730
Cdd:cd05911 169 R---NLIANLSQVqtflygnDGSNDVIL--GFLPLYHIYglFTTLASLLNGATVIIMPKfdsELFLDL------IEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1731 TTLWLTSSLFNQLSEQNERTFSDLS---RLILGGEALSPNHVNRVRNTAPDLALWNGYGPTEnTTFSTCFRIEHEYKHSi 1807
Cdd:cd05911 238 TFLYLVPPIAAALAKSPLLDKYDLSslrVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE-TGGILTVNPDGDDKPG- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1808 PIGRPIANSTAYIVNSRGR-LQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIdY 1886
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYL-Y 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1887 I-GRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSGhkEL-LAYMSLQAEMNI--EKVRSLLSQQLPGFmi 1961
Cdd:cd05911 389 IvDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIgIPDEVSG--ELpRAYVVRKPGEKLteKEVKDYVAKKVASY-- 464
|
490 500
....*....|....*....|..
gi 2040046167 1962 pAHL----VELAALPLTQNGKL 1979
Cdd:cd05911 465 -KQLrggvVFVDEIPKSASGKI 485
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1527-2370 |
9.72e-52 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 203.48 E-value: 9.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGVGSESVVALLTSrTPELAVGILGILKAG----GAYLP-VTEDMPTERLEWMLSDSNAVM 1601
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQARASFGDRAVLLFPS-GPDYVAAFFGCLYAGviavPAYPPeSARRHHQERLLSIIADAEPRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1602 LL----------QSDRLESHMAGKRLFIEdiQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVV---RL 1668
Cdd:PRK05691 120 LLtvadlrdsllQMEELAAANAPELLCVD--TLDPALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVaneQL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1669 VKNS-DMAFSPEDRILLTASLGFD-AMTFEVFGPLLNGA-CLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSE 1745
Cdd:PRK05691 198 IRHGfGIDLNPDDVIVSWLPLYHDmGLIGGLLQPIFSGVpCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1746 QNERtfSDLSRLIL--------GGEALSPNHVNRVRNT------APDlALWNGYGPTENTTFSTCFRieheYKHSIPIGR 1811
Cdd:PRK05691 278 RVSE--SALERLDLsrwrvaysGSEPIRQDSLERFAEKfaacgfDPD-SFFASYGLAEATLFVSGGR----RGQGIPALE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1812 PIANSTAY---------IVNSRGRLQPM----------------GVIGELCVGGDGLARGYFGRPELTKEKFVPNpftPG 1866
Cdd:PRK05691 351 LDAEALARnraepgtgsVLMSCGRSQPGhavlivdpqslevlgdNRVGEIWASGPSIAHGYWRNPEASAKTFVEH---DG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1867 ERMYRTGDLArWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAAL-RQIDGVKE---AAVIVRTGPSGHKELLAYMS---- 1938
Cdd:PRK05691 428 RTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVRKgrvAAFAVNHQGEEGIGIAAEISrsvq 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1939 --LQAEMNIEKVRSLLS---QQLPGFMIpahLVELAALPLTQNGKLDRRA---------------LPEPETTAINTAYAP 1998
Cdd:PRK05691 507 kiLPPQALIKSIRQAVAeacQEAPSVVL---LLNPGALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAAS 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1999 PrNQLEERLAVIWQEVLGVEKVGIEDSFFELGGDSIKALQVSARLG-RFDLKITAGDLFRHPTIKEAAPLIRK------- 2070
Cdd:PRK05691 584 G-DELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRdELGIDLNLRQLFEAPTLAAFSAAVARqlaggga 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2071 TERNIDQRPIEGEVPWTPVQR--WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIID-DGGQLQ 2147
Cdd:PRK05691 663 AQAAIARLPRGQALPQSLAQNrlWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYErDGVALQ 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2148 QFNRGIHGELYSLNIRDLSKTAQWEKLIEDEVADLQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLE 2226
Cdd:PRK05691 743 RIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHqLLVTLHHIVADGWSLNILLD 822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2227 DLSAAYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRTVEKEKAAL--LPCEKP------HSAADNIRK 2298
Cdd:PRK05691 823 EFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVleLATDHPrsarqaHSAARYSLR 902
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 2299 TeSFTLSEEdthvlIHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRdhtlPELDISRTVGWF 2370
Cdd:PRK05691 903 V-DASLSEA-----LRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR----PRLETQGLVGFF 964
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
508-957 |
1.05e-51 |
|
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: 190.73 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 508 KGVAKESVVGVLADRSPEMVIAVlAVLKAGGA----YVPLDPDYPEERLRYMLADSGARLLV--------TGPGLSVSGF 575
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSF-AVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLadagaadrLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 576 SGETLEVNLSSLRTEPAENEPVcAHTDggsLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFS 655
Cdd:cd05922 93 PGTVLDADGIRAARASAPAHEV-SHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 656 FDASIWQLFWWMIPGASM-----YLLPQGwekdpalMTEAFTNEGVTTAHFIPAMAnSFLDQVEMETEEkrtslAKTLKR 730
Cdd:cd05922 169 YDYGLSVLNTHLLRGATLvltndGVLDDA-------FWEDLREHGATGLAGVPSTY-AMLTRLGFDPAK-----LPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 731 VFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRermrlP--IGKPVPGARLYILDSEKAVQPIG 808
Cdd:cd05922 236 LTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEK-----PgsIGLAIPGGEFEILDDDGTPTPPG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 809 VAGELYIAGAGVARGYLNRP-ELTEERflddpfyRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAAL 887
Cdd:cd05922 311 EPGEIVHRGPNVMKGYWNDPpYRRKEG-------RGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 888 RQIDGVREAAVVA--RTEGEETELYAY-IEGQDQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05922 384 RSIGLIIEAAAVGlpDPLGEKLALFVTaPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
480-957 |
1.54e-51 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 189.42 E-value: 1.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 480 PAVRFSGGILTYRELDQYTNQLAIRL-KKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLAD 558
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 559 SGARLLVTGpglsvsgfsgetlevnlsslrtepaenepvcahtdggslAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQR 638
Cdd:cd05941 83 SEPSLVLDP---------------------------------------ALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 639 QFPLTEDDVI------------VLKSSfsfdASIWQlfwwmipGASMYLLPqgwEKDPALMTEAFTNEGVTTAHFIPAMA 706
Cdd:cd05941 124 AWRWTEDDVLlhvlplhhvhglVNALL----CPLFA-------GASVEFLP---KFDPKEVAISRLMPSITVFMGVPTIY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 707 NSFLDQVEMETEEKRTSLAKTLKRV---FAGGEALAPQTAARFArSLPETAVIHGYGPTEaTVDAAFFRYDHEkdrermR 783
Cdd:cd05941 190 TRLLQYYEAHFTDPQFARAAAAERLrlmVSGSAALPVPTLEEWE-AITGHTLLERYGMTE-IGMALSNPLDGE------R 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 784 LP--IGKPVPGARLYILDSEKA-VQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGT 860
Cdd:cd05941 262 RPgtVGMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFK------TGDLGVVDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 861 VEWLGRM-DGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETE-LYAYIEGQDQKTA------RTELGKRLPAY 932
Cdd:cd05941 336 YWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGErVVAVVVLRAGAAAlsleelKEWAKQRLAPY 415
|
490 500
....*....|....*....|....*
gi 2040046167 933 MMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05941 416 KRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
489-957 |
1.61e-51 |
|
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: 190.99 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP 568
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 GLSVS---------------GFSGETLEVNLSSLRTEPAENEPVCA----HTDGGSLAYVIYTSGSTGTPKGVAVEHRQA 629
Cdd:cd05926 95 GELGPasraasklglailelALDVGVLIRAPSAESLSNLLADKKNAksegVPLPDDLALILHTSGTTGRPKGVPLTHRNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 630 AAFLSGMQRQFPLTEDD--------------VIVLKSSF----------SFDASiwqLFW-WMIpgasmyllpqgwekdp 684
Cdd:cd05926 175 AASATNITNTYKLTPDDrtlvvmplfhvhglVASLLSTLaaggsvvlppRFSAS---TFWpDVR---------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 685 almteaftNEGVTTAHFIPAMANSFLDqveMETEEKRTSLAKtLKRVFAGGEALAPQTAARFARSLpETAVIHGYGPTEA 764
Cdd:cd05926 236 --------DYNATWYTAVPTIHQILLN---RPEPNPESPPPK-LRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 765 TVDAAFFRYDHEKDRermrlP--IGKPVpGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYR 842
Cdd:cd05926 303 AHQMTSNPLPPGPRK-----PgsVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 843 germyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA---RTEGEetELYAYI---EGQ 916
Cdd:cd05926 377 ------TGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGvpdEKYGE--EVAAAVvlrEGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2040046167 917 --DQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05926 449 svTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
480-957 |
2.41e-51 |
|
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: 188.82 E-value: 2.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 480 PAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADS 559
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 560 GARLLVTgpglsvsgfsgetlevnlsslrtepaenepvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQ 639
Cdd:cd05919 82 EARLVVT-----------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMARE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 640 -FPLTEDDVIVLKS----SFSFDASIWqlFWWMIpGASMYLLPqGWeKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVE 714
Cdd:cd05919 127 aLGLTPGDRVFSSAkmffGYGLGNSLW--FPLAV-GASAVLNP-GW-PTAERVLATLARFRPTVLYGVPTFYANLLDSCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 715 METEEKRTslaktLKRVFAGGEALAPQTAARFARSLPeTAVIHGYGPTE-------ATVDAAffRYDhekdrermrlPIG 787
Cdd:cd05919 202 GSPDALRS-----LRLCVSAGEALPRGLGERWMEHFG-GPILDGIGATEvghiflsNRPGAW--RLG----------STG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 788 KPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRM 867
Cdd:cd05919 264 RPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 868 DGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEE-TELYAYI-----EGQDQKTAR---TELGKRLPAYMMPSSF 938
Cdd:cd05919 337 DDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGlSRLTAFVvlkspAAPQESLARdihRHLLERLSAHKVPRRI 416
|
490
....*....|....*....
gi 2040046167 939 IEMREWPVTPSGKLDRKAL 957
Cdd:cd05919 417 AFVDELPRTATGKLQRFKL 435
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
13-251 |
3.68e-51 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 181.78 E-value: 3.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 13 LSFMQEGMLFhslLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQSRLQFVD 92
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 93 ISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKEQL 172
Cdd:COG4908 77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 173 PDFEPV-HPFSKYIKWLMRQ----DRKEAEAFWKTRLIDVKQTASLP---KTSSSSKGKLEQMAFTLSKEQTEGLRKLAL 244
Cdd:COG4908 157 PPLPELpIQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPtdrPRPAVQTFRGATLSFTLPAELTEALKALAK 236
|
....*..
gi 2040046167 245 QAGATLN 251
Cdd:COG4908 237 AHGATVN 243
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
11-327 |
4.92e-51 |
|
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: 187.56 E-value: 4.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 11 YPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQSRLQF 90
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVD-GEPVQVILPPLPLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 91 VDISHLDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKE 170
Cdd:cd19531 81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 171 QLPDFE--PVHpfskYI-------KWLMRQDRKEAEAFWKTRLIDVKQTASLP-----KTSSSSKGKLEqmAFTLSKEQT 236
Cdd:cd19531 161 RPSPLPplPIQ----YAdyavwqrEWLQGEVLERQLAYWREQLAGAPPVLELPtdrprPAVQSFRGARV--RFTLPAELT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 237 EGLRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRpsDLEDVEKMVGLFINTIPVRVK-SGPESFLTLVSH 315
Cdd:cd19531 235 AALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGR--NRAELEGLIGFFVNTLVLRTDlSGDPTFRELLAR 312
|
330
....*....|..
gi 2040046167 316 LQQESLkaEAYS 327
Cdd:cd19531 313 VRETAL--EAYA 322
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
489-957 |
2.79e-50 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 185.62 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGp 568
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 glsvsgfsgetlevnlsslrtepaENEPvcahtdggslAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI 648
Cdd:cd05972 80 ------------------------AEDP----------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 vlkssFSFDASIWQLFWW------MIPGASMYLLpQGWEKDPALMTEAFTNEGVTTAhFIPAMANSFLDQVEMETEEKrt 722
Cdd:cd05972 126 -----WNIADPGWAKGAWssffgpWLLGATVFVY-EGPRFDAERILELLERYGVTSF-CGPPTAYRMLIKQDLSSYKF-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 723 slaKTLKRVFAGGEALAPQTAARFARSLPETavIH-GYGPTEATVDAAFFRYDHEKdrermrlP--IGKPVPGARLYILD 799
Cdd:cd05972 197 ---SHLRLVVSAGEPLNPEVIEWWRAATGLP--IRdGYGQTETGLTVGNFPDMPVK-------PgsMGRPTPGYDVAIID 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 800 SEKAVQPIGVAGELYI--AGAGVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYR 877
Cdd:cd05972 265 DDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 878 IEPGEVEAALRQIDGVREAAVVARTEGEETELY-AYIEGQDQKTARTEL--------GKRLPAYMMPSSfIEMR-EWPVT 947
Cdd:cd05972 338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVLTSGYEPSEELaeelqghvKKVLAPYKYPRE-IEFVeELPKT 416
|
490
....*....|
gi 2040046167 948 PSGKLDRKAL 957
Cdd:cd05972 417 ISGKIRRVEL 426
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
10-430 |
1.08e-49 |
|
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: 182.88 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 10 IYPLSFMQEGMLFHSLldQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLKErqsrlq 89
Cdd:cd19545 1 IYPCTPLQEGLMALTA--RQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 90 fVDISHLDETAKETFVDQfehdDKKKGFDLqTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKAlgk 169
Cdd:cd19545 73 -SPISWTESTSLDEYLEE----DRAAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 170 eqlPDFEPVHPFSKYIKWLMRQDRKEAEAFWKTRLIDVKQT----ASLPKTSSSSKGKLEQMAFTLSKeqteglrklaLQ 245
Cdd:cd19545 144 ---EPVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfppLPSSRYQPRPDATLEHSISLPSS----------AS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 246 AGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPE-SFLTLVSHLQQESLKAE 324
Cdd:cd19545 211 SGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEqSVEDFLQTVQKDLLDMI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 325 AYSYYPLYDIQAQSMLKHE--LFDHIVVFEniPAqreiESLNQADAFDFTVDDFDMDEV--TNYGCSIKI-IPGSSLYIR 399
Cdd:cd19545 291 PFEHTGLQNIRRLGPDARAacNFQTLLVVQ--PA----LPSSTSESLELGIEEESEDLEdfSSYGLTLECqLSGSGLRVR 364
|
410 420 430
....*....|....*....|....*....|.
gi 2040046167 400 INFDIGLYDPAMMKKIELYLRHIIGSVIADP 430
Cdd:cd19545 365 ARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
490-957 |
1.09e-49 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 184.17 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGpg 569
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 570 lsvsgfsgetlevnlsslrtepAENEPvcahtdggslAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQ---RQFPLTEDd 646
Cdd:cd05971 86 ----------------------GSDDP----------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfNLFPRDGD- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 647 vivlkssfsfdasiwqLFW------WmIPGASMYLLP-------------QGWEKDPALmtEAFTNEGVTTAhFIPAMAN 707
Cdd:cd05971 133 ----------------LYWtpadwaW-IGGLLDVLLPslyfgvpvlahrmTKFDPKAAL--DLMSRYGVTTA-FLPPTAL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 708 SFLDQVEMETEEKRTSLaktlKRVFAGGEALAPQTAArFARSLPETAVIHGYGPTEATV----DAAFFRYDHEKdrermr 783
Cdd:cd05971 193 KMMRQQGEQLKHAQVKL----RAIATGGESLGEELLG-WAREQFGVEVNEFYGQTECNLvignCSALFPIKPGS------ 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 784 lpIGKPVPGARLYILDSEKAVQPIGVAGELYI--AGAGVARGYLNRPELTEERFLDDPFyrgermyQTGDLARWLPDGTV 861
Cdd:cd05971 262 --MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVelPDPVAFLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 862 EWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELY-AYI-----EGQDQKTAR--TELGK-RLPAY 932
Cdd:cd05971 333 WYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVkAFVvlnpgETPSDALAReiQELVKtRLAAH 412
|
490 500
....*....|....*....|....*
gi 2040046167 933 MMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05971 413 EYPREIEFVNELPRTATGKIRRREL 437
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2083-2514 |
4.33e-49 |
|
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: 181.84 E-value: 4.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2083 EVPWTPVQR--WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQFNRGiHGELYSL 2160
Cdd:cd19066 1 KIPLSPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLD-KTVRFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2161 NIRDLSKTAQWEKLIEDEVADLQRSIH-LQTGPLLKAGLFNTM-SGTYLFLTIHHLVVDGVSWRILLEDLSAAYSQAAAG 2238
Cdd:cd19066 80 EIIDLRNLADPEARLLELIDQIQQTIYdLERGPLVRVALFRLAdERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2239 QPVqLPRKTDSYQYFANRLAEYAESSKVIREQSYWRTVEKE--KAALLPCEKPHSA-ADNIRKTESFTLSEEDTHVLIHk 2315
Cdd:cd19066 160 KPT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGlpPPLPLPKAKRPSQvASYEVLTLEFFLRSEETKRLRE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2316 VNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRdhtlPELDISRTVGWFTTIYPVLIDLHHAAegELGLAVKTV 2395
Cdd:cd19066 238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDTSPDA--TFPELLKRT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2396 KDTLGRIPDKGMGYGILKYLTSSENKTIQFGKAPEIGFNYLGQFNDTERQQKFSFSGLasgkDITPTWQREQTLEMSAMV 2475
Cdd:cd19066 312 KEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTP----VYTSSEGTVFDLDLEASE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2040046167 2476 RQN-QLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKHC 2514
Cdd:cd19066 388 DPDgDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1062-1467 |
7.32e-49 |
|
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: 180.58 E-value: 7.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1062 YPVSSAQKrMYVLQQLEDGGVGYNmPAALKLTGPLDRARLDEVFRQLIRRHESLRTSF-ETGADGEPVQRIHDDVPFQLM 1140
Cdd:cd19542 2 YPCTPMQE-GMLLSQLRSPGLYFN-HFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSLDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1141 ELAAAEDFVRPFR--------LQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRTLHPlRIQYK 1212
Cdd:cd19542 80 EVETDEDSLDALTrdllddptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1213 DYAVWQQAFKQGEAYNrqeaYWLKQLDGELPVLElpadnarPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLL 1292
Cdd:cd19542 159 DYISYLQSQSQEESLQ----YWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1293 AAYSTLLARLSGQEDIIIGSPIAGR--AHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPFEEL 1370
Cdd:cd19542 228 AAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1371 VDRLdvvRDMSRNPLFDVMFALQNMERESLTLHDLHLTTIAHDAHKVSKFDMTLyAAEEDQETIRFDVEFNTDIYQKQTI 1450
Cdd:cd19542 308 QRAL---GLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAV-EVEPSGDSLKVSLAYSTSVLSEEQA 383
|
410
....*....|....*..
gi 2040046167 1451 KKWLSYYIHILHHVIEH 1467
Cdd:cd19542 384 EELLEQFDDILEALLAN 400
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1085-1450 |
9.95e-49 |
|
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: 180.07 E-value: 9.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1085 NMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGaDGEPVQRIHDDVP-FQLMELAAAEDFV-RPFRLQEAPLFRA 1162
Cdd:cd19537 25 NVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPR-DGGLRRSYSSSPPrVQRVDTLDVWKEInRPFDLEREDPIRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1163 ALVKeaeeSHLLLVdMHHIISDGVSVGTLIREFSELYASRTLHPLRIQYKDYAVWQQafkqgEAYNRQEAYWLKQLDGeL 1242
Cdd:cd19537 104 FISP----DTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSR-----PASPEDLDFWSEYLSG-L 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1243 PVLELPAdnaRPAVRSFAGDHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHKDL 1322
Cdd:cd19537 173 PLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEED 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1323 ESVIGMFVNTLAIR---TRPVENKCfSDFLREVRETALEAYEHQdYPFEELVDRLDVVRDMSRNPLFDVM--FALQNMER 1397
Cdd:cd19537 250 METVGLFLEPLPIRirfPSSSDASA-ADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVS 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1398 ESLTLHDL-HLTTIAhdahKVSKFDMTLYAAEEDQETIRFDVEFNTDIYQKQTI 1450
Cdd:cd19537 328 LALPIPGVePLYTWA----EGAKFPLMFEFTALSDDSLLLRLEYDTDCFSEEEI 377
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1526-1979 |
3.57e-48 |
|
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: 179.50 E-value: 3.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1526 TLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVtedMPTER---LEWMLSDSNAVML 1602
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFReheLAFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 LQSDRLESHmagkrlfiediqleagisanNPEQQggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKN--SDMAFSPED 1680
Cdd:cd05903 78 VVPERFRQF--------------------DPAAM--PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQyaERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1681 RILLTASLG-FDAMTFEVFGPLLNGACLYISDKetyLDSDRLKTFIQQNGITTLW----LTSSLFNQLSEQNERTfSDLS 1755
Cdd:cd05903 136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMMgatpFLTDLLNAVEEAGEPL-SRLR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1756 RLILGGeALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGE 1835
Cdd:cd05903 212 TFVCGG-ATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1836 LCVGGDGLARGYFGRPELTKEKFvpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDqVKIR-GYRIELGEIEAALRQID 1914
Cdd:cd05903 291 LLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLGHP 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 1915 GVKEAAVIV----RTGpsghKELLAYMSLQ--AEMNIEKVRSLLS-QQLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:cd05903 363 GVIEAAVVAlpdeRLG----ERACAVVVTKsgALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1523-1984 |
6.12e-48 |
|
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: 179.17 E-value: 6.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1523 DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAvml 1602
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 lqsdrleshmagkRLFIEDiqleagisannpeqqgGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFS----P 1678
Cdd:cd05971 80 -------------SALVTD----------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNlfprD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1679 EDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSS---LFNQLSEQNERTFSDLS 1755
Cdd:cd05971 131 GDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkMMRQQGEQLKHAQVKLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1756 RLILGGEALSPNHVNRVRNTAPDlALWNGYGPTE-NTTFSTCFRIEHEYKHSipIGRPIANSTAYIVNSRGRLQPMGVIG 1834
Cdd:cd05971 211 AIATGGESLGEELLGWAREQFGV-EVNEFYGQTEcNLVIGNCSALFPIKPGS--MGKPIPGHRVAIVDDNGTPLPPGEVG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1835 ELCVG-GDGLA-RGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQ 1912
Cdd:cd05971 288 EIAVElPDPVAfLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLK 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 1913 IDGVKEAAVIVRTGPSGHKELLAYMSLQA-----EMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05971 361 HPAVLMAAVVGIPDPIRGEIVKAFVVLNPgetpsDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1535-1984 |
1.39e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 178.40 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1535 RANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGA----YLPVTEDMPTERLEWMLSD-SNAVMLLQS---D 1606
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADaGGRIVLADAgaaD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 RLESHMAGKRLFIEDIQLEA--GISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRgvvRLVKNSD-----MAFSPE 1679
Cdd:cd05922 82 RLRDALPASPDPGTVLDADGirAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQ---NLLANARsiaeyLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1680 DRILLTASLGFDAMTFEVFGPLLNGACLYISdkETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQnerTFSD-----L 1754
Cdd:cd05922 159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRL---GFDPaklpsL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1755 SRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIG 1834
Cdd:cd05922 234 RYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1835 ELCVGGDGLARGYFGRPEltkekFVPNPFTPGERMYrTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQID 1914
Cdd:cd05922 314 EIVHRGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1915 GVKEAAVIVRTGPSGHKeLLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05922 388 LIIEAAAVGLPDPLGEK-LALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
489-957 |
2.34e-47 |
|
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: 176.90 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP 568
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 GLSvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI 648
Cdd:cd05935 82 ELD---------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 VLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALmtEAFTNEGVTTAHFIPAMANSFLDQVEMETEEkrtslAKTL 728
Cdd:cd05935 129 LACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETAL--ELIEKYKVTFWTNIPTMLVDLLATPEFKTRD-----LSSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 729 KrVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAaffrydHEKDRERMRLP-IGKPVPGARLYILDSEK-AVQP 806
Cdd:cd05935 202 K-VLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQT------HTNPPLRPKLQcLGIP*FGVDARVIDIETgRELP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 807 IGVAGELYIAGAGVARGYLNRPELTEERFLDDpfyRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAA 886
Cdd:cd05935 275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 887 LRQIDGVREAAVVARTE---GEETElyAYI---EGQDQKTARTELGK----RLPAYMMPSSFIEMREWPVTPSGKLDRKA 956
Cdd:cd05935 352 LYKHPAI*EVCVISVPDervGEEVK--AFIvlrPEYRGKVTEEDIIEwareQMAAYKYPREVEFVDELPRSASGKILWRL 429
|
.
gi 2040046167 957 L 957
Cdd:cd05935 430 L 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1518-1984 |
3.97e-47 |
|
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: 176.50 E-value: 3.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1518 PAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGG-AYLPVTEDMPTErLEWMLSD 1596
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAiAVVINPLLHPDD-YAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1597 SNAVMLLQSDrleshmagkrlfiediqleagisannpeqqggpDSLAYIMYTSGSTGTPKGVMVEQR---GVVRLVKNSD 1673
Cdd:cd05919 81 CEARLVVTSA---------------------------------DDIAYLLYSSGTTGPPKGVMHAHRdplLFADAMAREA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1674 MAFSPEDRILLTASLGFD-AMTFEVFGPLLNGACLYISDkeTYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQ---NER 1749
Cdd:cd05919 128 LGLTPGDRVFSSAKMFFGyGLGNSLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDScagSPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1750 TFSDLSRLILGGEALSPNHVNRVRNTApDLALWNGYGPTENTTFSTCFRI-EHEYKHSipiGRPIANSTAYIVNSRGRLQ 1828
Cdd:cd05919 206 ALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGHIFLSNRPgAWRLGST---GRPVPGYEIRLVDEEGHTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1829 PMGVIGELCVGGDGLARGYFGRPELTKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEA 1908
Cdd:cd05919 282 PPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1909 ALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMN-----IEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRA 1983
Cdd:cd05919 355 LIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFK 434
|
.
gi 2040046167 1984 L 1984
Cdd:cd05919 435 L 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
490-958 |
4.10e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 175.94 E-value: 4.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTgpg 569
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 570 lsvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDV-I 648
Cdd:cd05934 82 -----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVyL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 VLKSSFSFDASIWQLFWWMIPGASMYLLPQgwekdpaLMTEAFTNE----GVTTAHFIPAMANSFLDQVEMETEEkrtsl 724
Cdd:cd05934 127 TVLPLFHINAQAVSVLAALSVGATLVLLPR-------FSASRFWSDvrryGATVTNYLGAMLSYLLAQPPSPDDR----- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 725 AKTLKrvFAGGEALAPQTAARFARSLpETAVIHGYGPTEATVDAAffrydHEKDRERMRLPIGKPVPGARLYILDSEKAV 804
Cdd:cd05934 195 AHRLR--AAYGAPNPPELHEEFEERF-GVRLLEGYGMTETIVGVI-----GPRDEPRRPGSIGRPAPGYEVRIVDDDGQE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 805 QPIGVAGELYIAGA---GVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPG 881
Cdd:cd05934 267 LPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 882 EVEAALRQIDGVREAAVVA-RTEGEETELYAYIEGQDQKTARTE-----LGKRLPAYMMPsSFIEMR-EWPVTPSGKLDR 954
Cdd:cd05934 340 EVERAILRHPAVREAAVVAvPDEVGEDEVKAVVVLRPGETLDPEelfafCEGQLAYFKVP-RYIRFVdDLPKTPTEKVAK 418
|
....
gi 2040046167 955 KALP 958
Cdd:cd05934 419 AQLR 422
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1515-1986 |
7.85e-47 |
|
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: 177.12 E-value: 7.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQT--LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEW 1592
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1593 MLSDSNA-VMLLQSDRLESHMAGK---RLFIEDIQLEAGISANNP-----------------EQQGGPDSLAYIMYTSGS 1651
Cdd:cd05926 81 YLADLGSkLVLTPKGELGPASRAAsklGLAILELALDVGVLIRAPsaeslsnlladkknaksEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1652 TGTPKGVMVEQRGVVRLVKN--SDMAFSPEDRILLTASLgfdamtFEVFG-------PLLNGACLYISDKEtyldsdRLK 1722
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNitNTYKLTPDDRTLVVMPL------FHVHGlvasllsTLAAGGSVVLPPRF------SAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1723 TF---IQQNGITtlWLT------SSLFNQLSEQNERTFSDLsRLIL-GGEALSPNHVNRVRNT--APDLalwNGYGPTEN 1790
Cdd:cd05926 229 TFwpdVRDYNAT--WYTavptihQILLNRPEPNPESPPPKL-RFIRsCSASLPPAVLEALEATfgAPVL---EAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1791 TTFSTCFRIEHEYKHSIPIGRPIANSTAyIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermY 1870
Cdd:cd05926 303 AHQMTSNPLPPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------F 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1871 RTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIEKV 1948
Cdd:cd05926 376 RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRegASVTEEEL 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 2040046167 1949 RSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:cd05926 456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1527-1984 |
1.64e-46 |
|
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: 174.45 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSD 1606
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 rleshmagkrlfiediqleagisannpeqqggpDSLAYIMYTSGSTGTPKGV----------MVEQRGVVRLvKNSDMAF 1676
Cdd:cd05972 81 ---------------------------------EDPALIYFTSGTTGLPKGVlhthsyplghIPTAAYWLGL-RPDDIHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1677 SPEDRILLTASLgfdamtFEVFGPLLNGACLyISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQN--ERTFSDL 1754
Cdd:cd05972 127 NIADPGWAKGAW------SSFFGPWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDlsSYKFSHL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1755 SRLILGGEALSPNHVNRVRNTApDLALWNGYGPTENT-TFSTCfrieheykHSIPI-----GRPIANSTAYIVNSRGRLQ 1828
Cdd:cd05972 200 RLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGlTVGNF--------PDMPVkpgsmGRPTPGYDVAIIDDDGREL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1829 PMGVIGELCV--GGDGLARGYFGRPELTKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEI 1906
Cdd:cd05972 271 PPGEEGDIAIklPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1907 EAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ---------AEMNIEKVRSLLSQqlpgFMIPAHLVELAALPLTQNG 1977
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTsgyepseelAEELQGHVKKVLAP----YKYPREIEFVEELPKTISG 419
|
....*..
gi 2040046167 1978 KLDRRAL 1984
Cdd:cd05972 420 KIRRVEL 426
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
2087-2312 |
5.09e-46 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 166.75 E-value: 5.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2087 TPVQRWFLAqHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQFNRGIHG-ELYSLNIRDL 2165
Cdd:COG4908 2 SPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADlPLEVVDLSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2166 SKTAQWEKLIEDEVADLQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQPVQLP 2244
Cdd:COG4908 81 PEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPPLP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 2245 RKTDSYQYFANRLAEYAESSKVIREQSYWRTVEKE--KAALLPCEKPHSAADNIR-KTESFTLSEEDTHVL 2312
Cdd:COG4908 161 ELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGapPVLELPTDRPRPAVQTFRgATLSFTLPAELTEAL 231
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
10-318 |
5.41e-46 |
|
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: 172.62 E-value: 5.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 10 IYPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLkeRQSRLQ 89
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVW--RQAELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 90 fvdISHLDETAKETFVDQFEH--DDKKKGFDLQTDPLMRVSILK-RAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIykA 166
Cdd:cd19544 79 ---VEELTLDPGDDALAQLRArfDPRRYRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAI--L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 167 LGKE-QLPdfEPVhPFSKYI-KWLMRQDRKEAEAFWKTRLIDVKQTaSLP------KTSSSSkgkLEQMAFTLSKEQTEG 238
Cdd:cd19544 154 AGRAaALP--PPV-PYRNFVaQARLGASQAEHEAFFREMLGDVDEP-TAPfglldvQGDGSD---ITEARLALDAELAQR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 239 LRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEDVEKMVGLFINTIPVRVKSGPESFLTLVSHLQQ 318
Cdd:cd19544 227 LRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGGRSVREAVRQTHA 306
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1528-1984 |
1.96e-45 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 171.48 E-value: 1.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1528 TYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDR 1607
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1608 LEshmagKRLFIEDI--QLEA-GISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNS--DMAFSPEDRI 1682
Cdd:TIGR01923 81 LE-----EKDFQADSldRIEAaGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSkeNLGFTEDDNW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1683 LLTASL----GFDAmtfeVFGPLLNGACLYISDKetylDSDrLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSdLSRLI 1758
Cdd:TIGR01923 156 LLSLPLyhisGLSI----LFRWLIEGATLRIVDK----FNQ-LLEMIANERVTHISLVPTQLNRLLDEGGHNEN-LRKIL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1759 LGGEALSPNHVNRVRNTApdLALWNGYGPTENTTFSTCFRIEhEYKHSIPIGRPIANstayiVNSRGRLQPMGVIGELCV 1838
Cdd:TIGR01923 226 LGGSAIPAPLIEEAQQYG--LPIYLSYGMTETCSQVTTATPE-MLHARPDVGRPLAG-----REIKIKVDNKEGHGEIMV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1839 GGDGLARGYFGRPELtkekfvpNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKE 1918
Cdd:TIGR01923 298 KGANLMKGYLYQGEL-------TPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQE 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 1919 AAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:TIGR01923 371 AVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
473-957 |
2.70e-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: 172.94 E-value: 2.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERL 552
Cdd:cd05959 14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 553 RYMLADSGARLLVTGPGL-SVSGFSGETLEVNLSSL-RTEPAENEP--------VCAHTDGG--------SLAYVIYTSG 614
Cdd:cd05959 94 AYYLEDSRARVVVVSGELaPVLAAALTKSEHTLVVLiVSGGAGPEAgalllaelVAAEAEQLkpaathadDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 615 STGTPKGVAVEHRQAAAFLSGMQRQ-FPLTEDDVIVLKSSFSFDASIWQ-LFWWMIPGASMYLLPQgwEKDPALMTEAFT 692
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMPE--RPTPAAVFKRIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 693 NEGVTTAHFIPAMANSFL-DQVEMETEEKRTSLAktlkrvFAGGEALAPQTAARFaRSLPETAVIHGYGPTEATvdaaff 771
Cdd:cd05959 252 RYRPTVFFGVPTLYAAMLaAPNLPSRDLSSLRLC------VSAGEALPAEVGERW-KARFGLDILDGIGSTEML------ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 772 rydH--EKDRERMRLP--IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLddpfyrGErMY 847
Cdd:cd05959 319 ---HifLSNRPGRVRYgtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 848 QTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV-ARTEGEETELYAYI----EGQDQKTAR 922
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgVEDEDGLTKPKAFVvlrpGYEDSEALE 468
|
490 500 510
....*....|....*....|....*....|....*....
gi 2040046167 923 TELGK----RLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05959 469 EELKEfvkdRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
489-952 |
2.62e-44 |
|
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: 168.33 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTgP 568
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 GLsvsgFSGetlevnlsslrTEPAEnepvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI 648
Cdd:cd05903 81 ER----FRQ-----------FDPAA--------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 VLKSSFS-FDASIWQLFWWMIPGASMYLLpQGWEKDPALmtEAFTNEGVTTAhfipAMANSFLDQVeMETEEKRTSLAKT 727
Cdd:cd05903 138 LVASPMAhQTGFVYGFTLPLLLGAPVVLQ-DIWDPDKAL--ALMREHGVTFM----MGATPFLTDL-LNAVEEAGEPLSR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 728 LKRVFAGGeALAPQTAARFARSLPETAVIHGYGPTEatVDAAFFRYDHEKDRERMRLPiGKPVPGARLYILDSEKAVQPI 807
Cdd:cd05903 210 LRTFVCGG-ATVPRSLARRAAELLGAKVCSAYGSTE--CPGAVTSITPAPEDRRLYTD-GRPLPGVEIKVVDDTGATLAP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 808 GVAGELYIAGAGVARGYLNRPELTeERFLDDPFYRgermyqTGDLARWLPDGtveWLgRMDGQVK---IR-GYRIEPGEV 883
Cdd:cd05903 286 GVEGELLSRGPSVFLGYLDRPDLT-ADAAPEGWFR------TGDLARLDEDG---YL-RITGRSKdiiIRgGENIPVLEV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 884 EAALRQIDGVREAAVVA----RTeGEET---------------ELYAYIEGQdqktartelgkRLPAYMMPSSFIEMREW 944
Cdd:cd05903 355 EDLLLGHPGVIEAAVVAlpdeRL-GERAcavvvtksgalltfdELVAYLDRQ-----------GVAKQYWPERLVHVDDL 422
|
....*...
gi 2040046167 945 PVTPSGKL 952
Cdd:cd05903 423 PRTPSGKV 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
471-957 |
2.89e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 170.09 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 471 RRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEE 550
Cdd:PRK07656 13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 551 RLRYMLADSGARLLvtgpgLSVSGFSG--ETLEVNLSSLR------TEPAENEPVCAHT-----------------DGGS 605
Cdd:PRK07656 93 EAAYILARGDAKAL-----FVLGLFLGvdYSATTRLPALEhvviceTEEDDPHTEKMKTftdflaagdpaerapevDPDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 LAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDD--VIVLK--SSFSFDASIWQLFwwmIPGASMYLLPQgwe 681
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDryLAANPffHVFGYKAGVNAPL---MRGATILPLPV--- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 682 KDPALMTEAFTNEGVTTAHFIPAMANSFLdQVEMETEEKRTSLaktlkRVFA-GGEALAPQTAARFARSLPETAVIHGYG 760
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLL-QHPDRSAEDLSSL-----RLAVtGAASMPVALLERFESELGVDIVLTGYG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 761 PTEATVDAAFFRYDheKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFlddpf 840
Cdd:PRK07656 316 LSEASGVTTFNRLD--DDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI----- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 841 yRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV----ARTeGE----------- 905
Cdd:PRK07656 389 -DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgvpdERL-GEvgkayvvlkpg 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 906 ----ETELYAYiegqdqktARTELGKrlpaYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK07656 467 aeltEEELIAY--------CREHLAK----YKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1518-1984 |
3.06e-44 |
|
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: 169.86 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1518 PAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDS 1597
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1598 NAVMLLQS----DRLESHMA-------------GKRLFIEDIQLEAGISANNPEQQGG---PDSLAYIMYTSGSTGTPKG 1657
Cdd:cd05959 101 RARVVVVSgelaPVLAAALTksehtlvvlivsgGAGPEAGALLLAELVAAEAEQLKPAathADDPAFWLYSSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1658 VMVEQ---RGVVRLVKNSDMAFSPEDRILLTASLGF-----DAMTFevfgPLLNGA-CLYISDKETyldSDRLKTFIQQN 1728
Cdd:cd05959 181 VVHLHadiYWTAELYARNVLGIREDDVCFSAAKLFFayglgNSLTF----PLSVGAtTVLMPERPT---PAAVFKRIRRY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1729 GITTLWLTSSLFNQLSEQNERTFSDLSRLIL---GGEALsPNHVNRVRNTAPDLALWNGYGPTENT-TFSTCFRIEHEYK 1804
Cdd:cd05959 254 RPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLcvsAGEAL-PAEVGERWKARFGLDILDGIGSTEMLhIFLSNRPGRVRYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1805 HSipiGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVpnpftpGErMYRTGDLARWLKDGTI 1884
Cdd:cd05959 333 TT---GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDDGFY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1885 DYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ-----AEMNIEKVRSLLSQQLPGF 1959
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpgyedSEALEEELKEFVKDRLAPY 482
|
490 500
....*....|....*....|....*
gi 2040046167 1960 MIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05959 483 KYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1527-1984 |
1.77e-42 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 163.06 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSD 1606
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 RLESHMAgkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFS--PEDRILL 1684
Cdd:cd05969 81 ELYERTD-------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDlhPDDIYWC 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1685 TASLGFDAMTFE-VFGPLLNGACLYISDKEtyLDSDRLKTFIQQNGItTLWLTS----SLFNQLSEQNERTFsDLS--RL 1757
Cdd:cd05969 136 TADPGWVTGTVYgIWAPWLNGVTNVVYEGR--FDAESWYGIIERVKV-TVWYTAptaiRMLMKEGDELARKY-DLSslRF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1758 IL-GGEALSPNHVnRVRNTAPDLALWNGYGPTENTTFSTCfriehEYKhSIPI-----GRPIANSTAYIVNSRGRLQPMG 1831
Cdd:cd05969 212 IHsVGEPLNPEAI-RWGMEVFGVPIHDTWWQTETGSIMIA-----NYP-CMPIkpgsmGKPLPGVKAAVVDENGNELPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1832 VIGELCVGGD--GLARGYFGRPELTKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAA 1909
Cdd:cd05969 285 TKGILALKPGwpSMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1910 LRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ-----AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05969 358 LMEHPAVAEAGVIGKPDPLRGEIIKAFISLKegfepSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1062-1394 |
2.48e-42 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 161.85 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1062 YPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRIHD--DVPFQL 1139
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRqaQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1140 MELAA------------AEDFVRPFRLQEAPLFRAALVKEAEESHLLLV-DMHHIISDGVSVGTLIREFSELYASRTLH- 1205
Cdd:cd19536 82 LDLTPleeqldplraykEETKIRRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNQLLEYk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1206 ----PLRIQYKDYAVWQQAFKQGEAYnrqEAYWLKQLDG-ELPVLELP-----ADNARPAVrsfagdhVSFSLDADTSSG 1275
Cdd:cd19536 162 plslPPAQPYRDFVAHERASIQQAAS---ERYWREYLAGaTLATLPALseavgGGPEQDSE-------LLVSVPLPVRSR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1276 lyKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGR--AHKDLESVIGMFVNTLAIRTRPVENKcFSDFLREVR 1353
Cdd:cd19536 232 --SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTLSEET-VEDLLKRAQ 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2040046167 1354 ETALEAYEHQDYPFEelvdrlDVVRDMSRNPLFDVMFALQN 1394
Cdd:cd19536 309 EQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRH 343
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
471-956 |
5.12e-42 |
|
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: 164.33 E-value: 5.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 471 RRAALSPNLPAVRF---SGGI---LTYRELDQYTNQLAIRLKKKGVAKESVVgVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:cd05931 1 RRAAARPDRPAYTFlddEGGReetLTYAELDRRARAIAARLQAVGKPGDRVL-LLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPE---ERLRYMLADSGARLLVTGPGLSVS---GFSGETLEVNLSSLRTEPAENEP----VCAHTDGGSLAYVIYTSG 614
Cdd:cd05931 80 PPTPGrhaERLAAILADAGPRVVLTTAAALAAvraFAASRPAAGTPRLLVVDLLPDTSaadwPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 615 STGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVlkssfsfdasiwqlFW------------WMIP---GASMYLL-PQ 678
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVV--------------SWlplyhdmgliggLLTPlysGGPSVLMsPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 679 GWEKDPALMTEAFTNEGVTTAhfipAMANSFLDQ-VEMETEEKRTSLA-KTLKRVFAGGEALAPQT----AARFARS-LP 751
Cdd:cd05931 226 AFLRRPLRWLRLISRYRATIS----AAPNFAYDLcVRRVRDEDLEGLDlSSWRVALNGAEPVRPATlrrfAEAFAPFgFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 752 ETAVIHGYGPTEATVDAAF-----------FRYDHEKDRERMRLP----------IGKPVPGARLYILDSE-KAVQPIGV 809
Cdd:cd05931 302 PEAFRPSYGLAEATLFVSGgppgtgpvvlrVDRDALAGRAVAVAAddpaarelvsCGRPLPDQEVRIVDPEtGRELPDGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 810 AGELYIAGAGVARGYLNRPELTEERFL------DDPFYRgermyqTGDLARwLPDGTVEWLGRMDGQVKIRGYRIEPGEV 883
Cdd:cd05931 382 VGEIWVRGPSVASGYWGRPEATAETFGalaatdEGGWLR------TGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 884 EAALRQIDGV-REAAVVA----RTEGEETELYAYIEGQDQKTARTELGKRLPAY------MMPSS--FIEMREWPVTPSG 950
Cdd:cd05931 455 EATAEEAHPAlRPGCVAAfsvpDDGEERLVVVAEVERGADPADLAAIAAAIRAAvarehgVAPADvvLVRPGSIPRTSSG 534
|
....*.
gi 2040046167 951 KLDRKA 956
Cdd:cd05931 535 KIQRRA 540
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
454-899 |
2.70e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 162.96 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 454 QTEPAAPLAPTLHSFFTRRAALSPNLPAVRF-SGGI---LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIA 529
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 530 VLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTG---------------PGLSV------SGFSGETLEVNLSSLR 588
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdqeqldkllevrdelPSLRHivvldpRGLRDDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 589 ------TEPAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVlksSF-----SFd 657
Cdd:COG1022 162 algrevADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL---SFlplahVF- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 658 ASIWQLFWWMIpGASMYLLPqgwekDPALMTEAFtneGVTTAHFIPA-------MANSFLDQVEMETEEKR--------- 721
Cdd:COG1022 238 ERTVSYYALAA-GATVAFAE-----SPDTLAEDL---REVKPTFMLAvprvwekVYAGIQAKAEEAGGLKRklfrwalav 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 722 -------------TSLAKTLKRVFA---------------------GGEALAPQTaARFARSL--PetaVIHGYGPTEAT 765
Cdd:COG1022 309 grryararlagksPSLLLRLKHALAdklvfsklrealggrlrfavsGGAALGPEL-ARFFRALgiP---VLEGYGLTETS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 766 VDAAFFRYDHEKdrermrlP--IGKPVPGARLyildseKavqpIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRg 843
Cdd:COG1022 385 PVITVNRPGDNR-------IgtVGPPLPGVEV------K----IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLH- 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 844 ermyqTGDLARWLPDGTVEWLGR------MDGqvkirGYRIEPGEVEAALRQIDGVREAAVV 899
Cdd:COG1022 447 -----TGDIGELDEDGFLRITGRkkdlivTSG-----GKNVAPQPIENALKASPLIEQAVVV 498
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
480-960 |
5.20e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 159.38 E-value: 5.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 480 PAVRFSGGILTYRELDQYTNQLAIRlkkkgVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADS 559
Cdd:PRK07787 17 DAVRIGGRVLSRSDLAGAATAVAER-----VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 560 GARLLVTGPGLSVSGFsgETLEVNLSSlRTEPAENEPvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQ 639
Cdd:PRK07787 92 GAQAWLGPAPDDPAGL--PHVPVRLHA-RSWHRYPEP-----DPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 640 FPLTEDDVIV--LKssfsfdasiwqLFwwMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHF--------IPAMANSF 709
Cdd:PRK07787 164 WQWTADDVLVhgLP-----------LF--HVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQALSeggtlyfgVPTVWSRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 710 LDQVEmeteekrtsLAKTLK--RVFAGGEALAPQTAARFARSLPETAVIHGYGPTEA--TVDAaffRYDHEkdrermRLP 785
Cdd:PRK07787 231 AADPE---------AARALRgaRLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETliTLST---RADGE------RRP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 786 --IGKPVPGARLYILDSEKAVQPIGVA--GELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTV 861
Cdd:PRK07787 293 gwVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFR------TGDVAVVDPDGMH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 862 EWLGRMDGQ-VKIRGYRIEPGEVEAALRQIDGVREAAVVarteGEETE-----LYAYIEGQDQKTArTEL----GKRLPA 931
Cdd:PRK07787 367 RIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVV----GVPDDdlgqrIVAYVVGADDVAA-DELidfvAQQLSV 441
|
490 500 510
....*....|....*....|....*....|..
gi 2040046167 932 YMMPSsfiEMR---EWPVTPSGKLDRKALPAP 960
Cdd:PRK07787 442 HKRPR---EVRfvdALPRNAMGKVLKKQLLSE 470
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1516-1984 |
1.72e-40 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 157.07 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1516 HAPAVIYDRQTLTYRELNQRANRIAAALRANG-VGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLQsdrleshmagkrlfiediqleagisannpeqqggpdsLAYIMYTSGSTGTPKGVMVEQRGvvrLVKNSDM 1674
Cdd:cd05941 81 TDSEPSLVLD-------------------------------------PALILYTSGTTGRPKGVVLTHAN---LAANVRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1675 -----AFSPEDRILLTASLgfdamtFEVFG-------PLLNGACLYISDKetyLDSDRLKTFIQQNGITTLWLTSSLFNQ 1742
Cdd:cd05941 121 lvdawRWTEDDVLLHVLPL------HHVHGlvnallcPLFAGASVEFLPK---FDPKEVAISRLMPSITVFMGVPTIYTR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 LSEQNERTFSDLS----------RLILGGEALSPnhvnrvrntAPDLALWNG---------YGPTEnTTFSTCFRIEHEy 1803
Cdd:cd05941 192 LLQYYEAHFTDPQfaraaaaerlRLMVSGSAALP---------VPTLEEWEAitghtllerYGMTE-IGMALSNPLDGE- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1804 KHSIPIGRPIANSTAYIV-NSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDG 1882
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1883 TIDYIGRM-DDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAE---MNIEKVRSLLSQQLPG 1958
Cdd:cd05941 335 YYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaaaLSLEELKEWAKQRLAP 414
|
490 500
....*....|....*....|....*.
gi 2040046167 1959 FMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
455-950 |
1.87e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 159.52 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 455 TEPAAPLAPTLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVL 534
Cdd:PRK06164 2 PHDAAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 535 KAGGAYVPLDPDYPEERLRYMLADSGARLLVTGPGLSVSGFSGETLEVNLSSLRT------------------------- 589
Cdd:PRK06164 82 RLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPlraiavvddaadatpapapgarvql 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 590 -------EPAENEPVCAHTDGGSLAYViyTSGSTGTPKGVAveHRQAAAFLSGMQ--RQFPLTEDDVIVLKSSFSFDASI 660
Cdd:PRK06164 162 falpdpaPPAAAGERAADPDAGALLFT--TSGTTSGPKLVL--HRQATLLRHARAiaRAYGYDPGAVLLAALPFCGVFGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 661 WQLFWWMIPGASMYLLPQgweKDPALMTEAFTNEGVTTAHfipaMANSFLDQVeMETEEKRTSLAkTLKRVfaGGEALAP 740
Cdd:PRK06164 238 STLLGALAGGAPLVCEPV---FDAARTARALRRHRVTHTF----GNDEMLRRI-LDTAGERADFP-SARLF--GFASFAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 741 QTAARFARSLPETAVIHG-YGPTEatVDAAFFRYDHEKDRERMRLPIGKPV-PGARLYILDSEK-AVQPIGVAGELYIAG 817
Cdd:PRK06164 307 ALGELAALARARGVPLTGlYGSSE--VQALVALQPATDPVSVRIEGGGRPAsPEARVRARDPQDgALLPDGESGEIEIRA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 818 AGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAA 897
Cdd:PRK06164 385 PSLMRGYLDNPDATARALTDDGYFR------TGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 898 VVARTEGEETELYAYI-----EGQDQKTARTELGKRLPAYMMPSSFIEMREWPVTPSG 950
Cdd:PRK06164 459 VVGATRDGKTVPVAFViptdgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1502-1984 |
2.52e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 158.56 E-value: 2.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV 1581
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 TEDMPTERLEWMLSDSNAVMLLQSD----RLESHMAGKRL--FIEDIQL-----EAGISANNPEQQGGPDS--------- 1641
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLVDPalapTAEAALALLPVdtLILSLVLggreaPGGWLDFADWAEAGSVAepdveladd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1642 -LAYIMYTSGSTGTPKGVMVEQRGVVR-----LVknsDMAFSPEDRIL----LTASLGFDAMtfevFGP-LLNGACLYIS 1710
Cdd:PRK08316 172 dLAQILYTSGTESLPKGAMLTHRALIAeyvscIV---AGDMSADDIPLhalpLYHCAQLDVF----LGPyLYVGATNVIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1711 DKEtylDSDRLKTFIQQNGIT------TLW---LTSSLFNQlseqnertfSDLSRLILG--GEALSPNHV-NRVRNTAPD 1778
Cdd:PRK08316 245 DAP---DPELILRTIEAERITsffappTVWislLRHPDFDT---------RDLSSLRKGyyGASIMPVEVlKELRERLPG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1779 LALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKF 1858
Cdd:PRK08316 313 LRFYNCYGQTEIAPLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1859 VPNPFtpgermyRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMS 1938
Cdd:PRK08316 393 RGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVV 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2040046167 1939 LQAEMNI--EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK08316 466 PKAGATVteDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
488-957 |
2.59e-40 |
|
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: 158.98 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 488 ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD--PDYPE-----ERLRYMLADSG 560
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYDEpnarlRKLRHIWQLLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 561 ARLLVTGPGLsVSGFSGETLEVNLSSLRTEPAENEPVCA------HTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLS 634
Cdd:cd05906 119 SPVVLTDAEL-VAEFAGLETLSGLPGIRVLSIEELLDTAadhdlpQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 635 GMQRQFPLTEDDVIvlkssfsfdasiwqlFWWM----IPGASMYLL------------PQGWE-KDPALMTEAFTNEGVT 697
Cdd:cd05906 198 GKIQHNGLTPQDVF---------------LNWVpldhVGGLVELHLravylgcqqvhvPTEEIlADPLRWLDLIDRYRVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 698 TAhFIPAMANSFLDQVEMETEEKRTSLAkTLKRVFAGGEALAPQTAARFARSL-----PETAVIHGYGPTE----ATVDA 768
Cdd:cd05906 263 IT-WAPNFAFALLNDLLEEIEDGTWDLS-SLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPAFGMTEtcsgVIYSR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 769 AFFRYDHEKDRERMRLpiGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyq 848
Cdd:cd05906 341 SFPTYDHSQALEFVSL--GRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFR------ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 849 TGDLArWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVRE---AAVVARTEGEETELYA--YIEGQDQKTART 923
Cdd:cd05906 413 TGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAifFVPEYDLQDALS 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2040046167 924 ELGKRL-----------PAYMMPssfIEMREWPVTPSGKLDRKAL 957
Cdd:cd05906 492 ETLRAIrsvvsrevgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1492-1922 |
3.37e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 159.88 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1492 QTKQDYPKHETISRLFEYQAAKTPHAPAVIYDR----QTLTYRELNQRANRIAAALRANGVGSESVVALLtSRT-PELAV 1566
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAIL-SDNrPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1567 GILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLL-----QSDRLESHMAG-------------------KRLFIEDI 1622
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFvedqeQLDKLLEVRDElpslrhivvldprglrddpRLLSLDEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1623 qLEAGISANNPE------QQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSD--MAFSPEDRILL---------- 1684
Cdd:COG1022 161 -LALGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLerLPLGPGDRTLSflplahvfer 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1685 TASLGFdamtfevfgpLLNGACLYISDKETYLDSDrLKTF------------------IQQNGITTLWLTSSLFNQ---- 1742
Cdd:COG1022 240 TVSYYA----------LAAGATVAFAESPDTLAED-LREVkptfmlavprvwekvyagIQAKAEEAGGLKRKLFRWalav 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 -----LSEQNERTFSDLSRLIL------------------------GGEALSPnHVNRVRNTApDLALWNGYGPTENTTF 1793
Cdd:COG1022 309 grryaRARLAGKSPSLLLRLKHaladklvfsklrealggrlrfavsGGAALGP-ELARFFRAL-GIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1794 STCFRIEHEYKHSipIGRPIANSTAYIvnsrgrlqpmGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTG 1873
Cdd:COG1022 387 ITVNRPGDNRIGT--VGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTG 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1874 DLARWLKDGTIDYIGRMDDQVKIR-GYRIELGEIEAALRQIDGVKEAAVI 1922
Cdd:COG1022 449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
470-957 |
3.78e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 154.35 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 470 TRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPE 549
Cdd:PRK03640 9 KQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 550 ERLRYMLADSGARLLVTGPGLSVSGFSGEtlEVNLSSLRTEPAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVavEHRQA 629
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDFEAKLIPGI--SVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGV--IQTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 630 AAFLSGMQRQFPL--TEDD--VIVLK----SSFSFdasiwqLFWWMIPGASMYLLpqgwEK-DPALMTEAFTNEGVTTAH 700
Cdd:PRK03640 165 NHWWSAVGSALNLglTEDDcwLAAVPifhiSGLSI------LMRSVIYGMRVVLV----EKfDAEKINKLLQTGGVTIIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 701 FIPAMANSFLDQVEMET--EEKRTSLaktlkrvFAGGEALAPQTAARFARSLPetaVIHGYGPTE-----ATVDAAFfry 773
Cdd:PRK03640 235 VVSTMLQRLLERLGEGTypSSFRCML-------LGGGPAPKPLLEQCKEKGIP---VYQSYGMTEtasqiVTLSPED--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 774 dhekdrerMRLPI---GKPVPGARLYILDSEKAVQPiGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTG 850
Cdd:PRK03640 302 --------ALTKLgsaGKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWFK-------TG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 851 DLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVarteGEETEL-----YAYI---EGQDQKTAR 922
Cdd:PRK03640 366 DIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV----GVPDDKwgqvpVAFVvksGEVTEEELR 441
|
490 500 510
....*....|....*....|....*....|....*
gi 2040046167 923 TELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK03640 442 HFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
471-957 |
5.71e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 153.86 E-value: 5.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 471 RRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKK-GVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPE 549
Cdd:PRK06839 10 KRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 550 ERLRYMLADSGARLLVTGP-----GLSVSGFSGETLEVNLSSLRtEPAENEPVCAHTDGGSLAYVI-YTSGSTGTPKGVA 623
Cdd:PRK06839 90 NELIFQLKDSGTTVLFVEKtfqnmALSMQKVSYVQRVISITSLK-EIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 624 VEhrQAAAFLSGMQRQFP--LTEDDV-IVLKSSFSFDA-SIWQLFWWMIPGasMYLLPQGWEKDPALmtEAFTNEGVTTA 699
Cdd:PRK06839 169 LT--QENMFWNALNNTFAidLTMHDRsIVLLPLFHIGGiGLFAFPTLFAGG--VIIVPRKFEPTKAL--SMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 700 HFIPAMANSFLDQVEMETeekrTSLAKTlkRVFAGGEALAPQTAAR--FARSLPetaVIHGYGPTEaTVDAAFFRYdhEK 777
Cdd:PRK06839 243 MGVPTIHQALINCSKFET----TNLQSV--RWFYNGGAPCPEELMRefIDRGFL---FGQGFGMTE-TSPTVFMLS--EE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 778 DRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLP 857
Cdd:PRK06839 311 DARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC-------TGDLARVDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 858 DGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL-YAYIEGQD-----QKTARTELGKRLPA 931
Cdd:PRK06839 384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIpIAFIVKKSssvliEKDVIEHCRLFLAK 463
|
490 500
....*....|....*....|....*.
gi 2040046167 932 YMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK06839 464 YKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
459-957 |
5.74e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 155.58 E-value: 5.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 459 APLAPTLHSFftrrAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGG 538
Cdd:PRK06178 33 RPLTEYLRAW----ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 539 AYVPLDPDYPEERLRYMLADSGARLLVT-----------GPGLSVS---------------------GFSGETLEVN--- 583
Cdd:PRK06178 109 VHVPVSPLFREHELSYELNDAGAEVLLAldqlapvveqvRAETSLRhvivtsladvlpaeptlplpdSLRAPRLAAAgai 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 584 --LSSLRTEPAENEPVCAHTDggSLAYVIYTSGSTGTPKGVAVEHRQ----AAAFLSGMQrqfPLTEDDVivlksSFSFD 657
Cdd:PRK06178 189 dlLPALRACTAPVPLPPPALD--ALAALNYTGGTTGMPKGCEHTQRDmvytAAAAYAVAV---VGGEDSV-----FLSFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 658 ASIW------QLFWWMIPGASMYLLPQgWekDPALMTEAFTNEGVTTAhfipAMAnsfLDQ-VE-METEEKRTSLAKTLK 729
Cdd:PRK06178 259 PEFWiagenfGLLFPLFSGATLVLLAR-W--DAVAFMAAVERYRVTRT----VML---VDNaVElMDHPRFAEYDLSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 730 RVFAGG--EALAPQTAARFaRSLPETAVIHG-YGPTEATVDAAFFRYDHEKDRERMRLPI--GKPVPGARLYILDSEK-A 803
Cdd:PRK06178 329 QVRVVSfvKKLNPDYRQRW-RALTGSVLAEAaWGMTETHTCDTFTAGFQDDDFDLLSQPVfvGLPVPGTEFKICDFETgE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 804 VQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEV 883
Cdd:PRK06178 408 LLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 884 EAALRQIDGVREAAVVARTEGEETEL-YAYIE-----GQDQKTARTELGKRLPAYMMPSSFIeMREWPVTPSGKLDRKAL 957
Cdd:PRK06178 481 EALLGQHPAVLGSAVVGRPDPDKGQVpVAFVQlkpgaDLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1511-1984 |
5.85e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 155.58 E-value: 5.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERL 1590
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 EWMLSDSNAVMLLQSDRL----ESHMAGKRL---------------------------------FIEDIQLEAGISANNP 1633
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLapvvEQVRAETSLrhvivtsladvlpaeptlplpdslraprlaaagAIDLLPALRACTAPVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1634 EQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFSPEDRILLTasLGFDAMTF---EVFG---PLLNGACL 1707
Cdd:PRK06178 203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVF--LSFLPEFWiagENFGllfPLFSGATL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1708 YIS---DKETYLDSdrlktfIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLILGGEA-----LSPNHVNRVRNTAPDL 1779
Cdd:PRK06178 281 VLLarwDAVAFMAA------VERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVsfvkkLNPDYRQRWRALTGSV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1780 ALWNGYGPTE-NT--TFSTCFRIEHEYKHSIPI--GRPIANSTAYIVN-SRGRLQPMGVIGELCVGGDGLARGYFGRPEL 1853
Cdd:PRK06178 355 LAEAAWGMTEtHTcdTFTAGFQDDDFDLLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1854 TKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKEL 1933
Cdd:PRK06178 435 TAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVP 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1934 LAYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHLVeLAALPLTQNGKLDRRAL 1984
Cdd:PRK06178 508 VAFVQLKPGADLtaAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
463-955 |
6.68e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 155.16 E-value: 6.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 463 PTLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVP 542
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 543 LDPDYPEERLRYMLADSGARLLV----TGPglSVSGFSGET-LE----VNLSS---------LR-------------TEP 591
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIvwdkVAP--TVERLRRTTpLEtivsVNMIAampllqrlaLRlpipalrkaraalTGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 592 AEN----EPVCAHTDGG-------------SLAYVIYTSGSTGTPKGVAVEHR-------QAAAFLSGmqrqfpLTEDDV 647
Cdd:PRK05605 190 APGtvpwETLVDAAIGGdgsdvshprptpdDVALILYTSGTTGKPKGAQLTHRnlfanaaQGKAWVPG------LGDGPE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 648 IVLKSSFSFDA---SIWQLFWWMIpGASMYLLPQgweKDPALMTEAFTNEGVTtahFIPAMANSFlDQVEMETEEKRTSL 724
Cdd:PRK05605 264 RVLAALPMFHAyglTLCLTLAVSI-GGELVLLPA---PDIDLILDAMKKHPPT---WLPGVPPLY-EKIAEAAEERGVDL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 725 aKTLKRVFAGGEALAPQTAARFaRSLPETAVIHGYGPTE-ATVDAAFFRYDHekdrermRLP--IGKPVPGARLYILDSE 801
Cdd:PRK05605 336 -SGVRNAFSGAMALPVSTVELW-EKLTGGLLVEGYGLTEtSPIIVGNPMSDD-------RRPgyVGVPFPDTEVRIVDPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 802 KA--VQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIE 879
Cdd:PRK05605 407 DPdeTMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVY 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 880 PGEVEAALRQIDGVREAAVV--ARTEGEETELYAYI--EGQ--DQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLD 953
Cdd:PRK05605 480 PAEVEEVLREHPGVEDAAVVglPREDGSEEVVAAVVlePGAalDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVR 559
|
..
gi 2040046167 954 RK 955
Cdd:PRK05605 560 RR 561
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1502-1982 |
2.14e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 153.12 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV 1581
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 TEDMPTERLEWMLSDSNAVMLLQSDRLESHMA-------GKRLF--IED----------IQLEAGISANNPEQQGG---P 1639
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAevlprlpKLRTLvvVEDgsgndllpgaVDYEDALAAGSPERDFGersP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1640 DSLaYIMYTSGSTGTPKGVMVEQRGVVR-------------------LVKNSdmAFSPEDRILLTASLGFDAMTFEVFGP 1700
Cdd:PRK07798 164 DDL-YLLYTGGTTGMPKGVMWRQEDIFRvllggrdfatgepiedeeeLAKRA--AAGPGMRRFPAPPLMHGAGQWAAFAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1701 LLNGACLYISDKETyLDSDRLKTFIQQNGITTLWLTSSLFNQ--LSEQNERTFSDLSRLIL---GGEALSPNHVNRVRNT 1775
Cdd:PRK07798 241 LFSGQTVVLLPDVR-FDADEVWRTIEREKVNVITIVGDAMARplLDALEARGPYDLSSLFAiasGGALFSPSVKEALLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1776 APDLALWNGYGPTEnTTFSTcfrIEHEYKHSIPIGRP---IANSTAYIVNSRGRLQP-MGVIGELCVGGDgLARGYFGRP 1851
Cdd:PRK07798 320 LPNVVLTDSIGSSE-TGFGG---SGTVAKGAVHTGGPrftIGPRTVVLDEDGNPVEPgSGEIGWIARRGH-IPLGYYKDP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1852 ELTKEKFvpnPFTPGERMYRTGDLARWLKDGTIDYIGRmdDQVKIR--GYRIELGEIEAALRQIDGVKEAAVIVRTGPSG 1929
Cdd:PRK07798 395 EKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVADALVVGVPDERW 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1930 HKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRR 1982
Cdd:PRK07798 470 GQEVVAVVQLRegARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1528-1985 |
2.61e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 150.13 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1528 TYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSdr 1607
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1608 leshmagkrlfiediqleagisannpeqqggpdsLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNS--DMAFSPEDRILLT 1685
Cdd:cd05934 83 ----------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSarRFGLGEDDVYLTV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1686 ASLgF--DAMTFEVFGPLLNGACLYISDK---ETYLDSdrlktfIQQNGITTLWLTSSLFNQLSEQNERTfSD---LSRL 1757
Cdd:cd05934 129 LPL-FhiNAQAVSVLAALSVGATLVLLPRfsaSRFWSD------VRRYGATVTNYLGAMLSYLLAQPPSP-DDrahRLRA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1758 ILGGEALSPNH---VNR--VRntapdlaLWNGYGPTEnttfsTCFRIEHEYKHSIP---IGRPIANSTAYIVNSRGRLQP 1829
Cdd:cd05934 201 AYGAPNPPELHeefEERfgVR-------LLEGYGMTE-----TIVGVIGPRDEPRRpgsIGRPAPGYEVRIVDDDGQELP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1830 MGVIGELCV---GGDGLARGYFGRPELTKEKFvPNpftpgeRMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEI 1906
Cdd:cd05934 269 AGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RN------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1907 EAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05934 342 ERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRpgETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
.
gi 2040046167 1985 P 1985
Cdd:cd05934 422 R 422
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1502-1984 |
6.81e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 150.81 E-value: 6.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV 1581
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 TEDMPTERLEWMLSDSNAVMLLQSDRLESHMA-GKRLFIEDI-------QLEAGISANNPEQQGGPDSLAYIMYTSGSTG 1653
Cdd:PRK06145 83 NYRLAADEVAYILGDAGAKLLLVDEEFDAIVAlETPKIVIDAaaqadsrRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1654 TPKGVMVEQRGVVRlvKNSD----MAFSPEDRILLTASL----GFDAMTFEVfgpLLNGACLYIS---DKETYLDSdrlk 1722
Cdd:PRK06145 163 RPKGVMHSYGNLHW--KSIDhviaLGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGGTLRIHrefDPEAVLAA---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1723 tfIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRI 1799
Cdd:PRK06145 234 --IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLawcIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1800 EHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWL 1879
Cdd:PRK06145 312 GREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1880 KDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQLP 1957
Cdd:PRK06145 385 EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNpgATLTLEALDRHCRQRLA 464
|
490 500
....*....|....*....|....*..
gi 2040046167 1958 GFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK06145 465 SFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1511-1983 |
8.85e-38 |
|
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: 151.62 E-value: 8.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIY------DRQTLTYRELNQRANRIAAALRA-NGVGSesVVALLTSRTPELAVGILGILKAGGAYLPVTE 1583
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAvGKPGD--RVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1584 DMPT---ERLEWMLSDSNAVMLLQSDRLESHMA---------GKRLFIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGS 1651
Cdd:cd05931 81 PTPGrhaERLAAILADAGPRVVLTTAAALAAVRafaasrpaaGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1652 TGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILLTASLGFD-AMTFEVFGPLLNGACLYISDKEtyldsdrlkTFIQQN 1728
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAYglDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGPSVLMSPA---------AFLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1729 GittLWLtsslfnQLSEQNERTFS----------------------DLSRL---ILGGEALSPNHVNR-VRNTAP----D 1778
Cdd:cd05931 232 L---RWL------RLISRYRATISaapnfaydlcvrrvrdedleglDLSSWrvaLNGAEPVRPATLRRfAEAFAPfgfrP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1779 LALWNGYGPTENTTFSTCFRIEHEYK---------------------HSIPI---GRPIANSTAYIVNS-RGRLQPMGVI 1833
Cdd:cd05931 303 EAFRPSYGLAEATLFVSGGPPGTGPVvlrvdrdalagravavaaddpAARELvscGRPLPDQEVRIVDPeTGRELPDGEV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1834 GELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARwLKDGTIdYI-GRMDDQVKIRGYRIELGEIEAALRQ 1912
Cdd:cd05931 383 GEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGF-LHDGEL-YItGRLKDLIIVRGRNHYPQDIEATAEE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1913 IDGVKE----AAVIVRTGPSGHKELLA-----YMSLQAEMNIEKVRSLLSQQlpgFMIPAH---LVELAALPLTQNGKLD 1980
Cdd:cd05931 461 AHPALRpgcvAAFSVPDDGEERLVVVAevergADPADLAAIAAAIRAAVARE---HGVAPAdvvLVRPGSIPRTSSGKIQ 537
|
...
gi 2040046167 1981 RRA 1983
Cdd:cd05931 538 RRA 540
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1525-1984 |
1.37e-37 |
|
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: 150.90 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVT----EDMPTERLE-----WMLS 1595
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpptYDEPNARLRklrhiWQLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1596 DSNAVmlLQSDRLESHMAG--KRLFIEDIQLEAGISANNPEQ-----QGGPDSLAYIMYTSGSTGTPKGVMVEQRGVV-R 1667
Cdd:cd05906 118 GSPVV--LTDAELVAEFAGleTLSGLPGIRVLSIEELLDTAAdhdlpQSRPDDLALLMLTSGSTGFPKAVPLTHRNILaR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1668 LV-KNSDMAFSPEDRILltASLGFDAMT----FEVFGPLLNGACLYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQ 1742
Cdd:cd05906 196 SAgKIQHNGLTPQDVFL--NWVPLDHVGglveLHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1743 LSEQNER------TFSDLSRLILGGEALSPNHVNRV-----RNTAPDLALWNGYGPTEN---TTFSTCFRiehEYKHS-- 1806
Cdd:cd05906 274 LNDLLEEiedgtwDLSSLRYLVNAGEAVVAKTIRRLlrllePYGLPPDAIRPAFGMTETcsgVIYSRSFP---TYDHSqa 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1807 ---IPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLArWLKDGT 1883
Cdd:cd05906 351 lefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGN 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1884 IDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKE---AAVIVRTGPSGHKELLAYMS----LQAEMN--IEKVRSLLSQ 1954
Cdd:cd05906 424 LTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAIFFVpeydLQDALSetLRAIRSVVSR 503
|
490 500 510
....*....|....*....|....*....|..
gi 2040046167 1955 QLPGfmIPAHLVELA--ALPLTQNGKLDRRAL 1984
Cdd:cd05906 504 EVGV--SPAYLIPLPkeEIPKTSLGKIQRSKL 533
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
490-957 |
1.81e-37 |
|
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: 150.09 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGPG 569
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 570 LS----------------VSGFSGETLE----VNLSSLRTEPAENEPVCAHT--DGGSLAYVIYTSGSTGTPKGVAVEHR 627
Cdd:cd12119 107 FLplleaiaprlptvehvVVMTDDAAMPepagVGVLAYEELLAAESPEYDWPdfDENTAAAICYTSGTTGNPKGVVYSHR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 628 QAA--AFLSGMQRQFPLTEDDVIVLKSSFsFDASIWQL-FWWMIPGASMyLLPqGWEKDPALMTEAFTNEGVTTAHFIPA 704
Cdd:cd12119 187 SLVlhAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKL-VLP-GPYLDPASLAELIEREGVTFAAGVPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 705 MANSFLDqvEMETEEKRTSlakTLKRVFAGGEALAPQTAARF-ARSLPetaVIHGYGPTE----ATVDA--AFFRYDHEK 777
Cdd:cd12119 264 VWQGLLD--HLEANGRDLS---SLRRVVIGGSAVPRSLIEAFeERGVR---VIHAWGMTEtsplGTVARppSEHSNLSED 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 778 DRERMRLPIGKPVPGARLYILDSEKAVQPI-GVA-GELYIAGAGVARGYLNRPELTEErFLDDPFYRgermyqTGDLARW 855
Cdd:cd12119 336 EQLALRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEA-LTEDGWLR------TGDVATI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 856 LPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVAR---------------TEGEET---ELYAYIEGqd 917
Cdd:cd12119 409 DEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVphpkwgerplavvvlKEGATVtaeELLEFLAD-- 486
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2040046167 918 qktartelgkRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd12119 487 ----------KVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1515-1979 |
1.88e-37 |
|
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: 151.19 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYD------RQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTE 1588
Cdd:cd17634 67 GDRTAIIYEgddtsqSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1589 RLEWMLSDSNAVMLLQSD------RLESHMA-----------------------------GKRLFIEDIQLEAGISANNP 1633
Cdd:cd17634 147 AVAGRIIDSSSRLLITADggvragRSVPLKKnvddalnpnvtsvehvivlkrtgsdidwqEGRDLWWRDLIAKASPEHQP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1634 EQQGGPDSLaYIMYTSGSTGTPKGVmVEQRGVVRLVKNSDMA----FSPEDRILLTASLGF-DAMTFEVFGPLLNGACLY 1708
Cdd:cd17634 227 EAMNAEDPL-FILYTSGTTGKPKGV-LHTTGGYLVYAATTMKyvfdYGPGDIYWCTADVGWvTGHSYLLYGPLACGATTL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1709 ISD-KETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQN----ERTfsDLSRL-ILG--GEALSPN-------HVNRVR 1773
Cdd:cd17634 305 LYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaiEGT--DRSSLrILGsvGEPINPEayewywkKIGKEK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1774 ntAPDLALWngyGPTENTTFS-TCFRIEHEYKHSIPIgRPIANSTAYIVNSRGRLQPMGVIGELCVGGD--GLARGYFGR 1850
Cdd:cd17634 383 --CPVVDTW---WQTETGGFMiTPLPGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGD 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1851 PEltkeKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGH 1930
Cdd:cd17634 457 HE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKG 532
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1931 KELLAYMSLQA------EMNIEkVRSLLSQQLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:cd17634 533 QAPYAYVVLNHgvepspELYAE-LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
458-960 |
3.38e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 149.37 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 458 AAPLAPTLHSFFTRR----AALS--PNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVL 531
Cdd:PRK06188 1 QATMADLLHSGATYGhllvSALKryPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 532 AVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGPGLSVSgfSGETLEVNLSSLR-----------------TEPAEN 594
Cdd:PRK06188 81 AAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVE--RALALLARVPSLKhvltlgpvpdgvdllaaAAKFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 595 EPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIwqLFW-WMIPGASM 673
Cdd:PRK06188 159 APLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLpTLLRGGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 674 YLLPQgweKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEMETeekrTSLAkTLKRVFAGGEALAPqtaARFARSLPET 753
Cdd:PRK06188 237 IVLAK---FDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRT----RDLS-SLETVYYGASPMSP---VRLAEAIERF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 754 AVIHG--YGPTEATVDAAFFRY-DHEKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPEL 830
Cdd:PRK06188 306 GPIFAqyYGQTEAPMVITYLRKrDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 831 TEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV------------ 898
Cdd:PRK06188 386 TAEAFRDGWLH-------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekwgeav 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 899 ----VARTEG--EETELYAYIegqdqKTARTelgkrlpAYMMPSSFIEMREWPVTPSGKLDRKALPAP 960
Cdd:PRK06188 459 tavvVLRPGAavDAAELQAHV-----KERKG-------SVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
470-972 |
4.05e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 149.54 E-value: 4.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 470 TRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPE 549
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 550 ERLRYMLADSGARLLVT--------------GPGLSVSGFSGETLEVNLSSLRTEPAENEPVCAHTD--GGSLAYVIYTS 613
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTeaalapvatavrdiVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDipNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 614 GSTGTPKGVAVEHR----QAAAFLSGMQRQfplTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGwEKDPALMTE 689
Cdd:PRK07786 184 GTTGRPKGAVLTHAnltgQAMTCLRTNGAD---INSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLG-AFDPGQLLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 690 AFTNEGVTTAHFIPAMANSFLDqvEMETEEKRTSLaktlkRVFAGGEALAPQTAAR-FARSLPETAVIHGYGPTEATVDA 768
Cdd:PRK07786 260 VLEAEKVTGIFLVPAQWQAVCA--EQQARPRDLAL-----RVLSWGAAPASDTLLRqMAATFPEAQILAAFGQTEMSPVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 769 AFFRYDhekDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyq 848
Cdd:PRK07786 333 CMLLGE---DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 849 TGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTARTE---- 924
Cdd:PRK07786 403 SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTledl 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 925 ---LGKRLPAYMMPSSFIEMREWPVTPSGKLD----RKALPAPDGAAERRVYTAP 972
Cdd:PRK07786 483 aefLTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGF 537
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
489-900 |
1.03e-36 |
|
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: 146.20 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGp 568
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 glsvsgfsgetlevnlsslrtepaenepvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI 648
Cdd:cd05907 85 ---------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 V--LKSSFSFDASIWQLFWwMIPGASMYLLPqgwekdpaLMTEAFTNEGVTTAHFIPA-------MANSFldQVEMETEE 719
Cdd:cd05907 132 LsfLPLAHVFERRAGLYVP-LLAGARIYFAS--------SAETLLDDLSEVRPTVFLAvprvwekVYAAI--KVKAVPGL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 720 KRTSLAKT----LKRVFAGGEALAPQTAaRFARSL--PetaVIHGYGPTEATVDAAFfrydHEKDRERMRLpIGKPVPGA 793
Cdd:cd05907 201 KRKLFDLAvggrLRFAASGGAPLPAELL-HFFRALgiP---VYEGYGLTETSAVVTL----NPPGDNRIGT-VGKPLPGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 794 RLYIldsekavqpiGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRM-DGQVK 872
Cdd:cd05907 272 EVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKkDLIIT 335
|
410 420
....*....|....*....|....*...
gi 2040046167 873 IRGYRIEPGEVEAALRQIDGVREAAVVA 900
Cdd:cd05907 336 SGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
477-900 |
1.16e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 148.18 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLKKK-GVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYM 555
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 556 LADSGARLLVTGPGLS----------------VSGFSG---ETLEVNLSS-LRTEP-----------------AENEPVC 598
Cdd:PRK08314 104 VTDSGARVAIVGSELApkvapavgnlrlrhviVAQYSDylpAEPEIAVPAwLRAEPplqalapggvvawkealAAGLAPP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 599 AHTDG-GSLAYVIYTSGSTGTPKGVAVEHR--QAAAFLSGMQRQfpLTEDDVI--------VLKSSFSFDASIWQlfwwm 667
Cdd:PRK08314 184 PHTAGpDDLAVLPYTSGTTGVPKGCMHTHRtvMANAVGSVLWSN--STPESVVlavlplfhVTGMVHSMNAPIYA----- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 668 ipGASMYLLPQgWEKDPALmtEAFTNEGVTTAHFIPAMANSFLDQVEMEtEEKRTSLaktlkRVFAGGEALAPQTAARFA 747
Cdd:PRK08314 257 --GATVVLMPR-WDREAAA--RLIERYRVTHWTNIPTMVVDFLASPGLA-ERDLSSL-----RYIGGGGAAMPEAVAERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 748 RSLPETAVIHGYGPTEAtvdAAFfryDHEKDRERMRLP-IGKPVPG--ARlyILDSEK-AVQPIGVAGELYIAGAGVARG 823
Cdd:PRK08314 326 KELTGLDYVEGYGLTET---MAQ---THSNPPDRPKLQcLGIPTFGvdAR--VIDPETlEELPPGEVGEIVVHGPQVFKG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 824 YLNRPELTEERFLDdpfYRGERMYQTGDLARWLPDG---TVEWLGRMdgqVKIRGYRIEPGEVEAALRQIDGVREAAVVA 900
Cdd:PRK08314 398 YWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGyffITDRLKRM---INASGFKVWPAEVENLLYKHPAIQEACVIA 471
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
489-957 |
1.47e-36 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 145.35 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP 568
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 GlsvsgfsgetlevNLSSLRTEPAenepvcahtdggslaYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVi 648
Cdd:cd05973 81 A-------------NRHKLDSDPF---------------VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 vlkssfsfdasiwqlFWWMI-PGASMYL-------LPQGwekDPALMTEA-FTNE---------GVTTAHFIPAMANSFL 710
Cdd:cd05973 132 ---------------FWNAAdPGWAYGLyyaitgpLALG---HPTILLEGgFSVEstwrvierlGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 711 -DQVEMETEEKrtslaKTLKRVFAGGEALAPQTAARFARSLPETAVIHgYGPTEAtvdaAFFRYDHEKDRERMRL-PIGK 788
Cdd:cd05973 194 aAGAEVPARPK-----GRLRRVSSAGEPLTPEVIRWFDAALGVPIHDH-YGQTEL----GMVLANHHALEHPVHAgSAGR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 789 PVPGARLYILDSEKAVQPIGVAGELYIAGAGVA----RGYLNrpelteerfLDDPFYRGeRMYQTGDLARWLPDGTVEWL 864
Cdd:cd05973 264 AMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQL---------PDTPAIDG-GYYLTGDTVEFDPDGSFSFI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 865 GRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELY-AYI---EGQDQKTA-----RTELGKRLPAYMMP 935
Cdd:cd05973 334 GRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVkAFVvlrGGHEGTPAladelQLHVKKRLSAHAYP 413
|
490 500
....*....|....*....|..
gi 2040046167 936 SSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05973 414 RTIHFVDELPKTPSGKIQRFLL 435
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
464-957 |
1.96e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 147.51 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAV---RFSGGI---LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAG 537
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVtavRLGTGAprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 538 GAYVPLDPDYPEERLRYMLADSGARLLVTgPGLsVSGFS----GETLEVNLSSLR-----------------TEPA-ENE 595
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVV-PKT-FRGFDhaamARRLRPELPALRhvvvvggdgadsfeallITPAwEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 596 PVCAHT------DGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIwqLFWWMIP 669
Cdd:PRK13295 183 PDAPAIlarlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGF--MYGLMMP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 670 ---GASMYLLPQgWekDPALMTEAFTNEGVTtahFIPAmANSFLDQVEMETEEKRTSLAkTLkRVFAGGEALAPQTAARF 746
Cdd:PRK13295 261 vmlGATAVLQDI-W--DPARAAELIRTEGVT---FTMA-STPFLTDLTRAVKESGRPVS-SL-RTFLCAGAPIPGALVER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 747 ARSLPETAVIHGYGPTEatvDAAFFRYDHEKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLN 826
Cdd:PRK13295 332 ARAALGAKIVSAWGMTE---NGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 827 RPELTeerfLDDpfyrGERMYQTGDLARWLPDGTVEWLGRmDGQVKIRG-YRIEPGEVEAALRQIDGVREAAVVArtege 905
Cdd:PRK13295 409 RPQLN----GTD----ADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVA----- 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 906 etelYAyiegqDQKtarteLGKRLPAYMMPS-----SFIEMREW---------------------PVTPSGKLDRKAL 957
Cdd:PRK13295 475 ----YP-----DER-----LGERACAFVVPRpgqslDFEEMVEFlkaqkvakqyiperlvvrdalPRTPSGKIQKFRL 538
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
605-957 |
2.03e-36 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 142.08 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 605 SLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLpqgwEKDP 684
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLL----ERNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 685 ALMtEAFTNEGVTTAHFIPAMANSFLDqvemetEEKRTSLAKTLKRVFAGGEALAPQTAARFA-RSLPetaVIHGYGPTE 763
Cdd:cd17630 77 ALA-EDLAPPGVTHVSLVPTQLQRLLD------SGQGPAALKSLRAVLLGGAPIPPELLERAAdRGIP---LYTTYGMTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 764 ATVDAAFFRYDHEKDRErmrlpIGKPVPGARLYILDsekavqpigvAGELYIAGAGVARGYLNRPEltEERFLDDPFYrg 843
Cdd:cd17630 147 TASQVATKRPDGFGRGG-----VGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL--VPEFNEDGWF-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 844 ermyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA---RTEGEetELYAYIEGQ---D 917
Cdd:cd17630 208 ----TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGvpdEELGQ--RPVAVIVGRgpaD 281
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2040046167 918 QKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd17630 282 PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
464-957 |
2.18e-36 |
|
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: 146.83 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL 543
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGARLLVTG-------------------PGLS---VSGFSGEtlEVNLSSLRTEPAENEPvcAHT 601
Cdd:COG1021 106 LPAHRRAEISHFAEQSEAVAYIIPdrhrgfdyralarelqaevPSLRhvlVVGDAGE--FTSLDALLAAPADLSE--PRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 602 DGGSLAYVIYTSGSTGTPKGVAVEHR------QAAAFLSGmqrqfpLTEDDV--IVLKSSFSFDASIWQLFWWMIPGASM 673
Cdd:COG1021 182 DPDDVAFFQLSGGTTGLPKLIPRTHDdylysvRASAEICG------LDADTVylAALPAAHNFPLSSPGVLGVLYAGGTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 674 YLLPQGwekDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEMEteekRTSLAkTLKRVFAGGEALAPQTAARFARSLPET 753
Cdd:COG1021 256 VLAPDP---SPDTAFPLIERERVTVTALVPPLALLWLDAAERS----RYDLS-SLRVLQVGGAKLSPELARRVRPALGCT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 754 aVIHGYGPTEATVDaaFFRYDHekDRERMRLPIGKPV-PGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTE 832
Cdd:COG1021 328 -LQQVFGMAEGLVN--YTRLDD--PEEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 833 ERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVkIR-GYRIEPGEVEAALRQIDGVREAAVVA---RTEGEETe 908
Cdd:COG1021 403 RAFTPDGFYR------TGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAmpdEYLGERS- 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 909 lYAYIEGQDQKTARTEL-----GKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:COG1021 475 -CAFVVPRGEPLTLAELrrflrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1497-1984 |
3.53e-36 |
|
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: 145.16 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1497 YPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGG 1576
Cdd:cd05920 11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1577 ayLPVTEdMPTER---LEWMLSDSNAVMLLQSDRLES--HMAgkrLFIEdiqleagisannpEQQGGPDsLAYIMYTSGS 1651
Cdd:cd05920 91 --VPVLA-LPSHRrseLSAFCAHAEAVAYIVPDRHAGfdHRA---LARE-------------LAESIPE-VALFLLSGGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1652 TGTPKGVMVEQRGVVRLVKNSD--MAFSPEDRIL--LTASLGFDAMTFEVFGPLLNGACLYISDketylDSDRLKTF--I 1725
Cdd:cd05920 151 TGTPKLIPRTHNDYAYNVRASAevCGLDQDTVYLavLPAAHNFPLACPGVLGTLLAGGRVVLAP-----DPSPDAAFplI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1726 QQNGITTLWLTSSLFNQLSEQNERTFSDLSRLIL---GGEALSPNHVNRVRnTAPDLALWNGYGPTENTTFSTCFRIEHE 1802
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASRRADLSSLRLlqvGGARLSPALARRVP-PVLGCTLQQVFGMAEGLLNYTRLDDPDE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1803 YKHSIPiGRPI-ANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKD 1881
Cdd:cd05920 305 VIIHTQ-GRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1882 GTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPS-GHKELLAYMSLQAEMNIEKVRSLLSQQ-LPGF 1959
Cdd:cd05920 378 GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERSCAFVVLRDPPPSAAQLRRFLRERgLAAY 457
|
490 500
....*....|....*....|....*
gi 2040046167 1960 MIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05920 458 KLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
473-957 |
5.05e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 144.95 E-value: 5.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVR--FSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEE 550
Cdd:PRK09088 5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 551 RLRYMLADSGARLLVTGPGLSVSGFSGETLEVNLSSLRT-EPAENEPvcAHTDGGSLayVIYTSGSTGTPKGVAVEHR-- 627
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADAlEPADTPS--IPPERVSL--ILFTSGTSGQPKGVMLSERnl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 628 -QAAAFLSGMQRqfplteddvIVLKSSFSFDASIWQLFWW-------MIPGASMYLLP-------QGWEKDPALmteaft 692
Cdd:PRK09088 161 qQTAHNFGVLGR---------VDAHSSFLCDAPMFHIIGLitsvrpvLAVGGSILVSNgfepkrtLGRLGDPAL------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 693 neGVTTAHFIPAMANSFLDQVEMETEEKRtslakTLKRVFAGGealAPQTAARFARSLPE-TAVIHGYGPTEA-TVdaaf 770
Cdd:PRK09088 226 --GITHYFCVPQMAQAFRAQPGFDAAALR-----HLTALFTGG---APHAAEDILGWLDDgIPMVDGFGMSEAgTV---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 771 FRYDHEKDRERMRL-PIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqT 849
Cdd:PRK09088 292 FGMSVDCDVIRAKAgAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFR------T 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 850 GDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL-YAYI---EGQDQKTA--RT 923
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVgYLAIvpaDGAPLDLEriRS 445
|
490 500 510
....*....|....*....|....*....|....
gi 2040046167 924 ELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1511-1922 |
6.68e-36 |
|
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: 145.07 E-value: 6.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIyDRQT---LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPT 1587
Cdd:cd05904 15 ASAHPSRPALI-DAATgraLTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1588 ERLEWMLSDSNA-------------------VMLLQSDRLESHMAGKRLFIEDiqleagiSANNPEQQGGPDSLAYIMYT 1648
Cdd:cd05904 94 AEIAKQVKDSGAklafttaelaeklaslalpVVLLDSAEFDSLSFSDLLFEAD-------EAEPPVVVIKQDDVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1649 SGSTGTPKGVMVEQRGVV----RLVKNSDMAFSPEDRILLTASLgFDAMTFEVF--GPLLNGACLYIS---DKETYLDSd 1719
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIamvaQFVAGEGSNSDSEDVFLCVLPM-FHIYGLSSFalGLLRLGATVVVMprfDLEELLAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1720 rlktfIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL--ILGGEA-LSPNHVNRVRNTAPDLALWNGYGPTENTTFST- 1795
Cdd:cd05904 245 -----IERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLrqIMSGAApLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAm 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1796 CFRIEHEYKHSIPIGRPIANSTAYIVN-SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPnpftpgERMYRTGD 1874
Cdd:cd05904 320 CFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK------EGWLHTGD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2040046167 1875 LARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI 1922
Cdd:cd05904 394 LCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
12-430 |
1.10e-35 |
|
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: 142.52 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNVAKPRQVVLKERQSRLQFV 91
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 92 DISHLD---ETAKETFVDQFEHddkkKGFDLQTDPLMRVSILK-RAHEQYHCIwSHHHILMDGWCFGIVMKEFLAIYKAL 167
Cdd:cd19539 83 DLSDPDsdrERRLEELLRERES----RGFDLDEEPPIRAVLGRfDPDDHVLVL-VAHHTAFDAWSLDVFARDLAALYAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 168 GKEQLPDF-EPVHPFSKYIKWLMRQDRK----EAEAFWKTRLIDVKQTASLPKTSSSSKGKLE--QMAFTLSKEQTEGLR 240
Cdd:cd19539 158 RKGPAAPLpELRQQYKEYAAWQREALAApraaELLDFWRRRLRGAEPTALPTDRPRPAGFPYPgaDLRFELDAELVAALR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 241 KLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDleDVEKMVGLFINTIPVRVK-SGPESFLTLVSHLQQE 319
Cdd:cd19539 238 ELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDvSDCATFRDLIARVRKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 320 SLKAEAYSYYPLYDIQAQ-----SMLKHELFDHIVVFENIPA-QREIESLNQADAfdftvdDFDMDEVTNYGCSIKIIP- 392
Cdd:cd19539 316 LVDAQRHQELPFQQLVAElpvdrDAGRHPLVQIVFQVTNAPAgELELAGGLSYTE------GSDIPDGAKFDLNLTVTEe 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 2040046167 393 GSSLYIRINFDIGLYDPAMMKKIELYLRHIIGSVIADP 430
Cdd:cd19539 390 GTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1526-1984 |
2.14e-35 |
|
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: 141.33 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1526 TLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSnavmllqs 1605
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1606 drleshmagkrlfieDIQLeagisannpeqqggpDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNS--DMAFSPEDRIL 1683
Cdd:cd05912 73 ---------------DVKL---------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSalNLGLTEDDNWL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1684 LTASLgfdamtFEVFG------PLLNGACLYISDKetyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL 1757
Cdd:cd05912 123 CALPL------FHISGlsilmrSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRC 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1758 IL-GGEALSPNHVNRVRntAPDLALWNGYGPTEntTFSTCFRIEHEYKHSIP--IGRPIANSTAYIVNSrgrLQPMGVIG 1834
Cdd:cd05912 194 ILlGGGPAPKPLLEQCK--EKGIPVYQSYGMTE--TCSQIVTLSPEDALNKIgsAGKPLFPVELKIEDD---GQPPYEVG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1835 ELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQID 1914
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1915 GVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05912 340 AIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
473-953 |
5.11e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 142.72 E-value: 5.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERL 552
Cdd:PRK07798 13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 553 RYMLADSGARLLVTGpglsvSGFSGETLEV--NLSSLRT------EPAENEPVCAHTDGGSLA----------------Y 608
Cdd:PRK07798 93 RYLLDDSDAVALVYE-----REFAPRVAEVlpRLPKLRTlvvvedGSGNDLLPGAVDYEDALAagsperdfgerspddlY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAveHRQAAAFLSGMQRQFPLT----EDDVIVLKSSFSFDASIWQLFWWMIPGASMY---------- 674
Cdd:PRK07798 168 LLYTGGTTGMPKGVM--WRQEDIFRVLLGGRDFATgepiEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWaafaalfsgq 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 675 --LLPQGWEKDPALMTEAFTNEGVTTAHFI-PAMANSFLDqvemETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLP 751
Cdd:PRK07798 246 tvVLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLD----ALEARGPYDLSSLFAIASGGALFSPSVKEALLELLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 752 ETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGkpvPGARLyILDSEKAVQP-IGVAGelYIAGAG-VARGYLNRPE 829
Cdd:PRK07798 322 NVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIG---PRTVV-LDEDGNPVEPgSGEIG--WIARRGhIPLGYYKDPE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 830 LTEERFlddPFYRGERMYQTGDLARWLPDGTVEWLGRmdGQVKIR--GYRIEPGEVEAALRQIDGV-------------- 893
Cdd:PRK07798 396 KTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPDVadalvvgvpderwg 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 894 -REAAVVARTEG---EETELYAYiegqdqktARTelgkRLPAYMMPSSFIEMREWPVTPSGKLD 953
Cdd:PRK07798 471 qEVVAVVQLREGarpDLAELRAH--------CRS----SLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
459-951 |
5.23e-35 |
|
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: 142.05 E-value: 5.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 459 APLAPTlhSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGG 538
Cdd:cd12118 2 VPLTPL--SFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 539 AYVPLDPDYPEERLRYMLADSGARLLVTGpglsvSGFSGETLevnlssLRTEPAENEPVCAHTDGGSLAyVIYTSGSTGT 618
Cdd:cd12118 80 VLNALNTRLDAEEIAFILRHSEAKVLFVD-----REFEYEDL------LAEGDPDFEWIPPADEWDPIA-LNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 619 PKGVAVEHRQA------AAFLSGMQrqfplteDDVIVLKSSFSFDASIWqLFWWMIP--GASMYLLPQgweKDPALMTEA 690
Cdd:cd12118 148 PKGVVYHHRGAylnalaNILEWEMK-------QHPVYLWTLPMFHCNGW-CFPWTVAavGGTNVCLRK---VDAKAIYDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 691 FTNEGVTtaHFIPA------MANSfldqvemeTEEKRTSLAKTLkRVFAGGealAPQTAARFARSLPET-AVIHGYGPTE 763
Cdd:cd12118 217 IEKHKVT--HFCGAptvlnmLANA--------PPSDARPLPHRV-HVMTAG---APPPAAVLAKMEELGfDVTHVYGLTE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 764 ----ATVDAAFFRYDHEKDRERMRLpigKPVPGARLYILDSEKAVQPIGV---------AGELYIAGAGVARGYLNRPEL 830
Cdd:cd12118 283 tygpATVCAWKPEWDELPTEERARL---KARQGVRYVGLEEVDVLDPETMkpvprdgktIGEIVFRGNIVMKGYLKNPEA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 831 TEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEet 907
Cdd:cd12118 360 TAEAFRGGWFH-------SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDekwGE-- 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2040046167 908 ELYAYIEGQDQKTARTE-----LGKRLPAYMMPSSfIEMREWPVTPSGK 951
Cdd:cd12118 431 VPCAFVELKEGAKVTEEeiiafCREHLAGFMVPKT-VVFGELPKTSTGK 478
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
455-957 |
6.20e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 142.72 E-value: 6.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 455 TEPAAPLAPTLHSFFTRRAALSPNLPAVRFSGG--ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLA 532
Cdd:PRK05852 8 APMASDFGPRIADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 533 VLKAGGAYVPLDPDYPEERLRYMLADSGARLLV---TGPG----------------LSVSGFSGETLEVNLsslrTEPAE 593
Cdd:PRK05852 88 ASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidaDGPHdraepttrwwpltvnvGGDSGPSGGTLSVHL----DAATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 594 NEPVCAHTDG--GSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGA 671
Cdd:PRK05852 164 PTPATSTPEGlrPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 672 SMYLLPQG--------WEKDPALMTEAFTneGVTTAHFIpamansfldQVEMETEEKRTSLAKTLKRVFAGGEALAPQTA 743
Cdd:PRK05852 244 GAVLLPARgrfsahtfWDDIKAVGATWYT--AVPTIHQI---------LLERAATEPSGRKPAALRFIRSCSAPLTAETA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 744 ARFARSLpETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGkPVP---GARLYILDSEKAVQPIGVAGELYIAGAGV 820
Cdd:PRK05852 313 QALQTEF-AAPVVCAFGMTEATHQVTTTQIEGIGQTENPVVSTG-LVGrstGAQIRIVGSDGLPLPAGAVGEVWLRGTTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 821 ARGYLNRPELTEERFLDDPFyrgermyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA 900
Cdd:PRK05852 391 VRGYLGDPTITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFG 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 901 RTEG--EETELYAYIEGQDQKTARTELG----KRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK05852 464 VPDQlyGEAVAAVIVPRESAPPTAEELVqfcrERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
460-899 |
2.12e-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: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 460 PLAPTLHSFFTRRAALSPNLPAV--RFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAG 537
Cdd:cd05904 2 PTDLPLDSVSFLFASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 538 GAYVPLDPDYPEERLRYMLADSGARLLVTGPGL--SVSGFSGETleVNLSSLRTEPAENEPVCAHTDGGSLAYVI----- 610
Cdd:cd05904 82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELaeKLASLALPV--VLLDSAEFDSLSFSDLLFEADEAEPPVVVikqdd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 611 -----YTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDD------VIVLKSSFSFDASIWQLfwwMIPGASMYLLPQg 679
Cdd:cd05904 160 vaallYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSedvflcVLPMFHIYGLSSFALGL---LRLGATVVVMPR- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 680 weKDPALMTEAFTNEGVTTAHFIP----AMANSfldqvemeTEEKRTSLaKTLKRVFAGGEALAPQTAARFARSLPETAV 755
Cdd:cd05904 236 --FDLEELLAAIERYKVTHLPVVPpivlALVKS--------PIVDKYDL-SSLRQIMSGAAPLGKELIEAFRAKFPNVDL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 756 IHGYGPTEAT-VDAAFFryDHEKDRERmRLPIGKPVPGARLYILDSEK-AVQPIGVAGELYIAGAGVARGYLNRPELTEE 833
Cdd:cd05904 305 GQGYGMTESTgVVAMCF--APEKDRAK-YGSVGRLVPNVEAKIVDPETgESLPPNQTGELWIRGPSIMKGYLNNPEATAA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 834 RFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV 899
Cdd:cd05904 382 TIDKEGWLH------TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1509-1986 |
2.67e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 139.94 E-value: 2.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1509 YQAAKTPHAPAV--IYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMP 1586
Cdd:PRK09088 3 FHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1587 TERLEWMLSDSNAVMLLQSDrlesHMAGKRLFIEDIQ-LEAGISANNPEQQGG--PDSLAYIMYTSGSTGTPKGVMVEQR 1663
Cdd:PRK09088 83 ASELDALLQDAEPRLLLGDD----AVAAGRTDVEDLAaFIASADALEPADTPSipPERVSLILFTSGTSGQPKGVMLSER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1664 GVVRLVKNsdmaFSPEDRILLTASLGFDAMTFEVFG-------PLLNGACLYISDKetyLDSDR-LKTFIQQN-GITTLW 1734
Cdd:PRK09088 159 NLQQTAHN----FGVLGRVDAHSSFLCDAPMFHIIGlitsvrpVLAVGGSILVSNG---FEPKRtLGRLGDPAlGITHYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1735 LTSSLFNQLSEQNERTFSDLSRL--ILGGEALSPnhvnrvrntAPDLALW--------NGYGPTE-NTTFST---CFRIE 1800
Cdd:PRK09088 232 CVPQMAQAFRAQPGFDAAALRHLtaLFTGGAPHA---------AEDILGWlddgipmvDGFGMSEaGTVFGMsvdCDVIR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1801 HEYKHSipiGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVpnpftpGERMYRTGDLARWLK 1880
Cdd:PRK09088 303 AKAGAA---GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1881 DGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI----VRTGPSGHkeLLAYMSLQAEMNIEKVRSLLSQQL 1956
Cdd:PRK09088 374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVgmadAQWGEVGY--LAIVPADGAPLDLERIRSHLSTRL 451
|
490 500 510
....*....|....*....|....*....|
gi 2040046167 1957 PGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK09088 452 AKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
489-957 |
3.70e-34 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 137.86 E-value: 3.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLlvtgp 568
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 glsvsgfsgetlevnlsslrtepaenepvcahtdgGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDD-- 646
Cdd:cd05912 77 -----------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDnw 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 647 VIVLK----SSFSFdasiwqLFWWMIPGASMYLLPQgweKDPALMTEAFTNEGVTTAHFIPAMANSFLDQV-EMETEEKR 721
Cdd:cd05912 122 LCALPlfhiSGLSI------LMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLLEILgEGYPNNLR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 722 TSLaktlkrvFAGGEALAPQTAARFARSLPetaVIHGYGPTEAT--VDAAFFRYDHEKDRErmrlpIGKPVPGARLYIld 799
Cdd:cd05912 193 CIL-------LGGGPAPKPLLEQCKEKGIP---VYQSYGMTETCsqIVTLSPEDALNKIGS-----AGKPLFPVELKI-- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 800 sEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIE 879
Cdd:cd05912 256 -EDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 880 PGEVEAALRQIDGVREAAVVARTEGEETEL-YAYIEGQdQKTARTEL----GKRLPAYMMPSSFIEMREWPVTPSGKLDR 954
Cdd:cd05912 328 PAEIEEVLLSHPAIKEAGVVGIPDDKWGQVpVAFVVSE-RPISEEELiaycSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
...
gi 2040046167 955 KAL 957
Cdd:cd05912 407 HEL 409
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
464-957 |
4.90e-34 |
|
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: 139.00 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL 543
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGARLLVtGPGlSVSGFSGETLEVNLsslrtepaenepvcaHTDGGSLAYVIYTSGSTGTPKGVA 623
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYI-VPD-RHAGFDHRALAREL---------------AESIPEVALFLLSGGTTGTPKLIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 624 VEHR------QAAAFLSGmqrqfpLTEDDV--IVLKSSFSFDASIWQLFWWMIPGASMYLLPQGwekDPALMTEAFTNEG 695
Cdd:cd05920 159 RTHNdyaynvRASAEVCG------LDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 696 VTTAHFIPAMANSFLDQVEmeteeKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETaVIHGYGPTEATVDaaFFRYDH 775
Cdd:cd05920 230 VTVTALVPALVSLWLDAAA-----SRRADLSSLRLLQVGGARLSPALARRVPPVLGCT-LQQVFGMAEGLLN--YTRLDD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 776 EKDRermrlpI----GKPV-PGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTG 850
Cdd:cd05920 302 PDEV------IihtqGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYR------TG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 851 DLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEETELYAYIEGQDQKTAR----- 922
Cdd:cd05920 370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDellGERSCAFVVLRDPPPSAAQlrrfl 449
|
490 500 510
....*....|....*....|....*....|....*
gi 2040046167 923 TELGkrLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05920 450 RERG--LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
11-334 |
5.61e-34 |
|
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: 137.50 E-value: 5.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 11 YPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQSRLQF 90
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE-GEPYQWIDPYTPVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 91 VDIShlDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRA---HEQYHCIwshHHILMDGWCFGIVMKEFLAIYKAL 167
Cdd:cd19533 81 IDLS--GDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGdnrHFWYQRV---HHIVMDGFSFALFGQRVAEIYTAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 168 GKEQLPDFEPVHPFSKYIkwLMRQDRKEAE------AFWKTRLIDVKQTASL-PKTSSSSKGKLEQMAFtLSKEQTEGLR 240
Cdd:cd19533 156 LKGRPAPPAPFGSFLDLV--EEEQAYRQSErferdrAFWTEQFEDLPEPVSLaRRAPGRSLAFLRRTAE-LPPELTRTLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 241 KLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDLEdvEKMVGLFINTIPVRVKSGP-ESFLTLVSHLQQE 319
Cdd:cd19533 233 EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAA--RQTPGMVANTLPLRLTVDPqQTFAELVAQVSRE 310
|
330
....*....|....*
gi 2040046167 320 SLKAEAYSYYPLYDI 334
Cdd:cd19533 311 LRSLLRHQRYRYEDL 325
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
490-952 |
1.93e-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: 138.86 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTG-- 567
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAdg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 568 ---PGLSVS--GFSGETLEVNLSSLRT---------------------------EPAENEPvcAHTDGGSLAYVIYTSGS 615
Cdd:cd17634 166 gvrAGRSVPlkKNVDDALNPNVTSVEHvivlkrtgsdidwqegrdlwwrdliakASPEHQP--EAMNAEDPLFILYTSGT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 616 TGTPKGVAVEHRQAAAFLS-GMQRQFPLTEDDVIVLKSSFSF-DASIWQLFWWMIPGASMYLL---PQGweKDPALMTEA 690
Cdd:cd17634 244 TGKPKGVLHTTGGYLVYAAtTMKYVFDYGPGDIYWCTADVGWvTGHSYLLYGPLACGATTLLYegvPNW--PTPARMWQV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 691 FTNEGVTTAHFIP----AMANSFLDQVEmeteekRTSLAkTLKRVFAGGEALAPQTAARFARSLPETA--VIHGYGPTEA 764
Cdd:cd17634 322 VDKHGVNILYTAPtairALMAAGDDAIE------GTDRS-SLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTET 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 765 TVDAAFFRydhekdRERMRLPIG---KPVPGARLYILDSEKAVQPIGVAGELYIAGA--GVARGYLNRPelteERFLDDP 839
Cdd:cd17634 395 GGFMITPL------PGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTY 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 840 FYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA-RTEGEETELYAYI---EG 915
Cdd:cd17634 465 FSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGiPHAIKGQAPYAYVvlnHG 544
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2040046167 916 -QDQKTARTELGKRLPAYMMPSSFIEMREW----PVTPSGKL 952
Cdd:cd17634 545 vEPSPELYAELRNWVRKEIGPLATPDVVHWvdslPKTRSGKI 586
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
466-899 |
2.08e-33 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 137.31 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 466 HSFFTR-RAAL-SPNLPAVRFSGG-ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVP 542
Cdd:PRK07514 3 NNLFDAlRAAFaDRDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 543 LDPDYPEERLRYMLADSGARLLVTGP----GLS-VSGFSG----ETLEVNLS-SL----RTEPAENEPVcaHTDGGSLAY 608
Cdd:PRK07514 83 LNTAYTLAELDYFIGDAEPALVVCDPanfaWLSkIAAAAGaphvETLDADGTgSLleaaAAAPDDFETV--PRGADDLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIV----------LkssfsFDASIWQLFwwmiPGASMYLLPQ 678
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIhalpifhthgL-----FVATNVALL----AGASMIFLPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 679 gweKDP----ALMTEAFTNEGVTTAHfipamansfldqVEMETEEKRTSLAKTLKRVFAGGEA-LAPQTAARF-ARslpe 752
Cdd:PRK07514 232 ---FDPdavlALMPRATVMMGVPTFY------------TRLLQEPRLTREAAAHMRLFISGSApLLAETHREFqER---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 753 T--AVIHGYGPTEaTVDAAFFRYDHEkdrermRLP--IGKPVPGARLYILDSEK-AVQPIGVAGELYIAGAGVARGYLNR 827
Cdd:PRK07514 293 TghAILERYGMTE-TNMNTSNPYDGE------RRAgtVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRM 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 828 PELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV 899
Cdd:PRK07514 366 PEKTAEEFRADGFFI------TGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI 431
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1497-1984 |
2.33e-33 |
|
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: 137.97 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1497 YPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGS-ESVVALLTSRtPELAVGILGILKAG 1575
Cdd:COG1021 21 YWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVVVQLPNV-AEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1576 GayLPVTEdMPTER---LEWMLSDSNAVMLLQSDR-------------LESHMAGKRLFI-----EDIQLEAGISANNPE 1634
Cdd:COG1021 100 A--IPVFA-LPAHRraeISHFAEQSEAVAYIIPDRhrgfdyralarelQAEVPSLRHVLVvgdagEFTSLDALLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1635 QQGGPD--SLAYIMYTSGSTGTPKGV---------MVeqRGVVRLvknsdMAFSPEDRIL--LTASLGFdAMT-FEVFGP 1700
Cdd:COG1021 177 SEPRPDpdDVAFFQLSGGTTGLPKLIprthddylySV--RASAEI-----CGLDADTVYLaaLPAAHNF-PLSsPGVLGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1701 LLNGACLYISDketylDSDRLKTF--IQQNGIT---------TLWLTSSlfnqlsEQNERTFSDLSRLILGGEALSPNHV 1769
Cdd:COG1021 249 LYAGGTVVLAP-----DPSPDTAFplIERERVTvtalvpplaLLWLDAA------ERSRYDLSSLRVLQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1770 NRVRNTAPdLALWNGYGPTE---NTT---------FSTCfrieheykhsipiGRPIanSTA---YIVNSRGRLQPMGVIG 1834
Cdd:COG1021 318 RRVRPALG-CTLQQVFGMAEglvNYTrlddpeeviLTTQ-------------GRPI--SPDdevRIVDEDGNPVPPGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1835 ELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVkIR-GYRIELGEIEAALRQI 1913
Cdd:COG1021 382 ELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAH 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 1914 DGVKEAAVIvrtgpSGHKELL-----AYMSLQ-AEMNIEKVRSLLSQQ-LPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:COG1021 455 PAVHDAAVV-----AMPDEYLgerscAFVVPRgEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1523-1922 |
3.37e-33 |
|
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: 135.80 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1523 DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVML 1602
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 lqsdrleshmagkrlFIEDiqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSD--MAFSPED 1680
Cdd:cd05907 82 ---------------FVED-----------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAerLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1681 RILLTASLgfdAMTFE----VFGPLLNGACLYI--SDKETYLDSDRLK-TFIQqnGITTLWLTSSLFNQLSEQNE--RTF 1751
Cdd:cd05907 130 RHLSFLPL---AHVFErragLYVPLLAGARIYFasSAETLLDDLSEVRpTVFL--AVPRVWEKVYAAIKVKAVPGlkRKL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1752 SDL---SRL---ILGGEALSPNHVNRVRntAPDLALWNGYGPTENTTFSTCFRIEHEYKHSipIGRPIANSTAYIVNSrg 1825
Cdd:cd05907 205 FDLavgGRLrfaASGGAPLPAELLHFFR--ALGIPVYEGYGLTETSAVVTLNPPGDNRIGT--VGKPLPGVEVRIADD-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1826 rlqpmgviGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDD-QVKIRGYRIELG 1904
Cdd:cd05907 279 --------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPE 344
|
410
....*....|....*...
gi 2040046167 1905 EIEAALRQIDGVKEAAVI 1922
Cdd:cd05907 345 PIENALKASPLISQAVVI 362
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
489-961 |
8.38e-33 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 134.55 E-value: 8.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP 568
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 glsvsgfsgETLEvnlsslRTEPaeNEPvcahtdggslAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI 648
Cdd:cd05969 81 ---------ELYE------RTDP--EDP----------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 VLKSSFSFDASIWQLFW--WMiPGASMYLlpQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQ-VEMETEEKRTSla 725
Cdd:cd05969 134 WCTADPGWVTGTVYGIWapWL-NGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgDELARKYDLSS-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 726 ktLKRVFAGGEALAPQtAARFARSLPETAVIHGYGPTEaTVDAAFFRYDHEKDRERmrlPIGKPVPGARLYILDSEKAVQ 805
Cdd:cd05969 209 --LRFIHSVGEPLNPE-AIRWGMEVFGVPIHDTWWQTE-TGSIMIANYPCMPIKPG---SMGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 806 PIGVAGELYIAGA--GVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEV 883
Cdd:cd05969 282 PPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 884 EAALRQIDGVREAAVVARTEGEETELY-AYIEGQDQKTARTELG--------KRLPAYMMPSSFIEMREWPVTPSGKLDR 954
Cdd:cd05969 355 ESALMEHPAVAEAGVIGKPDPLRGEIIkAFISLKEGFEPSDELKeeiinfvrQKLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
....*..
gi 2040046167 955 KALPAPD 961
Cdd:cd05969 435 RVLKAKE 441
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1501-1984 |
8.66e-33 |
|
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: 135.33 E-value: 8.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1501 ETISRLFEYQAAKTPHAPA-VIYDRQT-LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAY 1578
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAiADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1579 LPVTEDMPTERLEWMLSDSNAV-MLLQSDRL---ESHMAGKRLFIEDIQLEAGISANN----PEQQGGPDSLAYIMYTSG 1650
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTaAVIAVDAQvmdAIFQSGVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1651 STGTPKGVMVEQRG----VVRLVKNSDMAFSPEDRIL----LTASLGFdamtFEVFGPLLNGACLYISdkETYLDSDRLK 1722
Cdd:cd05923 161 TTGLPKGAVIPQRAaesrVLFMSTQAGLRHGRHNVVLglmpLYHVIGF----FAVLVAALALDGTYVV--VEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1723 TFIQQNGITTLWLTSSLFNQL---SEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALwNGYGPTE--NTTFSTCF 1797
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKV-NIYGTTEamNSLYMRDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1798 RIEHEykhsipiGRPIANSTAYIVNSRGRLQ---PMGVIGELCV--GGDGLARGYFGRPELTKEKFVpnpftpgERMYRT 1872
Cdd:cd05923 314 RTGTE-------MRPGFFSEVRIVRIGGSPDealANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ-------DGWYRT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1873 GDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQaEMNIEKvrSLL 1952
Cdd:cd05923 380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPR-EGTLSA--DEL 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 2040046167 1953 SQ-----QLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05923 457 DQfcrasELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1096-1382 |
9.56e-33 |
|
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: 133.77 E-value: 9.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1096 LDRARLDEVFRQLIRRHESLRTSFEtgADGEpvQRIHDDVPFQLME-----LAAAEDFV------------RPFRLQEAP 1158
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVFL--DDGT--QQILPEVPWYGITvhdlrGLSEEEAEaaleelrerlshRVLDVERGP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1159 LFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASR--TLHPLRIQYKDYAVWQQAFKQgEAYNRQEAYWLK 1236
Cdd:cd19535 113 LFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPgePLPPLELSFRDYLLAEQALRE-TAYERARAYWQE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1237 QLDG-----ELPVLELPADNARPAVRsfagdHVSFSLDADTSSGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIG 1311
Cdd:cd19535 192 RLPTlppapQLPLAKDPEEIKEPRFT-----RREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLN 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1312 SPIAGRA--HKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPfeelvdRLDVVRDMSR 1382
Cdd:cd19535 267 LTLFNRLplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYS------GVVVVRRLLR 333
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1527-1984 |
9.68e-33 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 133.76 E-value: 9.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSD 1606
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 RLeshmagkrlfiediqleagisannpeqqggpDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILl 1684
Cdd:cd05935 82 EL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTglTPSDVIL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1685 tASLGFdamtFEVFGpLLNGACLYISDKETYL-----DSDRLKTFIQQNGITTLWLTSSLFNQL---SEQNERTFSDLSR 1756
Cdd:cd05935 130 -ACLPL----FHVTG-FVGSLNTAVYVGGTYVlmarwDRETALELIEKYKVTFWTNIPTMLVDLlatPEFKTRDLSSLKV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1757 LILGGEALSPNHVNRVRNTApDLALWNGYGPTEntTFSTCFRIEHEYKHSIPIGRPIANSTAYIVN-SRGRLQPMGVIGE 1835
Cdd:cd05935 204 LTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTE--TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1836 LCVGGDGLARGYFGRPELTKEKFVpnpFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDG 1915
Cdd:cd05935 281 IVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1916 VKEAAVIVRTGPSGHKELLAYMSLQAEMNI----EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05935 358 I*EVCVISVPDERVGEEVKAFIVLRPEYRGkvteEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
489-954 |
1.01e-32 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 135.35 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTG- 567
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 568 ---PGLSVSGFSGETLEVNLSSLRTEPAEN---EPVCAHTDGGS--------LAYVIYTSGSTGTPKGVAVEHR--QAAA 631
Cdd:TIGR02262 111 allPVIKAALGKSPHLEHRVVVGRPEAGEVqlaELLATESEQFKpaatqaddPAFWLYSSGSTGMPKGVVHTHSnpYWTA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 632 FLSGMQRqFPLTEDDVIVLKSSFSFDASIWQ-LFWWMIPGASMYLLPQgwEKDPALMTEAFTNEGVTTAHFIPAMANSFL 710
Cdd:TIGR02262 191 ELYARNT-LGIREDDVCFSAAKLFFAYGLGNaLTFPMSVGATTVLMGE--RPTPDAVFDRLRRHQPTIFYGVPTLYAAML 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 711 DQVEMETEEKrtslaKTLKRVFAGGEALAPQTAARFARSLPeTAVIHGYGPTEA-----TVDAAFFRYDHEkdrermrlp 785
Cdd:TIGR02262 268 ADPNLPSEDQ-----VRLRLCTSAGEALPAEVGQRWQARFG-VDIVDGIGSTEMlhiflSNLPGDVRYGTS--------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 786 iGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLddpfyrGErMYQTGDLARWLPDGTVEWLG 865
Cdd:TIGR02262 333 -GKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQ------GE-WTRSGDKYVRNDDGSYTYAG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 866 RMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV--ARTEGeETELYAYI-EGQDQKTARTEL----GKRLPAYMMPSSF 938
Cdd:TIGR02262 405 RTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVgvADEDG-LIKPKAFVvLRPGQTALETELkehvKDRLAPYKYPRWI 483
|
490
....*....|....*.
gi 2040046167 939 IEMREWPVTPSGKLDR 954
Cdd:TIGR02262 484 VFVDDLPKTATGKIQR 499
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
12-355 |
6.82e-32 |
|
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: 131.62 E-value: 6.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQSRLQFv 91
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEED-GVPYQLILEEDEATPKL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 92 DISHLDETAKETFVDQfehdDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKEQ 171
Cdd:cd19538 81 EIKEVDEEELESEINE----AVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 172 LPDFEPVhP--FSKYIKWLMR--QDRKEAE-------AFWKTRLIDVKQTASLP---KTSSSSKGKLEQMAFTLSKEQTE 237
Cdd:cd19538 157 APELAPL-PvqYADYALWQQEllGDESDPDsliarqlAYWKKQLAGLPDEIELPtdyPRPAESSYEGGTLTFEIDSELHQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 238 GLRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSDleDVEKMVGLFINTIPVRVK-SGPESFLTLVSHL 316
Cdd:cd19538 236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDtSGNPSFRELLERV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2040046167 317 QQESLKAEAYSYYPLYDI-----QAQSMLKHELFDHIVVFENIP 355
Cdd:cd19538 314 KETNLEAYEHQDIPFERLvealnPTRSRSRHPLFQIMLALQNTP 357
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1639-1981 |
2.51e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 127.78 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQRGVV---RLVKNSdMAFSPEDRILLTASLgfdamtFEVFGPLLN--------GACL 1707
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnngYFIGER-LGLTEQDRLCIPVPL------FHCFGSVLGvlaclthgATMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1708 YISdkETYLDSDRLKTfIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRNTAPDLALWNG 1784
Cdd:cd05917 74 FPS--PSFDPLAVLEA-IEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLrtgIMAGAPCPPELMKRVIEVMNMKDVTIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1785 YGPTENTTFSTCFRIEHEYKHSI-PIGRPIANSTAYIVNSRGRLQPM-GVIGELCVGGDGLARGYFGRPELTKEKFvpnp 1862
Cdd:cd05917 151 YGMTETSPVSTQTRTDDSIEKRVnTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAI---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1863 ftPGERMYRTGDLARWLKDGTIDYIGRMDDQVkIRG-YRIELGEIEAALRQIDGVKEAAVIvrtGPSGHK---ELLAYMS 1938
Cdd:cd05917 227 --DGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVV---GVPDERygeEVCAWIR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2040046167 1939 LQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:cd05917 301 LKegAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1527-1984 |
3.19e-31 |
|
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: 129.56 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSdsnavmllqsd 1606
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLR----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 rleshMAGKRLFIEDIQLEAGISannpeqqggpDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMA--FSPEDRILL 1684
Cdd:cd05973 70 -----TSGARLVVTDAANRHKLD----------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAvdLRPEDSFWN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1685 TASLGFD-AMTFEVFGPLLNG--ACLY---ISDKETYldsdrlkTFIQQNGITTLWLTSSLFNQL----SEQNERTFSDL 1754
Cdd:cd05973 135 AADPGWAyGLYYAITGPLALGhpTILLeggFSVESTW-------RVIERLGVTNLAGSPTAYRLLmaagAEVPARPKGRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1755 SRLILGGEALSPNhVNRVRNTAPDLALWNGYGPTENTTF-STCFRIEHEYkHSIPIGRPIANSTAYIVNSRGRLQPMGVI 1833
Cdd:cd05973 208 RRVSSAGEPLTPE-VIRWFDAALGVPIHDHYGQTELGMVlANHHALEHPV-HAGSAGRAMPGWRVAVLDDDGDELGPGEP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1834 GELCVGGDGLA----RGYFGRPELtkekfvpnpfTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAA 1909
Cdd:cd05973 286 GRLAIDIANSPlmwfRGYQLPDTP----------AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1910 LRQIDGVKEAAVIVRTGPSGHKELLAYMSLQA-----EMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05973 356 LIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGghegtPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1525-1910 |
3.21e-31 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 130.17 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLlq 1604
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 sdrleshmagkrlFIEDiqleagisannpeqqgGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKN-SDMA-FSPEDRI 1682
Cdd:cd17640 82 -------------VVEN----------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSlSDIVpPQPGDRF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1683 LLTASLGFDA-MTFEVFGPLLNGACLYISDKetYLDSDrLKTFIQQNGITTLWLTSSLFNQLSEQnertFSDLSR----- 1756
Cdd:cd17640 133 LSILPIWHSYeRSAEYFIFACGCSQAYTSIR--TLKDD-LKRVKPHYIVSVPRLWESLYSGIQKQ----VSKSSPikqfl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1757 ---LILGGE---ALS-----PNHVNRVRNtAPDLALWNGYGPTENTTFSTCFRIEHEYKHSipIGRPIANSTAYIV--NS 1823
Cdd:cd17640 206 flfFLSGGIfkfGISgggalPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGS--VGRPLPGTEIKIVdpEG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1824 RGRLQPmGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKIR-GYRIE 1902
Cdd:cd17640 283 NVVLPP-GEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVE 355
|
....*...
gi 2040046167 1903 LGEIEAAL 1910
Cdd:cd17640 356 PQPIEEAL 363
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1503-1986 |
6.31e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 129.98 E-value: 6.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1503 ISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRAN-GVGSESVVALLTSRTPELAVGILGILKAGGAYLPV 1581
Cdd:PRK06839 4 IAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 TEDMPTERLEWMLSDSNAVMLLQSDRLES---HMAGKRLFIEDIQLE--AGISANNPE--QQGGPDSLAYIMYTSGSTGT 1654
Cdd:PRK06839 84 NIRLTENELIFQLKDSGTTVLFVEKTFQNmalSMQKVSYVQRVISITslKEIEDRKIDnfVEKNESASFIICYTSGTTGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1655 PKGVMVEQRGVVRLVKNSDMA--FSPEDR-ILLTASLGFDAMTFEVFGPLLNGACLYISDKetyLDSDRLKTFIQQNGIT 1731
Cdd:PRK06839 164 PKGAVLTQENMFWNALNNTFAidLTMHDRsIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRK---FEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1732 TLWLTSSLFNQLSEQNERTFSDLS--RLILGGEALSPNHVNRVRNTApDLALWNGYGPTEntTFSTCFRIEHEYKHSIP- 1808
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFETTNLQsvRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTE--TSPTVFMLSEEDARRKVg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1809 -IGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEkfvpnpfTPGERMYRTGDLARWLKDGTIDYI 1887
Cdd:PRK06839 318 sIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE-------TIQDGWLCTGDLARVDEDGFVYIV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1888 GRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI--EKVRSLLSQQLPGFMIPAHL 1965
Cdd:PRK06839 391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLieKDVIEHCRLFLAKYKIPKEI 470
|
490 500
....*....|....*....|.
gi 2040046167 1966 VELAALPLTQNGKLDRRALPE 1986
Cdd:PRK06839 471 VFLKELPKNATGKIQKAQLVN 491
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1511-1988 |
7.58e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 128.95 E-value: 7.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELnqranRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERL 1590
Cdd:PRK07787 10 AAAADIADAVRIGGRVLSRSDL-----AGAATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 EWMLSDSNAVMLLqsDRLESHMAGkrLFIEDIQLEAGISANNPEQqgGPDSLAYIMYTSGSTGTPKGVMVEQRGVvrlVK 1670
Cdd:PRK07787 85 RHILADSGAQAWL--GPAPDDPAG--LPHVPVRLHARSWHRYPEP--DPDAPALIVYTSGTTGPPKGVVLSRRAI---AA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1671 NSDM-----AFSPEDrILLTA---------SLGfdamtfeVFGPLLNGACLYISDK---ETYLDSDRLKT---FiqqnGI 1730
Cdd:PRK07787 156 DLDAlaeawQWTADD-VLVHGlplfhvhglVLG-------VLGPLRIGNRFVHTGRptpEAYAQALSEGGtlyF----GV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1731 TTLWltsslfNQLSEQNE--RTFSDlSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTEnTTFSTCFRIEHEYKhsiP 1808
Cdd:PRK07787 224 PTVW------SRIAADPEaaRALRG-ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE-TLITLSTRADGERR---P 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1809 --IGRPIANSTAYIVNSRGRLQPMGV--IGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTI 1884
Cdd:PRK07787 293 gwVGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1885 DYIGRMD-DQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPA 1963
Cdd:PRK07787 367 RIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQLSVHKRPR 446
|
490 500
....*....|....*....|....*
gi 2040046167 1964 HLVELAALPLTQNGKLDRRALPEPE 1988
Cdd:PRK07787 447 EVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
456-957 |
8.62e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 130.26 E-value: 8.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 456 EPAAPLAPTLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLK 535
Cdd:PRK06155 14 DPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 536 AGGAYVPLDPDYPEERLRYMLADSGARLLVTGPGLS------------------VSGFSGETLEVNLSSLRTEPAENEPV 597
Cdd:PRK06155 94 LGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLaaleaadpgdlplpavwlLDAPASVSVPAGWSTAPLPPLDAPAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 598 CAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLP 677
Cdd:PRK06155 174 AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 678 QgweKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVemETEEKRTSlakTLKRvfaggeALAPQTAARFARSLPE---TA 754
Cdd:PRK06155 254 R---FSASGFWPAVRRHGATVTYLLGAMVSILLSQP--ARESDRAH---RVRV------ALGPGVPAALHAAFRErfgVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 755 VIHGYGPTEATvdaAFFRYDHEKDRermrlP--IGKPVPGARLYILDSEKAVQPIGVAGELYIAGA---GVARGYLNRPE 829
Cdd:PRK06155 320 LLDGYGSTETN---FVIAVTHGSQR-----PgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 830 LTEERFLDDPFYRGERMYQTgdlarwlPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA-RTEGEETE 908
Cdd:PRK06155 392 KTVEAWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPvPSELGEDE 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 909 LYAYI---EGQD---QKTARTELGkRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK06155 465 VMAAVvlrDGTAlepVALVRHCEP-RLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
473-961 |
9.54e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 130.05 E-value: 9.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERL 552
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 553 RYMLADSGARLLV-----TG---------PGLSVSGFSGETLEVNLSSLRT-----EPAENEPVCAHTDGGSLayVIYTS 613
Cdd:PRK07788 139 AEVAAREGVKALVyddefTDllsalppdlGRLRAWGGNPDDDEPSGSTDETlddliAGSSTAPLPKPPKPGGI--VILTS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 614 GSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKssfsfdASIWQLFWWMIPGASMYL-----LPQGWekDPALMT 688
Cdd:PRK07788 217 GTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLP------APMFHATGWAHLTLAMALgstvvLRRRF--DPEATL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 689 EAFTNEGVTTAHFIPAMANSFLDqVEMETEEKR-TSlakTLKRVFAGGEALAPQTAARFARSLPEtaVIHG-YGPTE--- 763
Cdd:PRK07788 289 EDIAKHKATALVVVPVMLSRILD-LGPEVLAKYdTS---SLKIIFVSGSALSPELATRALEAFGP--VLYNlYGSTEvaf 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 764 ATVdaaffrydheKDRERMRL-P--IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLN-RPELTEERFLddp 839
Cdd:PRK07788 363 ATI----------ATPEDLAEaPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgRDKQIIDGLL--- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 840 fyrgermyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVArTEGEET--ELYAYI---- 913
Cdd:PRK07788 430 --------SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG-VDDEEFgqRLRAFVvkap 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2040046167 914 -EGQDQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALPAPD 961
Cdd:PRK07788 501 gAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1498-1991 |
1.12e-30 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 129.88 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1498 PKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGA 1577
Cdd:PRK06155 18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1578 YLPVTEDMPTERLEWMLSDSNAVML-LQSDRLES--HMAGKRLFIEDIQLEAGISANNPEQ------------------- 1635
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLvVEAALLAAleAADPGDLPLPAVWLLDAPASVSVPAgwstaplppldapapaaav 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1636 QGGpDSLAyIMYTSGSTGTPKGVMVEQRGVVRLVKNS--DMAFSPEDRILLTASLgFDAMTFEVFGP-LLNGACLYISDK 1712
Cdd:PRK06155 178 QPG-DTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSaeDLEIGADDVLYTTLPL-FHTNALNAFFQaLLAGATYVLEPR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1713 etyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTEnTT 1792
Cdd:PRK06155 255 ---FSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTE-TN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1793 FSTCFRIEHEYKHSipIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGD---GLARGYFGRPELTKEKFVPNPFTPGERM 1869
Cdd:PRK06155 331 FVIAVTHGSQRPGS--MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1870 YRTGdlarwlkDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEK-- 1947
Cdd:PRK06155 409 VRDA-------DGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPva 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2040046167 1948 -VRSLLSqQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTA 1991
Cdd:PRK06155 482 lVRHCEP-RLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
480-957 |
1.30e-30 |
|
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: 127.59 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 480 PAVRFSGGILTYRELDQYTNQLAIRLKKKGVA-KESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLAd 558
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 559 sgarllvtgpglsvsgfsgetlevnlsslRTEPAEnePVCAHT-----DGGSLAYviyTSGSTGTPKGVAVEHRQAAAFL 633
Cdd:cd05958 81 -----------------------------KARITV--ALCAHAltasdDICILAF---TSGTTGAPKATMHFHRDPLASA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 634 SGMQRQ-FPLTEDDVIV----LKSSFSFDASiwqLFWWMIPGASMYLLPQgweKDPALMTEAFTNEGVTTAHFIPAMANS 708
Cdd:cd05958 127 DRYAVNvLRLREDDRFVgsppLAFTFGLGGV---LLFPFGVGASGVLLEE---ATPDLLLSAIARYKPTVLFTAPTAYRA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLDQVEmETEEKRTSLAKTLkrvfAGGEALAPQTAARF--ARSLPetaVIHGYGPTEATvdaAFFRYDHEKDRERMRLpi 786
Cdd:cd05958 201 MLAHPD-AAGPDLSSLRKCV----SAGEALPAALHRAWkeATGIP---IIDGIGSTEMF---HIFISARPGDARPGAT-- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 787 GKPVPGARLYILDSEKAVQPIGVAGELYIAGAgvargylnrpelTEERFLDDP----FYRGERMYqTGDLARWLPDGTVE 862
Cdd:cd05958 268 GKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------------TGCRYLADKrqrtYVQGGWNI-TGDTYSRDPDGYFR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 863 WLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV-ARTEGEETELYAYI-----EGQDQKTAR--TELGKR-LPAYM 933
Cdd:cd05958 335 HQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVvlrpgVIPGPVLARelQDHAKAhIAPYK 414
|
490 500
....*....|....*....|....
gi 2040046167 934 MPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05958 415 YPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1498-1921 |
1.31e-30 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 130.38 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1498 PKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGG- 1576
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1577 ---------------------------------AYLPVTEDMPTERLEWMLSDSNAVMLLQSDRLESHMAGKRLfiEDIQ 1623
Cdd:PRK08279 114 vallntqqrgavlahslnlvdakhlivgeelveAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPT--TNPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1624 LEAGISANNPeqqggpdslAYIMYTSGSTGTPKGVMVEQRgvvRLVKNSD-----MAFSPEDRILLTASLgFDAMTFEV- 1697
Cdd:PRK08279 192 SRSGVTAKDT---------AFYIYTSGTTGLPKAAVMSHM---RWLKAMGgfgglLRLTPDDVLYCCLPL-YHNTGGTVa 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1698 FGP-LLNGACLYISDKetyldsdrlktF--------IQQNGITTLW----LTSSLFNQLSEQNERTFSdlSRLILGgeal 1764
Cdd:PRK08279 259 WSSvLAAGATLALRRK-----------FsasrfwddVRRYRATAFQyigeLCRYLLNQPPKPTDRDHR--LRLMIG---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1765 spnhvNRVRntaPDlaLWN-------------GYGPTE-NTTFS-------TCFRIEHEYKHSIPIGRPIANSTAYIVNS 1823
Cdd:PRK08279 322 -----NGLR---PD--IWDefqqrfgiprileFYAASEgNVGFInvfnfdgTVGRVPLWLAHPYAIVKYDVDTGEPVRDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1824 RGRLQPMGViGE--LCVGG-DGLAR--GYfGRPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRG 1898
Cdd:PRK08279 392 DGRCIKVKP-GEvgLLIGRiTDRGPfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKG 469
|
490 500
....*....|....*....|...
gi 2040046167 1899 YRIELGEIEAALRQIDGVKEAAV 1921
Cdd:PRK08279 470 ENVATTEVENALSGFPGVEEAVV 492
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
464-957 |
1.67e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 129.48 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFS-GGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVP 542
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 543 LDPDYPEERLRYMLADSGARLLVT-----------------------GPGLSVSGFSGETLEVNLSSL--RTEPAeNEPV 597
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFAptlfkqtrpvdlilplqnqlpqlQQIVGVDKLAPATSSLSLSQIiaDYEPL-TTAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 598 CAHTDggSLAYVIYTSGSTGTPKGVAVEHRQ----AAAFLSGMQrqfpLTEDDVIVLKSSFSFDASIWQ-LFWWMIPGAS 672
Cdd:PRK06087 183 TTHGD--ELAAVLFTSGTEGLPKGVMLTHNNilasERAYCARLN----LTWQDVFMMPAPLGHATGFLHgVTAPFLIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 673 MYLLpQGWEKDPALmtEAFTNEGVTTAHfipaMANSFLDQVEMETEEKRTSLAkTLKRVFAGGeALAPQTAARFARSlpe 752
Cdd:PRK06087 257 SVLL-DIFTPDACL--ALLEQQRCTCML----GATPFIYDLLNLLEKQPADLS-ALRFFLCGG-TTIPKKVARECQQ--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 753 taviHG------YGPTEaTVDAAFFRYDheKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLN 826
Cdd:PRK06087 325 ----RGikllsvYGSTE-SSPHAVVNLD--DPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 827 RPELTeERFLDDpfyrgERMYQTGDLARWLPDGTVEWLGRMDgQVKIR-GYRIEPGEVEAALRQIDGVREAAVVARTE-- 903
Cdd:PRK06087 398 EPELT-ARALDE-----EGWYYSGDLCRMDEAGYIKITGRKK-DIIVRgGENISSREVEDILLQHPKIHDACVVAMPDer 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 904 -GEETELYAYIEGQDQKTARTEL-----GKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK06087 471 lGERSCAYVVLKAPHHSLTLEEVvaffsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1498-1977 |
2.37e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 128.71 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1498 PKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGA 1577
Cdd:PRK06164 7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1578 YLPVTEDMPTERLEWMLSDSNAVMLL---------------------------------QSDRLESHMAGKRLFIEDIQL 1624
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaavppdalpplraiavvddAADATPAPAPGARVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1625 EAGISANNPEQqGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILLTA----SLGFDAmtfeVF 1698
Cdd:PRK06164 167 PAPPAAAGERA-ADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYgyDPGAVLLAALpfcgVFGFST----LL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1699 GPLLNGACLYIsdkETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQ--NERTFSDLSRLilGGEALSP---NHVNRVR 1773
Cdd:PRK06164 242 GALAGGAPLVC---EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTagERADFPSARLF--GFASFAPalgELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1774 ntAPDLALWNGYGPTENTTFSTCFRIEHEYKHSI-PIGRPI-ANSTAYIVNSR-GRLQPMGVIGELCVGGDGLARGYFGR 1850
Cdd:PRK06164 317 --ARGVPLTGLYGSSEVQALVALQPATDPVSVRIeGGGRPAsPEARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1851 PELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTgPSGH 1930
Cdd:PRK06164 395 PDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-RDGK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2040046167 1931 KELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNG 1977
Cdd:PRK06164 468 TVPVAFVIPTdgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1506-1984 |
2.85e-30 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 129.53 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1506 LFEYQAAKTPHAPAVIYDRQ-----TLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLP 1580
Cdd:cd05968 66 LLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1581 VTEDMPTERLEWMLSDSNAVMLLQSD----------------RLESHMAG-------KRLFIEDIQLEAGISANNPEQQG 1637
Cdd:cd05968 146 IFSGFGKEAAATRLQDAEAKALITADgftrrgrevnlkeeadKACAQCPTvekvvvvRHLGNDFTPAKGRDLSYDEEKET 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 GPDSLA--------YIMYTSGSTGTPKGVmVEQRGVVRLVKNSDMAF----SPEDRILLTASLGFDAMTFEVFGPLLNGA 1705
Cdd:cd05968 226 AGDGAErtesedplMIIYTSGTTGKPKGT-VHVHAGFPLKAAQDMYFqfdlKPGDLLTWFTDLGWMMGPWLIFGGLILGA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1706 CLYISD-KETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTF--SDLSRL-ILG--GEALSPNHVNRVRNTAPD- 1778
Cdd:cd05968 305 TMVLYDgAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVnaHDLSSLrVLGstGEPWNPEPWNWLFETVGKg 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1779 -LALWNGYGPTENTTFSTCFRIEHEYKhSIPIGRPIANSTAYIVNSRGRLQPmGVIGELCVGGD--GLARGYFGRPeltk 1855
Cdd:cd05968 385 rNPIINYSGGTEISGGILGNVLIKPIK-PSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWRDE---- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1856 EKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLA 1935
Cdd:cd05968 459 DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVC 538
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1936 YMSLQ-----AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05968 539 FVVLKpgvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
11-331 |
5.23e-30 |
|
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: 125.89 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 11 YPLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQSRLQF 90
Cdd:cd20484 2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEED-GVPFQKIEPSKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 91 VDISHLDETAketfVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKE 170
Cdd:cd20484 81 EDISSLKESE----IIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 171 QLPDFEPVHP-FSKYIKW----LMRQDRKEAEAFWKTRLIDVKQTASLP----KTSSSS-KGKLEQMafTLSKEQTEGLR 240
Cdd:cd20484 157 KQPTLASSPAsYYDFVAWeqdmLAGAEGEEHRAYWKQQLSGTLPILELPadrpRSSAPSfEGQTYTR--RLPSELSNQIK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 241 KLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSdlEDVEKMVGLFINTIPVRVK-SGPESFLTLVSHLQQE 319
Cdd:cd20484 235 SFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPE--ERFDSLIGYFINMLPIRSRiLGEETFSDFIRKLQLT 312
|
330
....*....|..
gi 2040046167 320 SLKAEAYSYYPL 331
Cdd:cd20484 313 VLDGLDHAAYPF 324
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
488-920 |
7.07e-30 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 126.32 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 488 ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTg 567
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 568 pglsvsgfsgetlevnlsslrtepaENepvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQaaaFLSGMQR-----QFPL 642
Cdd:cd17640 84 -------------------------EN-------DSDDLATIIYTSGTTGNPKGVMLTHAN---LLHQIRSlsdivPPQP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 643 TEDDVIVLKSSFSFDASiwqlfwwmipgASMYLLPQGwekdpalMTEAFTNEGVTTAHF----------IP----AMANS 708
Cdd:cd17640 129 GDRFLSILPIWHSYERS-----------AEYFIFACG-------CSQAYTSIRTLKDDLkrvkphyivsVPrlweSLYSG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLDQVEMETEEKRtSLAKTL------KRVFAGGEALaPQTAARFARSLpETAVIHGYGPTEATVDAAFFRYDHEKdrerm 782
Cdd:cd17640 191 IQKQVSKSSPIKQ-FLFLFFlsggifKFGISGGGAL-PPHVDTFFEAI-GIEVLNGYGLTETSPVVSARRLKCNV----- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 783 RLPIGKPVPGARLYILDSE-KAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFyrgermYQTGDLARWLPDGTV 861
Cdd:cd17640 263 RGSVGRPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGEL 336
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 862 EWLGRM-DGQVKIRGYRIEPGEVEAALRQIDGVREAAVVartegeetelyayieGQDQKT 920
Cdd:cd17640 337 VLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV---------------GQDQKR 381
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1517-1984 |
9.77e-30 |
|
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: 125.28 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1517 APAVIYDRQTLTYRELNQRANRIAAALRANGVGSE-SVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLS 1595
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1596 DSNAVMLLQSDRLEShmagkrlfIEDIQLeagisannpeqqggpdslayIMYTSGSTGTPKGVMVEQRGVV---RLVKNS 1672
Cdd:cd05958 81 KARITVALCAHALTA--------SDDICI--------------------LAFTSGTTGAPKATMHFHRDPLasaDRYAVN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1673 DMAFSPEDRILLTASLGFdamTFEVFG----PLLNGACLYISDKETyldSDRLKTFIQQNGITTLWLTSSLFNQLSEQNE 1748
Cdd:cd05958 133 VLRLREDDRFVGSPPLAF---TFGLGGvllfPFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAMLAHPD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1749 RTFSDLSRLIL---GGEALsPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSipIGRPIANSTAYIVNSRG 1825
Cdd:cd05958 207 AAGPDLSSLRKcvsAGEAL-PAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGA--TGKPVPGYEAKVVDDEG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1826 RLQPMGVIGELCVGGDglaRGYFGRPELTKEKFVpnpftPGERMYrTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGE 1905
Cdd:cd05958 284 NPVPDGTIGRLAVRGP---TGCRYLADKRQRTYV-----QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1906 IEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMN-----IEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLD 1980
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
....
gi 2040046167 1981 RRAL 1984
Cdd:cd05958 435 RFAL 438
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1500-1986 |
2.75e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 125.55 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1500 HETISRLFEYQAAKTPHAPAVIYDR------QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILK 1573
Cdd:PRK13295 23 DRTINDDLDACVASCPDKTAVTAVRlgtgapRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1574 AGGAYLPVtedMPTER---LEWMLSDSNAVML-----------------LQS----------------DRLESHMAGKRL 1617
Cdd:PRK13295 103 IGAVLNPL---MPIFRereLSFMLKHAESKVLvvpktfrgfdhaamarrLRPelpalrhvvvvggdgaDSFEALLITPAW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1618 fiEDIQLEAGISANNpeqQGGPDSLAYIMYTSGSTGTPKGVMVEQR----GVVRLVKNsdMAFSPEDRILLTASLGFdaM 1693
Cdd:PRK13295 180 --EQEPDAPAILARL---RPGPDDVTQLIYTSGTTGEPKGVMHTANtlmaNIVPYAER--LGLGADDVILMASPMAH--Q 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1694 TFEVFG---PLLNGACLYISDKetyLDSDRLKTFIQQNGIT-TLWLTSSLFNQLSEQNE--RTFSDLSRLILGGEALSPN 1767
Cdd:PRK13295 251 TGFMYGlmmPVMLGATAVLQDI---WDPARAAELIRTEGVTfTMASTPFLTDLTRAVKEsgRPVSSLRTFLCAGAPIPGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1768 HVNRVRnTAPDLALWNGYGPTENTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGY 1847
Cdd:PRK13295 328 LVERAR-AALGAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1848 FGRPELTKekfvpnpfTPGERMYRTGDLARWLKDGTIDYIGRMDDqVKIRG-YRIELGEIEAALRQIDGVKEAAVIVRTG 1926
Cdd:PRK13295 407 LKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGRSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPD 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1927 PSGHKELLAYMSLQAEMNI---EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK13295 478 ERLGERACAFVVPRPGQSLdfeEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
12-327 |
4.08e-29 |
|
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: 122.95 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLF-HSLLDQESrAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFI-HKNVAKPRQVVLKERQSRLQ 89
Cdd:cd19532 3 PMSFGQSRFWFlQQYLEDPT-TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFtDPEDGEPMQGVLASSPLRLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 90 FVDISHLDEtAKETFvdqfeHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKalGK 169
Cdd:cd19532 82 HVQISDEAE-VEEEF-----ERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--GQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 170 EQLPdfepvhPFSKYIKWLMRQdRKEAE--------AFWKTRLIDVKQTASL---PKTSS---SSKGKLEQMAFTLSKEQ 235
Cdd:cd19532 154 PLLP------PPLQYLDFAARQ-RQDYEsgaldedlAYWKSEFSTLPEPLPLlpfAKVKSrppLTRYDTHTAERRLDAAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 236 TEGLRKLALQAGAT-----LnTVFQALwgiiLQKINRCDDAVFGSVISGRPSdlEDVEKMVGLFINTIPVRVKSGP-ESF 309
Cdd:cd19532 227 AARIKEASRKLRVTpfhfyL-AALQVL----LARLLDVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRRDPsQTF 299
|
330
....*....|....*...
gi 2040046167 310 LTLVSHLQQESLKAEAYS 327
Cdd:cd19532 300 ADVLKETRDKAYAALAHS 317
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
463-957 |
5.82e-29 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 123.77 E-value: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 463 PTLHSFFTRRAALSPNLPA-VRFSGGI-LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAY 540
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAiADPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 541 VPLDPDYPEERLRYMLADSGARLLVTGPGLSVSGFSgETLEVNLSSLRTEPAENEPvCAHTDG--------GSLAYVIYT 612
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAI-FQSGVRVLALSDLVGLGEP-ESAGPLiedpprepEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 613 SGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDD------VIVLKSSFSFDAsiwqLFWWMIPGASMYLLPQgwEKDPAL 686
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRhnvvlgLMPLYHVIGFFA----VLVAALALDGTYVVVE--EFDPAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 687 MTEAFTNEGVTTAHFIPAMANSFLDQVEMeTEEKRTSLAKTlkrVFAGgeALAPQTA-ARFARSLPETAVIHgYGPTEAT 765
Cdd:cd05923 233 ALKLIEQERVTSLFATPTHLDALAAAAEF-AGLKLSSLRHV---TFAG--ATMPDAVlERVNQHLPGEKVNI-YGTTEAM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 766 VdaafFRYDHE-KDRERMRLPIGKPVPGARlyILDSEKAVQPIGVAGELYIAGAGVA--RGYLNRPELTEERFLDdpfyr 842
Cdd:cd05923 306 N----SLYMRDaRTGTEMRPGFFSEVRIVR--IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD----- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 843 geRMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV---------------VARTEGEET 907
Cdd:cd05923 375 --GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVigvaderwgqsvtacVVPREGTLS 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 908 ElyayiEGQDQKTARTELG--KRlpaymmPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05923 453 A-----DELDQFCRASELAdfKR------PRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1524-1984 |
9.26e-29 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 124.24 E-value: 9.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1524 RQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTED-MPT---ERLEwmlsDSNA 1599
Cdd:PRK04319 71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAfMEEavrDRLE----DSEA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1600 VMLLQSDRLESHMAGKRL------FI--EDIQLEAGISANNPEQQGGPDSL----------AYIMYTSGSTGTPKGVMVE 1661
Cdd:PRK04319 147 KVLITTPALLERKPADDLpslkhvLLvgEDVEEGPGTLDFNALMEQASDEFdiewtdredgAILHYTSGSTGKPKGVLHV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1662 QRGVV------RLVknsdMAFSPEDRILLTASLGF-DAMTFEVFGPLLNGACLYISDKEtyLDSDRLKTFIQQNGItTLW 1734
Cdd:PRK04319 227 HNAMLqhyqtgKYV----LDLHEDDVYWCTADPGWvTGTSYGIFAPWLNGATNVIDGGR--FSPERWYRILEDYKV-TVW 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1735 LTS-SLFNQLSEQNERTFS--DLS--RLILG-GEALSPNHVnRVRNTAPDLALWNGYGPTE-------NTtfsTCFRIEh 1801
Cdd:PRK04319 300 YTApTAIRMLMGAGDDLVKkyDLSslRHILSvGEPLNPEVV-RWGMKVFGLPIHDNWWMTEtggimiaNY---PAMDIK- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1802 eykhsiP--IGRPIANSTAYIVNSRGRLQPMGVIGELCV--GGDGLARGYFGRPELTKEKFVPNpftpgerMYRTGDLAR 1877
Cdd:PRK04319 375 ------PgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD-------WYVSGDSAY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1878 WLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQA-----EMNIEKVRSLL 1952
Cdd:PRK04319 442 MDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPgyepsEELKEEIRGFV 521
|
490 500 510
....*....|....*....|....*....|..
gi 2040046167 1953 SQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK04319 522 KKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
465-982 |
1.01e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 125.53 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALS--PNLPAVrFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVP 542
Cdd:PRK06060 6 LAGLLAEQASEAgwYDRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 543 LDPDYPEERLRYMLADSGARLLVTGPGLSvSGFSGETL----EVNLSSLRTEPAENEPVcahtDGGSLAYVIYTSGSTGT 618
Cdd:PRK06060 85 ANPELHRDDHALAARNTEPALVVTSDALR-DRFQPSRVaeaaELMSEAARVAPGGYEPM----GGDALAYATYTSGTTGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 619 PKGVAVEHRQAAAFLSGMQRQ-FPLTEDDVIVLKSSFSFDASIWQLFWW-MIPGASMYL--LPQGWEKdPALMTEAFTNe 694
Cdd:PRK06060 160 PKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFpLATGGSAVInsAPVTPEA-AAILSARFGP- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 695 gvTTAHFIPAMANSFLDQVEMETeekrtslAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEatVDAAFFryD 774
Cdd:PRK06060 238 --SVLYGVPNFFARVIDSCSPDS-------FRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTE--VGQTFV--S 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 775 HEKDRERMRlPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPE--LTEERFLDdpfyrgermyqTGDL 852
Cdd:PRK06060 305 NRVDEWRLG-TLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 853 ARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE--GEETeLYAYI-----EGQDQKTAR--- 922
Cdd:PRK06060 373 VCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVREstGAST-LQAFLvatsgATIDGSVMRdlh 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 923 TELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALpapdgaaerRVYTAPRTITEMKLAK 982
Cdd:PRK06060 452 RGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL---------RKQSPTKPIWELSLTE 502
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1494-1984 |
1.35e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 123.12 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1494 KQDYPKHETISRLFEYQAAKTphapaviydrqtlTYRELNQRANRIAAALRANGVGSESVVALL---TSRTPELAVGILG 1570
Cdd:cd12119 6 ARLHGDREIVSRTHEGEVHRY-------------TYAEVAERARRLANALRRLGVKPGDRVATLawnTHRHLELYYAVPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1571 IlkagGAYL-PVTEDMPTERLEWMLSDSNAVMLLQSDRLE----------------------SHMAGKRLfIEDIQLEAG 1627
Cdd:cd12119 73 M----GAVLhTINPRLFPEQIAYIINHAEDRVVFVDRDFLplleaiaprlptvehvvvmtddAAMPEPAG-VGVLAYEEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1628 ISANNPEQqGGPD----SLAYIMYTSGSTGTPKGVMVEQRGVV----RLVKNSDMAFSPEDRILLTASLgFDAMTFEV-F 1698
Cdd:cd12119 148 LAAESPEY-DWPDfdenTAAAICYTSGTTGNPKGVVYSHRSLVlhamAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1699 GPLLNGACLYISDKetYLDSDRLKTFIQQNGIT------TLWLtsSLFNQLsEQNERTFSDLSRLILGGEALSPNHVNRV 1772
Cdd:cd12119 226 AAAMVGAKLVLPGP--YLDPASLAELIEREGVTfaagvpTVWQ--GLLDHL-EANGRDLSSLRRVVIGGSAVPRSLIEAF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1773 RntAPDLALWNGYGPTENTTFSTCFRI---------EHEYKHSIPIGRPIANSTAYIVNSRGRLQPM--GVIGELCVGGD 1841
Cdd:cd12119 301 E--ERGVRVIHAWGMTETSPLGTVARPpsehsnlseDEQLALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1842 GLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAV 1921
Cdd:cd12119 379 WVTKSYYKNDEESEALTEDGWL-------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1922 IVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd12119 452 IGVPHPKWGERPLAVVVLKegATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
609-954 |
1.53e-28 |
|
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: 119.29 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAVEHRQAAAFLSGMQR-QFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLpqGWEKDPALM 687
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG--GENTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 688 TEAFTNEGVTTAHFIPAMANSFldqVEMETEEKRTSlaKTLKRVFAGGEaLAPQTAARFARSLPETAVIHGYGPTEATVd 767
Cdd:cd17635 84 FKILTTNAVTTTCLVPTLLSKL---VSELKSANATV--PSLRLIGYGGS-RAIAADVRFIEATGLTNTAQVYGLSETGT- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 768 AAFFRYDHEKDRERmrlPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermy 847
Cdd:cd17635 157 ALCLPTDDDSIEIN---AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 848 qTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEETELYAYIEGQDQKTARTE 924
Cdd:cd17635 228 -TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDeefGELVGLAVVASAELDENAIRA 306
|
330 340 350
....*....|....*....|....*....|....
gi 2040046167 925 L----GKRLPAYMMPSSFIEMREWPVTPSGKLDR 954
Cdd:cd17635 307 LkhtiRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
469-1052 |
1.55e-28 |
|
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: 125.59 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 469 FTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:COG3319 7 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVTGPGLSVSGFSGETLEVNLSSLRTEPAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQ 628
Cdd:COG3319 87 ALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 629 AAAFLSGMQRQFPLTEDDVivlkSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAHFIPAMANS 708
Cdd:COG3319 167 VLAALLALLLAALLALALA----LAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLDQVEMETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERMRLPIGK 788
Cdd:COG3319 243 LLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 789 PVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMD 868
Cdd:COG3319 323 GLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 869 GQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQKTARTELG----KRLPAYMMPSSFIEMREW 944
Cdd:COG3319 403 LQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLllllLLLLPPPLPPALLLLLLL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 945 PVTPSGKLDRKALPAPDGAAERRVYTAPRTITEMKLAKLWEEVLKYGPAGTRDHFFEQGGHSLKATALVSRIAKAFGVQV 1024
Cdd:COG3319 483 LLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLL 562
|
570 580
....*....|....*....|....*...
gi 2040046167 1025 PLKEIFAKPTLEELAAVIQELDESPHAA 1052
Cdd:COG3319 563 LLLALLLAPTLAALAAALAAAAAAAALS 590
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1498-1988 |
1.58e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 123.15 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1498 PKHETISR--LF---EYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAAL-RANGVGSESVVALLTSRTPELAVGILGI 1571
Cdd:PRK08314 2 PKSLTLPEtsLFhnlEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1572 LKAGGAYLPVTEDMPTERLEWMLSDSNAVM-------------LLQSDRLE----SHMAG---------------KRLFI 1619
Cdd:PRK08314 82 LRANAVVVPVNPMNREEELAHYVTDSGARVaivgselapkvapAVGNLRLRhvivAQYSDylpaepeiavpawlrAEPPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1620 EDIQ----------LEAGISAnnPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFS--PEDRILLTAS 1687
Cdd:PRK08314 162 QALApggvvawkeaLAAGLAP--PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNstPESVVLAVLP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1688 LgfdamtFEVFG-------PLLNGACLYIS---DKETYLDsdrlktFIQQNGITTLWLTSS-LFNQLSEQNERTFsDLSR 1756
Cdd:PRK08314 240 L------FHVTGmvhsmnaPIYAGATVVLMprwDREAAAR------LIERYRVTHWTNIPTmVVDFLASPGLAER-DLSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1757 L--ILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFStcfrieheykHSIP--------IGRPIANSTAYIVN-SRG 1825
Cdd:PRK08314 307 LryIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQT----------HSNPpdrpklqcLGIPTFGVDARVIDpETL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1826 RLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPnpfTPGERMYRTGDLARWLKDG---TIDYIGRMddqVKIRGYRIE 1902
Cdd:PRK08314 377 EELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGyffITDRLKRM---INASGFKVW 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1903 LGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI----EKVRSLLSQQLPGFMIPaHLVELA-ALPLTQNG 1977
Cdd:PRK08314 451 PAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGktteEEIIAWAREHMAAYKYP-RIVEFVdSLPKSGSG 529
|
570
....*....|.
gi 2040046167 1978 KLDRRALPEPE 1988
Cdd:PRK08314 530 KILWRQLQEQE 540
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
489-954 |
4.65e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 120.62 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGp 568
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 glsvsgfsgetlevnlsslrtepaENEPVcahtdggslAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI 648
Cdd:cd05914 87 ------------------------DEDDV---------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 VlkSSFSFDASIWQLFWWMIP---GASMYLL----------PQGWEKDPALMT-------EAFTNE---GVTTAHFIPAM 705
Cdd:cd05914 134 L--SILPLHHIYPLTFTLLLPllnGAHVVFLdkipsakiiaLAFAQVTPTLGVpvplvieKIFKMDiipKLTLKKFKFKL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 706 ANSFLDQVEMETEEKRT--SLAKTLKRVFAGGEALAPQTAaRFARSLPETAVIhGYGPTEATVDAAFFRYdhekdrERMR 783
Cdd:cd05914 212 AKKINNRKIRKLAFKKVheAFGGNIKEFVIGGAKINPDVE-EFLRTIGFPYTI-GYGMTETAPIISYSPP------NRIR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 784 L-PIGKPVPGARLYILDSEkavqPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVE 862
Cdd:cd05914 284 LgSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFH------TGDLGKIDAEGYLY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 863 WLGRMDGQ-VKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYAYIEGQDQK-------------TARTELGKR 928
Cdd:cd05914 354 IRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKalkqrniidaikwEVRDKVNQK 433
|
490 500
....*....|....*....|....*..
gi 2040046167 929 LPAYMMPSSFIEMRE-WPVTPSGKLDR 954
Cdd:cd05914 434 VPNYKKISKVKIVKEeFEKTPKGKIKR 460
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1062-1457 |
4.88e-28 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 119.72 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1062 YPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRIHDDV--PF-- 1137
Cdd:cd19547 2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLapPWal 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1138 ------------QLMELAAAEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSV----GTLIREFSELYAS 1201
Cdd:cd19547 82 ldwsgedpdrraELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLsliwGDVFRVYEELAHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1202 RT--LHPLRiQYKDYAVWQQA-FKQGEAYNRQEAYWLKQLDGElPVLELPADnarpavRSFAGDHVSFSLDADTSSGLYK 1278
Cdd:cd19547 162 REpqLSPCR-PYRDYVRWIRArTAQSEESERFWREYLRDLTPS-PFSTAPAD------REGEFDTVVHEFPEQLTRLVNE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1279 IARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGRAHK--DLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETA 1356
Cdd:cd19547 234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPEleGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1357 LEAYEHQDYPFEELVDRLDVVRdMSRNPLFDVMFALQNMERESLTLHDLHLTTIAHDAHKVSKFDMTLYAAEedQETIRF 1436
Cdd:cd19547 314 ATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLP--LQKLAF 390
|
410 420
....*....|....*....|.
gi 2040046167 1437 DVEFNTDIYQKQTIKKWLSYY 1457
Cdd:cd19547 391 HFNYDTTHFTRAQVDRFIEVF 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1510-1984 |
5.66e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 120.45 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1510 QAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTER 1589
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1590 LEWMLSDSNAVMLLQSDRLES-HMAGKRLFIEDIQlEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMveQR----- 1663
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAkLIPGISVKFAELM-NGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI--QTygnhw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1664 -GVVRLVKNsdMAFSPEDRILLTASL----GFDAMtfevFGPLLNGACLYISDKetyLDSDRLKTFIQQNGITTLWLTSS 1738
Cdd:PRK03640 168 wSAVGSALN--LGLTEDDCWLAAVPIfhisGLSIL----MRSVIYGMRVVLVEK---FDAEKINKLLQTGGVTIISVVST 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1739 LFNQLSEQ--NERTFSDLSRLILGGEALSPNHVNRVRntAPDLALWNGYGPTEnttfsTCFRI---EHEY---KHSiPIG 1810
Cdd:PRK03640 239 MLQRLLERlgEGTYPSSFRCMLLGGGPAPKPLLEQCK--EKGIPVYQSYGMTE-----TASQIvtlSPEDaltKLG-SAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1811 RPIANSTAYIVNSrGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGRM 1890
Cdd:PRK03640 311 KPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLDRR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1891 DDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAA 1970
Cdd:PRK03640 383 SDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEE 462
|
490
....*....|....
gi 2040046167 1971 LPLTQNGKLDRRAL 1984
Cdd:PRK03640 463 LPRNASGKLLRHEL 476
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
473-899 |
6.04e-28 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 119.98 E-value: 6.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERL 552
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 553 RYMLADSGARLLVTgpglsvsgFSGETLEVNLSSLRTEPAENEPVCAHtDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAF 632
Cdd:PRK09029 93 EELLPSLTLDFALV--------LEGENTFSALTSLHLQLVEGAHAVAW-QPQRLATMTLTSGSTGLPKAAVHTAQAHLAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 633 LSGMQRQFPLTEDDVIVLkssfS---FDAS----IWQlfwWMIPGASMYlLPQGWEKDPALmteaftnEGVTTAHFIPAM 705
Cdd:PRK09029 164 AEGVLSLMPFTAQDSWLL----SlplFHVSgqgiVWR---WLYAGATLV-VRDKQPLEQAL-------AGCTHASLVPTQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 706 ANSFLDQVEMETeekrtslakTLKRVFAGGEALaPQTAARFARSLPetavIH---GYGPTEA--TVDAAffRYDHEKDre 780
Cdd:PRK09029 229 LWRLLDNRSEPL---------SLKAVLLGGAAI-PVELTEQAEQQG----IRcwcGYGLTEMasTVCAK--RADGLAG-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 781 rmrlpIGKPVPGaRLYILdsekavqpigVAGELYIAGAGVARGYLNRPELTeerflddPFYRGERMYQTGDLARWLpDGT 860
Cdd:PRK09029 291 -----VGSPLPG-REVKL----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGE 346
|
410 420 430
....*....|....*....|....*....|....*....
gi 2040046167 861 VEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV 899
Cdd:PRK09029 347 LTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV 385
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1641-1984 |
6.52e-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: 117.05 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1641 SLAYIMYTSGSTGTPKGVMVEQRGVVRLVK--NSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKETYLDS 1718
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAglHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 DRLktfiqQNGITTLWLTSSlfnQL-----SEQNERTFSDLSRLILGGEALSPNHVNRVrnTAPDLALWNGYGPTE-NTT 1792
Cdd:cd17630 81 DLA-----PPGVTHVSLVPT---QLqrlldSGQGPAALKSLRAVLLGGAPIPPELLERA--ADRGIPLYTTYGMTEtASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1793 FSTCFRIEHEYKHSipiGRPIANSTAYIVNSrgrlqpmgviGELCVGGDGLARGYFgrpeltkeKFVPNPFTPGERMYRT 1872
Cdd:cd17630 151 VATKRPDGFGRGGV---GVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1873 GDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIvrtgPSGHKEL----LAYMSLQAEMNIEKV 1948
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV----GVPDEELgqrpVAVIVGRGPADPAEL 285
|
330 340 350
....*....|....*....|....*....|....*.
gi 2040046167 1949 RSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd17630 286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
469-957 |
1.11e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 119.88 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 469 FTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGvAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:PRK07638 7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVTGPGLSvSGFSGETLEVNLSSLRTEPAENE-PVCAHTDGGSLA--YVIYTSGSTGTPKGVAVE 625
Cdd:PRK07638 86 QDELKERLAISNADMIVTERYKL-NDLPDEEGRVIEIDEWKRMIEKYlPTYAPIENVQNApfYMGFTSGSTGKPKAFLRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 626 HRQAAAFLSGMQRQFPLTEDDVIV----LKSSFSFDASIWQLFWwmipGASMYLLPQgweKDPALMTEAFTNEGVTTAHF 701
Cdd:PRK07638 165 QQSWLHSFDCNVHDFHMKREDSVLiagtLVHSLFLYGAISTLYV----GQTVHLMRK---FIPNQVLDKLETENISVMYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 702 IPAMANSFLdqvemetEEKRTsLAKTLKRVFAGGEALAPQTAaRFARSLPETAVIHGYGPTEATvdaaFFRYDHEKDRER 781
Cdd:PRK07638 238 VPTMLESLY-------KENRV-IENKMKIISSGAKWEAEAKE-KIKNIFPYAKLYEFYGASELS----FVTALVDEESER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 782 MRLPIGKPVPGARLYILDSE-KAVQPiGVAGELYIAGAGVARGYLN----RPELTEERFL--DDPFYRGErmyqtgdlar 854
Cdd:PRK07638 305 RPNSVGRPFHNVQVRICNEAgEEVQK-GEIGTVYVKSPQFFMGYIIggvlARELNADGWMtvRDVGYEDE---------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 855 wlpDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEETElyAYIEGQ-DQKTARTELGKRLP 930
Cdd:PRK07638 374 ---EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDsywGEKPV--AIIKGSaTKQQLKSFCLQRLS 448
|
490 500
....*....|....*....|....*..
gi 2040046167 931 AYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK07638 449 SFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
464-957 |
1.73e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 119.22 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL 543
Cdd:PRK06145 3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGARLLVTG------PGLSVS-GFSGETLEVNLSSLRT--EPAENEPVCAHTDggsLAYVIYTSG 614
Cdd:PRK06145 83 NYRLAADEVAYILGDAGAKLLLVDeefdaiVALETPkIVIDAAAQADSRRLAQggLEIPPQAAVAPTD---LVRLMYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 615 STGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSF----SFD----ASIWQlfwwmipGASMYLLPqgwEKDPAL 686
Cdd:PRK06145 160 TTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDlpgiAVLWV-------GGTLRIHR---EFDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 687 MTEAFTNEGVTTAHFIPAMansfLDQVEMETEEKRTSLAkTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATV 766
Cdd:PRK06145 230 VLAAIERHRLTCAWMAPVM----LSRVLTVPDRDRFDLD-SLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 767 DAAFFrydhEKDRERMRL-PIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFyrger 845
Cdd:PRK06145 305 GDTLM----EAGREIEKIgSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 846 myQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEE-TELYAYIEGQ--DQK 919
Cdd:PRK06145 376 --RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDdrwGERiTAVVVLNPGAtlTLE 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 2040046167 920 TARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK06145 454 ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
464-952 |
3.21e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 118.88 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL 543
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGARLLVTGPGL-------SVSGFSGETLEVNLSSLRTEPAENEPVCAHTDGGS----------- 605
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLVDPALaptaeaaLALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSvaepdveladd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 -LAYVIYTSGSTGTPKGVAVEHRQ-AAAFLSGMQrQFPLTEDDVIV----LKSSFSFDAsiwqlfwWMIP----GASMYL 675
Cdd:PRK08316 172 dLAQILYTSGTESLPKGAMLTHRAlIAEYVSCIV-AGDMSADDIPLhalpLYHCAQLDV-------FLGPylyvGATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 676 LPQgweKDPALMTEAFTNEGVtTAHFIP-----AMANS--FldqvemeteeKRTSLAkTLKRVFAGGEALAPQTAARFAR 748
Cdd:PRK08316 244 LDA---PDPELILRTIEAERI-TSFFAPptvwiSLLRHpdF----------DTRDLS-SLRKGYYGASIMPVEVLKELRE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 749 SLPETAVIHGYGPTE----ATVDAAffrydheKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGY 824
Cdd:PRK08316 309 RLPGLRFYNCYGQTEiaplATVLGP-------EEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 825 LNRPELTEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV------ 898
Cdd:PRK08316 382 WDDPEKTAEAFRGGWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAViglpdp 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 899 ---------VARTEGE---ETELYAYIEGqdqktartelgkRLPAYMMPSSFIEMREWPVTPSGKL 952
Cdd:PRK08316 455 kwieavtavVVPKAGAtvtEDELIAHCRA------------RLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1496-1984 |
3.69e-27 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 119.21 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1496 DYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRAN-GVGSESVVALLTSRTPELAVGILGILKA 1574
Cdd:PRK08751 20 DLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1575 GGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDRL---------------------------------------------E 1609
Cdd:PRK08751 100 GLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFgttvqqviadtpvkqvittglgdmlgfpkaalvnfvvkyvkklvpE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1610 SHMAGKRLFIEDIQLeaGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGvvrLVKNSDMA---------FSPED 1680
Cdd:PRK08751 180 YRINGAIRFREALAL--GRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRN---LVANMQQAhqwlagtgkLEEGC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1681 RILLTA-------SLGFDAMTFEVFGpllnGACLYIS---DKETYLDSDRLKTFIQQNGITTLW---LTSSLFNQLSeqn 1747
Cdd:PRK08751 255 EVVITAlplyhifALTANGLVFMKIG----GCNHLISnprDMPGFVKELKKTRFTAFTGVNTLFnglLNTPGFDQID--- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1748 ertFSDLSRLILGGEALSPNHVNRVRNTApDLALWNGYGPTEnTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRL 1827
Cdd:PRK08751 328 ---FSSLKMTLGGGMAVQRSVAERWKQVT-GLTLVEAYGLTE-TSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1828 QPMGVIGELCVGGDGLARGYFGRPELTKEKFvpnpftPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIE 1907
Cdd:PRK08751 403 LAIGEIGELCIKGPQVMKGYWKRPEETAKVM------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIE 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1908 AALRQIDGVKE-AAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPaHLVEL-AALPLTQNGKLDRRAL 1984
Cdd:PRK08751 477 DVIAMMPGVLEvAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQP-RIIEFrKELPKTNVGKILRREL 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1496-1986 |
5.39e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 118.95 E-value: 5.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1496 DYPKhETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAG 1575
Cdd:PRK05605 28 DYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1576 GAylpVTEDMP--TER-LEWMLSDSNAVMLLQSDRLESHMAGKRlfiEDIQLE--------------------------- 1625
Cdd:PRK05605 107 AV---VVEHNPlyTAHeLEHPFEDHGARVAIVWDKVAPTVERLR---RTTPLEtivsvnmiaampllqrlalrlpipalr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1626 --------------------------AGISANNPEQqgGPDSLAYIMYTSGSTGTPKGVMVEQRGvvrLVKNSDM--AFS 1677
Cdd:PRK05605 181 karaaltgpapgtvpwetlvdaaiggDGSDVSHPRP--TPDDVALILYTSGTTGKPKGAQLTHRN---LFANAAQgkAWV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1678 PE-----DRILltASLGFdamtFEVFGPLLNGA-CLYISDKETYL---DSDRLKTFIQQNGITTLWLTSSLFNQLSEQNE 1748
Cdd:PRK05605 256 PGlgdgpERVL--AALPM----FHAYGLTLCLTlAVSIGGELVLLpapDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1749 RTFSDLSRL---ILGGEALSPNHVnrvrntapdlALWN---------GYGPTENTTFSTCFRIEheyKHSIP--IGRPIA 1814
Cdd:PRK05605 330 ERGVDLSGVrnaFSGAMALPVSTV----------ELWEkltggllveGYGLTETSPIIVGNPMS---DDRRPgyVGVPFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1815 NSTAYIVNSR--GRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNpftpgerMYRTGDLARWLKDGTIDYIGRMDD 1892
Cdd:PRK05605 397 DTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1893 QVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAA 1970
Cdd:PRK05605 470 LIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEpgAALDPEGLRAYCREHLTRYKVPRRFYHVDE 549
|
570
....*....|....*.
gi 2040046167 1971 LPLTQNGKLDRRALPE 1986
Cdd:PRK05605 550 LPRDQLGKVRRREVRE 565
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
465-957 |
5.75e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.60 E-value: 5.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLVTGPGL--SVSGFSGET------------------------LEVNLSSLRTEPAENE--- 595
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILCLDLVfpRVTNVQSATkiehvivtriadflpfpknllypfVQKKQSNLVVKVSESEtih 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 596 ---PVCAHTDGG---------SLAYVIYTSGSTGTPKGVAVEHRQAAA-FLSGMQRQFPLTEDDVIVLK--SSFSFDASI 660
Cdd:PRK06710 186 lwnSVEKEVNTGvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSnTLMGVQWLYNCKEGEEVVLGvlPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 661 WQLFWWMIPGASMYLLPQgweKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEMETEEkrtslAKTLKRVFAGGEALAP 740
Cdd:PRK06710 266 AVMNLSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD-----ISSIRACISGSAPLPV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 741 QTAARFARsLPETAVIHGYGPTEAT-VDAAFFRYDhekdrERMRLPIGKPVPG--ARLYILDSEKAVQPiGVAGELYIAG 817
Cdd:PRK06710 338 EVQEKFET-VTGGKLVEGYGLTESSpVTHSNFLWE-----KRVPGSIGVPWPDteAMIMSLETGEALPP-GEIGEIVVKG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 818 AGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAA 897
Cdd:PRK06710 411 PQIMKGYWNKPEETAAVLQDGWLH-------TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 898 VVARTE---GEETELYAYIEgQDQKTARTELG----KRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK06710 484 TIGVPDpyrGETVKAFVVLK-EGTECSEEELNqfarKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
12-429 |
6.59e-27 |
|
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: 116.59 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLF-HSLLDQESrAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIhKNVAKPRQVVLKERQSRLQF 90
Cdd:cd20483 3 PMSTFQRRLWFlHNFLEDKT-FLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYF-EGDDFGEQQVLDDPSFHLIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 91 VDIShlDETAKETFVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKE 170
Cdd:cd20483 81 IDLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 171 QLPDFEPVHPFSkYI-------KWLMRQDRKEAEAFWKTRLIDVKQTASLPKTSSSSKGKLEQMA-----FTLSKEQTEG 238
Cdd:cd20483 159 RDLATVPPPPVQ-YIdftlwhnALLQSPLVQPLLDFWKEKLEGIPDASKLLPFAKAERPPVKDYErstveATLDKELLAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 239 LRKLALQAGAT----LNTVFQALwgiilqkINRC---DDAVFGSVISGRP-SDLEDvekMVGLFINTIPVRVKSGPE-SF 309
Cdd:cd20483 238 MKRICAQHAVTpfmfLLAAFRAF-------LYRYtedEDLTIGMVDGDRPhPDFDD---LVGFFVNMLPIRCRMDCDmSF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 310 LTLVSHLQQESLKAEAYSYYPlydiqaqsmlkhelFDHIVVFENIPAQREIESLNQ-------------ADAFDFTVDDF 376
Cdd:cd20483 308 DDLLESTKTTCLEAYEHSAVP--------------FDYIVDALDVPRSTSHFPIGQiavnyqvhgkfpeYDTGDFKFTDY 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 377 DMDEV-TNYGCSIKII--PGSSLYIRINFDIGLYDPAMMKKIELYLRHIIGSVIAD 429
Cdd:cd20483 374 DHYDIpTACDIALEAEedPDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1511-1921 |
8.46e-27 |
|
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: 117.98 E-value: 8.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIY-----DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDM 1585
Cdd:cd05970 27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1586 PTERLEWMLSDSN--AVMLLQSDRLESHMAG---------KRLFIED------IQLEAGISANNP-------EQQGGPDS 1641
Cdd:cd05970 107 TAKDIVYRIESADikMIVAIAEDNIPEEIEKaapecpskpKLVWVGDpvpegwIDFRKLIKNASPdferptaNSYPCGED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1642 LAYIMYTSGSTGTPKgvMVEQRGVVRLVKNSDMAF----SPEDRILLTASLGF-DAMTFEVFGPLLNGACLYISDKETYl 1716
Cdd:cd05970 187 ILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYwqnvREGGLHLTVADTGWgKAVWGKIYGQWIAGAAVFVYDYDKF- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1717 DSDRLKTFIQQNGITTLWLTSSLFNQL-SEQNER-TFSDLSRLILGGEALSPNHVNRVRNtAPDLALWNGYGPTENT--- 1791
Cdd:cd05970 264 DPKALLEKLSKYGVTTFCAPPTIYRFLiREDLSRyDLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEGFGQTETTlti 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1792 -TFStCFRIEheykhsiP--IGRPIANSTAYIVNSRGRLQPMGVIGELCVGGD-----GLARGYFGRPELTKEKFvpnpf 1863
Cdd:cd05970 343 aTFP-WMEPK-------PgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW----- 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 1864 tpGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAV 1921
Cdd:cd05970 410 --HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV 465
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1510-1984 |
9.08e-27 |
|
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: 118.50 E-value: 9.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1510 QAAKTPHAPAVIY------DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTE 1583
Cdd:TIGR02188 66 HLEARPDKVAIIWegdepgEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1584 DMPTERLEWMLSDSNAVMLLQSDrlESHMAGKRLFIEDI-------------------------------------QLEA 1626
Cdd:TIGR02188 146 GFSAEALADRINDAGAKLVITAD--EGLRGGKVIPLKAIvdealekcpvsvehvlvvrrtgnpvvpwvegrdvwwhDLMA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1627 GISAN-NPEQQGGPDSLaYIMYTSGSTGTPKGVMVEQRGVVRLVKNS-----DmaFSPEDRILLTASLGF-DAMTFEVFG 1699
Cdd:TIGR02188 224 KASAYcEPEPMDSEDPL-FILYTSGSTGKPKGVLHTTGGYLLYAAMTmkyvfD--IKDGDIFWCTADVGWiTGHSYIVYG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1700 PLLNGA-CLYISDKETYLDSDRLKTFIQQNGITTLWlTS----SLFNQLSEQNERTFsDLSRL-ILG--GEALSPNhvnr 1771
Cdd:TIGR02188 301 PLANGAtTVMFEGVPTYPDPGRFWEIIEKHKVTIFY-TAptaiRALMRLGDEWVKKH-DLSSLrLLGsvGEPINPE---- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1772 vrntapdlaLWNGY----GPTENTTFSTCFRIEheyKHSIPI--------------GRPIANSTAYIVNSRGRLQPM-GV 1832
Cdd:TIGR02188 375 ---------AWMWYykvvGKERCPIVDTWWQTE---TGGIMItplpgatptkpgsaTLPFFGIEPAVVDEEGNPVEGpGE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1833 IGELCVGGD--GLARGYFGRPeltkEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAAL 1910
Cdd:TIGR02188 443 GGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESAL 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1911 RQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI-----EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:TIGR02188 519 VSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPddelrKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLL 597
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
605-954 |
1.41e-26 |
|
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: 112.88 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 605 SLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIV----LKSSFSFDASIWQLFWW-MIPGASMYLLPQG 679
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILapgpLSHSLFLYGAISALYLGgTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 680 WEKDpalmteafTNEGVTTAHFIPAMANSFLDQVEMETeekrtslakTLKRVFAGGEALAPQTAARFARSLPETAVIHGY 759
Cdd:cd17633 81 IRKI--------NQYNATVIYLVPTMLQALARTLEPES---------KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 760 GPTEATVDAAFFrydheKDRERMRLPIGKPVPGARLYILDSEKavqpiGVAGELYIAGAGVARGYLNRPELTEERFlddp 839
Cdd:cd17633 144 GTSELSFITYNF-----NQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 840 fyrgermYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA---RTEGEETELYAYIEGQ 916
Cdd:cd17633 210 -------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGipdARFGEIAVALYSGDKL 282
|
330 340 350
....*....|....*....|....*....|....*...
gi 2040046167 917 DQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDR 954
Cdd:cd17633 283 TYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1509-1984 |
1.74e-26 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 115.74 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1509 YQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTE 1588
Cdd:PRK09029 11 HWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1589 RLEWMLSDSNAVMLLQSDrleshmaGKRLFIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVM--VEQ---- 1662
Cdd:PRK09029 91 LLEELLPSLTLDFALVLE-------GENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVhtAQAhlas 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1663 -RGVVRLvknsdMAFSPEDRILLTASLgfdamtFEVFGP------LLNGACLYISDKETYLDSdrlktfiqQNGI----- 1730
Cdd:PRK09029 164 aEGVLSL-----MPFTAQDSWLLSLPL------FHVSGQgivwrwLYAGATLVVRDKQPLEQA--------LAGCthasl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1731 --TTLW-LTSSLFNQLSeqnertfsdLSRLILGGEALSPNHVNRVRntAPDLALWNGYGPTEntTFSTCF--RIEheykh 1805
Cdd:PRK09029 225 vpTQLWrLLDNRSEPLS---------LKAVLLGGAAIPVELTEQAE--QQGIRCWCGYGLTE--MASTVCakRAD----- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1806 SIP-IGRPIANSTAYIVNsrgrlqpmgviGELCVGGDGLARGYFGRPELTkekfvpnPFTPGERMYRTGDLARWlKDGTI 1884
Cdd:PRK09029 287 GLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEW-QNGEL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1885 DYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIvrtgPSGHKEL----LAYMSLQAEMNIEKVRSLLSQQLPGFM 1960
Cdd:PRK09029 348 TILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV----PVADAEFgqrpVAVVESDSEAAVVNLAEWLQDKLARFQ 423
|
490 500
....*....|....*....|....*..
gi 2040046167 1961 IPahlVELAALPLT-QNG--KLDRRAL 1984
Cdd:PRK09029 424 QP---VAYYLLPPElKNGgiKISRQAL 447
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1510-1984 |
2.02e-26 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 117.28 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1510 QAAKTPHAPAVIY------DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV-- 1581
Cdd:cd05966 62 HLKERGDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfa 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 --TEDMPTERLEwmlsDSNAVMLLQSDrlESHMAGKRLFIEDI-----------------------------------QL 1624
Cdd:cd05966 142 gfSAESLADRIN----DAQCKLVITAD--GGYRGGKVIPLKEIvdealekcpsvekvlvvkrtggevpmtegrdlwwhDL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1625 EAGISANN-PEQQGGPDSLaYIMYTSGSTGTPKGVMVEQRGVVRLVKNS-DMAFS--PEDRILLTASLGF-DAMTFEVFG 1699
Cdd:cd05966 216 MAKQSPECePEWMDSEDPL-FILYTSGSTGKPKGVVHTTGGYLLYAATTfKYVFDyhPDDIYWCTADIGWiTGHSYIVYG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1700 PLLNGA-CLYISDKETYLDSDRLKTFIQQNGITTLWlTS-----SLFNQLSEQNERtfSDLSRL-ILG--GEALSP---- 1766
Cdd:cd05966 295 PLANGAtTVMFEGTPTYPDPGRYWDIVEKHKVTIFY-TAptairALMKFGDEWVKK--HDLSSLrVLGsvGEPINPeawm 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1767 ---NHVNRVRntapdLALWNGYGPTEntTFStcfrieheykHSI-PI-----------GRPIANSTAYIVNSRGRLQPMG 1831
Cdd:cd05966 372 wyyEVIGKER-----CPIVDTWWQTE--TGG----------IMItPLpgatplkpgsaTRPFFGIEPAILDEEGNEVEGE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1832 VIGELCVGGD--GLARGYFGRPEltkeKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAA 1909
Cdd:cd05966 435 VEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1910 LRQIDGVKEAAVIVRTGPSGHKELLAYMSL----QAEMNIEK-VRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05966 511 LVAHPAVAEAAVVGRPHDIKGEAIYAFVTLkdgeEPSDELRKeLRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1515-1984 |
3.28e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.85 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPE-LAVGILGILkAGGAYLPVTedmPTERLE-- 1591
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLMAIGAAQL-AGLRRTALH---PLGSLDdh 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1592 -WMLSDSNAVMLLQS-----DR----LESHMAGKRLFI-------EDIQLEAGISANNP-EQQGGPDSLAYIMYTSGSTG 1653
Cdd:PRK06188 102 aYVLEDAGISTLIVDpapfvERalalLARVPSLKHVLTlgpvpdgVDLLAAAAKFGPAPlVAAALPPDIAGLAYTGGTTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1654 TPKGVMVEQRGVVRLVKNSDMAFS-PED-RILLTASLGFDAMTFevFGP-LLNGACLYISDKetyLDSDRLKTFIQQNGI 1730
Cdd:PRK06188 182 KPKGVMGTHRSIATMAQIQLAEWEwPADpRFLMCTPLSHAGGAF--FLPtLLRGGTVIVLAK---FDPAEVLRAIEEQRI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1731 TTLWLTSSLFNQLSEQ---NERTFSDLSRLILGGEALSPNH-VNRVRNTAPDLALWngYGPTE-NTTFSTCFRIEHEYKH 1805
Cdd:PRK06188 257 TATFLVPTMIYALLDHpdlRTRDLSSLETVYYGASPMSPVRlAEAIERFGPIFAQY--YGQTEaPMVITYLRKRDHDPDD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1806 S---IPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFvpnpftpGERMYRTGDLARWLKDG 1882
Cdd:PRK06188 335 PkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGWLHTGDVAREDEDG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1883 TIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI--EKVRSLLSQQLPGFM 1960
Cdd:PRK06188 408 FYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVdaAELQAHVKERKGSVH 487
|
490 500
....*....|....*....|....
gi 2040046167 1961 IPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK06188 488 APKQVDFVDSLPLTALGKPDKKAL 511
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1639-1984 |
3.40e-26 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 115.51 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPEDRILltASLGFdamtFEVFG-------PLLNGACLYI 1709
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFdpNPEDVVF--GALPF----FHSFGltgclwlPLLSGIKVVF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1710 SDKEtyLDSDRLKTFIQQNGITTLWLTSSLFNQ-LSEQNERTFSDLSRLILGGEALSPnhvnRVRNTAPD---LALWNGY 1785
Cdd:cd05909 220 HPNP--LDYKKIPELIYDKKATILLGTPTFLRGyARAAHPEDFSSLRLVVAGAEKLKD----TLRQEFQEkfgIRILEGY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1786 GPTENTTFSTCFRIEHEYKHSIpIGRPIANSTAYIVNSRGRLQ-PMGVIGELCVGGDGLARGYFGRPELTKEKFvpnpft 1864
Cdd:cd05909 294 GTTECSPVISVNTPQSPNKEGT-VGRPLPGMEVKIVSVETHEEvPIGEGGLLLVRGPNVMLGYLNEPELTSFAF------ 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1865 pGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVK--EAAVIVRTGPSGHKELLAYmsLQAE 1942
Cdd:cd05909 367 -GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDneVAVVSVPDGRKGEKIVLLT--TTTD 443
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2040046167 1943 MNIEKVRSLLSQ-QLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05909 444 TDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
464-954 |
3.41e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 116.03 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAV--RFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYV 541
Cdd:PRK12583 19 TIGDAFDATVARFPDREALvvRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 542 PLDPDYPEERLRYMLADSGARLLVTGPGLSVSGFSGETLEVNLSSLRTEPAENEP-----------VCAHTDGGSLAY-- 608
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACerlpelrgvvsLAPAPPPGFLAWhe 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 ---------------------------VIYTSGSTGTPKGVAVEHRQAA--AFLSGmqRQFPLTEDDVIVLKSSF--SFD 657
Cdd:PRK12583 179 lqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILnnGYFVA--ESLGLTEHDRLCVPVPLyhCFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 658 ASIWQLFWwMIPGASMyLLPQGwEKDPALMTEAFTNEGVTTAHFIPAMansFLDQVEmETEEKRTSLAkTLKRVFAGGEA 737
Cdd:PRK12583 257 MVLANLGC-MTVGACL-VYPNE-AFDPLATLQAVEEERCTALYGVPTM---FIAELD-HPQRGNFDLS-SLRTGIMAGAP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 738 LAPQTAARFARSLPETAVIHGYGPTEATvdAAFFRYDHEKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAG 817
Cdd:PRK12583 329 CPIEVMRRVMDEMHMAEVQIAYGMTETS--PVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 818 AGVARGYLNRPELTEERFLDDPFyrgerMYqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAA 897
Cdd:PRK12583 407 YSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 898 VVARTE---GEETELYAYIEgQDQKTARTELGK----RLPAYMMPSSFIEMREWPVTPSGKLDR 954
Cdd:PRK12583 481 VFGVPDekyGEEIVAWVRLH-PGHAASEEELREfckaRIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1502-1984 |
4.37e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.88 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVgILGILKAGGAYLPV 1581
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIEFLQL-FAGAAMAGWTCVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1582 -TEDMPTERLEwMLSDSNAVMLLQSDRLESHMAGKRLFIEDI-QLEAGISANNPEQQGGPDSLA---YIMYTSGSTGTPK 1656
Cdd:PRK07638 81 dIKWKQDELKE-RLAISNADMIVTERYKLNDLPDEEGRVIEIdEWKRMIEKYLPTYAPIENVQNapfYMGFTSGSTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1657 GVMVEQRGVVRLVKNS--DMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYIsdKETYLDSDRLKTfIQQNGITTLW 1734
Cdd:PRK07638 160 AFLRAQQSWLHSFDCNvhDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL--MRKFIPNQVLDK-LETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1735 LTSSLFNQLSEQNeRTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTEnTTFSTCFRIEHEYKHSIPIGRPIA 1814
Cdd:PRK07638 237 TVPTMLESLYKEN-RVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE-LSFVTALVDEESERRPNSVGRPFH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1815 NSTAYIVNSRG-RLQPmGVIGELCVGGDGLARGYFGRPELTKEkfvpnpFTPGERMyRTGDLARWLKDGTIDYIGRMDDQ 1893
Cdd:PRK07638 315 NVQVRICNEAGeEVQK-GEIGTVYVKSPQFFMGYIIGGVLARE------LNADGWM-TVRDVGYEDEEGFIYIVGREKNM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1894 VKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAemNIEKVRSLLSQQLPGFMIPAHLVELAALPL 1973
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA--TKQQLKSFCLQRLSSFKIPKEWHFVDEIPY 464
|
490
....*....|.
gi 2040046167 1974 TQNGKLDRRAL 1984
Cdd:PRK07638 465 TNSGKIARMEA 475
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
466-959 |
5.87e-26 |
|
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: 116.05 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 466 HSFFTRRAALSPNLPAVRFSG-----GILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAY 540
Cdd:cd05968 64 EQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 541 VPLDPDYPEERLRYMLADSGARLLVTgpglsVSGFSGETLEVNLSSLRTEPAENEPVCAH-------------TDGGSLA 607
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKALIT-----ADGFTRRGREVNLKEEADKACAQCPTVEKvvvvrhlgndftpAKGRDLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 608 Y---------------------VIYTSGSTGTPKGVAVEHR----QAAAflsGMQRQFPLTEDDVIVLKSSFSFDASIWQ 662
Cdd:cd05968 219 YdeeketagdgaertesedplmIIYTSGTTGKPKGTVHVHAgfplKAAQ---DMYFQFDLKPGDLLTWFTDLGWMMGPWL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 663 LFWWMIPGASMYLLpQGWEKDPAL-----MTEAF--TNEGVtTAHFIPAMANSFLDQVEmetEEKRTSLaktlkRVFAG- 734
Cdd:cd05968 296 IFGGLILGATMVLY-DGAPDHPKAdrlwrMVEDHeiTHLGL-SPTLIRALKPRGDAPVN---AHDLSSL-----RVLGSt 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 735 GEALAPQTAARFARSL--PETAVIHGYGPTEAT---VDAAFFRydhekdrermrlPI-----GKPVPGARLYILDSEKav 804
Cdd:cd05968 366 GEPWNPEPWNWLFETVgkGRNPIINYSGGTEISggiLGNVLIK------------PIkpssfNGPVPGMKADVLDESG-- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 805 QPI-GVAGELYIAGA--GVARGYLNrpelTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPG 881
Cdd:cd05968 432 KPArPEVGELVLLAPwpGMTRGFWR----DEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPA 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 882 EVEAALRQIDGVREAAVVA---RTEGEETELYAYIEGQDQKTA--RTELGKRLPAYM----MPSSFIEMREWPVTPSGKL 952
Cdd:cd05968 508 EIESVLNAHPAVLESAAIGvphPVKGEAIVCFVVLKPGVTPTEalAEELMERVADELgkplSPERILFVKDLPKTRNAKV 587
|
....*..
gi 2040046167 953 DRKALPA 959
Cdd:cd05968 588 MRRVIRA 594
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1065-1461 |
1.03e-25 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 112.01 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1065 SSAQKRMYVLQQledggvgynmpaALKLTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRIHDDVPFQLMELAA 1144
Cdd:cd19545 15 TARQPGAYVGQR------------VFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWTESTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1145 AEDFVRPFRLQE----APLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRTLhPLRIQYKDYAVWQQA 1220
Cdd:cd19545 83 LDEYLEEDRAAPmglgGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPV-PQPPPFSRFVKYLRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1221 FKQGEAynrqEAYWLKQLDGELPVL--ELPADNARPAVRSFAgDHvSFSLDADTSSGLykiardngcTLYMVLLAAYSTL 1298
Cdd:cd19545 162 LDDEAA----AEFWRSYLAGLDPAVfpPLPSSRYQPRPDATL-EH-SISLPSSASSGV---------TLATVLRAAWALV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1299 LARLSGQEDIIIGSPIAGRAH--KDLESVIGMFVNTLAIRTRPVENKCFSDFLREVRETALEAYEHQDYPfeelvdrLDV 1376
Cdd:cd19545 227 LSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTG-------LQN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1377 VRDMSRN----PLFDVMFALQNmeRESLTLHDLHLTTIAHDAHKVSKFD---MTLYaAEEDQETIRFDVEFNTDIYQKQT 1449
Cdd:cd19545 300 IRRLGPDaraaCNFQTLLVVQP--ALPSSTSESLELGIEEESEDLEDFSsygLTLE-CQLSGSGLRVRARYDSSVISEEQ 376
|
410
....*....|..
gi 2040046167 1450 IKKWLSYYIHIL 1461
Cdd:cd19545 377 VERLLDQFEHVL 388
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1489-1981 |
2.51e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 113.33 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1489 TFNQTKQDYP-KHETISRLFEYQAAKTPHAPAVIYDRQTL--TYRELNQRANRIAAALRANGVGSESVVALLTSRTPELA 1565
Cdd:PRK12583 5 SYYQGGGDKPlLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1566 VGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDRLES----HMAGKRL-FIEDIQLEAGISANNPEQQG--- 1637
Cdd:PRK12583 85 LTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTsdyhAMLQELLpGLAEGQPGALACERLPELRGvvs 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 -----GPDSLAY-----------------------------IMYTSGSTGTPKGVMVEQRGVV---RLVKNSdMAFSPED 1680
Cdd:PRK12583 165 lapapPPGFLAWhelqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILnngYFVAES-LGLTEHD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1681 RILLTASL--GFdAMTFEVFGPLLNGACLYISDKetYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL- 1757
Cdd:PRK12583 244 RLCVPVPLyhCF-GMVLANLGCMTVGACLVYPNE--AFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLr 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1758 --ILGGEALSPNHVNRVRNT--APDLALwnGYGPTENT--TFSTCFRIEHEyKHSIPIGRPIANSTAYIVNSRGRLQPMG 1831
Cdd:PRK12583 321 tgIMAGAPCPIEVMRRVMDEmhMAEVQI--AYGMTETSpvSLQTTAADDLE-RRVETVGRTQPHLEVKVVDPDGATVPRG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1832 VIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgerMYrTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALR 1911
Cdd:PRK12583 398 EIGELCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLF 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 1912 QIDGVKEAAVIVRTGPSGHKELLAYMSLQA--EMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:PRK12583 472 THPAVADVQVFGVPDEKYGEEIVAWVRLHPghAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
457-971 |
3.29e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 113.90 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 457 PAAPLAPTLHSFFTRRAALSPNLPAVRF--SGG------ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVI 528
Cdd:PRK07529 19 AARDLPASTYELLSRAAARHPDAPALSFllDADpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 529 AVLAVLKAGGAyVPLDPDYPEERLRYMLADSGARLLVT-GPGL------SVSGFSGE------TLEVNLSSLRTEPAE-- 593
Cdd:PRK07529 99 ALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTlGPFPgtdiwqKVAEVLAAlpelrtVVEVDLARYLPGPKRla 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 594 --------------------NEPVCAHTDG-----GSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI 648
Cdd:PRK07529 178 vplirrkaharildfdaelaRQPGDRLFSGrpigpDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 V----LkssFSFDASIWQLFWWMIPGASMYLL-PQGWeKDPALM------TEAFtneGVTTAHFIPAMANSFLDqveMET 717
Cdd:PRK07529 258 FcglpL---FHVNALLVTGLAPLARGAHVVLAtPQGY-RGPGVIanfwkiVERY---RINFLSGVPTVYAALLQ---VPV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 718 EEKRTSlakTLKRVFAGGEALAPQTAARFARSLPETaVIHGYGPTEAT-VDAAFFRydhekDRERMRLPIGKPVPGARLY 796
Cdd:PRK07529 328 DGHDIS---SLRYALCGAAPLPVEVFRRFEAATGVR-IVEGYGLTEATcVSSVNPP-----DGERRIGSVGLRLPYQRVR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 797 I--LDSEKAVQ---PIGVAGELYIAGAGVARGYL----NRPELTEERFLDdpfyrgermyqTGDLARWLPDGTVeWL-GR 866
Cdd:PRK07529 399 VviLDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLeaahNKGLWLEDGWLN-----------TGDLGRIDADGYF-WLtGR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 867 MDGQVkIR-GYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL-YAYIEGQDQKTARTElgkRLPAYM---------MP 935
Cdd:PRK07529 467 AKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVQLKPGASATEA---ELLAFArdhiaeraaVP 542
|
570 580 590
....*....|....*....|....*....|....*.
gi 2040046167 936 SSFIEMREWPVTPSGKLDRKALPApdgAAERRVYTA 971
Cdd:PRK07529 543 KHVRILDALPKTAVGKIFKPALRR---DAIRRVLRA 575
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
488-957 |
3.74e-25 |
|
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: 112.59 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 488 ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVP------------------------L 543
Cdd:cd05970 47 IFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqltakdivyriesadikmivaI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYPEERLRYMLADSGA--RLLVTGPGLSVSGFSGETLEVNLSSLRTEPAENEPVCahtdGGSLAYVIYTSGSTGTPKG 621
Cdd:cd05970 127 AEDNIPEEIEKAAPECPSkpKLVWVGDPVPEGWIDFRKLIKNASPDFERPTANSYPC----GEDILLVYFSSGTTGMPKM 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 622 VAVEHRQAAA-FLSGMQRQfPLTEDDVIVLKSSFSFDASIW-QLFWWMIPGASMYLLPQGwEKDPALMTEAFTNEGVTTa 699
Cdd:cd05970 203 VEHDFTYPLGhIVTAKYWQ-NVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYD-KFDPKALLEKLSKYGVTT- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 700 HFIPAMANSFLDQVEMEteekRTSLAkTLKRVFAGGEALAPQTAARFaRSLPETAVIHGYGPTEATVDAAFFRYDHEKDR 779
Cdd:cd05970 280 FCAPPTIYRFLIREDLS----RYDLS-SLRYCTTAGEALNPEVFNTF-KEKTGIKLMEGFGQTETTLTIATFPWMEPKPG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 780 ErmrlpIGKPVPGARLYILDSEKAVQPIGVAGELYIAGA-----GVARGYLNRPELTEERFLDDpfyrgerMYQTGDLAR 854
Cdd:cd05970 354 S-----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG-------YYHTGDAAW 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 855 WLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVvartegeeTELYAYIEGQDQK---------TARTEL 925
Cdd:cd05970 422 MDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV--------TGVPDPIRGQVVKativlakgyEPSEEL 493
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2040046167 926 GKRL--------PAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05970 494 KKELqdhvkkvtAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1641-1981 |
3.89e-25 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 108.65 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1641 SLAYIMYTSGSTGTPKGVMVEQRG--VVRLVKNSDMAFSPEDRILLTASLGFDAMTFEVFGPLLNGACLYISDKetyLDS 1718
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSwiESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK---FNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 DRLKTFIQQNGITTLWLTSSLFNQLSEQNErTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFR 1798
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALARTLE-PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1799 IEHEYKHSIpiGRPIANSTAYIVNSRGrlqpmGVIGELCVGGDGLARGYFGRPELTKEKFvpnpftpgermYRTGDLARW 1878
Cdd:cd17633 157 QESRPPNSV--GRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIGYV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1879 LKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI----VRTGpsghkELLAYMSLQAEMNIEKVRSLLSQ 1954
Cdd:cd17633 219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgipdARFG-----EIAVALYSGDKLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 2040046167 1955 QLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
463-957 |
4.56e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 114.64 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 463 PTLHSFFTRRAALSPNLPAVRFSGGI-LTYRELdqYTNQLAI-RLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAY 540
Cdd:PRK08633 615 PPLAEAWIDTAKRNWSRLAVADSTGGeLSYGKA--LTGALALaRLLKRELKDEENVGILLPPSVAGALANLALLLAGKVP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 541 VPLDPDYPEERLRYMLADSGARLLVTG----PGLSVSGFSGETLE----VNLSSLRTEPAENEPVCA------------- 599
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSrkflEKLKNKGFDLELPEnvkvIYLEDLKAKISKVDKLTAllaarllparllk 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 600 -------HTDggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIV----LKSSFSFDASIWQLfwwMI 668
Cdd:PRK08633 773 rlygptfKPD--DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILsslpFFHSFGLTVTLWLP---LL 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 669 PGASMYLLPqgwekDPalmTEAFT------NEGVT----TAHFIPAMA-NSFLDQVEMETeekrtslaktLKRVFAGGEA 737
Cdd:PRK08633 848 EGIKVVYHP-----DP---TDALGiaklvaKHRATillgTPTFLRLYLrNKKLHPLMFAS----------LRLVVAGAEK 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 738 LAPQTAARFARSLpETAVIHGYGPTEATVDAAFFRYDHEkDRERMRLP------IGKPVPGARLYILDSEK-AVQPIGVA 810
Cdd:PRK08633 910 LKPEVADAFEEKF-GIRILEGYGATETSPVASVNLPDVL-AADFKRQTgskegsVGMPLPGVAVRIVDPETfEELPPGED 987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 811 GELYIAGAGVARGYLNRPELTEERFLDdpfYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQI 890
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKA 1064
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 891 --DGVREAAVVARTEGEETE----LYAYIEGQDQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK08633 1065 lgGEEVVFAVTAVPDEKKGEklvvLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1527-1988 |
7.96e-25 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 110.35 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEwmlsdsnavmllqsD 1606
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLR--------------D 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 RLEShmaGKRLFIEDIQLEAgisANNPeqqggpdSLAYimYTSGSTGTPKGVMVEQRG--VVRLVKNSDMAFSPEDRILL 1684
Cdd:cd05974 67 RVDR---GGAVYAAVDENTH---ADDP-------MLLY--FTSGTTSKPKLVEHTHRSypVGHLSTMYWIGLKPGDVHWN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1685 TASLGFDAMTFE-VFGPLLNGACLYISDkETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLILG-GE 1762
Cdd:cd05974 132 ISSPGWAKHAWScFFAPWNAGATVFLFN-YARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGaGE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1763 ALSPNHVNRVRNtAPDLALWNGYGPTENTTfstcfRIEHEYKHSI---PIGRPIANSTAYIVNSRGRLQPMGvigELCVG 1839
Cdd:cd05974 211 PLNPEVIEQVRR-AWGLTIRDGYGQTETTA-----LVGNSPGQPVkagSMGRPLPGYRVALLDPDGAPATEG---EVALD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1840 -GD----GLARGYFGRPELTKEKFvpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQID 1914
Cdd:cd05974 282 lGDtrpvGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1915 GVKEAAVIvrtgPSGHKELL----AYMSLQA--EMNIEKVRSLLS---QQLPGFMIPAHLvELAALPLTQNGKLDRRALP 1985
Cdd:cd05974 355 AVAEAAVV----PSPDPVRLsvpkAFIVLRAgyEPSPETALEIFRfsrERLAPYKRIRRL-EFAELPKTISGKIRRVELR 429
|
...
gi 2040046167 1986 EPE 1988
Cdd:cd05974 430 RRE 432
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1639-1982 |
1.09e-24 |
|
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: 108.62 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLaYIMYTSGSTGTPKGVMVEQRGVVRLVKNS-DMAFSPE--DRILLTASLGFDAMTFEVFGPLLNGA---------- 1705
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDIFRMLMGGaDFGTGEFtpSEDAHKAAAAAAGTVMFPAPPLMHGTgswtafggll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1706 ---CLYISDKEtyLDSDRLKTFIQQNGITTLWLTSS-----LFNQLSEQNERTFSDLSRLILGGEALSPNHVNRVRNTAP 1777
Cdd:cd05924 82 ggqTVVLPDDR--FDPEEVWRTIEKHKVTSMTIVGDamarpLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1778 DLALWNGYGPTEnttfsTCFRIEHEYKHSIPIGRP--IANSTAYIVNSRGRLQPMGVIGELCVGGDGL-ARGYFGRPELT 1854
Cdd:cd05924 160 NITLVDAFGSSE-----TGFTGSGHSAGSGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1855 KEKFvpnPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELL 1934
Cdd:cd05924 235 AETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1935 AYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRR 1982
Cdd:cd05924 312 AVVQLRegAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1501-1990 |
1.91e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 111.20 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1501 ETISRLFEYQAAKTPHAPAVIY--------DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILG-- 1570
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGge 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1571 -------------------ILKAGGAYLPVT-EDMPTERLeW--------MLSDSNAVmlLQSDRLESHMAGKRLFIEDI 1622
Cdd:PRK07529 105 aagianpinpllepeqiaeLLRAAGAKVLVTlGPFPGTDI-WqkvaevlaALPELRTV--VEVDLARYLPGPKRLAVPLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1623 QLEAGISANN--------------PEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRL--VKNSDMAFSPEDRILLTA 1686
Cdd:PRK07529 182 RRKAHARILDfdaelarqpgdrlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANawLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1687 SLgfdamtFEVFG-------PLLNGACLYISDKETYLDS---DRLKTFIQQNGITTLWLTSSLFNQLSEQ--NERTFSDL 1754
Cdd:PRK07529 262 PL------FHVNAllvtglaPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQVpvDGHDISSL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1755 sRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTTFSTCFRIEHEYK-HSIPIGRPIANSTAYIVNSRGRLQ---PM 1830
Cdd:PRK07529 336 -RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRiGSVGLRLPYQRVRVVILDDAGRYLrdcAV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1831 GVIGELCVGGDGLARGYFgRPELTKEKFVpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVkIR-GYRIELGEIEAA 1909
Cdd:PRK07529 415 DEVGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1910 LRQIDGVKEAAVIVRtgPSGHK-EL-LAYMSLQAEMNIEkvrsllSQQLPGFM---------IPAHLVELAALPLTQNGK 1978
Cdd:PRK07529 487 LLRHPAVALAAAVGR--PDAHAgELpVAYVQLKPGASAT------EAELLAFArdhiaeraaVPKHVRILDALPKTAVGK 558
|
570
....*....|..
gi 2040046167 1979 LDRRALPEPETT 1990
Cdd:PRK07529 559 IFKPALRRDAIR 570
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1806-2069 |
2.05e-24 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 105.99 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1806 SIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPF----TPGERMYRTGDLARWLKD 1881
Cdd:COG3433 14 DEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPvpypAQPGRQADDLRLLLRRGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1882 GTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGP-SGHKELLAYMSLQAEMNIEKVRSLLSQQLPgFM 1960
Cdd:COG3433 94 GPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAgVGLLLIVGAVAALDGLAAAAALAALDKVPP-DV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1961 IPAHLVELAALPLTQNGKLDRRALPEPETTAINTAYAPPRN-----QLEERLAVIWQEVLGV--EKVGIEDSFFELGGDS 2033
Cdd:COG3433 173 VAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaletaLTEEELRADVAELLGVdpEEIDPDDNLFDLGLDS 252
|
250 260 270
....*....|....*....|....*....|....*.
gi 2040046167 2034 IKALQVSARLGRFDLKITAGDLFRHPTIKEAAPLIR 2069
Cdd:COG3433 253 IRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLA 288
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
459-959 |
2.31e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 110.16 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 459 APLAPTLHSFFTRRAalSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKK-GVAKESVVGVLADRSPEMVIAVLAVLKAG 537
Cdd:PRK07867 1 TSSAPTVAELLLPLA--EDDDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 538 GAYVPLDPDYPEERLR---------YMLADSGARLLVTGPGLSVSGFSGETLEvnLSSLRTEPAENEPVCAHTDGGSLAY 608
Cdd:PRK07867 79 IVPVGLNPTRRGAALArdiahadcqLVLTESAHAELLDGLDPGVRVINVDSPA--WADELAAHRDAEPPFRVADPDDLFM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLkssfsfdasiwqlfwwmipgaSMYL-----LPQGWEkd 683
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYV---------------------SMPLfhsnaVMAGWA-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 684 PALMTEAFTnegVTTAHFipaMANSFLDQVE-----------------METEEKRTSLAKTLKRVFaGGEAlAPQTAARF 746
Cdd:PRK07867 214 VALAAGASI---ALRRKF---SASGFLPDVRrygatyanyvgkplsyvLATPERPDDADNPLRIVY-GNEG-APGDIARF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 747 ARSLpETAVIHGYGPTEATVDAAffrydhekdrermRLP------IGKPVPGARLY-----------ILDSEKAVQPIGV 809
Cdd:PRK07867 286 ARRF-GCVVVDGFGSTEGGVAIT-------------RTPdtppgaLGPLPPGVAIVdpdtgtecppaEDADGRLLNADEA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 810 AGELY-IAGAGVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALR 888
Cdd:PRK07867 352 IGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 889 QIDGVREAAVVAR---TEGEETElyAYIEGQDQKT-----------ARTELG-KRLPAYMMPSSfiemrEWPVTPSGKLD 953
Cdd:PRK07867 425 RYPDATEVAVYAVpdpVVGDQVM--AALVLAPGAKfdpdafaeflaAQPDLGpKQWPSYVRVCA-----ELPRTATFKVL 497
|
....*.
gi 2040046167 954 RKALPA 959
Cdd:PRK07867 498 KRQLSA 503
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
785-1050 |
2.34e-24 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 105.99 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 785 PIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVA-RGYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEW 863
Cdd:COG3433 19 VIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLlRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 864 LGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGE--ETELYAYIEGQDQKTARTELGKR--LPAYMMPSSFI 939
Cdd:COG3433 99 LERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGvgLLLIVGAVAALDGLAAAAALAALdkVPPDVVAASAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 940 EMREWPVTPSGKLDRKALPAPDGAAERRVYTAPRTITEM-----KLAKLWEEVLKYGPA--GTRDHFFEQGGHSLKATAL 1012
Cdd:COG3433 179 VALDALLLLALKVVARAAPALAAAEALLAAASPAPALETalteeELRADVAELLGVDPEeiDPDDNLFDLGLDSIRLMQL 258
|
250 260 270
....*....|....*....|....*....|....*...
gi 2040046167 1013 VSRiAKAFGVQVPLKEIFAKPTLEELAAVIQELDESPH 1050
Cdd:COG3433 259 VER-WRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1639-1986 |
2.70e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 112.32 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFSPE--DRIL----LTASLGFDAMTfevFGPLLNG-ACLYISD 1711
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRndDVILsslpFFHSFGLTVTL---WLPLLEGiKVVYHPD 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1712 KetyLDSDRLKTFIQQNGITTLWLTSSLFnQLSEQNERT----FSDLSRLILGGEALSPnhvnRVRNTAPD---LALWNG 1784
Cdd:PRK08633 858 P---TDALGIAKLVAKHRATILLGTPTFL-RLYLRNKKLhplmFASLRLVVAGAEKLKP----EVADAFEEkfgIRILEG 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1785 YGPTENT---------TFSTCFRIEHEYKHSiPIGRPIANSTAYIVN-SRGRLQPMGVIGELCVGGDGLARGYFGRPELT 1854
Cdd:PRK08633 930 YGATETSpvasvnlpdVLAADFKRQTGSKEG-SVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKT 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1855 KEKFVPnpfTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHK-EL 1933
Cdd:PRK08633 1009 AEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAVPDEKKgEK 1085
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1934 LAYMSLQAEMNIEKVRSLLSQ-QLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK08633 1086 LVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
489-968 |
3.79e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 109.40 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVT-- 566
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAha 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 567 ----------GPGLSVsgFSGETLEVNLSSLRTEPAENEPVCAHTD-GGSLAY--------------VIYTSGSTGTPKG 621
Cdd:PRK12406 92 dllhglasalPAGVTV--LSVPTPPEIAAAYRISPALLTPPAGAIDwEGWLAQqepydgppvpqpqsMIYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 622 V---AVEHRQAAAFLSGMQRQFPLTEDDVIVL------KSSFSFDASIWQLfwwmipGASMYLLPQgweKDPALMTEAFT 692
Cdd:PRK12406 170 VrraAPTPEQAAAAEQMRALIYGLKPGIRALLtgplyhSAPNAYGLRAGRL------GGVLVLQPR---FDPEELLQLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 693 NEGVTTAHFIPAMansFLDQVEMETEEKRTSLAKTLKRVFAGGeALAPqtaARFARSLPE--TAVIHG-YGPTEATVdAA 769
Cdd:PRK12406 241 RHRITHMHMVPTM---FIRLLKLPEEVRAKYDVSSLRHVIHAA-APCP---ADVKRAMIEwwGPVIYEyYGSTESGA-VT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 770 FFRYDhekdrERMRLP--IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVAR-GYLNRPEltEERFLDdpfyRGErM 846
Cdd:PRK12406 313 FATSE-----DALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPE--KRAEID----RGG-F 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 847 YQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETE-LYAYIEGQ-----DQKT 920
Cdd:PRK12406 381 ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEaLMAVVEPQpgatlDEAD 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2040046167 921 ARTELGKRLPAYMMPsSFIE-MREWPVTPSGKLDRKALPAPDGAAERRV 968
Cdd:PRK12406 461 IRAQLKARLAGYKVP-KHIEiMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
490-956 |
8.47e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 108.54 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGPG 569
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 570 LSVSG--F--SGETLE------VNLSSLRTEPAENEPVcahTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQ 639
Cdd:PRK07768 111 AVVVGepFlaAAPVLEekgirvLTVADLLAADPIDPVE---TGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 640 FPLT-EDDVIVlkssfsfdaSIWQLFWWM-------IP---GASM-YLLPQGWEKDPALMTEAFTN-EGVTTAHfiPAMA 706
Cdd:PRK07768 188 AEFDvETDVMV---------SWLPLFHDMgmvgfltVPmyfGAELvKVTPMDFLRDPLLWAELISKyRGTMTAA--PNFA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 707 NSFLDQV-EMETEEKRTSLAkTLKRVFAGGEALAPQTAARFARS-----LPETAVIHGYGPTEATVDAAF------FRYD 774
Cdd:PRK07768 257 YALLARRlRRQAKPGAFDLS-SLRFALNGAEPIDPADVEDLLDAgarfgLRPEAILPAYGMAEATLAVSFspcgagLVVD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 775 H---------------EKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYlnrpeLTEERFLddP 839
Cdd:PRK07768 336 EvdadllaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFI--P 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 840 FYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA-RTE-GEETELYAYI---- 913
Cdd:PRK07768 409 AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAvRLDaGHSREGFAVAvesn 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 914 EGQDQKTAR-----------TELGKR------LPAYMMPSsfiemrewpvTPSGKLDRKA 956
Cdd:PRK07768 489 AFEDPAEVRrirhqvahevvAEVGVRprnvvvLGPGSIPK----------TPSGKLRRAN 538
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1515-1979 |
1.05e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 108.33 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVMLLQSDRLESHMAGKR--------------------LFIEDIQLEAGIS---ANNPEqqggpDSLAYIMYTSGS 1651
Cdd:PRK07786 111 SDCGAHVVVTEAALAPVATAVRdivpllstvvvaggssddsvLGYEDLLAEAGPAhapVDIPN-----DSPALIMYTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1652 TGTPKGVMVEQRGVV----------RLVKNSDMAF--SPEDRIlltASLGfdamtfEVFGPLLNGACLYISDKETYlDSD 1719
Cdd:PRK07786 186 TGRPKGAVLTHANLTgqamtclrtnGADINSDVGFvgVPLFHI---AGIG------SMLPGLLLGAPTVIYPLGAF-DPG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1720 RLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLS-RLILGGEALSPNHVNR-VRNTAPDLALWNGYGPTENTTFSTCF 1797
Cdd:PRK07786 256 QLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLAlRVLSWGAAPASDTLLRqMAATFPEAQILAAFGQTEMSPVTCML 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1798 RIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLAR 1877
Cdd:PRK07786 336 LGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGDLVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1878 WLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ---AEMNIEKVRSLLSQ 1954
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnddAALTLEDLAEFLTD 488
|
490 500
....*....|....*....|....*
gi 2040046167 1955 QLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:PRK07786 489 RLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
486-957 |
1.10e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 108.18 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 486 GGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGA---- 561
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAeaiv 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 562 -------------------RLLVTGPGlSVSGFSGetLEVNLSSLRTE---PAENEPVC-----------------AHTD 602
Cdd:PRK07059 126 vlenfattvqqvlaktavkHVVVASMG-DLLGFKG--HIVNFVVRRVKkmvPAWSLPGHvrfndalaegarqtfkpVKLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 603 GGSLAYVIYTSGSTGTPKGVAVEHR-------QAAAFLSGMQRQFPLTEDDVIV----LKSSFSFDASiwqLFWWMIPGA 671
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRnivanvlQMEAWLQPAFEKKPRPDQLNFVcalpLYHIFALTVC---GLLGMRTGG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 672 SMYLLPQgwEKDPALMTEAFTNEGVttaHFIPAMaNSFLDQVeMETEEKRTSLAKTLKRVFAGGEALAPQTAARFARsLP 751
Cdd:PRK07059 280 RNILIPN--PRDIPGFIKELKKYQV---HIFPAV-NTLYNAL-LNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLE-MT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 752 ETAVIHGYGPTE----ATVDAAffrydhekDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNR 827
Cdd:PRK07059 352 GCPITEGYGLSEtspvATCNPV--------DATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 828 PELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEET 907
Cdd:PRK07059 424 PDETAKVMTADGFFR------TGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSG 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 908 E-LYAYIEGQDQKTARTELGK----RLPAYMMPsSFIEMR-EWPVTPSGKLDRKAL 957
Cdd:PRK07059 498 EaVKLFVVKKDPALTEEDVKAfckeRLTNYKRP-KFVEFRtELPKTNVGKILRREL 552
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1062-1362 |
1.49e-23 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 105.98 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1062 YPVSSAQKRMYVLQQLEDGGVGYNMPAALKLTgplDRARLDEV---FRQLIRRHESLRTSFETgaDG--EPVQRIH---- 1132
Cdd:cd19544 2 YPLAPLQEGILFHHLLAEEGDPYLLRSLLAFD---SRARLDAFlaaLQQVIDRHDILRTAILW--EGlsEPVQVVWrqae 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1133 -----------DDVPFQLMELAAAEDFvrPFRLQEAPLFRAALVKEAE-ESHLLLVDMHHIISDGVSVGTLIREFSELYA 1200
Cdd:cd19544 77 lpveeltldpgDDALAQLRARFDPRRY--RLDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQAILA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1201 SRTLHPLR-IQYKDYAVwqQAFKQGEAyNRQEAYWLKQLDG--E--LP--VLELPADNARPavrsfagDHVSFSLDADTS 1273
Cdd:cd19544 155 GRAAALPPpVPYRNFVA--QARLGASQ-AEHEAFFREMLGDvdEptAPfgLLDVQGDGSDI-------TEARLALDAELA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1274 SGLYKIARDNGCTLYMVLLAAYSTLLARLSGQEDIIIGSPIAGR--AHKDLESVIGMFVNTLAIR----TRPVEnkcfsD 1347
Cdd:cd19544 225 QRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRmqGGAGADRALGMFINTLPLRvrlgGRSVR-----E 299
|
330
....*....|....*..
gi 2040046167 1348 FLREVRE--TALEAYEH 1362
Cdd:cd19544 300 AVRQTHArlAELLRHEH 316
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1503-1893 |
1.73e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 107.68 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1503 ISRLFEYQAAKTPHAPAVI----------YDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGIL 1572
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAvpggrgadgkLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1573 KAGGayLPVTED--MPTERLEWMLSDSNAVMLLQSDRleSHMA-----------------GKRLFIEDIQLE----AGIS 1629
Cdd:PRK09274 88 KAGA--VPVLVDpgMGIKNLKQCLAEAQPDAFIGIPK--AHLArrlfgwgkpsvrrlvtvGGRLLWGGTTLAtllrDGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1630 ANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQR---GVVRLVKNsDMAFSPEDRILLTASLgfdamtFEVFGPLLNGAC 1706
Cdd:PRK09274 164 APFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGmfeAQIEALRE-DYGIEPGEIDLPTFPL------FALFGPALGMTS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1707 LyISD----KETYLDSDRLKTFIQQNGITTLWLTSSLFNQLS---EQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDL 1779
Cdd:PRK09274 237 V-IPDmdptRPATVDPAKLFAAIERYGVTNLFGSPALLERLGrygEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1780 A-LWNGYGPTENTTFSTcfrIE-HEYKHS----------IPIGRPIANSTAYIVN---------SRGRLQPMGVIGELCV 1838
Cdd:PRK09274 316 AeILTPYGATEALPISS---IEsREILFAtraatdngagICVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVV 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1839 GGDGLARGYFGRPELTKEKFVPNPftPGERMYRTGDLarwlkdgtidyiGRMDDQ 1893
Cdd:PRK09274 393 AGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDL------------GYLDAQ 433
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1494-1984 |
1.82e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 107.53 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1494 KQDYPKHETISRLFEYQAAKTPHAPAVIYDRQT-LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGIL 1572
Cdd:PRK06087 16 QQGYWGDASLADYWQQTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1573 KAGGAYLPVTEDMPTERLEWMLSDSNAVMLL------QSDRLE---------SHMAGKRLF------IEDIQLEAGISAN 1631
Cdd:PRK06087 96 KVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlfkQTRPVDlilplqnqlPQLQQIVGVdklapaTSSLSLSQIIADY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1632 NPEQQGGP---DSLAYIMYTSGSTGTPKGVMV--------EQRGVVRLVKNSDmafspeDRILLTASLGfDAMTF--EVF 1698
Cdd:PRK06087 176 EPLTTAITthgDELAAVLFTSGTEGLPKGVMLthnnilasERAYCARLNLTWQ------DVFMMPAPLG-HATGFlhGVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1699 GPLLNGACLYISDKETyldSDRLKTFIQQNGIT-TLWLTSSLFNQLS--EQNERTFSDLsRLILGGEALSPNHVNRvRNT 1775
Cdd:PRK06087 249 APFLIGARSVLLDIFT---PDACLALLEQQRCTcMLGATPFIYDLLNllEKQPADLSAL-RFFLCGGTTIPKKVAR-ECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1776 APDLALWNGYGPTENttfstcfrIEHEYkhsIPI-----------GRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLA 1844
Cdd:PRK06087 324 QRGIKLLSVYGSTES--------SPHAV---VNLddplsrfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1845 RGYFGRPELTkekfvpNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDqVKIR-GYRIELGEIEAALRQIDGVKEAAVIV 1923
Cdd:PRK06087 393 MGYLDEPELT------ARALDEEGWYYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVA 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1924 ----RTGpsghKELLAYMSLQAEMNIEKVRSLLS----QQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK06087 466 mpdeRLG----ERSCAYVVLKAPHHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1496-1995 |
1.92e-23 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 107.45 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1496 DYPKHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRaNGVGSE--SVVALLTSRTPELAVGILGILK 1573
Cdd:PRK08974 18 NPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQ-NGLGLKkgDRVALMMPNLLQYPIALFGILR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1574 AGGAYLPVTEDMPTERLEWMLSDSNA------------------------VMLLQ-SDRLEshmAGKRLFIEDI------ 1622
Cdd:PRK08974 97 AGMIVVNVNPLYTPRELEHQLNDSGAkaivivsnfahtlekvvfktpvkhVILTRmGDQLS---TAKGTLVNFVvkyikr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1623 -----QLEAGISANNPEQQG----------GPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFSP----EDRIL 1683
Cdd:PRK08974 174 lvpkyHLPDAISFRSALHKGrrmqyvkpelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPllhpGKELV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1684 LTA-------SLGFDAMTFEVFGpllnGACLYIS---DKETYLDSDRLKTFIQQNGITTL---WLTSSLFNQLSeqnert 1750
Cdd:PRK08974 254 VTAlplyhifALTVNCLLFIELG----GQNLLITnprDIPGFVKELKKYPFTAITGVNTLfnaLLNNEEFQELD------ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1751 FSDLSRLILGGEALSPNHVNRVRNTApDLALWNGYGPTENTTFSTCFRIEHEyKHSIPIGRPIANSTAYIVNSRGRLQPM 1830
Cdd:PRK08974 324 FSSLKLSVGGGMAVQQAVAERWVKLT-GQYLLEGYGLTECSPLVSVNPYDLD-YYSGSIGLPVPSTEIKLVDDDGNEVPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1831 GVIGELCVGGDGLARGYFGRPELTKEKFvpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAAL 1910
Cdd:PRK08974 402 GEPGELWVKGPQVMLGYWQRPEATDEVI-------KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1911 RQIDGVKEAAVI-VRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPaHLVELA-ALPLTQNGKLDRRALPEPE 1988
Cdd:PRK08974 475 MLHPKVLEVAAVgVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVP-KLVEFRdELPKSNVGKILRRELRDEA 553
|
....*..
gi 2040046167 1989 TTAINTA 1995
Cdd:PRK08974 554 RAKVDNK 560
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
461-970 |
2.15e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 107.40 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 461 LAPTLHSFFTRRAALSPNLPAVRFSGGI--LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGG 538
Cdd:PRK05857 12 LPSTVLDRVFEQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 539 AYVPLDPDYPEERL-RY-MLADSGARLLVTGPGLSVSGF-----SGETLEVNLSSLRTEPAENEPV---CAHTDGGS--- 605
Cdd:PRK05857 92 IAVMADGNLPIAAIeRFcQITDPAAALVAPGSKMASSAVpealhSIPVIAVDIAAVTRESEHSLDAaslAGNADQGSedp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 LAyVIYTSGSTGTPKGVAVEHRQAAAfLSGMQRQFPLTEDDVIVLKSSFS-FDASIWQLFWWMIPGAsMY--LLPQGWEK 682
Cdd:PRK05857 172 LA-MIFTSGTTGEPKAVLLANRTFFA-VPDILQKEGLNWVTWVVGETTYSpLPATHIGGLWWILTCL-MHggLCVTGGEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 683 DPALMtEAFTNEGVTTAHFIPAMANSFLdqvemeTEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLP-ETAVIhgYGP 761
Cdd:PRK05857 249 TTSLL-EILTTNAVATTCLVPTLLSKLV------SELKSANATVPSLRLVGYGGSRAIAADVRFIEATGvRTAQV--YGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 762 TEATVDAAFFRYDHEKDRERMRLPIGKPVPGARLYILDSEKAVQPIGVAGE------LYIAGAGVARGYLNRPELTEERF 835
Cdd:PRK05857 320 SETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfgtLWIKSPANMLGYWNNPERTAEVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 836 LDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL--YAYI 913
Cdd:PRK05857 400 IDG-------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALvgLAVV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 914 EGQD-QKTARTELGKRLPAY--------MMPSSFIEMREWPVTPSGKLDRKALPAPDGAAERRVYT 970
Cdd:PRK05857 473 ASAElDESAARALKHTIAARfrresepmARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVVV 538
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
490-957 |
2.37e-23 |
|
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: 107.23 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLL-VTGP 568
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVfCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 GL--------------------SVSGFSGETLEVNLSSLRTEPAENE----PVCAHTDGgSLAYVIYTSGSTGTPKGVAV 624
Cdd:cd17642 126 GLqkvlnvqkklkiiktiiildSKEDYKGYQCLYTFITQNLPPGFNEydfkPPSFDRDE-QVALIMNSSGSTGLPKGVQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 625 EHRQAAAFLSGmQRQ----FPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKdpaLMTEAFTNEGVTTAH 700
Cdd:cd17642 205 THKNIVARFSH-ARDpifgNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEE---LFLRSLQDYKVQSAL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 701 FIPAMAnSFLDQVEMETEEKRTSLaktlKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATvdAAFFRYDHEKDRE 780
Cdd:cd17642 281 LVPTLF-AFFAKSTLVDKYDLSNL----HEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETT--SAILITPEGDDKP 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 781 RmrlPIGKPVPG--ARLYILDSEKAVQPiGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPD 858
Cdd:cd17642 354 G---AVGKVVPFfyAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKALIDKDGWLH------SGDIAYYDED 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 859 GTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL-YAYIEGQDQKTArTE-------LGKRLP 930
Cdd:cd17642 424 GHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELpAAVVVLEAGKTM-TEkevmdyvASQVST 502
|
490 500
....*....|....*....|....*..
gi 2040046167 931 AYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd17642 503 AKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1528-1986 |
3.17e-23 |
|
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: 106.84 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1528 TYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDR 1607
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1608 LESHMAG---KRLFIEDI-------------QLEAGISANNP----EQQGGPDS------LAYIMYTSGSTGTPKGVMVE 1661
Cdd:cd17642 126 GLQKVLNvqkKLKIIKTIiildskedykgyqCLYTFITQNLPpgfnEYDFKPPSfdrdeqVALIMNSSGSTGLPKGVQLT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1662 QRG-VVRLVKNSDMAF----SPEDRILLTASL--GFDAMTfeVFGPLLNGA---CLYISDKETYLDSdrlktfIQQNGIT 1731
Cdd:cd17642 206 HKNiVARFSHARDPIFgnqiIPDTAILTVIPFhhGFGMFT--TLGYLICGFrvvLMYKFEEELFLRS------LQDYKVQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1732 TLWLTSSLFNQLSEQ---NERTFSDLSRLILGGEALSPN---------HVNRVRNtapdlalwnGYGPTEnTTFSTCFRI 1799
Cdd:cd17642 278 SALLVPTLFAFFAKStlvDKYDLSNLHEIASGGAPLSKEvgeavakrfKLPGIRQ---------GYGLTE-TTSAILITP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1800 EHEYKHSiPIGRPIANSTAYIVN-SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARW 1878
Cdd:cd17642 348 EGDDKPG-AVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW------LHSGDIAYY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1879 LKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQA--EMNIEKVRSLLSQQL 1956
Cdd:cd17642 421 DEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAgkTMTEKEVMDYVASQV 500
|
490 500 510
....*....|....*....|....*....|.
gi 2040046167 1957 -PGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:cd17642 501 sTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
611-954 |
3.90e-23 |
|
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: 103.51 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 611 YTSGSTGTPKGVAVEHRQAA--AFLSGMQRQFplTEDDVIVLKSSF--SFDASIWQLFWWMIpGASMYLLPQGWekDPAL 686
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVnnGYFIGERLGL--TEQDRLCIPVPLfhCFGSVLGVLACLTH-GATMVFPSPSF--DPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 687 MTEAFTNEGVTTAHFIPAMansFLDqvEMETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEAT- 765
Cdd:cd05917 84 VLEAIEKEKCTALHGVPTM---FIA--ELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 766 VDAAFFRYDhekDRERMRLPIGKPVPGARLYILDSE-KAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLddpfyrGE 844
Cdd:cd05917 159 VSTQTRTDD---SIEKRVNTVGRIMPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAID------GD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 845 RMYQTGDLARWLPDGTVEWLGRMDGQVkIRG-YRIEPGEVEAALRQIDGVREAAVVA---RTEGEetELYAYIEGQDQKT 920
Cdd:cd05917 230 GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGvpdERYGE--EVCAWIRLKEGAE 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 2040046167 921 ARTE-----LGKRLPAYMMPSSFIEMREWPVTPSGKLDR 954
Cdd:cd05917 307 LTEEdikayCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
609-899 |
5.87e-23 |
|
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: 102.77 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAVEHRQ--AAAFLSGMQRQfplteddvivLKSSFSFDAS-----IWQLFWWM----IPGASMYLlP 677
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQAllAQALVLAVLQA----------IDEGTVFLNSgplfhIGTLMFTLatfhAGGTNVFV-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 678 QgweKDPALMTEAFTNEGVTTAHFIPAMansfLDQVeMETEEKRTSLAKTLKRVFA--GGEALAPQTAARFARSLPetav 755
Cdd:cd17636 74 R---VDAEEVLELIEAERCTHAFLLPPT----IDQI-VELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPG---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 756 ihGYGPTEATVDAAFFRYDhEKDRERMrlpiGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERF 835
Cdd:cd17636 142 --GYGQTEVMGLATFAALG-GGAIGGA----GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 836 LDdpfyrgeRMYQTGDLARWLPDGTVEWLG---RMdgqVKIRGYRIEPGEVEAALRQIDGVREAAVV 899
Cdd:cd17636 215 RG-------GWHHTNDLGRREPDGSLSFVGpktRM---IKSGAENIYPAEVERCLRQHPAVADAAVI 271
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1502-1987 |
5.97e-23 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 106.00 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSR-----TPELAVGILG----IL 1572
Cdd:PRK13382 44 GPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNhrgfvEALLAANRIGadilLL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1573 KAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSDRLESHMAGKRLFIEDIQ---LEAGISANNPEQQ--GGPDSLAYIMY 1647
Cdd:PRK13382 124 NTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQATRIVAWTDEDhdlTVEVLIAAHAGQRpePTGRKGRVILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1648 TSGSTGTPKGVMVEQRGVVRLVKnSDMAFSP---EDRILLTASLgFDAMTFE--VFGPLLngACLYIS----DKETYLDs 1718
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLK-AILDRTPwraEEPTVIVAPM-FHAWGFSqlVLAASL--ACTIVTrrrfDPEATLD- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 drlktFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLIL-----GGEALSPNHVNRVRNTAPDlALWNGYGPTENTTF 1793
Cdd:PRK13382 279 -----LIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLrfaaaSGSRMRPDVVIAFMDQFGD-VIYNNYNATEAGMI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1794 STCfRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYfgRPELTKEkfvpnpFTPGerMYRTG 1873
Cdd:PRK13382 353 ATA-TPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD------FHDG--FMASG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1874 DLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI--EKVRSL 1951
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASAtpETLKQH 501
|
490 500 510
....*....|....*....|....*....|....*.
gi 2040046167 1952 LSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEP 1987
Cdd:PRK13382 502 VRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1502-1986 |
6.10e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 105.78 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLT--SR---TPELAVGILG----IL 1572
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLArnHRgfvLALYAAGKVGariiLL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1573 KAG-------------GAYLPVTEDMPTERLEWMLSDSNAVMLLQ--SDRLESHMAGKRLFIEDIQLEAGISANNPEQQG 1637
Cdd:PRK07788 130 NTGfsgpqlaevaareGVKALVYDDEFTDLLSALPPDLGRLRAWGgnPDDDEPSGSTDETLDDLIAGSSTAPLPKPPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 GpdslaYIMYTSGSTGTPKGVMveqRGVVRlvknsdmAFSPE----DRILLTASlgfdaMTFEVFGPLLNG---ACLYIS 1710
Cdd:PRK07788 210 G-----IVILTSGTTGTPKGAP---RPEPS-------PLAPLagllSRVPFRAG-----ETTLLPAPMFHAtgwAHLTLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1711 -------------DKETYLDSdrlktfIQQNGITTLWLTSSLFNQLSEQNERTFS--DLSRL---ILGGEALSPNHVNRV 1772
Cdd:PRK07788 270 malgstvvlrrrfDPEATLED------IAKHKATALVVVPVMLSRILDLGPEVLAkyDTSSLkiiFVSGSALSPELATRA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1773 RNTAPDLaLWNGYGPTENtTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGrpe 1852
Cdd:PRK07788 344 LEAFGPV-LYNLYGSTEV-AFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD--- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1853 ltkekfVPNPFTPGERMyRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSGHK 1931
Cdd:PRK07788 419 ------GRDKQIIDGLL-SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFGQR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 1932 eLLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK07788 492 -LRAFVVKApgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1527-1889 |
6.51e-23 |
|
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: 105.76 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGV--GSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQ 1604
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 SdrleshmAGKRLF-IEDIqLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLV------KNSDMAFS 1677
Cdd:cd05927 86 D-------AGVKVYsLEEF-EKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfkiLEILNKIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1678 PEDRILLTASLG--FDAMTFEVFgpLLNGAC---------LYISD----KETYLDS-----DRLKTFIQQNGITTLWLTS 1737
Cdd:cd05927 158 PTDVYISYLPLAhiFERVVEALF--LYHGAKigfysgdirLLLDDikalKPTVFPGvprvlNRIYDKIFNKVQAKGPLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1738 SLFN--------QLSEQNERT--------FS--------DLSRLILGGEALSPNHVNRVRnTAPDLALWNGYGPTENTTF 1793
Cdd:cd05927 236 KLFNfalnyklaELRSGVVRAspfwdklvFNkikqalggNVRLMLTGSAPLSPEVLEFLR-VALGCPVLEGYGQTECTAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1794 STCfriEHEYKHSI-PIGRPIANSTA---------YIVNS-RGRlqpmgviGELCVGGDGLARGYFGRPELTKEKFVPNP 1862
Cdd:cd05927 315 ATL---TLPGDTSVgHVGGPLPCAEVklvdvpemnYDAKDpNPR-------GEVCIRGPNVFSGYYKDPEKTAEALDEDG 384
|
410 420
....*....|....*....|....*..
gi 2040046167 1863 FtpgermYRTGDLARWLKDGTIDYIGR 1889
Cdd:cd05927 385 W------LHTGDIGEWLPNGTLKIIDR 405
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1645-1981 |
8.72e-23 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 102.34 E-value: 8.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1645 IMYTSGSTGTPKGVMVEQRGVVRLVKN---SDMAFSPEDRILLTASLGFD-----AMTFEVFGpllnGACLYISDKETYl 1716
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDIlqkEGLNWVVGDVTYLPLPATHIgglwwILTCLIHG----GLCVTGGENTTY- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1717 dsdrlKTF---IQQNGITTLWLTSSLFNQLSE--QNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTEnT 1791
Cdd:cd17635 81 -----KSLfkiLTTNAVTTTCLVPTLLSKLVSelKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSE-T 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1792 TFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVpnpftpgERMYR 1871
Cdd:cd17635 155 GTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1872 TGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNIEKVRSL 1951
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRAL 307
|
330 340 350
....*....|....*....|....*....|...
gi 2040046167 1952 ---LSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:cd17635 308 khtIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
456-871 |
8.96e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 105.90 E-value: 8.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 456 EPAAPLAPTLHSFFTRRAALSPNLP--AVRFSGG----ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIA 529
Cdd:PRK12582 42 HPLGPYPRSIPHLLAKWAAEAPDRPwlAQREPGHgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 530 VLAVLKAGGAYVPLDPDYP-----EERLRYM---------LADSGAR-------LLVTGPGLSVSGFSGE-TLEVNLSSL 587
Cdd:PRK12582 122 TLAAMQAGVPAAPVSPAYSlmshdHAKLKHLfdlvkprvvFAQSGAPfaralaaLDLLDVTVVHVTGPGEgIASIAFADL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 588 RTEP--AENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVI-----------VLKSSF 654
Cdd:PRK12582 202 AATPptAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPpvsldwmpwnhTMGGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 655 SFDASIWQlfwwmipGASMYL-----LPQGWEKDPALMTE----AFTNEGVTTAHFIPAMANSfldqvemetEEKRTSLA 725
Cdd:PRK12582 282 NFNGLLWG-------GGTLYIddgkpLPGMFEETIRNLREisptVYGNVPAGYAMLAEAMEKD---------DALRRSFF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 726 KTLKRVFAGGEALAPQTAARF-ARSLPETA----VIHGYGPTEA---TVDAAFfrydhekDRERMRLpIGKPVPGARLYI 797
Cdd:PRK12582 346 KNLRLMAYGGATLSDDLYERMqALAVRTTGhripFYTGYGATETaptTTGTHW-------DTERVGL-IGLPLPGVELKL 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 798 LdsekavqPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWL-PDGTVEWLgRMDGQV 871
Cdd:PRK12582 418 A-------PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYR------LGDAARFVdPDDPEKGL-IFDGRV 478
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1519-1987 |
1.47e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 104.40 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1519 AVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSN 1598
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1599 AVMLLQSDRLESHMAG------KRLFIE---------------------DIQLEAGISANNPEQQGGPDSLAYIMYTSGS 1651
Cdd:PRK12406 84 ARVLIAHADLLHGLASalpagvTVLSVPtppeiaaayrispalltppagAIDWEGWLAQQEPYDGPPVPQPQSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1652 TGTPKGV-----MVEQRGVVRLVKNSDMAFSPEDRILLTASL--------GFDAMTFevfgpllnGACLYISDKetyLDS 1718
Cdd:PRK12406 164 TGHPKGVrraapTPEQAAAAEQMRALIYGLKPGIRALLTGPLyhsapnayGLRAGRL--------GGVLVLQPR---FDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 DRLKTFIQQNGITTLWLTSSLFNQLSEQNE--RTFSDLS--RLILGGEALSPNHVNRVrntapdLALWNG------YGPT 1788
Cdd:PRK12406 233 EELLQLIERHRITHMHMVPTMFIRLLKLPEevRAKYDVSslRHVIHAAAPCPADVKRA------MIEWWGpviyeyYGST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1789 ENTTFSTCFRiEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLAR-GYFGRPE----LTKEKFVpnpf 1863
Cdd:PRK12406 307 ESGAVTFATS-EDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEkraeIDRGGFI---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1864 TPGERMYRTGDLARWLKDgtidyigRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--A 1941
Cdd:PRK12406 382 TSGDVGYLDADGYLFLCD-------RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQpgA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2040046167 1942 EMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEP 1987
Cdd:PRK12406 455 TLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1496-1922 |
1.54e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 104.68 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1496 DYPKHETISR-LFEyQAAKTPHAPAVIyDRQT---LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGI 1571
Cdd:PLN02246 18 YIPNHLPLHDyCFE-RLSEFSDRPCLI-DGATgrvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1572 ----------------------LKAGGAYLPVTEDMPTERLEwMLSDSNAVMLLQSDrleSHMAGKRLFIEDIQLEagiS 1629
Cdd:PLN02246 96 srrgavtttanpfytpaeiakqAKASGAKLIITQSCYVDKLK-GLAEDDGVTVVTID---DPPEGCLHFSELTQAD---E 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1630 ANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLV------KNSDMAFSPEDRILLTASLgfdamtFEVFGplLN 1703
Cdd:PLN02246 169 NELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVaqqvdgENPNLYFHSDDVILCVLPM------FHIYS--LN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1704 ---------GACLYISDKetyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLS--RLILGGEA-LSPNHVNR 1771
Cdd:PLN02246 241 svllcglrvGAAILIMPK---FEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSsiRMVLSGAApLGKELEDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1772 VRNTAPDLALWNGYGPTE-NTTFSTCFRIEheyKHSIPI-----GRPIANSTAYIVN-----SRGRLQPmgviGELCVGG 1840
Cdd:PLN02246 318 FRAKLPNAVLGQGYGMTEaGPVLAMCLAFA---KEPFPVksgscGTVVRNAELKIVDpetgaSLPRNQP----GEICIRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1841 DGLARGYFGRPELTKekfvpnpftpgermyRTGDLARWLKDGTIDYIGRmDDQV----------KIRGYRIELGEIEAAL 1910
Cdd:PLN02246 391 PQIMKGYLNDPEATA---------------NTIDKDGWLHTGDIGYIDD-DDELfivdrlkeliKYKGFQVAPAELEALL 454
|
490
....*....|..
gi 2040046167 1911 RQIDGVKEAAVI 1922
Cdd:PLN02246 455 ISHPSIADAAVV 466
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
467-899 |
1.93e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 104.60 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 467 SFFTRRAALSPNLPAVRFSGGI----------LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKA 536
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 537 GGAYVPLDPDYPEERLRYMLADS-----------------------GARLLVT-GPGLSVSGFSgetlevnLSSLRTEPA 592
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAqpdafigipkahlarrlfgwgkpSVRRLVTvGGRLLWGGTT-------LATLLRDGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 593 ENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVivlkssfsfDASIWQLFWWMIP--G 670
Cdd:PRK09274 163 AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI---------DLPTFPLFALFGPalG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 671 ASMYLLPQGWEK----DPALMTEAFTNEGVTTAHFIPAMansfLDQVEMETEEKRTSLAkTLKRVFAGGEALAPQTAARF 746
Cdd:PRK09274 234 MTSVIPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPAL----LERLGRYGEANGIKLP-SLRRVISAGAPVPIAVIERF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 747 ARSLPETAVIH-GYGPTEA------TVDAAFFRYDHEKDRERMRLpIGKPVPGARLYILD---------SEKAVQPIGVA 810
Cdd:PRK09274 309 RAMLPPDAEILtPYGATEAlpissiESREILFATRAATDNGAGIC-VGRPVDGVEVRIIAisdapipewDDALRLATGEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 811 GELYIAGAGVARGYLNRPELTEERFLDDPfyRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQI 890
Cdd:PRK09274 388 GEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTH 465
|
....*....
gi 2040046167 891 DGVREAAVV 899
Cdd:PRK09274 466 PGVKRSALV 474
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1511-1978 |
2.11e-22 |
|
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: 103.53 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVtedmpTERL 1590
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNAL-----NTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 EwmlSDSNAVMLlqsdrleSHmAGKRLFIEDIQL--EAGISANNPEQQGGP-----DSLAyIMYTSGSTGTPKGVMVEQR 1663
Cdd:cd12118 89 D---AEEIAFIL-------RH-SEAKVLFVDREFeyEDLLAEGDPDFEWIPpadewDPIA-LNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1664 GV----VRLVKNSDMAFSPedRILLT------ASLGFDAMTFEVFGpllNGACL-YISDKETYldsdrlkTFIQQNGITT 1732
Cdd:cd12118 157 GAylnaLANILEWEMKQHP--VYLWTlpmfhcNGWCFPWTVAAVGG---TNVCLrKVDAKAIY-------DLIEKHKVTH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1733 LWLTSSLFNQL---SEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLAlwNGYGPTENTTFSTcFRIEHEYKHSIPI 1809
Cdd:cd12118 225 FCGAPTVLNMLanaPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVT--HVYGLTETYGPAT-VCAWKPEWDELPT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1810 ----------GRPIANSTAYIVNSRGRLQPM---GV-IGELCVGGDGLARGYFGRPELTKEKFvpnpftpgeR--MYRTG 1873
Cdd:cd12118 302 eerarlkarqGVRYVGLEEVDVLDPETMKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAF---------RggWFHSG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1874 DLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIEKVRSL 1951
Cdd:cd12118 373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKegAKVTEEEIIAF 452
|
490 500
....*....|....*....|....*..
gi 2040046167 1952 LSQQLPGFMIPAHlVELAALPLTQNGK 1978
Cdd:cd12118 453 CREHLAGFMVPKT-VVFGELPKTSTGK 478
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
489-899 |
2.68e-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: 102.92 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPdypeerlrymladsgarllvtgp 568
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP----------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 GLSVSGFSGETLEVNLSSLRTEPAENEPvcahtdggslAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVi 648
Cdd:cd05910 60 GMGRKNLKQCLQEAEPDAFIGIPKADEP----------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 vlkssfsfDASIWQLFWWMIPGASM--------YLLPQgwEKDPALMTEAFTNEGVTTAHFIPAMansfLDQVEMETEEK 720
Cdd:cd05910 129 --------DLATFPLFALFGPALGLtsvipdmdPTRPA--RADPQKLVGAIRQYGVSIVFGSPAL----LERVARYCAQH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 721 RTSLAkTLKRVFAGGEALAPQTAARFARSLPETA-VIHGYGPTEATVDAAFfrYDHEKDRERMRLP-------IGKPVPG 792
Cdd:cd05910 195 GITLP-SLRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATEALPVSSI--GSRELLATTTAATsggagtcVGRPIPG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 793 ARLYIL----------DSEKAVqPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPfyRGERMYQTGDLARWLPDGTVE 862
Cdd:cd05910 272 VRVRIIeiddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDEGRLW 348
|
410 420 430
....*....|....*....|....*....|....*..
gi 2040046167 863 WLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV 899
Cdd:cd05910 349 FCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1520-1959 |
2.81e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 102.91 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1520 VIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNA 1599
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1600 VMLLQSDrleshmagkrlfiediqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGV---VRLVKNSDMAf 1676
Cdd:cd05914 81 KAIFVSD--------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIvsnVDGVKEVVLL- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1677 SPEDRILLTASLGFD-AMTFEVFGPLLNGACLYISDKetyLDSDRLKTfIQQN------GITTLW--------------- 1734
Cdd:cd05914 128 GKGDKILSILPLHHIyPLTFTLLLPLLNGAHVVFLDK---IPSAKIIA-LAFAqvtptlGVPVPLviekifkmdiipklt 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1735 LTSSLFNQLSEQNERTFSDLSR-------------LILGGEALSPNhVNRVRNTApDLALWNGYGPTEnTTFSTCFRIEH 1801
Cdd:cd05914 204 LKKFKFKLAKKINNRKIRKLAFkkvheafggnikeFVIGGAKINPD-VEEFLRTI-GFPYTIGYGMTE-TAPIISYSPPN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1802 EYKhSIPIGRPIANSTAYIVNSrgrlQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKD 1881
Cdd:cd05914 281 RIR-LGSAGKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1882 GTIDYIGRMDDQ-VKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSghkELLAYM--------SLQAEMNIEK----V 1948
Cdd:cd05914 350 GYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL---VALAYIdpdfldvkALKQRNIIDAikweV 426
|
490
....*....|.
gi 2040046167 1949 RSLLSQQLPGF 1959
Cdd:cd05914 427 RDKVNQKVPNY 437
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
486-957 |
3.09e-22 |
|
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: 103.18 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 486 GGILTYRELdqYTNQLAIRLK-KKGVAKESVVGVLADRSPEMVIAVLAVLKAGgaYVPLDPDYP--EERLRYMLADSGAR 562
Cdd:cd05909 5 GTSLTYRKL--LTGAIALARKlAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 563 LLVTG----------PGLSVSGFSG----ETLEVNLS-----------SLRTEPAENEPVCAHTDGGSLAYVIYTSGSTG 617
Cdd:cd05909 81 TVLTSkqfieklklhHLFDVEYDARivylEDLRAKISkadkckaflagKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 618 TPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIV----LKSSFSFDASIWQLFWWMIPGAsMYLLPQGWEKDPALMTEAftn 693
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFgalpFFHSFGLTGCLWLPLLSGIKVV-FHPNPLDYKKIPELIYDK--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 694 eGVTTAHFIPAMANSFLDQVEMETeekrtslAKTLKRVFAGGEALAPQTAARFARSLpETAVIHGYGPTEA-------TV 766
Cdd:cd05909 237 -KATILLGTPTFLRGYARAAHPED-------FSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECspvisvnTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 767 DAAFfrydhekdRERMrlpIGKPVPGARLYILDSEKAVQ-PIGVAGELYIAGAGVARGYLNRPELTEERFlddpfyrGER 845
Cdd:cd05909 308 QSPN--------KEGT---VGRPLPGMEVKIVSVETHEEvPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------GDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 846 MYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGV-REAAVVA---RTEGEETELYAYIEGQDQKTA 921
Cdd:cd05909 370 WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSvpdGRKGEKIVLLTTTTDTDPSSL 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 2040046167 922 RTELGK-RLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05909 450 NDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1525-1984 |
3.58e-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: 102.54 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGayLPVTEDMPTERlewmlsdSNAVMLLQ 1604
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGA--VPVLIDPGMGR-------KNLKQCLQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 sdrleshmagkrlfieDIQLEAGIsannpeqqGGP--DSLAYIMYTSGSTGTPKGVMVEQR---GVVRLVKnSDMAFSPE 1679
Cdd:cd05910 72 ----------------EAEPDAFI--------GIPkaDEPAAILFTSGSTGTPKGVVYRHGtfaAQIDALR-QLYGIRPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1680 DRILLTASLgfdamtFEVFGPLLnGACLYISD----KETYLDSDRLKTFIQQNGITTLWLTSSLFNQLS---EQNERTFS 1752
Cdd:cd05910 127 EVDLATFPL------FALFGPAL-GLTSVIPDmdptRPARADPQKLVGAIRQYGVSIVFGSPALLERVArycAQHGITLP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1753 DLSRLILGGEALSPNHVNRVRNTAPDLA-LWNGYGPTENTTFSTCFRIEHEYKHSIP--------IGRPIANSTAYIV-- 1821
Cdd:cd05910 200 SLRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATEALPVSSIGSRELLATTTAAtsggagtcVGRPIPGVRVRIIei 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1822 --------NSRGRLqPMGVIGELCVGGDGLARGYFGRPELTKEKFVPnpfTPGERM-YRTGDLARWLKDGTIDYIGRMDD 1892
Cdd:cd05910 280 ddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKID---DNSEGFwHRMGDLGYLDDEGRLWFCGRKAH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1893 QVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMN-----IEKVRSLLSQQLPGFMIPAHLVE 1967
Cdd:cd05910 356 RVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPLPGTITprarlEQELRALAKDYPHTQRIGRFLIH 435
|
490
....*....|....*....
gi 2040046167 1968 lAALP--LTQNGKLDRRAL 1984
Cdd:cd05910 436 -PSFPvdIRHNAKIFREKL 453
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
481-959 |
4.49e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 103.44 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 481 AVRFSGG----ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYML 556
Cdd:PRK04319 62 ALRYLDAsrkeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 ADSGARLLVTGPGLS---------------VSGFSGETLE--VNLSSLRTEpAENEPVCAHTDGGSLAYVIYTSGSTGTP 619
Cdd:PRK04319 142 EDSEAKVLITTPALLerkpaddlpslkhvlLVGEDVEEGPgtLDFNALMEQ-ASDEFDIEWTDREDGAILHYTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 620 KGV------AVEHRQAAAFLsgmqrqFPLTEDDVivlkssfsfdasiwqlFWWMipgasmyllpqgweKDPALMTEafTN 693
Cdd:PRK04319 221 KGVlhvhnaMLQHYQTGKYV------LDLHEDDV----------------YWCT--------------ADPGWVTG--TS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 694 EGVttahFIPAM--ANSFLDQVEMETE-------EKRTSL---AKTLKRVFAG-GEALAPQ---TAARFARSL-----PE 752
Cdd:PRK04319 263 YGI----FAPWLngATNVIDGGRFSPErwyrileDYKVTVwytAPTAIRMLMGaGDDLVKKydlSSLRHILSVgeplnPE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 753 tAVIHGygpteatvdaaffrydhekdRERMRLPI---------------------------GKPVPGARLYILDSEKAVQ 805
Cdd:PRK04319 339 -VVRWG--------------------MKVFGLPIhdnwwmtetggimianypamdikpgsmGKPLPGIEAAIVDDQGNEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 806 PIGVAGELYIAgAG---VARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGE 882
Cdd:PRK04319 398 PPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 883 VEAALRQIDGVREAAVVARTEGEETELY-AYI------EGQDQ--KTARTELGKRLPAYMMPSSfIEMRE-WPVTPSGKL 952
Cdd:PRK04319 470 VESKLMEHPAVAEAGVIGKPDPVRGEIIkAFValrpgyEPSEElkEEIRGFVKKGLGAHAAPRE-IEFKDkLPKTRSGKI 548
|
....*..
gi 2040046167 953 DRKALPA 959
Cdd:PRK04319 549 MRRVLKA 555
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
442-935 |
4.51e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 103.80 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 442 EETAKKMLYEFNQTEPAAPLAP-TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLA 520
Cdd:PRK08279 15 LPDLPGILRGLKRTALITPDSKrSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 521 DRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGPGL-----SVSG----------FSGETLE---- 581
Cdd:PRK08279 95 ENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELveafeEARAdlarpprlwvAGGDTLDdpeg 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 582 -VNL-SSLRTEPAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDV------------ 647
Cdd:PRK08279 175 yEDLaAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVlycclplyhntg 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 648 --------------IVLKSSFSfdASiwqLFWwmipgasmyllpqgweKDPALmteaftnEGVTTAHFIPAMANSFLDQV 713
Cdd:PRK08279 255 gtvawssvlaagatLALRRKFS--AS---RFW----------------DDVRR-------YRATAFQYIGELCRYLLNQP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 714 EMETeEKRTSLAKtlkrvfAGGEALAP----QTAARFArslpETAVIHGYGPTEATVdaAFFRYDhEKDRERMRLPIGKP 789
Cdd:PRK08279 307 PKPT-DRDHRLRL------MIGNGLRPdiwdEFQQRFG----IPRILEFYAASEGNV--GFINVF-NFDGTVGRVPLWLA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 790 VPGARL-YILDSEKAVQ---------PIGVAGELY--IAGAGVARGYlNRPELTEERFLDDPFYRGERMYQTGDLARWLP 857
Cdd:PRK08279 373 HPYAIVkYDVDTGEPVRdadgrcikvKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 858 DGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV----VARTEG---------------EETELYAYIEgqdq 918
Cdd:PRK08279 452 FGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygveVPGTDGragmaaivladgaefDLAALAAHLY---- 527
|
570
....*....|....*..
gi 2040046167 919 ktartelgKRLPAYMMP 935
Cdd:PRK08279 528 --------ERLPAYAVP 536
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1070-1467 |
7.60e-22 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 101.17 E-value: 7.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1070 RMYVLQQLEDGGvGYNMPAALKLTGPLDRARLDEVFRQLIRRHESLRTSFeTGADGEPVQRIHDD----VPFQLMEL--- 1142
Cdd:cd19534 9 RWFFEQNLAGRH-HFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRF-RREDGGWQQRIRGDveelFRLEVVDLssl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1143 -------AAAEDFVRPFRLQEAPLFRAALVKEAEESHLLLVDMHHIISDGVSVGTLIREFSELYASRTLH-----PLRIQ 1210
Cdd:cd19534 87 aqaaaieALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGepiplPSKTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1211 YKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPvlELPADNarPAVRSFAGDhVSFSLDAD-TSSGLYKIARDNGCTLYM 1289
Cdd:cd19534 167 FQTWAELLAEYAQSPALLEELAYWRELPAADYW--GLPKDP--EQTYGDART-VSFTLDEEeTEALLQEANAAYRTEIND 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1290 VLLAAYSTLLARLSGQEDIIIGSPIAGR----AHKDLESVIGMFVNTLAIRTRPVENKCFSDFLREVREtALEAYEHQ-- 1363
Cdd:cd19534 242 LLLAALALAFQDWTGRAPPAIFLEGHGReeidPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKE-QLRRIPNKgi 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1364 DY-PFEELVDRLDvvRDMSRNPLFDVMF----ALQNMER-ESLTLHDLHLTT--IAHDAHKVSKFDMTlYAAEEDQetIR 1435
Cdd:cd19534 321 GYgILRYLTPEGT--KRLAFHPQPEISFnylgQFDQGERdDALFVSAVGGGGsdIGPDTPRFALLDIN-AVVEGGQ--LV 395
|
410 420 430
....*....|....*....|....*....|..
gi 2040046167 1436 FDVEFNTDIYQKQTIKKWLSYYIHILHHVIEH 1467
Cdd:cd19534 396 ITVSYSRNMYHEETIQQLADSYKEALEALIEH 427
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
2090-2307 |
7.76e-22 |
|
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: 100.89 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2090 QR-WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQFnrgIHGEL-YSLNIRDLS- 2166
Cdd:cd19531 9 QRlWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQV---ILPPLpLPLPVVDLSg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2167 -----KTAQWEKLIEDEVadlQRSIHLQTGPLLKAGLFnTMSGT--YLFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQ 2239
Cdd:cd19531 86 lpeaeREAEAQRLAREEA---RRPFDLARGPLLRATLL-RLGEDehVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 2240 PVQLPRKtdSYQYfanrlAEYAE------SSKVIREQ-SYWRTV-EKEKAAL-LPCEKPHSAADNIR-KTESFTLSEE 2307
Cdd:cd19531 162 PSPLPPL--PIQY-----ADYAVwqrewlQGEVLERQlAYWREQlAGAPPVLeLPTDRPRPAVQSFRgARVRFTLPAE 232
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
460-957 |
9.25e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 102.33 E-value: 9.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 460 PLAPTlhSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGA 539
Cdd:PRK08162 17 PLTPL--SFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 540 Y----VPLDPdypeERLRYMLADSGARLLVTGPglsvsgfsgETLEVNLSSLRTEPAENEPVCAHTDG--------GSLA 607
Cdd:PRK08162 95 LntlnTRLDA----ASIAFMLRHGEAKVLIVDT---------EFAEVAREALALLPGPKPLVIDVDDPeypggrfiGALD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 608 Y---------------------VI---YTSGSTGTPKGVAVEHRqaAAFLSGMQRQfplteddvivlkssfsfdasiwqL 663
Cdd:PRK08162 162 YeaflasgdpdfawtlpadewdAIalnYTSGTTGNPKGVVYHHR--GAYLNALSNI-----------------------L 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 664 FWWMiPGASMYL--LP----QGW-----------------EKDPALMTEAFTNEGVTtaHFIPA------MANSfldqve 714
Cdd:PRK08162 217 AWGM-PKHPVYLwtLPmfhcNGWcfpwtvaaragtnvclrKVDPKLIFDLIREHGVT--HYCGApivlsaLINA------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 715 meTEEKRTSLAKTLKRVFAGgealAPQTAARFARSlpETA---VIHGYGPTE----ATVDAAFFRYDHEKDRERMRLPIG 787
Cdd:PRK08162 288 --PAEWRAGIDHPVHAMVAG----AAPPAAVIAKM--EEIgfdLTHVYGLTEtygpATVCAWQPEWDALPLDERAQLKAR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 788 KPVP-----GARlyILDSEkAVQPIG----VAGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPD 858
Cdd:PRK08162 360 QGVRyplqeGVT--VLDPD-TMQPVPadgeTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFH-------TGDLAVLHPD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 859 GTVewlgrmdgQVKIR--------GYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL-YAYIEGQDQKTARTE----- 924
Cdd:PRK08162 430 GYI--------KIKDRskdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVpCAFVELKDGASATEEeiiah 501
|
570 580 590
....*....|....*....|....*....|...
gi 2040046167 925 LGKRLPAYMMPSSfIEMREWPVTPSGKLDRKAL 957
Cdd:PRK08162 502 CREHLAGFKVPKA-VVFGELPKTSTGKIQKFVL 533
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
480-957 |
1.05e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 102.21 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 480 PAVRFSGGILTYRELDQYTNQLAIRLKKKgvaKESVVG-VLADRSPEMV---IAVLAVLKAGGAYVPLDPDYPEERLRYM 555
Cdd:PRK12492 41 PAFSNLGVTLSYAELERHSAAFAAYLQQH---TDLVPGdRIAVQMPNVLqypIAVFGALRAGLIVVNTNPLYTAREMRHQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 556 LADSGARLLV--TGPGLSVSGFSGET-----LEVNLSSL-----------------RTEPAEN----------------- 594
Cdd:PRK12492 118 FKDSGARALVylNMFGKLVQEVLPDTgieylIEAKMGDLlpaakgwlvntvvdkvkKMVPAYHlpqavpfkqalrqgrgl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 595 --EPVCAHTDggSLAYVIYTSGSTGTPKGVAVEH-------RQAAAFLSGMQRQ-FPLTED--DVIV----LKSSFSFDA 658
Cdd:PRK12492 198 slKPVPVGLD--DIAVLQYTGGTTGLAKGAMLTHgnlvanmLQVRACLSQLGPDgQPLMKEgqEVMIaplpLYHIYAFTA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 659 SIWQLfwwMIPGASMYLL--PQ---GWEKDpaLMTEAFTNE-GVTTAhFIPAMANSFLDQVEMETeekrtslaktLKRVF 732
Cdd:PRK12492 276 NCMCM---MVSGNHNVLItnPRdipGFIKE--LGKWRFSALlGLNTL-FVALMDHPGFKDLDFSA----------LKLTN 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 733 AGGEALAPQTAARFArSLPETAVIHGYGPTEATVDAAFFRYDhekdrERMRL-PIGKPVPGARLYILDSEKAVQPIGVAG 811
Cdd:PRK12492 340 SGGTALVKATAERWE-QLTGCTIVEGYGLTETSPVASTNPYG-----ELARLgTVGIPVPGTALKVIDDDGNELPLGERG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 812 ELYIAGAGVARGYLNRPELTEErFLDdpfyrGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQID 891
Cdd:PRK12492 414 ELCIKGPQVMKGYWQQPEATAE-ALD-----AEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 892 GVREAAVVA---RTEGEETELyaYIEGQDQKTARTELG----KRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK12492 488 KVANCAAIGvpdERSGEAVKL--FVVARDPGLSVEELKayckENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1501-1988 |
1.22e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 102.03 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1501 ETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLP 1580
Cdd:PRK06710 24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1581 vTEDMPTER-LEWMLSDSNAVMLL------------QSDRLESHMAGKRL-------------FIEDIQLEAGISA---- 1630
Cdd:PRK06710 104 -TNPLYTEReLEYQLHDSGAKVILcldlvfprvtnvQSATKIEHVIVTRIadflpfpknllypFVQKKQSNLVVKVsese 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1631 -----NNPEQQGGP---------DSLAYIMYTSGSTGTPKGVMVEQRGvvrLVKNSDMAFS-----PEDRILLTASLGFd 1691
Cdd:PRK06710 183 tihlwNSVEKEVNTgvevpcdpeNDLALLQYTGGTTGFPKGVMLTHKN---LVSNTLMGVQwlyncKEGEEVVLGVLPF- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1692 amtFEVFGPLlngACLYISDKETY-------LDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLS--RLILGGE 1762
Cdd:PRK06710 259 ---FHVYGMT---AVMNLSIMQGYkmvlipkFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISsiRACISGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1763 ALSPNHVNRVRNTAPDLALWNGYGPTENTTFS-TCFRIEHEYKHSIpiGRPIANSTAYIVN-SRGRLQPMGVIGELCVGG 1840
Cdd:PRK06710 333 APLPVEVQEKFETVTGGKLVEGYGLTESSPVThSNFLWEKRVPGSI--GVPWPDTEAMIMSlETGEALPPGEIGEIVVKG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1841 DGLARGYFGRPELTKEKFvpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAA 1920
Cdd:PRK06710 411 PQIMKGYWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1921 VIVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPE 1988
Cdd:PRK06710 484 TIGVPDPYRGETVKAFVVLKegTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
461-960 |
1.97e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 100.99 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 461 LAPTlhSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAY 540
Cdd:PRK13382 43 MGPT--SGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 541 VPLDPDYPEERLRYMLADSGA--------------RLLVTGPGLSVS-GFSGETLEVNLSSLRTEPAENEPVCAHTDGGS 605
Cdd:PRK13382 121 LLLNTSFAGPALAEVVTREGVdtviydeefsatvdRALADCPQATRIvAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 layVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFsFDAsiWQlFWWMIPGASMyllpqgweKDPA 685
Cdd:PRK13382 201 ---ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPM-FHA--WG-FSQLVLAASL--------ACTI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 686 LMTEAFTNEGV---------TTAHFIPAMANSFLDQVEmetEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPEtAVI 756
Cdd:PRK13382 266 VTRRRFDPEATldlidrhraTGLAVVPVMFDRIMDLPA---EVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD-VIY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 757 HGYGPTEATVDAAffrydhEKDRERMRLP--IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYlnRPELTEEr 834
Cdd:PRK13382 342 NNYNATEAGMIAT------ATPADLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 835 flddpFYRGerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEETELYA 911
Cdd:PRK13382 413 -----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDeqyGQRLAAFV 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 912 YIEGQDQKT---ARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALPAP 960
Cdd:PRK13382 486 VLKPGASATpetLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
484-968 |
2.42e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 100.36 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 484 FSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARL 563
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 564 LVTGPGL-----------------------SVSGFsgETLEVNLSSLRTEPAENEpvcahTDGGSLAyviYTSGSTGTPK 620
Cdd:PRK08276 87 LIVSAALadtaaelaaelpagvplllvvagPVPGF--RSYEEALAAQPDTPIADE-----TAGADML---YSSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 621 GV--AVEHRQ----AAAFLSGMQRQFPLTEDDViVLKSSFSFDASIWQLFWWMIPGASMYLLPQGWEKDPALmtEAFTNE 694
Cdd:PRK08276 157 GIkrPLPGLDpdeaPGMMLALLGFGMYGGPDSV-YLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEAL--ALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 695 GVTTAHFIPAMansFldqVEM--ETEEKRTSL-AKTLKRVFAGGeALAPQTAARfarslpetAVIHGYGP--------TE 763
Cdd:PRK08276 234 RVTHSQLVPTM---F---VRMlkLPEEVRARYdVSSLRVAIHAA-APCPVEVKR--------AMIDWWGPiiheyyasSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 764 A---TVDAAffrydhekdRERMRLP--IGKPVPGaRLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERfldd 838
Cdd:PRK08276 299 GggvTVITS---------EDWLAHPgsVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA---- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 839 pfYRGERMYQTGDLArWLPDgtvewlgrmDGQVKIR----------GYRIEPGEVEAALRQIDGVREAAV--VARTE-GE 905
Cdd:PRK08276 365 --RNPHGWVTVGDVG-YLDE---------DGYLYLTdrksdmiisgGVNIYPQEIENLLVTHPKVADVAVfgVPDEEmGE 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 906 etELYAYIEGQDQKTARTELG--------KRLPAYMMPSSFIEMREWPVTPSGKLDRKALPAPD-GAAERRV 968
Cdd:PRK08276 433 --RVKAVVQPADGADAGDALAaeliawlrGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYwEGRQRAI 502
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
490-957 |
2.64e-21 |
|
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: 100.62 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKK-GVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTG- 567
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSd 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 568 -------------PGLS----VSGFSGETLeVNLSSLRTEpAENEPVCAHTDGGSLAYVIYTSGSTGTPKgvAVEHRQAA 630
Cdd:cd05928 123 elapevdsvasecPSLKtkllVSEKSRDGW-LNFKELLNE-ASTEHHCVETGSQEPMAIYFTSGTTGSPK--MAEHSHSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 631 A---FLSGMQRQFPLTEDDVIVLKSSFSF-DASIWQLFWWMIPGASMY--LLPQgweKDPALMTEAFTNEGVTTAHFIPA 704
Cdd:cd05928 199 LglgLKVNGRYWLDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGACVFvhHLPR---FDPLVILKTLSSYPITTFCGAPT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 705 MANSFLDQvemetEEKRTSLaKTLKRVFAGGEALAPQTAARFaRSLPETAVIHGYGPTEATVDAAFFRydhekdreRMRL 784
Cdd:cd05928 276 VYRMLVQQ-----DLSSYKF-PSLQHCVTGGEPLNPEVLEKW-KAQTGLDIYEGYGQTETGLICANFK--------GMKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 785 P---IGKPVPGARLYILDSEKAVQPIGVAGELYI-----AGAGVARGYLNRPELTEERFlddpfyRGErMYQTGDLARWL 856
Cdd:cd05928 341 KpgsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATI------RGD-FYLTGDRGIMD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 857 PDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEETE----LYAYIEGQDQKTARTELG--- 926
Cdd:cd05928 414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDpirGEVVKafvvLAPQFLSHDPEQLTKELQqhv 493
|
490 500 510
....*....|....*....|....*....|..
gi 2040046167 927 KRLPA-YMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05928 494 KSVTApYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
608-953 |
2.94e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 98.22 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 608 YVIYTSGSTGTPKGVAveHRQAAAFLS---GMQRQFPLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYL---LPQGWE 681
Cdd:cd05924 7 YILYTGGTTGMPKGVM--WRQEDIFRMlmgGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTafgGLLGGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 682 K--------DPALMTEAFTNEGVTTAHFI-PAMANSFLDqvemETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPE 752
Cdd:cd05924 85 TvvlpddrfDPEEVWRTIEKHKVTSMTIVgDAMARPLID----ALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 753 TAVIHGYGPTEAtvdaAFFRYDHEKDRERMRLPIGKPVPGARLyiLDSEKAVQPIGVAGELYIAGAG-VARGYLNRPELT 831
Cdd:cd05924 161 ITLVDAFGSSET----GFTGSGHSAGSGPETGPFTRANPDTVV--LDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 832 EERFlddPFYRGERMYQTGDLARWLPDGTVEWLGRmdGQVKIR--GYRIEPGEVEAALRQIDGVREA------------- 896
Cdd:cd05924 235 AETF---PEVDGVRYAVPGDRATVEADGTVTLLGR--GSVCINtgGEKVFPEEVEEALKSHPAVYDVlvvgrpderwgqe 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 897 --AVVARTEGEETELYAYIEGQDQKTARtelgkrlpaYMMPSSFIEMREWPVTPSGKLD 953
Cdd:cd05924 310 vvAVVQLREGAGVDLEELREHCRTRIAR---------YKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1503-1986 |
5.21e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.96 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1503 ISRLFEYQAAKTPHAPAVIY--DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLP 1580
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVtaDRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1581 VTEDMP-TERLEWMLSDSNAVMLLQSD-----RLESH--------MAGKRLFIEDI-QLEAGISANNPEQQGGPDSL--- 1642
Cdd:PRK05852 98 LDPALPiAEQRVRSQAAGARVVLIDADgphdrAEPTTrwwpltvnVGGDSGPSGGTlSVHLDAATEPTPATSTPEGLrpd 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1643 -AYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFSPEDRilltaslgfDAmTFEVFgPLLNGACLYISDKETYLDSDRL 1721
Cdd:PRK05852 178 dAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPR---------DA-TVAVM-PLYHGHGLIAALLATLASGGAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1722 ----------KTF---IQQNGITtlWLTSS------LFNQLSEQNERTFSDLSRLILGGEA-LSPNHVNRVRNT--APDL 1779
Cdd:PRK05852 247 llpargrfsaHTFwddIKAVGAT--WYTAVptihqiLLERAATEPSGRKPAALRFIRSCSApLTAETAQALQTEfaAPVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1780 AlwnGYGPTENTTFSTCFRIEHEYKHSIPIGR--PIANSTA---YIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELT 1854
Cdd:PRK05852 325 C---AFGMTEATHQVTTTQIEGIGQTENPVVStgLVGRSTGaqiRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTIT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1855 KEKFvpnpfTPGerMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSgHKELL 1934
Cdd:PRK05852 402 AANF-----TDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL-YGEAV 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1935 AYMSLQAEMNIEKVRSLLSQ---QLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK05852 474 AAVIVPRESAPPTAEELVQFcreRLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1525-1978 |
5.73e-21 |
|
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: 98.58 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAylpvtedmpterlewmlsdsnAVMLLQ 1604
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV---------------------AALINY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 SDRLES--H---MAGKRLFIEDiqleagisannpeqqggpdsLAYIMYTSGSTGTPKGVMVEQRGVVR---LVKNSDMAF 1676
Cdd:cd05940 61 NLRGESlaHclnVSSAKHLVVD--------------------AALYIYTSGTTGLPKAAIISHRRAWRggaFFAGSGGAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1677 sPEDRILLTASLGFD-AMTFEVFGPLLNGACLYISDKETYLD--SDRLK---TFIQQNGittlWLTSSLFNQLSEQNERT 1750
Cdd:cd05940 121 -PSDVLYTCLPLYHStALIVGWSACLASGATLVIRKKFSASNfwDDIRKyqaTIFQYIG----ELCRYLLNQPPKPTERK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1751 FSdlSRLILGgEALSPNHVNRVRNTAPDLALWNGYGPTE-NTTF-------STCFRIEHEYKHSIPI---------GRPI 1813
Cdd:cd05940 196 HK--VRMIFG-NGLRPDIWEEFKERFGVPRIAEFYAATEgNSGFinffgkpGAIGRNPSLLRKVAPLalvkydlesGEPI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1814 ANSTAYIVNSrgrlqPMGVIGELCVGGDGLAR--GYFGrPELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMD 1891
Cdd:cd05940 273 RDAEGRCIKV-----PRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1892 DQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSGHKELLAYMSLQA--EMNIEKVRSLLSQQLPGFMIPAHLVEL 1968
Cdd:cd05940 347 DTFRWKGENVSTTEVAAVLGAFPGVEEANVYgVQVPGTDGRAGMAAIVLQPneEFDLSALAAHLEKNLPGYARPLFLRLQ 426
|
490
....*....|
gi 2040046167 1969 AALPLTQNGK 1978
Cdd:cd05940 427 PEMEITGTFK 436
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
464-957 |
6.37e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 99.57 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLK-----KKGvakeSVVGVLADRSPEMVIAVLAVLKAGG 538
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgelqlKKG----DRVALMMPNCLQYPIATFGVLRAGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 539 AYVPLDPDYPEERLRYMLADSGARLLV-----------------------TGPGlSVSGFSGETLeVNL----------- 584
Cdd:PRK08751 102 TVVNVNPLYTPRELKHQLIDSGASVLVvidnfgttvqqviadtpvkqvitTGLG-DMLGFPKAAL-VNFvvkyvkklvpe 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 585 ----SSLRTEPA-----ENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHR-------QAAAFLSGMQRQFPLTEDDVI 648
Cdd:PRK08751 180 yrinGAIRFREAlalgrKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRnlvanmqQAHQWLAGTGKLEEGCEVVIT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 649 VLKSSFSFDASIWQLFWWMIPGASmYLLPQgwEKD-PALMTE-------AFTneGVTTAhFIPAMANSFLDQVEMETeek 720
Cdd:PRK08751 260 ALPLYHIFALTANGLVFMKIGGCN-HLISN--PRDmPGFVKElkktrftAFT--GVNTL-FNGLLNTPGFDQIDFSS--- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 721 rtslaktLKRVFAGGEALAPQTAARFARSLPETaVIHGYGPTEATVDAAFfrydHEKDRERMRLPIGKPVPGARLYILDS 800
Cdd:PRK08751 331 -------LKMTLGGGMAVQRSVAERWKQVTGLT-LVEAYGLTETSPAACI----NPLTLKEYNGSIGLPIPSTDACIKDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 801 EKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEP 880
Cdd:PRK08751 399 AGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLH------TGDIARMDEQGFVYIVDRKKDMILVSGFNVYP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 881 GEVEAALRQIDGVREAAVVARTEGEETELY-AYIEGQDQKTARTELGKR----LPAYMMPsSFIEMR-EWPVTPSGKLDR 954
Cdd:PRK08751 473 NEIEDVIAMMPGVLEVAAVGVPDEKSGEIVkVVIVKKDPALTAEDVKAHaranLTGYKQP-RIIEFRkELPKTNVGKILR 551
|
...
gi 2040046167 955 KAL 957
Cdd:PRK08751 552 REL 554
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
420-959 |
7.70e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 98.92 E-value: 7.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 420 RHIIGSVIADPNQQIAQIALLGEetakkmLYEfNQTEPAAPLAPTlhsfftrrAALSPNLPAVRFSGGILTYRELDQYTN 499
Cdd:PRK13383 7 RALVRSGLLNPPSPRAVLRLLRE------ASR-GGTNPYTLLAVT--------AARWPGRTAIIDDDGALSYRELQRATE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 500 QLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERL---------RYMLADSGARLLVTGPGL 570
Cdd:PRK13383 72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALaaalrahhiSTVVADNEFAERIAGADD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 571 SVsgfsgetLEVNLSSLRTEPAENEPVCAhtdgGSLAYVIYTSGSTGTPKGVAvehrQAAAFLSGMQRQFPLTEDDVIVL 650
Cdd:PRK13383 152 AV-------AVIDPATAGAEESGGRPAVA----APGRIVLLTSGTTGKPKGVP----RAPQLRSAVGVWVTILDRTRLRT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 651 KSSFSFDASIWQ-----LFWWMIPGASMYLLPQGWEKDPALMTEAFTNEGVTTAhfIPAMANSFLDqveMETEEKRTSLA 725
Cdd:PRK13383 217 GSRISVAMPMFHglglgMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTA--VPVVLARILE---LPPRVRARNPL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 726 KTLKRVFAGGEALAPQTAARFARSLPETaVIHGYGPTEATVDAAFFRYDHEKDRErmrlPIGKPVPGARLYILDSEKavQ 805
Cdd:PRK13383 292 PQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALATPADLRDAPE----TVGKPVAGCPVRILDRNN--R 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 806 PIG--VAGELYIAGagvargylnrpELTEERFLDDpfyrGER-----MYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRI 878
Cdd:PRK13383 365 PVGprVTGRIFVGG-----------ELAGTRYTDG----GGKavvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENV 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 879 EPGEVEAALRQIDGVREAAVVARTEGE-ETELYAYI-----EGQDQKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKL 952
Cdd:PRK13383 430 YPRAVENALAAHPAVADNAVIGVPDERfGHRLAAFVvlhpgSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKV 509
|
....*..
gi 2040046167 953 DRKALPA 959
Cdd:PRK13383 510 LRKELPG 516
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
457-957 |
8.87e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 99.15 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 457 PAAPLAPTLHSFFTRRAalSPNLPAV--RFSGGILTYRELDQYTNQLAIRLKKK-GVAKESVVGVLADRSPEMVIAVLAV 533
Cdd:PLN02574 35 PSDPNLDAVSFIFSHHN--HNGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 534 LKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP---------GLSVSGFSGEtleVNLSSLRTEPAEN---------- 594
Cdd:PLN02574 113 LSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPenveklsplGVPVIGVPEN---YDFDSKRIEFPKFyelikedfdf 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 595 --EPVCAHTDggsLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQR----QFPLTEDDVIVLKSSFSFDASIWQLFwwmi 668
Cdd:PLN02574 190 vpKPVIKQDD---VAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDNVYLAALPMFHIYGLSLF---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 669 pgaSMYLLPQGW------EKDPALMTEAFTNEGVTtaHF--IPAMansfLDQVEMETEEKRTSLAKTLKRVFAGGEALAP 740
Cdd:PLN02574 263 ---VVGLLSLGStivvmrRFDASDMVKVIDRFKVT--HFpvVPPI----LMALTKKAKGVCGEVLKSLKQVSCGAAPLSG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 741 QTAARFARSLPETAVIHGYGPTEATvdAAFFR-YDHEKDRERMRlpIGKPVPGARLYILD-SEKAVQPIGVAGELYIAGA 818
Cdd:PLN02574 334 KFIQDFVQTLPHVDFIQGYGMTEST--AVGTRgFNTEKLSKYSS--VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 819 GVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV 898
Cdd:PLN02574 410 GVMKGYLNNPKATQSTIDKDGWLR------TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 899 VARTEGEETELYAYIEGQDQKTARTE------LGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PLN02574 484 TAVPDKECGEIPVAFVVRRQGSTLSQeavinyVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
473-952 |
1.26e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 98.16 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 473 AALSPNLPAVRF--SGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEE 550
Cdd:PRK13390 7 AQIAPDRPAVIVaeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 551 RLRYMLADSGARLLVTGPGLS-VSGFSGETLEVNLS---------SLRTEPAENEPVCAHTDGGslAYVIYTSGSTGTPK 620
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDgLAAKVGADLPLRLSfggeidgfgSFEAALAGAGPRLTEQPCG--AVMLYSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 621 GVAVEhrqaaafLSGMQRQFPltEDDVIVLKSSFsFDASIWQLFWWMIPgaSMYLLPQGWekdpALMTEAFTNEGVTTAH 700
Cdd:PRK13390 165 GIQPD-------LPGRDVDAP--GDPIVAIARAF-YDISESDIYYSSAP--IYHAAPLRW----CSMVHALGGTVVLAKR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 701 FIPAMANSFLdqvemetEEKRTSLAKTLKRVFAGGEALAPQTAARFarSLPE-TAVIHGYGPTEATVDAAF--------F 771
Cdd:PRK13390 229 FDAQATLGHV-------ERYRITVTQMVPTMFVRLLKLDADVRTRY--DVSSlRAVIHAAAPCPVDVKHAMidwlgpivY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 772 RYDHEKDRERMRL-----------PIGKPVPGArLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELT-EERFLDDP 839
Cdd:PRK13390 300 EYYSSTEAHGMTFidspdwlahpgSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTaAAQHPAHP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 840 FYRgermyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETE-------LYAY 912
Cdd:PRK13390 379 FWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEqvkaviqLVEG 453
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2040046167 913 IEGQDQkTARTELG---KRLPAYMMPSSFIEMREWPVTPSGKL 952
Cdd:PRK13390 454 IRGSDE-LARELIDytrSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1645-1980 |
1.45e-20 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 95.45 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1645 IMYTSGSTGTPKGVMVEQRGVvrLVKNSDMAFS---PEDRILLTAS----LGFDAMTFEVFgpLLNGACLYISDketyLD 1717
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQAL--LAQALVLAVLqaiDEGTVFLNSGplfhIGTLMFTLATF--HAGGTNVFVRR----VD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1718 SDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLilggEALSPNHvNRVRNTAPDLALWN----GYGPTENTTF 1793
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSL----RSSPAAP-EWNDMATVDTSPWGrkpgGYGQTEVMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1794 STcfrIEHEYKHSIPI-GRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVpnpftpgERMYRT 1872
Cdd:cd17636 152 AT---FAALGGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGWHHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1873 GDLARWLKDGTIDYIG---RMddqVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSL-------QAE 1942
Cdd:cd17636 222 NDLGRREPDGSLSFVGpktRM---IKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLkpgasvtEAE 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 2040046167 1943 MnIEKVRSLLSQqlpgFMIPAHLVELAALPLTQNGKLD 1980
Cdd:cd17636 299 L-IEHCRARIAS----YKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1511-1922 |
1.94e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 97.64 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAV-IYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPV-TEDMPTE 1588
Cdd:PRK07514 12 AFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLnTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1589 rLEWMLSDSN-AVMLLQSDRLE--SHMAGKR----LFIED-------IQLEAGISANNPEQQGGPDSLAYIMYTSGSTGT 1654
Cdd:PRK07514 92 -LDYFIGDAEpALVVCDPANFAwlSKIAAAAgaphVETLDadgtgslLEAAAAAPDDFETVPRGADDLAAILYTSGTTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1655 PKGVMVEQRgvvRLVKNSDM-----AFSPEDR------ILLTASLgFDAMTfevfGPLLNGACLYISDKetyLDSDRLKT 1723
Cdd:PRK07514 171 SKGAMLSHG---NLLSNALTlvdywRFTPDDVlihalpIFHTHGL-FVATN----VALLAGASMIFLPK---FDPDAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1724 FIQQN----GITTLWltsslfnqlseqnertfsdlSRLiLGGEALSPNHVNRVR----NTAPDLA-------------LW 1782
Cdd:PRK07514 240 LMPRAtvmmGVPTFY--------------------TRL-LQEPRLTREAAAHMRlfisGSAPLLAethrefqertghaIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1783 NGYGPTEnttfsTCFRIEHEYKHS-IP--IGRPIANSTAYIVNSR-GRLQPMGVIGELCVGGDGLARGYFGRPELTKEKF 1858
Cdd:PRK07514 299 ERYGMTE-----TNMNTSNPYDGErRAgtVGFPLPGVSLRVTDPEtGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1859 VPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI 1922
Cdd:PRK07514 374 RADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI 431
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
489-893 |
1.97e-20 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 97.67 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAG----GAYVPLDpdypEERLRYMLADSGARLL 564
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNipivTVYATLG----EDALIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 565 VTGPGLSvsgfsgetlevnlsslrtepaenepvcahtdggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFP--L 642
Cdd:cd17639 82 FTDGKPD---------------------------------DLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 643 TEDDVIV----LKSSFSFDASIWQLFWWMIPG-ASMYLL-------PQG--WEKDPALMTeaftneGVttahfiPAMANS 708
Cdd:cd17639 129 GPDDRYLaylpLAHIFELAAENVCLYRGGTIGyGSPRTLtdkskrgCKGdlTEFKPTLMV------GV------PAIWDT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 709 FLDQVEMETEEKrTSLAKTL----------------------KRVFA---------------GGEALAPQTAaRFARSL- 750
Cdd:cd17639 197 IRKGVLAKLNPM-GGLKRTLfwtayqsklkalkegpgtplldELVFKkvraalggrlrymlsGGAPLSADTQ-EFLNIVl 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 751 -PetaVIHGYGPTEATVDAAFFRYDH-EKDRermrlpIGKPVPGARLYILDSE------KAVQPigvAGELYIAGAGVAR 822
Cdd:cd17639 275 cP---VIQGYGLTETCAGGTVQDPGDlETGR------VGPPLPCCEIKLVDWEeggystDKPPP---RGEILIRGPNVFK 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 823 GYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIR-GYRIEPGEVEAALRQ---IDGV 893
Cdd:cd17639 343 GYYKNPEKTKEAFDGDGWFH------TGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSnplVNNI 411
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1638-1988 |
2.40e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 97.91 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 GPDSLAYIMYTSGSTGTPKGVMVEQRGVVrlvknSDMAfspEDRILLTASLG--------------FDAMTFEVFGPLLN 1703
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLV-----ANML---QCRALMGSNLNegceiliaplplyhIYAFTFHCMAMMLI 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1704 GA-CLYISD--------KEtyLDSDRLKTFIqqnGITTLwltsslFNQLSeQNER----TFSDLSRLILGGEALSPNHVN 1770
Cdd:PRK05677 277 GNhNILISNprdlpamvKE--LGKWKFSGFV---GLNTL------FVALC-NNEAfrklDFSALKLTLSGGMALQLATAE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1771 RVRNTApDLALWNGYGPTENTTFSTCFRIEHEYKHSIpiGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGR 1850
Cdd:PRK05677 345 RWKEVT-GCAICEGYGMTETSPVVSVNPSQAIQVGTI--GIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQR 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1851 PELTKEKFvpnpftPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSG 1929
Cdd:PRK05677 422 PEATDEIL------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIgVPDEKSG 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1930 -HKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPE 1988
Cdd:PRK05677 496 eAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
477-957 |
2.44e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 97.91 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAV------RFS--------GGILTYRELDQYTNQLAIRLKKKGVAKESvvGVLADRSPEMV---IAVLAVLKAGGA 539
Cdd:PRK05677 24 PNIQAVlkqscqRFAdkpafsnlGKTLTYGELYKLSGAFAAWLQQHTDLKPG--DRIAVQLPNVLqypVAVFGAMRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 540 YVPLDPDYPEERLRYMLADSGARLLV---------------TG-------------PGLS--------------VSGFS- 576
Cdd:PRK05677 102 VVNTNPLYTAREMEHQFNDSGAKALVclanmahlaekvlpkTGvkhvivtevadmlPPLKrllinavvkhvkkmVPAYHl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 577 GETLEVN--LSSLRTEPAENepvcAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAflsGMQRQFPLTEDDV-----IV 649
Cdd:PRK05677 182 PQAVKFNdaLAKGAGQPVTE----ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVA---NMLQCRALMGSNLnegceIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 650 LKS-------SFSFDASIWqlfwwMIPGASMYLLPQgwEKD-PALMTE-------AFTneGVTTAhFIpAMANSfldqve 714
Cdd:PRK05677 255 IAPlplyhiyAFTFHCMAM-----MLIGNHNILISN--PRDlPAMVKElgkwkfsGFV--GLNTL-FV-ALCNN------ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 715 metEEKRTSLAKTLKRVFAGGEALAPQTAARFaRSLPETAVIHGYGPTEATVDAAFFRYDHekdrerMRL-PIGKPVPGA 793
Cdd:PRK05677 318 ---EAFRKLDFSALKLTLSGGMALQLATAERW-KEVTGCAICEGYGMTETSPVVSVNPSQA------IQVgTIGIPVPST 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 794 RLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKI 873
Cdd:PRK05677 388 LCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLK------TGDIALIQEDGYMRIVDRKKDMILV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 874 RGYRIEPGEVEAALRQIDGVREAAVVA---RTEGEETELYAYI---EGQDQKTARTELGKRLPAYMMPSSfIEMR-EWPV 946
Cdd:PRK05677 462 SGFNVYPNELEDVLAALPGVLQCAAIGvpdEKSGEAIKVFVVVkpgETLTKEQVMEHMRANLTGYKVPKA-VEFRdELPT 540
|
570
....*....|.
gi 2040046167 947 TPSGKLDRKAL 957
Cdd:PRK05677 541 TNVGKILRREL 551
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1499-2043 |
2.75e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 98.57 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1499 KHETISRLFEYQAAKT--PHAPAViYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGG 1576
Cdd:PRK06060 2 RNGNLAGLLAEQASEAgwYDRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1577 AYLPVTEDMPTERLEWMLSDSNAVMLLQSDRLESHMAGKRLfIEDIQLEAGISANNP---EQQGGpDSLAYIMYTSGSTG 1653
Cdd:PRK06060 81 MAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRV-AEAAELMSEAARVAPggyEPMGG-DALAYATYTSGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1654 TPKGVMVEQRGVVRLVK---NSDMAFSPEDRILLTASLGFD-AMTFEVFGPLLNGACLYISdkETYLDSDRLKTFIQQNG 1729
Cdd:PRK06060 159 PPKAAIHRHADPLTFVDamcRKALRLTPEDTGLCSARMYFAyGLGNSVWFPLATGGSAVIN--SAPVTPEAAAILSARFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1730 ITTLWLTSSLFNQLSEQ-NERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTE-NTTFSTcfRIEHEYKHSi 1807
Cdd:PRK06060 237 PSVLYGVPNFFARVIDScSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEvGQTFVS--NRVDEWRLG- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1808 PIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPEltkekfvpnPFTPGERMYRTGDLARWLKDGTIDYI 1887
Cdd:PRK06060 314 TLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1888 GRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIvrtgpsGHKELLAYMSLQA-----------EMNIEKVRSLLSQQL 1956
Cdd:PRK06060 385 CRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVV------AVRESTGASTLQAflvatsgatidGSVMRDLHRGLLNRL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1957 PGFMIPAHLVELAALPLTQNGKLDRRAL--------------------------PEPETTAINTAYAPPRNQLEERLAVI 2010
Cdd:PRK06060 459 SAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsptkpiwelsltepgsgvraqrdDLSASNMTIAGGNDGGATLRERLVAL 538
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 2011 WQE--------VLG--VEKVGIED--------SFFELGGDSIKALQVSARL 2043
Cdd:PRK06060 539 RQErqrlvvdaVCAeaAKMLGEPDpwsvdqdlAFSELGFDSQMTVTLCKRL 589
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
609-952 |
6.20e-20 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 93.72 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDD--VIV--LKSSFSFDASIwqlFWWMIPGASMYllPQGWEKDP 684
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDryLIInpFFHTFGYKAGI---VACLLTGATVV--PVAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 685 ALMtEAFTNEGVTTAHFIPAMANSFLDqvemETEEKRTSLAkTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEA 764
Cdd:cd17638 80 AIL-EAIERERITVLPGPPTLFQSLLD----HPGRKKFDLS-SLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 765 TVdAAFFRYDheKDRERMRLPIGKPVPGARLYILDsekavqpigvAGELYIAGAGVARGYLNRPELTEERFLDDPFYrge 844
Cdd:cd17638 154 GV-ATMCRPG--DDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWL--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 845 rmyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETEL-YAYIEGQDQKTART 923
Cdd:cd17638 218 ---HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVgKAFVVARPGVTLTE 294
|
330 340 350
....*....|....*....|....*....|....
gi 2040046167 924 E-----LGKRLPAYMMPSSFIEMREWPVTPSGKL 952
Cdd:cd17638 295 EdviawCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
2085-2513 |
6.26e-20 |
|
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: 94.68 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2085 PWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGqlqqfnrgiHGELYSLNIRD 2164
Cdd:cd19542 3 PCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSA---------EGTFLQVVLKS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2165 LSKTAQWEKLIEDEVADLQRS----IHLQTGPLLKAGLFNTMSG-TYLFLTIHHLVVDGVSWRILLEDLSAAYSqaaaGQ 2239
Cdd:cd19542 74 LDPPIEEVETDEDSLDALTRDllddPTLFGQPPHRLTLLETSSGeVYLVLRISHALYDGVSLPIILRDLAAAYN----GQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2240 PvqLPRKTDSYQYfanrlAEYAESSKVIREQSYWRTV-EKEKAALLPCEKPHSAADN-IRKTESFTLSeedthvlIHKVN 2317
Cdd:cd19542 150 L--LPPAPPFSDY-----ISYLQSQSQEESLQYWRKYlQGASPCAFPSLSPKRPAERsLSSTRRSLAK-------LEAFC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2318 NAYNTDTQDILLTAASLALCDWMGERKlrIAMeGH---GRDhtLPELDISRTVGWFTTIYPVLIDLHHAAegelglavkT 2394
Cdd:cd19542 216 ASLGVTLASLFQAAWALVLARYTGSRD--VVF-GYvvsGRD--LPVPGIDDIVGPCINTLPVRVKLDPDW---------T 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2395 VKDTLGRIPD---KGMGYG------ILKYLTSSENKTiqfgkapeiGFNYLGQFNDTERQQKFSFSG--LASGKDITPTW 2463
Cdd:cd19542 282 VLDLLRQLQQqylRSLPHQhlslreIQRALGLWPSGT---------LFNTLVSYQNFEASPESELSGssVFELSAAEDPT 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2464 QREQTLEMSAmvRQNQLHFNLSYPPSRFHTTTMKQLLHMVKHNLHQIIKH 2513
Cdd:cd19542 353 EYPVAVEVEP--SGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1528-1989 |
1.65e-19 |
|
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: 94.84 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1528 TYRELNQRANRIAAALR-ANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQSD 1606
Cdd:cd05928 43 SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1607 RLESHMAGKRLFIEDIQLEAGISANNPE-------------------QQGGPDSLAyIMYTSGSTGTPK----------- 1656
Cdd:cd05928 123 ELAPEVDSVASECPSLKTKLLVSEKSRDgwlnfkellneastehhcvETGSQEPMA-IYFTSGTTGSPKmaehshsslgl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1657 GVMVEQRGVVRLvKNSDMAFSPEDRILLTASLGfdamtfEVFGPLLNGACLYIS-----DKETYLDSdrLKTFiqqnGIT 1731
Cdd:cd05928 202 GLKVNGRYWLDL-TASDIMWNTSDTGWIKSAWS------SLFEPWIQGACVFVHhlprfDPLVILKT--LSSY----PIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1732 TLWLTSSLFNQLSEQNERT--FSDLSRLILGGEALSPNHVNRVRNTApDLALWNGYGPTEntTFSTCFRIEHEYKHSIPI 1809
Cdd:cd05928 269 TFCGAPTVYRMLVQQDLSSykFPSLQHCVTGGEPLNPEVLEKWKAQT-GLDIYEGYGQTE--TGLICANFKGMKIKPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1810 GRPIANSTAYIVNSRGRLQPMGVIGELC--VGGD---GLARGYFGRPELTKEKFVPNpftpgerMYRTGDLARWLKDGTI 1884
Cdd:cd05928 346 GKASPPYDVQIIDDNGNVLPPGTEGDIGirVKPIrpfGLFSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1885 DYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEM---NIEKVRSLLSQQLPGFMI 1961
Cdd:cd05928 419 WFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFlshDPEQLTKELQQHVKSVTA 498
|
490 500 510
....*....|....*....|....*....|..
gi 2040046167 1962 P---AHLVELAA-LPLTQNGKLDRRALPEPET 1989
Cdd:cd05928 499 PykyPRKVEFVQeLPKTVTGKIQRNELRDKEW 530
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
472-931 |
2.74e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 94.62 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 472 RAALSPNLPAVRF------SGGI---LTYRELDQYTNQLAIRLKKKGVAKESVVgVLADRSPEMVIAVLAVLKAGGAYVP 542
Cdd:PRK05850 10 RASLQPDDAAFTFidyeqdPAGVaetLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 543 LDPDYP---EERLRYMLADSG-ARLLVTGPGLS-----VSGFSGET----LEVNLSSLrtePAENEPVCAHTDGGSLAYV 609
Cdd:PRK05850 89 LSVPQGgahDERVSAVLRDTSpSVVLTTSAVVDdvteyVAPQPGQSappvIEVDLLDL---DSPRGSDARPRDLPSTAYL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 610 IYTSGSTGTPKGVAVEHRQAAA-FLSGMQRQFP-----LTEDDVIVLKSSFSFDAS-IWQLFWWMIPGASMYLL-PQGWE 681
Cdd:PRK05850 166 QYTSGSTRTPAGVMVSHRNVIAnFEQLMSDYFGdtggvPPPDTTVVSWLPFYHDMGlVLGVCAPILGGCPAVLTsPVAFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 682 KDPA-LMTEAFTNEGVTTAhfipamANSFldqvEMETEEKRTS---LA-KTLKRVFA---GGEALAPQT----AARFAR- 748
Cdd:PRK05850 246 QRPArWMQLLASNPHAFSA------APNF----AFELAVRKTSdddMAgLDLGGVLGiisGSERVHPATlkrfADRFAPf 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 749 SLPETAVIHGYGPTEATVDAA---------FFRYDHEKdrermrLPIGKPVP-----GARL--Y---------ILDSEKA 803
Cdd:PRK05850 316 NLRETAIRPSYGLAEATVYVAtrepgqppeSVRFDYEK------LSAGHAKRcetggGTPLvsYgsprsptvrIVDPDTC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 804 VQ-PIGVAGELYIAGAGVARGYLNRPELTEERF---LDD--------PFYRgermyqTGDLArWLPDGTVEWLGRMDGQV 871
Cdd:PRK05850 390 IEcPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDpspgtpegPWLR------TGDLG-FISEGELFIVGRIKDLL 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 872 KIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEEtELYAYIEGQDQKTARTELGKRLPA 931
Cdd:PRK05850 463 IVDGRNHYPDDIEATIQEITGGRVAAISVPDDGTE-KLVAIIELKKRGDSDEEAMDRLRT 521
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
454-855 |
3.92e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 94.18 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 454 QTEPAAPLAPTLHSFFTRRAALSPNLPAV--RFSGG---ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVI 528
Cdd:PRK08180 30 SAEPLGDYPRRLTDRLVHWAQEAPDRVFLaeRGADGgwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 529 AVLAVLKAGGAYVPLDPDY-----PEERLRYML---------ADSGAR----LLVTGPG----LSVSGFSGETLEVNLSS 586
Cdd:PRK08180 110 LALAAMYAGVPYAPVSPAYslvsqDFGKLRHVLelltpglvfADDGAAfaraLAAVVPAdvevVAVRGAVPGRAATPFAA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 587 L--RTEPAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHR-----QAaaflsgMQRQ---FPLTEDDVIV--LKSSF 654
Cdd:PRK08180 190 LlaTPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRmlcanQQ------MLAQtfpFLAEEPPVLVdwLPWNH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 655 SFDASI---WQLFWwmipGASMYLlpqgwekD-----PALMTEAFTN--EGVTTAHF-IPAMANSFLDqvEMET-EEKRT 722
Cdd:PRK08180 264 TFGGNHnlgIVLYN----GGTLYI-------DdgkptPGGFDETLRNlrEISPTVYFnVPKGWEMLVP--ALERdAALRR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 723 SLAKTLKRVFAGGEALAPQTAARfarsLPETAVIH---------GYGPTEAtvdAAFFRYDHEKdRERMRLpIGKPVPGA 793
Cdd:PRK08180 331 RFFSRLKLLFYAGAALSQDVWDR----LDRVAEATcgerirmmtGLGMTET---APSATFTTGP-LSRAGN-IGLPAPGC 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 794 RLyildseKAVqPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARW 855
Cdd:PRK08180 402 EV------KLV-PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYR------SGDAVRF 450
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
485-959 |
4.88e-19 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 93.51 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 485 SGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLL 564
Cdd:PLN02246 47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 565 VTGPGLS--VSGFSGE------TLE------VNLSSLrTEPAENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHR--- 627
Cdd:PLN02246 127 ITQSCYVdkLKGLAEDdgvtvvTIDdppegcLHFSEL-TQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKglv 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 628 -QAAAFLSGMQRQFPLTEDDVIV----LKSSFSFDaSIwqLFWWMIPGASMYLLPQgweKDPALMTEAFTNEGVTTAHFI 702
Cdd:PLN02246 206 tSVAQQVDGENPNLYFHSDDVILcvlpMFHIYSLN-SV--LLCGLRVGAAILIMPK---FEIGALLELIQRHKVTIAPFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 703 P----AMANSflDQVEmeteekRTSLAkTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEA-TVDA---AFfryd 774
Cdd:PLN02246 280 PpivlAIAKS--PVVE------KYDLS-SIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAgPVLAmclAF---- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 775 hekdrERMRLPI-----GKPVPGARLYILDSEKAVQ-PIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFyrgermYQ 848
Cdd:PLN02246 347 -----AKEPFPVksgscGTVVRNAELKIVDPETGASlPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW------LH 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 849 TGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GE---------------ETELY 910
Cdd:PLN02246 416 TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDevaGEvpvafvvrsngseitEDEIK 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2040046167 911 AYIEGQdqktarTELGKRLPAYMmpssFIEmrEWPVTPSGKLDRKALPA 959
Cdd:PLN02246 496 QFVAKQ------VVFYKRIHKVF----FVD--SIPKAPSGKILRKDLRA 532
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
603-957 |
5.01e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 91.39 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 603 GGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSS-FSFDASIWQLFWWMIPGASMYLL-PQGW 680
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAgPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 681 eKDPALMTEAFtneGVTTAHFIPAM-----ANSFLDQVEMETEekrtslAKTLKRVFAGGEALAPQTAARF--ARSLPet 753
Cdd:cd05944 81 -RNPGLFDNFW---KLVERYRITSLstvptVYAALLQVPVNAD------ISSLRFAMSGAAPLPVELRARFedATGLP-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 754 aVIHGYGPTEATVDAAFfrydHEKDRERMRLPIGKPVPGA--RLYILDSEKAVQ-PIGV--AGELYIAGAGVARGYLNRp 828
Cdd:cd05944 149 -VVEGYGLTEATCLVAV----NPPDGPKRPGSVGLRLPYArvRIKVLDGVGRLLrDCAPdeVGEICVAGPGVFGGYLYT- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 829 ELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVkIR-GYRIEPGEVEAALRQIDGVREAAVVARTEGEET 907
Cdd:cd05944 223 EGNKNAFVADGWLN------TGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 908 EL-YAYIE-GQDQKTARTEL----GKRLPAY-MMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05944 296 ELpVAYVQlKPGAVVEEEELlawaRDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1638-1987 |
5.90e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 93.35 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 GPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFS---PEDRILLTAslGFDAMT-----FEVFGPLLNGACLYI 1709
Cdd:PRK12492 205 GLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgPDGQPLMKE--GQEVMIaplplYHIYAFTANCMCMMV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1710 SDKETYLDSD--RLKTFIQQNG---ITTLWLTSSLFNQLSEQNERTFSDLSRLIL---GGEALspnhvnrVRNTAPDLA- 1780
Cdd:PRK12492 283 SGNHNVLITNprDIPGFIKELGkwrFSALLGLNTLFVALMDHPGFKDLDFSALKLtnsGGTAL-------VKATAERWEq 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1781 -----LWNGYGPTEnTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTK 1855
Cdd:PRK12492 356 ltgctIVEGYGLTE-TSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1856 EKFvpnpftPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSGHKELL 1934
Cdd:PRK12492 435 EAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIgVPDERSGEAVKL 508
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1935 AYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEP 1987
Cdd:PRK12492 509 FVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
489-957 |
6.08e-19 |
|
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: 92.25 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVP----LDPDYPEERLRYMLADSGARLL 564
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 565 VTgpglsvsgfsgetlevnlsslrtepaenepvcaHTDGGSLAYviYTSGSTGTPKGVAVEHRQ-AAAFLSGMQrQFPLT 643
Cdd:cd05974 81 NT---------------------------------HADDPMLLY--FTSGTTSKPKLVEHTHRSyPVGHLSTMY-WIGLK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 644 EDDVIVLKSSFSFDASIWQLFW--WMIpGASMYLLPQGwEKDPALMTEAFTNEGVTTAHFIPAMAnsfldqvEMETEEKR 721
Cdd:cd05974 125 PGDVHWNISSPGWAKHAWSCFFapWNA-GATVFLFNYA-RFDAKRVLAALVRYGVTTLCAPPTVW-------RMLIQQDL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 722 TSLAKTLKRVFAGGEALAPQTAARFARSLPETaVIHGYGPTEATVDAAffrydHEKDRERMRLPIGKPVPGARLYILDse 801
Cdd:cd05974 196 ASFDVKLREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTALVG-----NSPGQPVKAGSMGRPLPGYRVALLD-- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 802 kAVQPIGVAGELYIA-----GAGVARGYLNRPELTEERfLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGY 876
Cdd:cd05974 268 -PDGAPATEGEVALDlgdtrPVGLMKGYAGDPDKTAHA-MRGGYYR------TGDIAMRDEDGYLTYVGRADDVFKSSDY 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 877 RIEPGEVEAALRQIDGVREAAVVARTEGEETEL---YAYIEGQDQKTARTELG------KRLPAYMMPSSfIEMREWPVT 947
Cdd:cd05974 340 RISPFELESVLIEHPAVAEAAVVPSPDPVRLSVpkaFIVLRAGYEPSPETALEifrfsrERLAPYKRIRR-LEFAELPKT 418
|
490
....*....|
gi 2040046167 948 PSGKLDRKAL 957
Cdd:cd05974 419 ISGKIRRVEL 428
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
514-954 |
8.36e-19 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 92.91 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 514 SVVGVLADRSPEMVIAVLAVLKAGGAYVPL-------DPDYPEERLRYMLADSGARLLVTgpglsvSGFSGETLEVNLSS 586
Cdd:PRK05851 55 GAVGLVGEPTVELVAAIQGAWLAGAAVSILpgpvrgaDDGRWADATLTRFAGIGVRTVLS------HGSHLERLRAVDSS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 587 LRTEpaeNEPVCAHT---------DGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTED-DVIVLKSSFSF 656
Cdd:PRK05851 129 VTVH---DLATAAHTnrsasltppDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 657 DASIWQLFWWMIPGASMYLLPQG-WEKDPALMTEAFTNEGVT-TAhfIPAMANSFLDQVEMETEEKRTSlakTLKRVFAG 734
Cdd:PRK05851 206 DMGLAFLLTAALAGAPLWLAPTTaFSASPFRWLSWLSDSRATlTA--APNFAYNLIGKYARRVSDVDLG---ALRVALNG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 735 GEALAPQTAARFARSLPE-----TAVIHGYGPTEAT------VDAAFFRYDHEKDRE----RMRLPIGKPVPGARLYILD 799
Cdd:PRK05851 281 GEPVDCDGFERFATAMAPfgfdaGAAAPSYGLAESTcavtvpVPGIGLRVDEVTTDDgsgaRRHAVLGNPIPGMEVRISP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 800 SEkavQPIGVA----GELYIAGAGVARGYLNrpelteerflDDPFYRGErMYQTGDLArWLPDGTVEWLGRMDGQVKIRG 875
Cdd:PRK05851 361 GD---GAAGVAgreiGEIEIRGASMMSGYLG----------QAPIDPDD-WFPTGDLG-YLVDGGLVVCGRAKELITVAG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 876 YRIEPGEVEAALRQIDGVREAAVVARTEGEETE-----LYAYIEGQDQKTARTELGKRLPAY--MMPSSFIEMR--EWPV 946
Cdd:PRK05851 426 RNIFPTEIERVAAQVRGVREGAVVAVGTGEGSArpglvIAAEFRGPDEAGARSEVVQRVASEcgVVPSDVVFVApgSLPR 505
|
....*...
gi 2040046167 947 TPSGKLDR 954
Cdd:PRK05851 506 TSSGKLRR 513
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
611-959 |
8.63e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 92.99 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 611 YTSGSTGTPKGVAVEHRQA------AAFLSGMQrqfplteDDVIVLKSSFSFDASIWQLFWWM--IPGASMyLLPQGWEK 682
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAylmalsNALIWGMN-------EGAVYLWTLPMFHCNGWCFTWTLaaLCGTNI-CLRQVTAK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 683 DpalMTEAFTNEGVTtaHFI--PAMANSFldqVEMETEEKRTSLAKTLKRVFAGGealAPQTAARFARSLPETAVIHGYG 760
Cdd:PLN02479 274 A---IYSAIANYGVT--HFCaaPVVLNTI---VNAPKSETILPLPRVVHVMTAGA---APPPSVLFAMSEKGFRVTHTYG 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 761 PTE----ATVDAAFFRYDHEKDRERMRLPIGKPVPGARLYILD--SEKAVQPI----GVAGELYIAGAGVARGYLNRPEL 830
Cdd:PLN02479 343 LSEtygpSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDvvDTKTMKPVpadgKTMGEIVMRGNMVMKGYLKNPKA 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 831 TEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEE- 906
Cdd:PLN02479 423 NEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDerwGESp 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 907 ---TELYAYIEGQDQKTARTELGK----RLPAYMMPSSFIeMREWPVTPSGKLDRKALPA 959
Cdd:PLN02479 496 cafVTLKPGVDKSDEAALAEDIMKfcreRLPAYWVPKSVV-FGPLPKTATGKIQKHVLRA 554
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1645-1979 |
8.83e-19 |
|
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: 90.25 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1645 IMYTSGSTGTPKGVMVEQRGVVRLVKN-SDMA-FSPEDRILLTASLgfdamtFEVFG-------PLLNGACLYisdKETY 1715
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAwADCAdLTEDDRYLIINPF------FHTFGykagivaCLLTGATVV---PVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1716 LDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTT 1792
Cdd:cd17638 76 FDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLraaVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1793 FSTCFRIEHEYKHSIPIGRPIANSTAYIVNSrgrlqpmgviGELCVGGDGLARGYFGRPELTKEKFvpnpftPGERMYRT 1872
Cdd:cd17638 156 ATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI------DADGWLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1873 GDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI----VRTGPSGHkellAYMSLQAEMNI--E 1946
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgvpdERMGEVGK----AFVVARPGVTLteE 295
|
330 340 350
....*....|....*....|....*....|...
gi 2040046167 1947 KVRSLLSQQLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:cd17638 296 DVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
465-957 |
9.67e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 92.41 E-value: 9.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 465 LHSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLD 544
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLV--------------TGPGLSV-----SGFSGETLEVNLSSLRTEPAENEPVcAHTDGgs 605
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMIchadfpehaaavraASPDLTHvvaigGARAGLDYEALVARHLGARVANAAV-DHDDP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 lAYVIYTSGSTGTPKGVAVEHRQAAAFLSG-MQRQFP-LTEDDVIVLKSSFSFDASIWQLFWwMIPGASMYLLPQgwEK- 682
Cdd:PRK07470 166 -CWFFFTSGTTGRPKAAVLTHGQMAFVITNhLADLMPgTTEQDASLVVAPLSHGAGIHQLCQ-VARGAATVLLPS--ERf 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 683 DPALMTEAFTNEGVTTAHFIPAMansfldqVEMETEEKRTSLAK--TLKRVFAGGealAPQTAARFARSLPE--TAVIHG 758
Cdd:PRK07470 242 DPAEVWALVERHRVTNLFTVPTI-------LKMLVEHPAVDRYDhsSLRYVIYAG---APMYRADQKRALAKlgKVLVQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 759 YGPTEATVDAAFF-RYDHEKDRERM-RL-PIGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERF 835
Cdd:PRK07470 312 FGLGEVTGNITVLpPALHDAEDGPDaRIgTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 836 LDDPFyrgermyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV----------------V 899
Cdd:PRK07470 392 RDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlgvpdpvwgevgvavcV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 900 ARtEG---EETELYAYIEGqdqktartelgkRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK07470 465 AR-DGapvDEAELLAWLDG------------KVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1500-1978 |
1.13e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 92.57 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1500 HETISRLFEYQAAKTPHAPAVIYDRQTL--TYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGA 1577
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1578 YLPVTEDMPTERLEWMLSDSNAVMLLQSDR----------------LESHMAG----KRL-------FIEDIQ------- 1623
Cdd:PRK08315 95 LVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelapeLATCEPGqlqsARLpelrrviFLGDEKhpgmlnf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1624 ---LEAGISANNPEQQGGPDSLAY-----IMYTSGSTGTPKGVMVEQRGVV---RLVKNSdMAFSPEDRILLTASLgfda 1692
Cdd:PRK08315 175 delLALGRAVDDAELAARQATLDPddpinIQYTSGTTGFPKGATLTHRNILnngYFIGEA-MKLTEEDRLCIPVPL---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1693 mtFEVFGPLL-NGACL-------YISDKetyldSDRLKTF--IQQNGITTLWLTSSLFnqLSEQNERTFS--DLSRL--- 1757
Cdd:PRK08315 250 --YHCFGMVLgNLACVthgatmvYPGEG-----FDPLATLaaVEEERCTALYGVPTMF--IAELDHPDFArfDLSSLrtg 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1758 ILGGeALSPNHV-NRV--RNTAPDLALwnGYGPTENTTFSTCFRIEHEYKHSI-PIGRPIANSTAYIVN-SRGRLQPMGV 1832
Cdd:PRK08315 321 IMAG-SPCPIEVmKRVidKMHMSEVTI--AYGMTETSPVSTQTRTDDPLEKRVtTVGRALPHLEVKIVDpETGETVPRGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1833 IGELCVGGDGLARGYFGRPELTKEKFVPnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVkIRG----Y-RielgEIE 1907
Cdd:PRK08315 398 QGELCTRGYSVMKGYWNDPEKTAEAIDA------DGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGgeniYpR----EIE 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 1908 AALRQIDGVKEAAVI----VRTGpsghKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGK 1978
Cdd:PRK08315 467 EFLYTHPKIQDVQVVgvpdEKYG----EEVCAWIILRpgATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1514-1984 |
1.20e-18 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 92.76 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1514 TPHAPAVIYD------RQTLTYRELNQRANRIAAALRANGVGS------------ESVVALLT-SR-------------T 1561
Cdd:cd05967 64 RGDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVKgdrviiympmipEAAIAMLAcARigaihsvvfggfaA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1562 PELAVGI------LGILKAGGA-------YLPVTEdmptERLEWMLSDSNAVMLLQSDRLESHMA--GKRLFIEDIQLEA 1626
Cdd:cd05967 144 KELASRIddakpkLIVTASCGIepgkvvpYKPLLD----KALELSGHKPHHVLVLNRPQVPADLTkpGRDLDWSELLAKA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1627 G------ISANNPeqqggpdslAYIMYTSGSTGTPKGVMVEQRG-VVRLVKNSDMAFS-PEDRILLTAS-LGFD-AMTFE 1696
Cdd:cd05967 220 EpvdcvpVAATDP---------LYILYTSGTTGKPKGVVRDNGGhAVALNWSMRNIYGiKPGDVWWAASdVGWVvGHSYI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1697 VFGPLLNGAC--LYISDKETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNE-----RTFsDLSRL---ILGGEALSP 1766
Cdd:cd05967 291 VYGPLLHGATtvLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgkyiKKY-DLSSLrtlFLAGERLDP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1767 NHVNRVRNTAPDLALwNGYGPTEN----TTFSTCFrieheYKHSIPIGRPIANSTAY---IVNSRGRLQPMGVIGELCVG 1839
Cdd:cd05967 370 PTLEWAENTLGVPVI-DHWWQTETgwpiTANPVGL-----EPLPIKAGSPGKPVPGYqvqVLDEDGEPVGPNELGNIVIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1840 GD---GLARGYFGRPELTKEKFVPNpfTPGerMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGV 1916
Cdd:cd05967 444 LPlppGCLLTLWKNDERFKKLYLSK--FPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAV 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1917 KEAAVI-VRTGPSGHKElLAYMSLQAEMNI------EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05967 520 AECAVVgVRDELKGQVP-LGLVVLKEGVKItaeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
470-954 |
1.42e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 92.17 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 470 TRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPE 549
Cdd:PLN02860 14 TRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 550 ERLRYMLADSGARLLVTG---------------PGLSVSGFSGETLEVN----LSSLRTE--------PAENEPVCAHTD 602
Cdd:PLN02860 94 EEAKSAMLLVRPVMLVTDetcsswyeelqndrlPSLMWQVFLESPSSSVfiflNSFLTTEmlkqralgTTELDYAWAPDD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 603 ggsLAYVIYTSGSTGTPKGVAVEHR----QAAAFLSGMQrqfpLTEDDVIVLKSSFSFDASIWQLFWWMIPGASMYLLPQ 678
Cdd:PLN02860 174 ---AVLICFTSGTTGRPKGVTISHSalivQSLAKIAIVG----YGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 679 gweKDPALMTEAFTNEGVTTAHFIPAMansFLDQVEMETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHG 758
Cdd:PLN02860 247 ---FDAKAALQAIKQHNVTSMITVPAM---MADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 759 YGPTEATVDAAFFR-YDHEKDRERMRLP-----------------IGKPVPGARLYI-LDSEKAVqpigvaGELYIAGAG 819
Cdd:PLN02860 321 YGMTEACSSLTFMTlHDPTLESPKQTLQtvnqtksssvhqpqgvcVGKPAPHVELKIgLDESSRV------GRILTRGPH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 820 VARGYLNRP-----ELTEERFLDdpfyrgermyqTGDLArWLPDGTVEWL-GRMDGQVKIRGYRIEPGEVEAALRQIDGV 893
Cdd:PLN02860 395 VMLGYWGQNsetasVLSNDGWLD-----------TGDIG-WIDKAGNLWLiGRSNDRIKTGGENVYPEEVEAVLSQHPGV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 894 REAAVVARTEGEETEL------------YAYIEGQDQKTART----EL-----GKRLPAYMMPSSFIEMRE-WPVTPSGK 951
Cdd:PLN02860 463 ASVVVVGVPDSRLTEMvvacvrlrdgwiWSDNEKENAKKNLTlsseTLrhhcrEKNLSRFKIPKLFVQWRKpFPLTTTGK 542
|
...
gi 2040046167 952 LDR 954
Cdd:PLN02860 543 IRR 545
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
12-323 |
2.01e-18 |
|
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: 90.56 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQSRlqfV 91
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDD-GGPYQVVLPAAEAR---P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 92 DISHLDETAKEtfVDQFEHDDKKKGFDLQTDPLMRVSILKRAHEQyhciwsH------HHILMDGWCFGIVMKEFLAIYK 165
Cdd:cd19540 79 DLTVVDVTEDE--LAARLAEAARRGFDLTAELPLRARLFRLGPDE------HvlvlvvHHIAADGWSMAPLARDLATAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 166 ALGKEQLPDFEP--VHpFSKYIKW----LMRQDRKEAE-----AFWKTRLIDVKQTASLP-----KTSSSSKGklEQMAF 229
Cdd:cd19540 151 ARRAGRAPDWAPlpVQ-YADYALWqrelLGDEDDPDSLaarqlAYWRETLAGLPEELELPtdrprPAVASYRG--GTVEF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 230 TLSKEQTEGLRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSD-LEDvekMVGLFINTIPVRVK-SGPE 307
Cdd:cd19540 228 TIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEaLDD---LVGMFVNTLVLRTDvSGDP 304
|
330
....*....|....*.
gi 2040046167 308 SFLTLVSHLQQESLKA 323
Cdd:cd19540 305 TFAELLARVRETDLAA 320
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
516-977 |
4.97e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 90.47 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 516 VGVLADRSPEMVIAVLAVLKAGGAYVPLDPdypEERLRYMLAD---SGARLLVTGP-------GLSVSGFsgETLEVNLS 585
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNT---TRRGAALAADirrADCQLLVTDAehrplldGLDLPGV--RVLDVDTP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 586 SLRTEPAENEPVCAHTDGG--SLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLkssfsfdasiwql 663
Cdd:PRK13388 130 AYAELVAAAGALTPHREVDamDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYV------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 664 fwwmipgaSMYL-----LPQGWEkdPALMTEAFTnegVTTAHFipaMANSFLDQVE-----------------METEEKR 721
Cdd:PRK13388 197 --------SMPLfhsnaVMAGWA--PAVASGAAV---ALPAKF---SASGFLDDVRrygatyfnyvgkplayiLATPERP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 722 TSLAKTLKRVFaGGEAlAPQTAARFARSLPETaVIHGYGPTEATVDAAffrydhekdRERMRLP--IGKPVPGARLYILD 799
Cdd:PRK13388 261 DDADNPLRVAF-GNEA-SPRDIAEFSRRFGCQ-VEDGYGSSEGAVIVV---------REPGTPPgsIGRGAPGVAIYNPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 800 S--EKAVQPIGVAGELY-----------IAGAGVARGYLNRPELTEERFLDDpfyrgerMYQTGDLARWLPDGTVEWLGR 866
Cdd:PRK13388 329 TltECAVARFDAHGALLnadeaigelvnTAGAGFFEGYYNNPEATAERMRHG-------MYWSGDLAYRDADGWIYFAGR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 867 MDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA-RTEGEETELYAYIEGQDQKT-----------ARTELG-KRLPAYM 933
Cdd:PRK13388 402 TADWMRVDGENLSAAPIERILLRHPAINRVAVYAvPDERVGDQVMAALVLRDGATfdpdafaaflaAQPDLGtKAWPRYV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 934 MPSsfiemREWPVTPSGKLDRKAL-------PAPDGAAERRVYTAPRTITE 977
Cdd:PRK13388 482 RIA-----ADLPSTATNKVLKRELiaqgwatGDPVTLWVRRGGPAYRLMSE 527
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1523-1916 |
7.61e-18 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 89.58 E-value: 7.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1523 DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVML 1602
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 LQSdrleshmagkrlfiediqleagisannpeqqGGPDSLAYIMYTSGSTGTPKGVMVEQR----GVVRLVKNSDMAFSP 1678
Cdd:cd17639 82 FTD-------------------------------GKPDDLACIMYTSGSTGNPKGVMLTHGnlvaGIAGLGDRVPELLGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1679 EDRILltASLGFdAMTFEVFGPLLngaCLYI---------------SDKETYLDSDRLKTFIQQnGITTLW--------- 1734
Cdd:cd17639 131 DDRYL--AYLPL-AHIFELAAENV---CLYRggtigygsprtltdkSKRGCKGDLTEFKPTLMV-GVPAIWdtirkgvla 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1735 -------LTSSLF--------NQLSEQ------NERTFSDLS-------RLIL-GGEALSP---NHVNRVrnTAPDLalw 1782
Cdd:cd17639 204 klnpmggLKRTLFwtayqsklKALKEGpgtpllDELVFKKVRaalggrlRYMLsGGAPLSAdtqEFLNIV--LCPVI--- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1783 NGYGPTEnTTFSTCFRIEHEYKHSIpIGRPIANSTAYIVNsrgrLQPMGVI-------GELCVGGDGLARGYFGRPELTK 1855
Cdd:cd17639 279 QGYGLTE-TCAGGTVQDPGDLETGR-VGPPLPCCEIKLVD----WEEGGYStdkppprGEILIRGPNVFKGYYKNPEKTK 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1856 EKFVpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVKIR-GYRIELGEIEAALRQ---IDGV 1916
Cdd:cd17639 353 EAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSnplVNNI 411
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
489-935 |
7.67e-18 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 88.95 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP 568
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 glsvsgfsgetlevnlsslrtepaenepvcahtdggslAYVIYTSGSTGTPKGVAVEHRQA------AAFLSGMQRQ--- 639
Cdd:cd05940 84 --------------------------------------ALYIYTSGTTGLPKAAIISHRRAwrggafFAGSGGALPSdvl 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 640 ---FPLTEDD--------------VIVLKSSFSfdASiwqLFWwmipgasmyllpqgwekdpalmTEAFTNEgVTTAHFI 702
Cdd:cd05940 126 ytcLPLYHSTalivgwsaclasgaTLVIRKKFS--AS---NFW----------------------DDIRKYQ-ATIFQYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 703 PAMANSFLDQVEMETEEKRTslaktLKRVFagGEALAPQTAARFARSLPETAVIHGYGPTEATVdaAFFRYDHeKDRERM 782
Cdd:cd05940 178 GELCRYLLNQPPKPTERKHK-----VRMIF--GNGLRPDIWEEFKERFGVPRIAEFYAATEGNS--GFINFFG-KPGAIG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 783 RLP-IGKPVPGARLYILDSEKAvQPI------------GVAGEL--YIAGAGVARGYLNrPELTEERFLDDPFYRGERMY 847
Cdd:cd05940 248 RNPsLLRKVAPLALVKYDLESG-EPIrdaegrcikvprGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKKGDAWF 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 848 QTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV----VARTEG------------EETELya 911
Cdd:cd05940 326 NTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDGragmaaivlqpnEEFDL-- 403
|
490 500
....*....|....*....|....
gi 2040046167 912 yiegqdQKTARTeLGKRLPAYMMP 935
Cdd:cd05940 404 ------SALAAH-LEKNLPGYARP 420
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
489-861 |
8.11e-18 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 89.58 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGV--AKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVT 566
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 567 GPGLSVSGFSgETLEV-NLSSLRTEPAENEpvcahtdggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGM----QRQFP 641
Cdd:cd05927 86 DAGVKVYSLE-EFEKLgKKNKVPPPPPKPE---------DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 642 LTEDDV-------------IVLKSSFSFDASI--WQlfwwmipGASMYLLPQGWEKDPALMTeaftneGVttahfiPAMA 706
Cdd:cd05927 156 INPTDVyisylplahiferVVEALFLYHGAKIgfYS-------GDIRLLLDDIKALKPTVFP------GV------PRVL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 707 NSFLDQVeMETEEKRTSLAKTL------------------------KRVF---------------AGGEALAPqTAARFA 747
Cdd:cd05927 217 NRIYDKI-FNKVQAKGPLKRKLfnfalnyklaelrsgvvraspfwdKLVFnkikqalggnvrlmlTGSAPLSP-EVLEFL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 748 RSLPETAVIHGYGPTEaTVDAAFFRYDHEKDRERmrlpIGKPVPGA--RL-------YILDSEKAvqpigvAGELYIAGA 818
Cdd:cd05927 295 RVALGCPVLEGYGQTE-CTAGATLTLPGDTSVGH----VGGPLPCAevKLvdvpemnYDAKDPNP------RGEVCIRGP 363
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2040046167 819 GVARGYLNRPELTEERFLDDPFyrgermYQTGDLARWLPDGTV 861
Cdd:cd05927 364 NVFSGYYKDPEKTAEALDEDGW------LHTGDIGEWLPNGTL 400
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1499-1984 |
1.48e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 88.92 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1499 KHETISRLFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAY 1578
Cdd:PRK07059 21 QYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1579 LPVTEDMPTERLEWMLSDSNA---VML------LQS----------------DRL-------------------ESHMAG 1614
Cdd:PRK07059 101 VNVNPLYTPRELEHQLKDSGAeaiVVLenfattVQQvlaktavkhvvvasmgDLLgfkghivnfvvrrvkkmvpAWSLPG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1615 KRLFIEDIQLEAGISANNPEQqgGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDM----AFSPEDRIlltaslgf 1690
Cdd:PRK07059 181 HVRFNDALAEGARQTFKPVKL--GPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAwlqpAFEKKPRP-------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1691 DAMTFEVFGPL---------------LNGACLYISD--------KEtyLDSDRLKTFIQQNgittlwltsSLFNQLSEQN 1747
Cdd:PRK07059 251 DQLNFVCALPLyhifaltvcgllgmrTGGRNILIPNprdipgfiKE--LKKYQVHIFPAVN---------TLYNALLNNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1748 ERTFSDLSRLIL---GGEALSPNHVNR-VRNTAPDLAlwNGYGPTENTTFSTCFRIE-HEYKHSIpiGRPIANSTAYIVN 1822
Cdd:PRK07059 320 DFDKLDFSKLIVangGGMAVQRPVAERwLEMTGCPIT--EGYGLSETSPVATCNPVDaTEFSGTI--GLPLPSTEVSIRD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1823 SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIE 1902
Cdd:PRK07059 396 DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVY 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1903 LGEIEAALRQIDGVKEAAVI-VRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:PRK07059 470 PNEIEEVVASHPGVLEVAAVgVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILR 549
|
...
gi 2040046167 1982 RAL 1984
Cdd:PRK07059 550 REL 552
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
471-957 |
1.57e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 88.59 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 471 RRAALSPNLPAVRF--SGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP 548
Cdd:PRK13391 5 IHAQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 549 EERLRYMLADSGARLLVTG--------------PGLS---VSGFSGE-----TLEVNLSSLRTEPAENEPVcahtdGGSL 606
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSaakldvarallkqcPGVRhrlVLDGDGElegfvGYAEAVAGLPATPIADESL-----GTDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 607 ayvIYTSGSTGTPKGVavehrQAAAFLSGMQRQFPLTEddviVLKSSFSFDASIWQLfwwmIPGASMYLLPQGW------ 680
Cdd:PRK13391 160 ---LYSSGTTGRPKGI-----KRPLPEQPPDTPLPLTA----FLQRLWGFRSDMVYL----SPAPLYHSAPQRAvmlvir 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 681 --------EK-DPALMTEAFTNEGVTTAHFIPAMansFLDQVEMETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSL- 750
Cdd:PRK13391 224 lggtvivmEHfDAEQYLALIEEYGVTHTQLVPTM---FSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWg 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 751 PetaVIHG-YGPTEAtvdAAFFRYDHEKDRERmRLPIGKPVPGaRLYILDSEKAVQPIGVAGELYIAGaGVARGYLNRPE 829
Cdd:PRK13391 301 P---IIHEyYAATEG---LGFTACDSEEWLAH-PGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 830 LTEERFLDDPfyrgeRMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV--VARTE-GEE 906
Cdd:PRK13391 372 KTAEARHPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfgVPNEDlGEE 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 907 TElyAYIEGQDQKTARTELGKRLPAYM--------MPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK13391 447 VK--AVVQPVDGVDPGPALAAELIAFCrqrlsrqkCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
472-957 |
2.84e-17 |
|
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: 87.43 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 472 RAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEER 551
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 552 LRymladsgARLLVTGPGLSVSGFSG-------ETLEVNLSSLRTEPAENEpvcAHTDggslaYVIYTSGSTGTPKGV-- 622
Cdd:cd05929 81 AC-------AIIEIKAAALVCGLFTGggaldglEDYEAAEGGSPETPIEDE---AAGW-----KMLYSGGTTGRPKGIkr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 623 -------AVEHRQAAAFLSGMqrqfplTEDDVIVLKSSFSFDASiwqLFWWMIP---GASMYLLPQgweKDPALMTEAFT 692
Cdd:cd05929 146 glpggppDNDTLMAAALGFGP------GADSVYLSPAPLYHAAP---FRWSMTAlfmGGTLVLMEK---FDPEEFLRLIE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 693 NEGVTTAHFIPAMANSFLdQVEmETEEKRTSLAkTLKRVFAGGEALAPQTAARFARSLPETaVIHGYGPTEAtVDAAFFR 772
Cdd:cd05929 214 RYRVTFAQFVPTMFVRLL-KLP-EAVRNAYDLS-SLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEG-QGLTIIN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 773 YD----HekdrermRLPIGKPVpGARLYILDSEKAVQPIGVAGELYIAGAGvARGYLNRPELTEERflddpfyRGERMYQ 848
Cdd:cd05929 289 GEewltH-------PGSVGRAV-LGKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAA-------RNEGGWS 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 849 T-GDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA--RTE-GEetELYAYIEGQDQKTARTE 924
Cdd:cd05929 353 TlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGvpDEElGQ--RVHAVVQPAPGADAGTA 430
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2040046167 925 --------LGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05929 431 laeeliafLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
458-956 |
3.68e-17 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 87.87 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 458 AAPLAPTLHSFFTRRAALSPNLPAVR---FSGGILTyRELDQYTNQLAIRLKKKGVAKESV------VGVLADRSPEMVI 528
Cdd:PRK12476 29 ALPPGTTLISLIERNIANVGDTVAYRyldHSHSAAG-CAVELTWTQLGVRLRAVGARLQQVagpgdrVAILAPQGIDYVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 529 AVLAVLKAGGAYVPL-DPDYP--EERLRYMLADSGARLLVTGPGL--SVSGFSGetlevNLSSLR------------TEP 591
Cdd:PRK12476 108 GFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAaeAVEGFLR-----NLPRLRrprviaidaipdSAG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 592 AENEPVCAHTDGgsLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVivlkSSFSF-----DASIWQLFWW 666
Cdd:PRK12476 183 ESFVPVELDTDD--VSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNT----HGVSWlplyhDMGLSMIGFP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 667 MIPGASMYLL--------PQGWEKdpALMTEAFTNEGVTTAhfiPAMANSFLDQVEMETEEKRTSLAKTLkrVFAGGEAL 738
Cdd:PRK12476 257 AVYGGHSTLMsptafvrrPQRWIK--ALSEGSRTGRVVTAA---PNFAYEWAAQRGLPAEGDDIDLSNVV--LIIGSEPV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 739 APQTAARFARS-----LPETAVIHGYGPTEATVDAAFFRYDHEK-----DRERM------RLPIGKPVPGARL---YILD 799
Cdd:PRK12476 330 SIDAVTTFNKAfapygLPRTAFKPSYGIAEATLFVATIAPDAEPsvvylDREQLgagravRVAADAPNAVAHVscgQVAR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 800 SEKAV---------QPIGVAGELYIAGAGVARGYLNRPELTEERF-------LDDPFYRGE-----RMYQTGDLARWLpD 858
Cdd:PRK12476 410 SQWAVivdpdtgaeLPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrLAEGSHADGaaddgTWLRTGDLGVYL-D 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 859 GTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDG-VREAAVVART-EGEETELYAYIEGQDQKTARTELGKRLPAY---- 932
Cdd:PRK12476 489 GELYITGRIADLIVIDGRNHYPQDIEATVAEASPmVRRGYVTAFTvPAEDNERLVIVAERAAGTSRADPAPAIDAIraav 568
|
570 580 590
....*....|....*....|....*....|....*.
gi 2040046167 933 ------------MMPSSFIemrewPVTPSGKLDRKA 956
Cdd:PRK12476 569 srrhglavadvrLVPAGAI-----PRTTSGKLARRA 599
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1527-1983 |
3.71e-17 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 87.87 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAAL-RANGVGSEsvVALLTSRTPELAVGILGILKAGGAYLPV-TEDMP--TERLEWMLSDSNAVML 1602
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLqQVAGPGDR--VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 LQS--------DRLESHMAGKR---LFIEDIQLEAGISANNPEQQggPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKN 1671
Cdd:PRK12476 147 LTTtaaaeaveGFLRNLPRLRRprvIAIDAIPDSAGESFVPVELD--TDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1672 SDMAFSPEDRILLTAS-------LGFDAMTFevfgPLLNGACLYISDKETYLDsdRLKTFIQQ--NGITTLWLTSSLFN- 1741
Cdd:PRK12476 225 MILSIDLLDRNTHGVSwlplyhdMGLSMIGF----PAVYGGHSTLMSPTAFVR--RPQRWIKAlsEGSRTGRVVTAAPNf 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1742 --QLSEQN----ERTFSDLSR--LILGGEALSPNHVnRVRNTA------PDLALWNGYGPTENTTF-ST----------- 1795
Cdd:PRK12476 299 ayEWAAQRglpaEGDDIDLSNvvLIIGSEPVSIDAV-TTFNKAfapyglPRTAFKPSYGIAEATLFvATiapdaepsvvy 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1796 ----------CFRIEHEYKHSIP---IGRPIANSTAYIVN-SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKF--- 1858
Cdd:PRK12476 378 ldreqlgagrAVRVAADAPNAVAhvsCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgak 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1859 -------------VPnpftPGERMYRTGDLARWLkDGTIDYIGRMDDQVKIRGYRIELGEIEAAlrqidgVKEAAVIVRT 1925
Cdd:PRK12476 458 lqsrlaegshadgAA----DDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEAT------VAEASPMVRR 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 1926 G-------PSGHKELLAYMSLQAEMN--------IEKVRSLLSQQlpgFMIPAH---LVELAALPLTQNGKLDRRA 1983
Cdd:PRK12476 527 GyvtaftvPAEDNERLVIVAERAAGTsradpapaIDAIRAAVSRR---HGLAVAdvrLVPAGAIPRTTSGKLARRA 599
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1645-1981 |
5.46e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 85.01 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1645 IMYTSGSTGTPKGVMVEQRGVV--RLVKNSDMAFSPEDRILL------TASLGFDAMTFEVfgpllnGACLYISDKetyL 1716
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIaaNLQLIHAMGLTEADVYLNmlplfhIAGLNLALATFHA------GGANVVMEK---F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1717 DSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLS--RLILGGEAlsPNHVNRVRNTAPDlALWNGYGPTENTTFS 1794
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSslRHVLGLDA--PETIQRFEETTGA-TFWSLYGQTETSGLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1795 TCFRIEhEYKHSIpiGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFvpnpftpgeR--MYRT 1872
Cdd:cd17637 153 TLSPYR-ERPGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWHHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1873 GDLARWLKDGTIDYIGRM--DDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGP---SGHK---ELLAYMSLQAEMN 1944
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPkwgEGIKavcVLKPGATLTADEL 300
|
330 340 350
....*....|....*....|....*....|....*..
gi 2040046167 1945 IEKVRSLLSqqlpGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:cd17637 301 IEFVGSRIA----RYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
609-954 |
6.21e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 84.63 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAVEHRQAAAflSGMQRQFP--LTEDDVIVlkssfsfdaSIWQLFWWMIPGASMYLLPQG-----WE 681
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIA--ANLQLIHAmgLTEADVYL---------NMLPLFHIAGLNLALATFHAGganvvME 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 682 K-DPALMTEAFTNEGVTTAHFIPAMANSFLDQVEmETEEKRTSLaktlkRVFAGGEAlaPQTAARFARSLPETAVIhGYG 760
Cdd:cd17637 74 KfDPAEALELIEEEKVTLMGSFPPILSNLLDAAE-KSGVDLSSL-----RHVLGLDA--PETIQRFEETTGATFWS-LYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 761 PTEATVDAAFFRYdhekdRERmrlP--IGKPVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDD 838
Cdd:cd17637 145 QTETSGLVTLSPY-----RER---PgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 839 pfyrgerMYQTGDLARWLPDGTVEWLGRMDGQ--VKIRGYRIEPGEVEAALRQIDGVREA---------------AVVAR 901
Cdd:cd17637 217 -------WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVcvigvpdpkwgegikAVCVL 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 902 TEGEETELYAYIEGQDQKTARTelgKRlPAYMmpsSFIEmrEWPVTPSGKLDR 954
Cdd:cd17637 290 KPGATLTADELIEFVGSRIARY---KK-PRYV---VFVE--ALPKTADGSIDR 333
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1638-1984 |
7.16e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 86.79 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1638 GPDSLAYIMYTSGSTGTPKGV-------MVEQRGVVRLvknsdmaFSP-EDRILLTASLGFDAMTFEVFG--PLLNGACL 1707
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVplthanlLANQRACLKF-------FSPkEDDVMMSFLPPFHAYGFNSCTlfPLLSGVPV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1708 YISDKEtyLDSDRLKTFIQQNGITTLWLTSSLFNQL---SEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNG 1784
Cdd:PRK06334 254 VFAYNP--LYPKKIVEMIDEAKVTFLGSTPVFFDYIlktAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1785 YGPTENTTFSTcFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQ-PMGVIGELCVGGDGLARGYFGRPEltKEKFVPnpf 1863
Cdd:PRK06334 332 YGTTECSPVIT-INTVNSPKHESCVGMPIRGMDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE--- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1864 TPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEA---AVIVRTGPSGHKELLAYMSLQ 1940
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAAdhaGPLVVCGLPGEKVRLCLFTTF 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2040046167 1941 AeMNIEKVRSLL-SQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK06334 486 P-TSISEVNDILkNSKTSSILKISYHHQVESIPMLGTGKPDYCSL 529
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1495-1984 |
8.56e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 86.58 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1495 QDYPKHETISRlfeyQAAktPHAPAVIYDRQTLTYRELNQRANRIAAALRANGV--GSESVVALltSRTPELAVGILGIL 1572
Cdd:PRK10946 23 QDLPLTDILTR----HAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIkpGDTALVQL--GNVAEFYITFFALL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1573 KAGGAylPVTEDMPTERLEwMLSDSNAVM--LLQSDRLESHMAGKRlFIEDIQ-------------------LEAGISAN 1631
Cdd:PRK10946 95 KLGVA--PVNALFSHQRSE-LNAYASQIEpaLLIADRQHALFSDDD-FLNTLVaehsslrvvlllnddgehsLDDAINHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1632 NPEQQGGP---DSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSD--MAFSPEDRIL--LTASLGFDAMTFEVFGPLLNG 1704
Cdd:PRK10946 171 AEDFTATPspaDEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVeiCGFTPQTRYLcaLPAAHNYPMSSPGALGVFLAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1705 ACLYISDketylDSDRLKTF--IQQNGIT---------TLWLTSSlfnQLSEQNERTFSdLSRLILGGEALSPNHVNRVr 1773
Cdd:PRK10946 251 GTVVLAP-----DPSATLCFplIEKHQVNvtalvppavSLWLQAI---AEGGSRAQLAS-LKLLQVGGARLSETLARRI- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1774 ntaPDL---ALWNGYGPTE---NTTfstcfRIEHEYKHSIPI-GRPIA-NSTAYIVNSRGRLQPMGVIGELCVGGDGLAR 1845
Cdd:PRK10946 321 ---PAElgcQLQQVFGMAEglvNYT-----RLDDSDERIFTTqGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1846 GYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIE-----------AALRQID 1914
Cdd:PRK10946 393 GYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIEnlllrhpavihAALVSME 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1915 ----GVKEAAVIVRTGPsghkellaymsLQAemnIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK10946 467 delmGEKSCAFLVVKEP-----------LKA---VQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1518-1987 |
9.50e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 86.11 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1518 PAVI--YDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLS 1595
Cdd:PRK08276 1 PAVImaPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1596 DSNAVMLLQSDRLESHMAGkrlFIEDIQLEAGISANNPEQQGGPDSLA-----------------YIM-YTSGSTGTPKG 1657
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAE---LAAELPAGVPLLLVVAGPVPGFRSYEealaaqpdtpiadetagADMlYSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1658 VMVEQRGV---------VRLVkNSDMAFSPEDRILL------TASLGFDAMTFEVFGPLLngaclyISDK---ETYLDsd 1719
Cdd:PRK08276 158 IKRPLPGLdpdeapgmmLALL-GFGMYGGPDSVYLSpaplyhTAPLRFGMSALALGGTVV------VMEKfdaEEALA-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1720 rlktFIQQNGITTLWLTSSLFN---QLSEQnERTFSDLS--RLILGGEALSPNHVNRvrntapdlAL--WNG------YG 1786
Cdd:PRK08276 229 ----LIERYRVTHSQLVPTMFVrmlKLPEE-VRARYDVSslRVAIHAAAPCPVEVKR--------AMidWWGpiiheyYA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1787 PTE--NTTFSTCfriEHEYKHSIPIGRPIAnSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFT 1864
Cdd:PRK08276 296 SSEggGVTVITS---EDWLAHPGSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1865 PgermyrTGDLArWL-KDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI--------------------V 1923
Cdd:PRK08276 372 T------VGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgvpdeemgervkavvqpadgA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1924 RTGPSGHKELLAYmslqaemniekvrslLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEP 1987
Cdd:PRK08276 445 DAGDALAAELIAW---------------LRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1526-1984 |
1.25e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.49 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1526 TLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSD--------S 1597
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDckpkvvitC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1598 NAV---------------MLLQSDR----------LESHMAGKRlfiEDIQLEAG-------ISANNP-----EQQGGPD 1640
Cdd:PLN02654 200 NAVkrgpktinlkdivdaALDESAKngvsvgicltYENQLAMKR---EDTKWQEGrdvwwqdVVPNYPtkcevEWVDAED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1641 SLaYIMYTSGSTGTPKGVMVEQRG-VVRLVKNSDMAFS--PEDRILLTASLGF-DAMTFEVFGPLLNGACLYISD-KETY 1715
Cdd:PLN02654 277 PL-FLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDykPTDVYWCTADCGWiTGHSYVTYGPMLNGATVLVFEgAPNY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1716 LDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSR---LILG--GEALSPNHVNRVRNTAPDlalwnGYGPTEN 1790
Cdd:PLN02654 356 PDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRkslRVLGsvGEPINPSAWRWFFNVVGD-----SRCPISD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1791 TTFST---CFRIEheykhSIPIGRPIANSTA---------YIVNSRGRLQPMGVIGELCVGGD--GLARGYFGrpelTKE 1856
Cdd:PLN02654 431 TWWQTetgGFMIT-----PLPGAWPQKPGSAtfpffgvqpVIVDEKGKEIEGECSGYLCVKKSwpGAFRTLYG----DHE 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1857 KFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAY 1936
Cdd:PLN02654 502 RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAF 581
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1937 MSL-QAEMNIEKVRSLL----SQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PLN02654 582 VTLvEGVPYSEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1524-1983 |
1.37e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 86.15 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1524 RQTLTYRELNQRANRIAAALRANGVGSESVVALltsrTP---ELAVGILGILKAGGAYLPVTEDMP---TERLEWMLSDS 1597
Cdd:PRK05850 33 AETLTWSQLYRRTLNVAEELRRHGSTGDRAVIL----APqglEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1598 NAVMLLQS----DRLESHMAGKRL-----FIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVV-- 1666
Cdd:PRK05850 109 SPSVVLTTsavvDDVTEYVAPQPGqsappVIEVDLLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIan 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1667 --RLVKNsdmAFSPEDRIlltASLGFDAMT-----------FEVFGPLLNGaclyisdKETYLDSDrlKTFIQQngiTTL 1733
Cdd:PRK05850 189 feQLMSD---YFGDTGGV---PPPDTTVVSwlpfyhdmglvLGVCAPILGG-------CPAVLTSP--VAFLQR---PAR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1734 WLtsslfnQLSEQNERTFS-----------------DLSRLILGG--------EALSPNHVNR-VRNTAP----DLALWN 1783
Cdd:PRK05850 251 WM------QLLASNPHAFSaapnfafelavrktsddDMAGLDLGGvlgiisgsERVHPATLKRfADRFAPfnlrETAIRP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1784 GYGPTENTTF-----------STCFRIEheykhSIPIGR--PIAN--------------STAYIVNSRGRLQ-PMGVIGE 1835
Cdd:PRK05850 325 SYGLAEATVYvatrepgqppeSVRFDYE-----KLSAGHakRCETgggtplvsygsprsPTVRIVDPDTCIEcPAGTVGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1836 LCVGGDGLARGYFGRPELTKEKF-----VPNPFTPGERMYRTGDLArWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAAL 1910
Cdd:PRK05850 400 IWVHGDNVAAGYWQKPEETERTFgatlvDPSPGTPEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDGRNHYPDDIEATI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1911 RQIDGVKEAAVIVrtgPSGHKE-LLAYMSL-----QAEMNIEKVRSL-------LSQqlpgfmipAH--------LVELA 1969
Cdd:PRK05850 479 QEITGGRVAAISV---PDDGTEkLVAIIELkkrgdSDEEAMDRLRTVkrevtsaISK--------SHglsvadlvLVAPG 547
|
570
....*....|....
gi 2040046167 1970 ALPLTQNGKLDRRA 1983
Cdd:PRK05850 548 SIPITTSGKIRRAA 561
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
477-957 |
1.83e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 85.49 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 477 PNLPAVRFSGGILTYRELDQYTNQLAIRLK-----KKGvakesvvgvlaDRSPEMV-------IAVLAVLKAGGAYVPLD 544
Cdd:PRK08974 37 ADQPAFINMGEVMTFRKLEERSRAFAAYLQnglglKKG-----------DRVALMMpnllqypIALFGILRAGMIVVNVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 545 PDYPEERLRYMLADSGARLLVTgpglsVSGFSgETLE----------VNLSSL--------------------RTEPAEN 594
Cdd:PRK08974 106 PLYTPRELEHQLNDSGAKAIVI-----VSNFA-HTLEkvvfktpvkhVILTRMgdqlstakgtlvnfvvkyikRLVPKYH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 595 EP-----------------VCAHTDGGSLAYVIYTSGSTGTPKGVAVEHR-------QAAAFLSGMQRqfPLTEDDVIVL 650
Cdd:PRK08974 180 LPdaisfrsalhkgrrmqyVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRnmlanleQAKAAYGPLLH--PGKELVVTAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 651 KSSFSFDASIWQLFWWMIPGASmyLLPQGWEKDPALMTE-------AFTneGVTTahfipaMANSFLDqvemeTEEKRTS 723
Cdd:PRK08974 258 PLYHIFALTVNCLLFIELGGQN--LLITNPRDIPGFVKElkkypftAIT--GVNT------LFNALLN-----NEEFQEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 724 LAKTLKRVFAGGEALAPQTAARFArSLPETAVIHGYGPTEATVDAAFFRYDHEKDRERmrlpIGKPVPGARLYILDSEKA 803
Cdd:PRK08974 323 DFSSLKLSVGGGMAVQQAVAERWV-KLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGS----IGLPVPSTEIKLVDDDGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 804 VQPIGVAGELYIAGAGVARGYLNRPELTEErFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEV 883
Cdd:PRK08974 398 EVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 884 EAALRQIDGVREAAVVA---RTEGEETELyaYIEGQDQKTARTELGKR----LPAYMMPsSFIEMR-EWPVTPSGKLDRK 955
Cdd:PRK08974 471 EDVVMLHPKVLEVAAVGvpsEVSGEAVKI--FVVKKDPSLTEEELITHcrrhLTGYKVP-KLVEFRdELPKSNVGKILRR 547
|
..
gi 2040046167 956 AL 957
Cdd:PRK08974 548 EL 549
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
490-854 |
2.35e-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: 85.18 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYP-----EERLRYML-------- 556
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsqdLAKLKHLFellkpglv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 557 --------ADSGARLLVTGPGLSVSGFSGETLEVNL--SSLRTEP-AENEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVE 625
Cdd:cd05921 107 faqdaapfARALAAIFPLGTPLVVSRNAVAGRGAISfaELAATPPtAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 626 HRQAAAFLSGMQRQFPLTEDDVIVL------KSSFSFDASIWQLFWwmiPGASMYL-----LPQGWEKdpalmTEAFTNE 694
Cdd:cd05921 187 QRMLCANQAMLEQTYPFFGEEPPVLvdwlpwNHTFGGNHNFNLVLY---NGGTLYIddgkpMPGGFEE-----TLRNLRE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 695 GVTTAHF-IPAMANSFLDqvEMETEEK-RTSLAKTLKRVFAGGEALAPQTAARfarsLPETAVIH---------GYGPTE 763
Cdd:cd05921 259 ISPTVYFnVPAGWEMLVA--ALEKDEAlRRRFFKRLKLMFYAGAGLSQDVWDR----LQALAVATvgeripmmaGLGATE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 764 AtvdAAFFRYDHEkDRERMRLpIGKPVPGARLyildseKAVqPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFYRg 843
Cdd:cd05921 333 T---APTATFTHW-PTERSGL-IGLPAPGTEL------KLV-PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYC- 399
|
410
....*....|.
gi 2040046167 844 ermyqTGDLAR 854
Cdd:cd05921 400 -----LGDAAK 405
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1511-1984 |
2.98e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 84.74 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIY--DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTE 1588
Cdd:PRK13391 7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1589 RLEWMLSDSNAVMLLQS-------DRLESHMAGKRLFI--------EDIQLEAGISANNPEQQGGPDSLAYIM-YTSGST 1652
Cdd:PRK13391 87 EAAYIVDDSGARALITSaakldvaRALLKQCPGVRHRLvldgdgelEGFVGYAEAVAGLPATPIADESLGTDMlYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1653 GTPKGVM--------VEQRGVVRLVKN-----SDMAF---------SPEDRILLTASLGFDAMTFEVFgpllngaclyis 1710
Cdd:PRK13391 167 GRPKGIKrplpeqppDTPLPLTAFLQRlwgfrSDMVYlspaplyhsAPQRAVMLVIRLGGTVIVMEHF------------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1711 DKETYLDsdrlktFIQQNGITTLWLTSSLFN---QLSEQNERTFsDLSRL--ILGGEALSPNHVNRvrntapDLALWNG- 1784
Cdd:PRK13391 235 DAEQYLA------LIEEYGVTHTQLVPTMFSrmlKLPEEVRDKY-DLSSLevAIHAAAPCPPQVKE------QMIDWWGp 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1785 -----YGPTENTTFSTCfRIEHEYKHSIPIGRPIAnSTAYIVNSRGRLQPMGVIGELCVGGdGLARGYFGRPELTKEKFV 1859
Cdd:PRK13391 302 iiheyYAATEGLGFTAC-DSEEWLAHPGTVGRAMF-GDLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1860 PNPftpgeRMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI----------------- 1922
Cdd:PRK13391 379 PDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFgvpnedlgeevkavvqp 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1923 ---VRTGPSGHKELLAYmslqaemniekvrslLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK13391 454 vdgVDPGPALAAELIAF---------------CRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1511-1985 |
3.98e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 84.28 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERL 1590
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 EWMLSDSNAVMLLQSDRLESHMAGKrlfiEDIQLEAGISANNPEQQGGPDSLA----YIMYTSGSTGTPKGVMVEQR--- 1663
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGA----DDAVAVIDPATAGAEESGGRPAVAapgrIVLLTSGTTGKPKGVPRAPQlrs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1664 --GV-------VRLVKNSDMAFSPE-------DRILLTASLGFDAMTFEVFgpllngaclyisDKETYLDSDRLKtfiQQ 1727
Cdd:PRK13383 201 avGVwvtildrTRLRTGSRISVAMPmfhglglGMLMLTIALGGTVLTHRHF------------DAEAALAQASLH---RA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1728 NGITTLWLTSSLFNQLSEQ--NERTFSDLSRLILGGEALSPNHVNRVRNTAPDLaLWNGYGPTENTTFSTCFRIE-HEYK 1804
Cdd:PRK13383 266 DAFTAVPVVLARILELPPRvrARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALATPADlRDAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1805 HSIpiGRPIANSTAYIVNSRGRlqPMG--VIGELCVGGDGLARGYFGrpelTKEKFVPnpftpgERMYRTGDLARWLKDG 1882
Cdd:PRK13383 345 ETV--GKPVAGCPVRILDRNNR--PVGprVTGRIFVGGELAGTRYTD----GGGKAVV------DGMTSTGDMGYLDNAG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1883 TIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSGHKeLLAYMSLQ--AEMNIEKVRSLLSQQLPGF 1959
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIgVPDERFGHR-LAAFVVLHpgSGVDAAQLRDYLKDRVSRF 489
|
490 500
....*....|....*....|....*.
gi 2040046167 1960 MIPAHLVELAALPLTQNGKLDRRALP 1985
Cdd:PRK13383 490 EQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
2085-2309 |
4.50e-16 |
|
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: 83.41 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2085 PWTPVQRWFLAQHIEERQ---HFNQSVM-LHSseGFQEQPLRTALQHLVIHHDALRMTIIDDGGQ--LQQFNRGIHGELY 2158
Cdd:cd19543 3 PLSPMQEGMLFHSLLDPGsgaYVEQMVItLEG--PLDPDRFRAAWQAVVDRHPILRTSFVWEGLGepLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2159 SLNIRDLSKTAQWEKLIEDEVADLQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLEDLSAAYSQAAA 2237
Cdd:cd19543 81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 2238 GQPVQLPRkTDSYQYFANRLAEY-AESSKvireqSYWRTVEK---EKAALLPCEKPHSAADNIRKTESFTLSEEDT 2309
Cdd:cd19543 161 GQPPSLPP-VRPYRDYIAWLQRQdKEAAE-----AYWREYLAgfeEPTPLPKELPADADGSYEPGEVSFELSAELT 230
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
459-954 |
5.78e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 83.90 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 459 APLAPTLHSFFTRRAALSPNLPavrfsggiltYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGG 538
Cdd:PRK09192 30 AALGEAGMNFYDRRGQLEEALP----------YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 539 AYVPLDPDYP-------EERLRYMLADSGARLLVTGPGLS------------VSGFSGETLEvnlssLRTEPAENEPVCA 599
Cdd:PRK09192 100 VPVPLPLPMGfggresyIAQLRGMLASAQPAAIITPDELLpwvneathgnplLHVLSHAWFK-----ALPEADVALPRPT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 600 HTDggsLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQ-------------FPLTEDDVIV------LKSSFSFDasi 660
Cdd:PRK09192 175 PDD---IAYLQYSSGSTRFPRGVIITHRALMANLRAISHDglkvrpgdrcvswLPFYHDMGLVgflltpVATQLSVD--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 661 wqlfwwMIPGASMYLLPQGWEKdpaLMTEaftNEGvtTAHFIPamanSF---LDQVEMETEEKrTSLAKTLKRVFA-GGE 736
Cdd:PRK09192 249 ------YLPTRDFARRPLQWLD---LISR---NRG--TISYSP----PFgyeLCARRVNSKDL-AELDLSCWRVAGiGAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 737 ALAPQT----AARFA-RSLPETAVIHGYGPTEAT----------------VDAAFFRYDH-----EKDRERMR--LPIGK 788
Cdd:PRK09192 310 MIRPDVlhqfAEAFApAGFDDKAFMPSYGLAEATlavsfsplgsgivveeVDRDRLEYQGkavapGAETRRVRtfVNCGK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 789 PVPGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEE----RFLDdpfyrgermyqTGDLArWLPDGTVEWL 864
Cdd:PRK09192 390 ALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVlaadGWLD-----------TGDLG-YLLDGYLYIT 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 865 GRMDGQVKIRGYRIEPGEVEAALRQIDGVR--EAAVVARTEGEETELYAYIE--GQDQkTARTELGKRLPAYM-----MP 935
Cdd:PRK09192 458 GRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVLLVQcrISDE-ERRGQLIHALAALVrsefgVE 536
|
570 580
....*....|....*....|..
gi 2040046167 936 SSfIEM---REWPVTPSGKLDR 954
Cdd:PRK09192 537 AA-VELvppHSLPRTSSGKLSR 557
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
490-957 |
6.93e-16 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 83.58 E-value: 6.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTGP- 568
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 -----------------GLSVSGFSGETLE--VNLSSLRTE-PAE-NEPVCAHTDggSLAYVIYTSGSTGTPKGVAVEHR 627
Cdd:PRK08008 119 fypmyrqiqqedatplrHICLTRVALPADDgvSSFTQLKAQqPATlCYAPPLSTD--DTAEILFTSGTTSRPKGVVITHY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 628 --QAAAFLSGMQRQfpLTEDDV-IVLKSSFSFDASIWQLFWWMIPGASMYLLpqgwEKDPAlmtEAFTNE----GVTTAH 700
Cdd:PRK08008 197 nlRFAGYYSAWQCA--LRDDDVyLTVMPAFHIDCQCTAAMAAFSAGATFVLL----EKYSA---RAFWGQvckyRATITE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 701 FIPAMANSFLDQVEMETEEKRTslaktLKRVF-----AGGEALAPQTaaRFARSLpetavIHGYGPTEATVDAAffrydh 775
Cdd:PRK08008 268 CIPMMIRTLMVQPPSANDRQHC-----LREVMfylnlSDQEKDAFEE--RFGVRL-----LTSYGMTETIVGII------ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 776 eKDR--ERMRLP-IGKPVPGARLYILDSEKAVQPIGVAGELYI---AGAGVARGYLNRPELTEERFlddpfyRGERMYQT 849
Cdd:PRK08008 330 -GDRpgDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVL------EADGWLHT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 850 GDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV---------------VARTEGE---ETELYA 911
Cdd:PRK08008 403 GDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvgikdsirdeaikafVVLNEGEtlsEEEFFA 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2040046167 912 YIEgqdqktartelgKRLPAYMMPsSFIEMRE-WPVTPSGKLDRKAL 957
Cdd:PRK08008 483 FCE------------QNMAKFKVP-SYLEIRKdLPRNCSGKIIKKNL 516
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1515-1981 |
1.09e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 82.92 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTedmpterLEWML 1594
Cdd:PLN02860 21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN-------YRWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSNAVML-------------------LQSDRLESHMAgkRLFIEDIQLEAGISANNPE------QQGG----------P 1639
Cdd:PLN02860 94 EEAKSAMLlvrpvmlvtdetcsswyeeLQNDRLPSLMW--QVFLESPSSSVFIFLNSFLttemlkQRALgtteldyawaP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1640 DSLAYIMYTSGSTGTPKGVMVEQRGVV--RLVKNSDMAFSPEDRILLTASL----GF-DAMTFevfgpLLNGAC-LYIS- 1710
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIvqSLAKIAIVGYGEDDVYLHTAPLchigGLsSALAM-----LMVGAChVLLPk 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1711 -DKETYLDSdrlktfIQQNGITTLWLTSSLFNQL-----SEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNG 1784
Cdd:PLN02860 247 fDAKAALQA------IKQHNVTSMITVPAMMADLisltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1785 YGPTEnTTFSTCFRIEHEYKHSIPigrPIANSTAYIVNSRGRLQPMGVigelCVG------------------GDGLARG 1846
Cdd:PLN02860 321 YGMTE-ACSSLTFMTLHDPTLESP---KQTLQTVNQTKSSSVHQPQGV----CVGkpaphvelkigldessrvGRILTRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1847 yfgrPELTKEKFVPNPFTPGERM----YRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI 1922
Cdd:PLN02860 393 ----PHVMLGYWGQNSETASVLSndgwLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1923 ----VRTGpsghKELLAYMSLQ-------AEMNIEKVRSLLSQQ----------LPGFMIPAHLVEL-AALPLTQNGKLD 1980
Cdd:PLN02860 469 gvpdSRLT----EMVVACVRLRdgwiwsdNEKENAKKNLTLSSEtlrhhcreknLSRFKIPKLFVQWrKPFPLTTTGKIR 544
|
.
gi 2040046167 1981 R 1981
Cdd:PLN02860 545 R 545
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1525-1986 |
1.64e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 82.33 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQ 1604
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 SDRLESHMAGKRL---FIEDIQLEAGISANNPEQQG--GPDSLAY----------IMYTSGSTGTPKGVMVEQRGVVRLV 1669
Cdd:PLN02330 134 NDTNYGKVKGLGLpviVLGEEKIEGAVNWKELLEAAdrAGDTSDNeeilqtdlcaLPFSSGTTGISKGVMLTHRNLVANL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1670 KNSDMAFSPEdRILLTASLGFDAMtFEVFGplLNGAC---LYISDKETYLDSDRLKTFIqqNGITTLWLTSS-------- 1738
Cdd:PLN02330 214 CSSLFSVGPE-MIGQVVTLGLIPF-FHIYG--ITGICcatLRNKGKVVVMSRFELRTFL--NALITQEVSFApivppiil 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1739 --LFNQLSEQNERTFSDLSRLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENTtfstCFRIEH---EYKHSIP----I 1809
Cdd:PLN02330 288 nlVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHS----CITLTHgdpEKGHGIAkknsV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1810 GRPIAN-STAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKekfvpnpftpgermyRTGDLARWLKDGTIDYIG 1888
Cdd:PLN02330 364 GFILPNlEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETD---------------RTIDEDGWLHTGDIGYID 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1889 ---------RMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIvrtgPSGHKE------LLAYMSLQAEMNIEKVRSLLS 1953
Cdd:PLN02330 429 ddgdifivdRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVV----PLPDEEageipaACVVINPKAKESEEDILNFVA 504
|
490 500 510
....*....|....*....|....*....|....*
gi 2040046167 1954 QQLPGF--MIPAHLVElaALPLTQNGKLDRRALPE 1986
Cdd:PLN02330 505 ANVAHYkkVRVVQFVD--SIPKSLSGKIMRRLLKE 537
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1999-2070 |
1.67e-15 |
|
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: 73.35 E-value: 1.67e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 1999 PRNQLEERLAVIWQEVLGV--EKVGIEDSFF-ELGGDSIKALQVSARLG-RFDLKITAGDLFRHPTIKEAAPLIRK 2070
Cdd:COG0236 2 PREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEeEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
489-957 |
1.93e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 82.35 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGgaYVPLDPDYPEERL-----------RYMLA 557
Cdd:PRK10946 49 FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSelnayasqiepALLIA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 558 DSGARLLVTG----------PGLSVSGFSGETLEVNLSSLRTEPAENEPVCAhTDGGSLAYVIYTSGSTGTPKGVAVEHR 627
Cdd:PRK10946 127 DRQHALFSDDdflntlvaehSSLRVVLLLNDDGEHSLDDAINHPAEDFTATP-SPADEVAFFQLSGGSTGTPKLIPRTHN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 628 ------QAAAFLSGMQRQ------------FPLteddvivlkSSfsfdasiwqlfwwmiPGASMYLLPQG---WEKDPAL 686
Cdd:PRK10946 206 dyyysvRRSVEICGFTPQtrylcalpaahnYPM---------SS---------------PGALGVFLAGGtvvLAPDPSA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 687 MT--EAFTNEGVTTAHFIPAMANSFLDQVEmetEEKRTSLAKTLKRVFAGGEALAPQTAARFarslpeTAVI-----HGY 759
Cdd:PRK10946 262 TLcfPLIEKHQVNVTALVPPAVSLWLQAIA---EGGSRAQLASLKLLQVGGARLSETLARRI------PAELgcqlqQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 760 GPTEATVDaaFFRYDheKDRERMRLPIGKPV-PGARLYILDSEKAVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDD 838
Cdd:PRK10946 333 GMAEGLVN--YTRLD--DSDERIFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDAN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 839 PFYrgermyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEETelYAYIEG 915
Cdd:PRK10946 409 GFY------CSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDelmGEKS--CAFLVV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2040046167 916 QDQKTART------ELGkrLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK10946 481 KEPLKAVQlrrflrEQG--IAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1510-1979 |
2.55e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1510 QAAKTPHAPAVIYDR--QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPT 1587
Cdd:PRK13390 6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1588 ERLEWMLSDSNAVMLLQSDRLESHMAGK------RL-FIEDI----QLEAGISANNP---EQQGGpdslAYIMYTSGSTG 1653
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVgadlplRLsFGGEIdgfgSFEAALAGAGPrltEQPCG----AVMLYSSGTTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1654 TPKGVMVEQRGvvrlvKNSDmafSPEDRILLTASLGFDAMTFEVF---GPLLNGACLYISDKETYL----------DSDR 1720
Cdd:PRK13390 162 FPKGIQPDLPG-----RDVD---APGDPIVAIARAFYDISESDIYyssAPIYHAAPLRWCSMVHALggtvvlakrfDAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1721 LKTFIQQNGITTLWLTSSLFNQLSEQNE--RTFSDLSRLILGGEALSPNHVNrVRNTAPDL---ALWNGYGPTENTTFsT 1795
Cdd:PRK13390 234 TLGHVERYRITVTQMVPTMFVRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVD-VKHAMIDWlgpIVYEYYSSTEAHGM-T 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1796 CFRIEHEYKHSIPIGRPIAnSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVP-NPFtpgerMYRTGD 1874
Cdd:PRK13390 312 FIDSPDWLAHPGSVGRSVL-GDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPaHPF-----WTTVGD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1875 LARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEM--NIEKVRSLL 1952
Cdd:PRK13390 386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIrgSDELARELI 465
|
490 500 510
....*....|....*....|....*....|
gi 2040046167 1953 S---QQLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:PRK13390 466 DytrSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
450-957 |
2.80e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 81.56 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 450 YEFNQTEPAAPLAP--TLHSFFTRRAAL-SPNLPAVR-FSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPE 525
Cdd:PLN02330 13 HIFRSRYPSVPVPDklTLPDFVLQDAELyADKVAFVEaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 526 MVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVT---------GPGLSVSGFSGETLE--VNLSSL-----RT 589
Cdd:PLN02330 93 YGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTndtnygkvkGLGLPVIVLGEEKIEgaVNWKELleaadRA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 590 EPAENEPVCAHTDggsLAYVIYTSGSTGTPKGVAVEHRQAAAFL-SGMQRQFPLTEDDVIVLKssfsfdasiwqlfwwMI 668
Cdd:PLN02330 173 GDTSDNEEILQTD---LCALPFSSGTTGISKGVMLTHRNLVANLcSSLFSVGPEMIGQVVTLG---------------LI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 669 PGASMY---------LLPQG-----WEKDPALMTEAFTNEGVTTAHFIPAMansFLDQVEMETEEKRTSLAKTLKRVFAG 734
Cdd:PLN02330 235 PFFHIYgitgiccatLRNKGkvvvmSRFELRTFLNALITQEVSFAPIVPPI---ILNLVKNPIVEEFDLSKLKLQAIMTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 735 GEALAPQTAARFARSLPETAVIHGYGPTEATVdAAFFRYDHEKDRE-RMRLPIGKPVPGARLYILDSEKAVQ-PIGVAGE 812
Cdd:PLN02330 312 AAPLAPELLTAFEAKFPGVQVQEAYGLTEHSC-ITLTHGDPEKGHGiAKKNSVGFILPNLEVKFIDPDTGRSlPKNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 813 LYIAGAGVARGYLNRPELTEERFLDDPFYrgermyQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDG 892
Cdd:PLN02330 391 LCVRSQCVMQGYYNNKEETDRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPS 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 893 VREAAVVARTEGEETELYAYIEGQDQKTARTE------LGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PLN02330 465 VEDAAVVPLPDEEAGEIPAACVVINPKAKESEedilnfVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
488-957 |
2.84e-15 |
|
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: 81.84 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 488 ILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLA---------VLKAGgayvpldpdYPEERLRYMLAD 558
Cdd:cd05966 84 TITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFAG---------FSAESLADRIND 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 559 SGARLLVTGPGlsvsGFSGETLeVNLSSLRTEPAENEP-------------VCAHTDGGSL------------------- 606
Cdd:cd05966 155 AQCKLVITADG----GYRGGKV-IPLKEIVDEALEKCPsvekvlvvkrtggEVPMTEGRDLwwhdlmakqspecepewmd 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 607 ----AYVIYTSGSTGTPKGVavEHRQAAaFLSG----MQRQFPLTEDDVivlkssfsfdasiwqlFW------WmIPGAS 672
Cdd:cd05966 230 sedpLFILYTSGSTGKPKGV--VHTTGG-YLLYaattFKYVFDYHPDDI----------------YWctadigW-ITGHS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 673 mYLL--PqgwekdpaLMteaftnEGVTTAHF--IPAMANS--FLDQVEmetEEKRTSL--AKTLKRVFAGGEALAPQTAA 744
Cdd:cd05966 290 -YIVygP--------LA------NGATTVMFegTPTYPDPgrYWDIVE---KHKVTIFytAPTAIRALMKFGDEWVKKHD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 745 RFarSLpetAVIHGYG----PtEAtvdaafFRYDHEKDRERmRLPI----------------------------GKPVPG 792
Cdd:cd05966 352 LS--SL---RVLGSVGepinP-EA------WMWYYEVIGKE-RCPIvdtwwqtetggimitplpgatplkpgsaTRPFFG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 793 ARLYILDSEKAVQPIGVAGELYIAGA--GVARGYLNRPElteeRFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQ 870
Cdd:cd05966 419 IEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 871 VKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEetELYAYI------EGQDQ------KTARTELGkrlpAYMMP 935
Cdd:cd05966 495 INVSGHRLGTAEVESALVAHPAVAEAAVVGRPHdikGE--AIYAFVtlkdgeEPSDElrkelrKHVRKEIG----PIATP 568
|
570 580
....*....|....*....|..
gi 2040046167 936 SSFIEMREWPVTPSGKLDRKAL 957
Cdd:cd05966 569 DKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1521-1981 |
4.59e-15 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 81.20 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1521 IYDRQ-----TLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGayLPVTEDMPT-------- 1587
Cdd:PRK09192 39 FYDRRgqleeALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGL--VPVPLPLPMgfggresy 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1588 -ERLEWMLSDSNAVMLLQSDRL--------ESHMAGKRLFIEDIQLEAGISANNPEQQggPDSLAYIMYTSGSTGTPKGV 1658
Cdd:PRK09192 117 iAQLRGMLASAQPAAIITPDELlpwvneatHGNPLLHVLSHAWFKALPEADVALPRPT--PDDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1659 MVEQRGV---VRLVKNSDMAFSPEDRIL------------------LTASLGFDAMTFEVFG--PLLngaclyisdketY 1715
Cdd:PRK09192 195 IITHRALmanLRAISHDGLKVRPGDRCVswlpfyhdmglvgflltpVATQLSVDYLPTRDFArrPLQ------------W 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1716 LDsdrlktFIQQNGITTLWltSSLFN------QLSEQNERTFsDLSRLIL---GGEALSPNHVNRVRNT-AP----DLAL 1781
Cdd:PRK09192 263 LD------LISRNRGTISY--SPPFGyelcarRVNSKDLAEL-DLSCWRVagiGADMIRPDVLHQFAEAfAPagfdDKAF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1782 WNGYGPTENT---TFS---TCFRIE--------------------HEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGE 1835
Cdd:PRK09192 334 MPSYGLAEATlavSFSplgSGIVVEevdrdrleyqgkavapgaetRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1836 LCVGGDGLARGYFGRPELTKEKFVPNpftpgerMYRTGDLArWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDG 1915
Cdd:PRK09192 414 ICVRGPSLMSGYFRDEESQDVLAADG-------WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPE 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1916 VK--EAAVIVRTGPSGHKELLAymsLQAEMNIEKVRSLLSQQLPGFMIPAH----LVELA---ALPLTQNGKLDR 1981
Cdd:PRK09192 486 LRsgDAAAFSIAQENGEKIVLL---VQCRISDEERRGQLIHALAALVRSEFgveaAVELVpphSLPRTSSGKLSR 557
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1492-1997 |
5.03e-15 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 80.82 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1492 QTKQDYPKhETISRLFEyQAAKTPHAPAVIYDRQT--LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGIL 1569
Cdd:PRK05857 7 QAMPQLPS-TVLDRVFE-QARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1570 GILKAGGAYLPVTEDMPTERLEWM--LSDSNAVML-----LQSDRLESHMAGKRLFIEDIQLEAGISANNPEQQ------ 1636
Cdd:PRK05857 85 ACAKLGAIAVMADGNLPIAAIERFcqITDPAAALVapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAslagna 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1637 --GGPDSLAYImYTSGSTGTPKGVMVEQR---GVVRLVKNSDMA----------FSPedriLLTASLGfdaMTFEVFGPL 1701
Cdd:PRK05857 165 dqGSEDPLAMI-FTSGTTGEPKAVLLANRtffAVPDILQKEGLNwvtwvvgettYSP----LPATHIG---GLWWILTCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1702 LNGAcLYISDKETYLDsdrLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSD---LSRLILGGEALSPNHVNRVRNTAPD 1778
Cdd:PRK05857 237 MHGG-LCVTGGENTTS---LLEILTTNAVATTCLVPTLLSKLVSELKSANATvpsLRLVGYGGSRAIAADVRFIEATGVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1779 LAlwNGYGPTENTTFSTCFRIEHEYKHSI---PIGRPIANSTAYIVNSRG------RLQPMGVIGELCVGGDGLARGYFG 1849
Cdd:PRK05857 313 TA--QVYGLSETGCTALCLPTDDGSIVKIeagAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1850 RPELTKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIvrTGPSG 1929
Cdd:PRK05857 391 NPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY--EIPDE 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 1930 HKELLAYMSL--QAEMNIEKVRSL-------LSQQLPGFMIPAHLVELAALPLTQNGKLDRRALpepeTTAINTAYA 1997
Cdd:PRK05857 462 EFGALVGLAVvaSAELDESAARALkhtiaarFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL----AAAATADKA 534
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2092-2274 |
6.87e-15 |
|
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: 79.42 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2092 WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDG--GQLQQfnrGIHGE-LYSLNIRDLSKT 2168
Cdd:cd19532 12 WFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPedGEPMQ---GVLASsPLRLEHVQISDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2169 AQweklIEDEVADLQRSIH-LQTGPLLKAGLFnTMSGTYLFLTI--HHLVVDGVSWRILLEDLSAAYSqaaaGQPvqLPR 2245
Cdd:cd19532 89 AE----VEEEFERLKNHVYdLESGETMRIVLL-SLSPTEHYLIFgyHHIAMDGVSFQIFLRDLERAYN----GQP--LLP 157
|
170 180
....*....|....*....|....*....
gi 2040046167 2246 KTDSYQYFANRLAEYAESSKVIREQSYWR 2274
Cdd:cd19532 158 PPLQYLDFAARQRQDYESGALDEDLAYWK 186
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1525-1922 |
7.19e-15 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 80.21 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML--SDSNAVML 1602
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLehSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 LQSDRLESHMAG--KRLFI----------EDIQLEAGISANNPEQQG---GPDSLAYIMYTSGSTGTPKGVMVE------ 1661
Cdd:cd05932 85 GKLDDWKAMAPGvpEGLISislpppsaanCQYQWDDLIAQHPPLEERptrFPEQLATLIYTSGTTGQPKGVMLTfgsfaw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1662 --QRGVVRLvknsdmAFSPEDRILLTASLgfdAMTFE-VF---GPLLNGACLYISDKetyldsdrLKTFIQ--QNGITTL 1733
Cdd:cd05932 165 aaQAGIEHI------GTEENDRMLSYLPL---AHVTErVFvegGSLYGGVLVAFAES--------LDTFVEdvQRARPTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1734 WLTS----SLFnQLSEQNERTFSDLSRL--------ILGGEALSPNHVNRVRNTA-------PDLALW---------NGY 1785
Cdd:cd05932 228 FFSVprlwTKF-QQGVQDKIPQQKLNLLlkipvvnsLVKRKVLKGLGLDQCRLAGcgsapvpPALLEWyrslglnilEAY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1786 GPTENTTFSTcfrieheykhsipIGRPIANSTAYI-VNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFt 1864
Cdd:cd05932 307 GMTENFAYSH-------------LNYPGRDKIGTVgNAGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF- 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1865 pgermYRTGDLARWLKDGTIDYIGRMDDQVKI-RGYRIELGEIEAALRQIDGVKEAAVI 1922
Cdd:cd05932 373 -----LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1525-1922 |
1.35e-14 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 79.77 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQ 1604
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 SD------------RLES--------------HMAGKRLFIEDIqLEAG--ISANNPEQ------QGGPDSLAYIMYTSG 1650
Cdd:cd17641 90 EDeeqvdklleiadRIPSvryviycdprgmrkYDDPRLISFEDV-VALGraLDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1651 STGTPKGVMVEQRGVVRLVKNSdMAF---SPEDRILLTASLGF--DAMtFEVFGPLLNGACL-YISDKETYL-------- 1716
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGHCAAY-LAAdplGPGDEYVSVLPLPWigEQM-YSVGQALVCGFIVnFPEEPETMMedlreigp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1717 ----------------------DSDRLKTFIQQNGI-----------------TTLWLTSSLFNQL---SEQNERTFSDL 1754
Cdd:cd17641 247 tfvllpprvwegiaadvrarmmDATPFKRFMFELGMklglraldrgkrgrpvsLWLRLASWLADALlfrPLRDRLGFSRL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1755 SRLILGGEALSPNHVNRVRntAPDLALWNGYGPTENTTFSTCFRiEHEYKHSIpIGRPIANSTAYIVNsrgrlqpmgvIG 1834
Cdd:cd17641 327 RSAATGGAALGPDTFRFFH--AIGVPLKQLYGQTELAGAYTVHR-DGDVDPDT-VGVPFPGTEVRIDE----------VG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1835 ELCVGGDGLARGYFGRPELTKEKFVpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVKI-RGYRIELGEIEAALRQI 1913
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFD------EDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFS 466
|
....*....
gi 2040046167 1914 DGVKEAAVI 1922
Cdd:cd17641 467 PYIAEAVVL 475
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
482-888 |
1.42e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 79.77 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 482 VRFSGGILTYRELDQYTN-----------QLAIRLKKKGVAKESV------VGVLADRSPEMVIAVLAVLKAGGAYVPL- 543
Cdd:PRK07769 31 AKVRGDKLAYRFLDFSTErdgvardltwsQFGARNRAVGARLQQVtkpgdrVAILAPQNLDYLIAFFGALYAGRIAVPLf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 544 DPDYP--EERLRYMLADS--GARLLVTGPGLSVSGFsgetlevnlssLRTEPAEN------------------EPVCAHT 601
Cdd:PRK07769 111 DPAEPghVGRLHAVLDDCtpSAILTTTDSAEGVRKF-----------FRARPAKErprviavdavpdevgatwVPPEANE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 602 DggSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDAS-IWQLFWWMIPGASMYLLPQGW 680
Cdd:PRK07769 180 D--TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGlITVLLPALLGHYITFMSPAAF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 681 EKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEMETEEKRTSLAKTLKRVFA---GGEALAPQTAARFARS-----LPE 752
Cdd:PRK07769 258 VRRPGRWIRELARKPGGTGGTFSAAPNFAFEHAAARGLPKDGEPPLDLSNVKGllnGSEPVSPASMRKFNEAfapygLPP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 753 TAVIHGYGPTEATVDAAFFRYDHEK-----DRERM------RLPIGKP--VPGAR---------LYILDSEKAV-QPIGV 809
Cdd:PRK07769 338 TAIKPSYGMAEATLFVSTTPMDEEPtviyvDRDELnagrfvEVPADAPnaVAQVSagkvgvsewAVIVDPETASeLPDGQ 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 810 AGELYIAGAGVARGYLNRPELTEERF-------LDDPFYRG----ERMYQTGDLARWLpDGTVEWLGRMDGQVKIRGYRI 878
Cdd:PRK07769 418 IGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAEGapddALWVRTGDYGVYF-DGELYITGRVKDLVIIDGRNH 496
|
490
....*....|....*..
gi 2040046167 879 EPGEVEA-------ALR 888
Cdd:PRK07769 497 YPQDLEYtaqeatkALR 513
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
12-351 |
2.10e-14 |
|
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: 78.00 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESrayfeqASFTIN------GSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKE-- 83
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGT------SSFNVSfacrlsGDVDRDRLASAWNTVLARHRILRSRYVPRD-GGLRRSYSSSpp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 84 RQSRLQFVDISHldetaketFVDqfehddkkKGFDLQTDPLMRVSIlkrAHEQYHCIWSHhhILMDGWCFGIVMKEFLAI 163
Cdd:cd19537 76 RVQRVDTLDVWK--------EIN--------RPFDLEREDPIRVFI---SPDTLLVVMSH--IICDLTTLQLLLREVSAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 164 YKAlgkeqlpdFEPVHPFSKYIKWLM--RQDRKEAEAFWKTRLIDVkQTASLPKTSSSSKGKLEQMAFTLSKEQTEGLRK 241
Cdd:cd19537 135 YNG--------KLLPPVRREYLDSTAwsRPASPEDLDFWSEYLSGL-PLLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQ 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 242 LALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISGRPSdlEDVEKMVGLFINTIPVRVKSGPE---SFLTLVSHLQQ 318
Cdd:cd19537 206 FSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTS--EEDMETVGLFLEPLPIRIRFPSSsdaSAADFLRAVRR 283
|
330 340 350
....*....|....*....|....*....|....*....
gi 2040046167 319 ESLKAEAYsYYP------LYDIQAQSmLKHELFDHIVVF 351
Cdd:cd19537 284 SSQAALAH-AIPwhqlleHLGLPPDS-PNHPLFDVMVTF 320
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
460-957 |
2.53e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 78.91 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 460 PLAPTlhSFFTRRAALSPNLPAVRFSGGILTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGA 539
Cdd:PLN03102 13 PLTPI--TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 540 YVP----LDPDYPEERLRYM-------------LADSGARLLVT---GPGLSV---------SGFSGETLEVNLSSLRTE 590
Cdd:PLN03102 91 LNPintrLDATSIAAILRHAkpkilfvdrsfepLAREVLHLLSSedsNLNLPVifiheidfpKRPSSEELDYECLIQRGE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 591 PAEN---EPVCAHTDGGSLAyVIYTSGSTGTPKGVAVEHRqaAAFLSgmqrqfplteddviVLKSSFSFDASIWQLFWWM 667
Cdd:PLN03102 171 PTPSlvaRMFRIQDEHDPIS-LNYTSGTTADPKGVVISHR--GAYLS--------------TLSAIIGWEMGTCPVYLWT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 668 IPgasMYLLpQGWEKDPALMTEAFTN-----------------EGVTTAHFIPAMANSFLDQVEMETEEKRTSLaktlkR 730
Cdd:PLN03102 234 LP---MFHC-NGWTFTWGTAARGGTSvcmrhvtapeiykniemHNVTHMCCVPTVFNILLKGNSLDLSPRSGPV-----H 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 731 VFAGGEAlAPQTAARFARSLpETAVIHGYGPTEATVDAAFFRYDHEKDR----ERMRLPIGKPVPGARLYILD-----SE 801
Cdd:PLN03102 305 VLTGGSP-PPAALVKKVQRL-GFQVMHAYGLTEATGPVLFCEWQDEWNRlpenQQMELKARQGVSILGLADVDvknkeTQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 802 KAVQPIG-VAGELYIAGAGVARGYLNRPELTEERFlddpfyrGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEP 880
Cdd:PLN03102 383 ESVPRDGkTMGEIVIKGSSIMKGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 881 GEVEAALRQIDGVREAAVVAR---TEGEETELYAYIEGQDQKTARTELG-------------KRLPAYMMPSSFIEMREW 944
Cdd:PLN03102 456 VEVENVLYKYPKVLETAVVAMphpTWGETPCAFVVLEKGETTKEDRVDKlvtrerdlieycrENLPHFMCPRKVVFLQEL 535
|
570
....*....|...
gi 2040046167 945 PVTPSGKLDRKAL 957
Cdd:PLN03102 536 PKNGNGKILKPKL 548
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1485-1879 |
2.53e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 78.93 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1485 SFIHTFNQTKQDYPKHetISRLFEYQAAKTPHAPAVIYDRQT------LTYRELNQRANRIAAALRANGVGSESVVALLT 1558
Cdd:PRK12582 35 SIVIKSRHPLGPYPRS--IPHLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1559 SRTPELAVGILGILKAGGAYLPVTED---MPTE--RLEWM--LSDSNAVMLLQSDRLESHMAGKRLfiEDIQL------- 1624
Cdd:PRK12582 113 GNSIEHALMTLAAMQAGVPAAPVSPAyslMSHDhaKLKHLfdLVKPRVVFAQSGAPFARALAALDL--LDVTVvhvtgpg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1625 --EAGIS----ANNP-----EQ---QGGPDSLAYIMYTSGSTGTPKGVMVEQRgvvRLVKNSDM-----AFSPEDRIllt 1685
Cdd:PRK12582 191 egIASIAfadlAATPptaavAAaiaAITPDTVAKYLFTSGSTGMPKAVINTQR---MMCANIAMqeqlrPREPDPPP--- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1686 aSLGFDAM----TF---EVFGPLL-NGACLYISD--------KETyldsdrLKTfIQQNGITTLWLTSSLFNQLSEQNER 1749
Cdd:PRK12582 265 -PVSLDWMpwnhTMggnANFNGLLwGGGTLYIDDgkplpgmfEET------IRN-LREISPTVYGNVPAGYAMLAEAMEK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1750 T-------FSDLSRLILGGEALSPNHVNR-----VRNTAPDLALWNGYGPTEN--TTFSTCFRIEHEYKhsipIGRPIAN 1815
Cdd:PRK12582 337 DdalrrsfFKNLRLMAYGGATLSDDLYERmqalaVRTTGHRIPFYTGYGATETapTTTGTHWDTERVGL----IGLPLPG 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1816 STAyivnsrgRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWL 1879
Cdd:PRK12582 413 VEL-------KLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFV 463
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1498-1984 |
2.61e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 78.73 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1498 PKHETISRLFEYqaAKTPHAPAVIyDRQT---LTYRELNQRANRIAAALRAN-GVGSESVVALLTSRTPELAVGILGILK 1573
Cdd:PLN02574 38 PNLDAVSFIFSH--HNHNGDTALI-DSSTgfsISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1574 AGGaylpVTEDM-----PTERLEWMLSDSNAVMLLQSDRLE----------------SHMAGKRLFIEDIQLEAGISANN 1632
Cdd:PLN02574 115 LGG----IVTTMnpsssLGEIKKRVVDCSVGLAFTSPENVEklsplgvpvigvpenyDFDSKRIEFPKFYELIKEDFDFV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1633 PEQQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVK------NSDMAFSPEDRILLTASLGFDAMTFEVF--GPLLNG 1704
Cdd:PLN02574 191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfeASQYEYPGSDNVYLAALPMFHIYGLSLFvvGLLSLG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1705 ACLYISDKetyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNE----RTFSDLSRLILGGEALSPNHVNRVRNTAPDLA 1780
Cdd:PLN02574 271 STIVVMRR---FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgvcgEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1781 LWNGYGPTENTTFST-CFRIEHEYKHSiPIGRPIANSTAYIVN-SRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKF 1858
Cdd:PLN02574 348 FIQGYGMTESTAVGTrGFNTEKLSKYS-SVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1859 VPnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIvrtgPSGHKEL----L 1934
Cdd:PLN02574 427 DK------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVT----AVPDKECgeipV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 1935 AYMSLQAE--MNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PLN02574 497 AFVVRRQGstLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1522-1984 |
3.14e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 78.64 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1522 YDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAG-------GAYLPvteDMPTERLEwml 1594
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGFSA---EALADRII--- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 sDSNAVMLLQSDrlESHMAGKRLFIEDI-----------------------------------QLEAGISANN-PEQQGG 1638
Cdd:PRK00174 168 -DAGAKLVITAD--EGVRGGKPIPLKANvdealancpsvekvivvrrtggdvdwvegrdlwwhELVAGASDECePEPMDA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLaYIMYTSGSTGTPKGVMVEQRGVvrLVKNSdMAFS------PEDRILLTASLGF-DAMTFEVFGPLLNGAC--LYi 1709
Cdd:PRK00174 245 EDPL-FILYTSGSTGKPKGVLHTTGGY--LVYAA-MTMKyvfdykDGDVYWCTADVGWvTGHSYIVYGPLANGATtlMF- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1710 sdkE---TYLDSDRLKTFIQQNGITTLWlTS-----SLFNQLSEQNERTfsDLSRL-ILG--GEALSPnhvnrvrnTApd 1778
Cdd:PRK00174 320 ---EgvpNYPDPGRFWEVIDKHKVTIFY-TAptairALMKEGDEHPKKY--DLSSLrLLGsvGEPINP--------EA-- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1779 lalWNGYgptenttfstcfrieheYKH----SIPI----------------------------GRPIANSTAYIVNSRGR 1826
Cdd:PRK00174 384 ---WEWY-----------------YKVvggeRCPIvdtwwqtetggimitplpgatplkpgsaTRPLPGIQPAVVDEEGN 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1827 LQPMGVIGELCVGGD--GLARGYFGRPEltkeKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELG 1904
Cdd:PRK00174 444 PLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTA 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1905 EIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSL----QAEMNIEK-VRSLLSQQLPGFMIPAHLVELAALPLTQNGKL 1979
Cdd:PRK00174 520 EIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLkggeEPSDELRKeLRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKI 599
|
....*
gi 2040046167 1980 DRRAL 1984
Cdd:PRK00174 600 MRRIL 604
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1506-1984 |
4.26e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.96 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1506 LFEYQAAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDM 1585
Cdd:PLN02479 25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1586 PTERLEWML--SDSNAVML------LQSDRLEShMAGKR---------LFIED----------------IQLEAGISANN 1632
Cdd:PLN02479 105 NAPTIAFLLehSKSEVVMVdqefftLAEEALKI-LAEKKkssfkppllIVIGDptcdpkslqyalgkgaIEYEKFLETGD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1633 PEQQGGP-----DSLAyIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMAFS-PEDRILLtaslgfdaMTFEVFGplLNGAC 1706
Cdd:PLN02479 184 PEFAWKPpadewQSIA-LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGmNEGAVYL--------WTLPMFH--CNGWC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1707 L---------------YISDKETYldsdrlkTFIQQNGITTLWLTSSLFNQL-SEQNERTFSDLSRLIlggealspnHVN 1770
Cdd:PLN02479 253 FtwtlaalcgtniclrQVTAKAIY-------SAIANYGVTHFCAAPVVLNTIvNAPKSETILPLPRVV---------HVM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1771 rvrnTApdlalwnGYGPTENTTFSTC---FRIEHEYKHSIPIG-------RPIANSTAYI----VNSRGRLQPMGV---- 1832
Cdd:PLN02479 317 ----TA-------GAAPPPSVLFAMSekgFRVTHTYGLSETYGpstvcawKPEWDSLPPEeqarLNARQGVRYIGLegld 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1833 ----------------IGELCVGGDGLARGYFGRPELTKEKFVPNpftpgerMYRTGDLARWLKDGTIDYIGRMDDQVKI 1896
Cdd:PLN02479 386 vvdtktmkpvpadgktMGEIVMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIIS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1897 RGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMN-------IEKVRSLLSQQLPGFMIPAHLVeLA 1969
Cdd:PLN02479 459 GGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDksdeaalAEDIMKFCRERLPAYWVPKSVV-FG 537
|
570
....*....|....*
gi 2040046167 1970 ALPLTQNGKLDRRAL 1984
Cdd:PLN02479 538 PLPKTATGKIQKHVL 552
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1639-1984 |
5.45e-14 |
|
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: 75.98 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKgvmVEQRGVVRLVKNSDMA-----FSPEDRILLTASLgfdamtFEVFG-------PLLNGAC 1706
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPK---LAQHTHSNEVYNAWMLalnslFDPDDVLLCGLPL------FHVNGsvvtlltPLASGAH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1707 LYISDKETYLDSDRLKTF---IQQNGITTLWLTSSLFNQLSEQ-NERTFSDLsRLILGGEALSPNHVNRVRNTAPDLALW 1782
Cdd:cd05944 72 VVLAGPAGYRNPGLFDNFwklVERYRITSLSTVPTVYAALLQVpVNADISSL-RFAMSGAAPLPVELRARFEDATGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1783 NGYGPTENTTFSTCFRIEHEYK-HSIPIGRPIANSTAYIVNSRGRLQ-PMGV--IGELCVGGDGLARGYFgRPELTKEKF 1858
Cdd:cd05944 151 EGYGLTEATCLVAVNPPDGPKRpGSVGLRLPYARVRIKVLDGVGRLLrDCAPdeVGEICVAGPGVFGGYL-YTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1859 VpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVkIR-GYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYM 1937
Cdd:cd05944 230 V------ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1938 SLQ--AEMNIEKVRSLLSQQLPG-FMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05944 303 QLKpgAVVEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
490-901 |
5.70e-14 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 77.46 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTG-- 567
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEde 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 568 -------------PGL---------SVSGFS-------GETLEVNLSSLRTEPAENEPVCAHTDGGSLAYVIYTSGSTGT 618
Cdd:cd17641 93 eqvdklleiadriPSVryviycdprGMRKYDdprlisfEDVVALGRALDRRDPGLYEREVAAGKGEDVAVLCTTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 619 PKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVlkssfsfdaSIWQLFWWMipgASMYLLPQG-WE-------KDPALMTEA 690
Cdd:cd17641 173 PKLAMLSHGNFLGHCAAYLAADPLGPGDEYV---------SVLPLPWIG---EQMYSVGQAlVCgfivnfpEEPETMMED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 691 FTNEGVTTAHFIPAMANSFLDQVEMETEE--------------------------KRTSLAKTLKRVFA----------- 733
Cdd:cd17641 241 LREIGPTFVLLPPRVWEGIAADVRARMMDatpfkrfmfelgmklglraldrgkrgRPVSLWLRLASWLAdallfrplrdr 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 734 -----------GGEALAPQTAaRFARSL--PETAVihgYGPTEATVdAAFFRYDHEKDRErmrlPIGKPVPGARLYILDs 800
Cdd:cd17641 321 lgfsrlrsaatGGAALGPDTF-RFFHAIgvPLKQL---YGQTELAG-AYTVHRDGDVDPD----TVGVPFPGTEVRIDE- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 801 ekavqpigvAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRM-DGQVKIRGYRIE 879
Cdd:cd17641 391 ---------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLH------TGDAGYFKENGHLVVIDRAkDVGTTSDGTRFS 455
|
490 500
....*....|....*....|..
gi 2040046167 880 PGEVEAALRQIDGVREAAVVAR 901
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVLGA 477
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1511-1877 |
7.77e-14 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 77.09 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPaVIYDRQ------TLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVT-- 1582
Cdd:cd05921 5 ARQAPDRT-WLAEREgnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1583 -------------------------EDMPTER--LEWMLSDSNAVMLLQSdrlesHMAGKR--LFIEDIQLEAGISANNP 1633
Cdd:cd05921 84 yslmsqdlaklkhlfellkpglvfaQDAAPFAraLAAIFPLGTPLVVSRN-----AVAGRGaiSFAELAATPPTAAVDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1634 EQQGGPDSLAYIMYTSGSTGTPKGVMVEQRgvvRLVKNSDM------AFSPEDRILLtaslgfDAM----TF---EVFGP 1700
Cdd:cd05921 159 FAAVGPDTVAKFLFTSGSTGLPKAVINTQR---MLCANQAMleqtypFFGEEPPVLV------DWLpwnhTFggnHNFNL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1701 LL-NGACLYIsdketyldsDRLKTFIQQNGIT---------TLWLT-----SSLFNQLsEQNE----RTFSDLSRLILGG 1761
Cdd:cd05921 230 VLyNGGTLYI---------DDGKPMPGGFEETlrnlreispTVYFNvpagwEMLVAAL-EKDEalrrRFFKRLKLMFYAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1762 EALSPNHVNR-----VRNTAPDLALWNGYGPTEntTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLqpmgvigEL 1836
Cdd:cd05921 300 AGLSQDVWDRlqalaVATVGERIPMMAGLGATE--TAPTATFTHWPTERSGLIGLPAPGTELKLVPSGGKY-------EV 370
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2040046167 1837 CVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLAR 1877
Cdd:cd05921 371 RVKGPNVTPGYWRQPELTAQAFDEEGF------YCLGDAAK 405
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1522-1978 |
1.28e-13 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 75.93 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1522 YDRQTLTYRELNQRANRIAAALR-ANGVGSESVVALLTSRTPELAVGILGILKAGGAylpvtedmpTERLEWMLSDSNAV 1600
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1601 MLLQsdrleshMAGKRLFIEDiqleagisannpeqqggPDSLAYIMYTSGSTGTPKGVMVEQRGVVR--LVKNSDMAFSP 1678
Cdd:cd05937 72 HCLK-------LSGSRFVIVD-----------------PDDPAILIYTSGTTGLPKAAAISWRRTLVtsNLLSHDLNLKN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1679 EDRI-----LLTASLGFDAMTFEvfgpLLNGACLYISDK---ETYLDSDRLK--TFIQQNGITTLWLTSSLFNQlSEQNE 1748
Cdd:cd05937 128 GDRTytcmpLYHGTAAFLGACNC----LMSGGTLALSRKfsaSQFWKDVRDSgaTIIQYVGELCRYLLSTPPSP-YDRDH 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1749 RTfsdlsRLILGgEALSPNHVNRVRN-------------TAPDLALWN------------GYGPTENTTFS---TCFRIE 1800
Cdd:cd05937 203 KV-----RVAWG-NGLRPDIWERFRErfnvpeigefyaaTEGVFALTNhnvgdfgagaigHHGLIRRWKFEnqvVLVKMD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1801 HEYKHsiPIGRPianSTAYIVNS-RGRlqPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTPGERMYRTGDLARWL 1879
Cdd:cd05937 277 PETDD--PIRDP---KTGFCVRApVGE--PGEMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1880 KDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPsGHKELLAYMSLQ--------AEMNIEKVRSL 1951
Cdd:cd05937 350 ADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVP-GHDGRAGCAAITleessavpTEFTKSLLASL 428
|
490 500
....*....|....*....|....*..
gi 2040046167 1952 LSQQLPGFMIPAHLVELAALPLTQNGK 1978
Cdd:cd05937 429 ARKNLPSYAVPLFLRLTEEVATTDNHK 455
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
12-252 |
1.95e-13 |
|
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: 74.98 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEgMLFHslLDQESRAYFEQA-SFTINGSLDTERFQKSLDALIERYDIFRTAFIHKNvAKPRQVVLKERQS--RL 88
Cdd:cd19534 3 PLTPIQR-WFFE--QNLAGRHHFNQSvLLRVPQGLDPDALRQALRALVEHHDALRMRFRRED-GGWQQRIRGDVEElfRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 89 QFVDISHLDETAK-ETFVDQFEhddkkKGFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDG--WcfGIVMKEFLAIYK 165
Cdd:cd19534 79 EVVDLSSLAQAAAiEALAAEAQ-----SSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW--RILLEDLEAAYE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 166 ALGKEQLPDFEPVHPFSKYIKWL----MRQDRKEAEAFWKTRLIDvkQTASLPKTSSSSKGKLEQMAFTLSKEQTEglrK 241
Cdd:cd19534 152 QALAGEPIPLPSKTSFQTWAELLaeyaQSPALLEELAYWRELPAA--DYWGLPKDPEQTYGDARTVSFTLDEEETE---A 226
|
250
....*....|.
gi 2040046167 242 LALQAGATLNT 252
Cdd:cd19534 227 LLQEANAAYRT 237
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1501-1984 |
2.25e-13 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 75.49 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1501 ETISRLFEYQAAKTPHAPAVIY-----DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAG 1575
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIFessggVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1576 GAYLPVTEDMPTERLEWMLSDSNAVMLLQSD---------RLESHMAGKRLFIEDIQLEAGISANNPEQQGG-------- 1638
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAqfypmyrqiQQEDATPLRHICLTRVALPADDGVSSFTQLKAqqpatlcy 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 -----PDSLAYIMYTSGSTGTPKGVMVeqrgvvrlvKNSDMAFS----------PEDRILLTASLGFD-------AM-TF 1695
Cdd:PRK08008 167 applsTDDTAEILFTSGTTSRPKGVVI---------THYNLRFAgyysawqcalRDDDVYLTVMPAFHidcqctaAMaAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1696 EVfgpllnGACLYISDKetYldSDRlkTFIQQ-----NGIT--------TLWLTSS-------------LFNQLSEQNER 1749
Cdd:PRK08008 238 SA------GATFVLLEK--Y--SAR--AFWGQvckyrATITecipmmirTLMVQPPsandrqhclrevmFYLNLSDQEKD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1750 TFsdLSRLilggealspnhvnRVRntapdlaLWNGYGPTEnTTFSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQP 1829
Cdd:PRK08008 306 AF--EERF-------------GVR-------LLTSYGMTE-TIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1830 MGVIGELC---VGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEI 1906
Cdd:PRK08008 363 AGEIGEICikgVPGKTIFKEYYLDPKATAKVLEADGW------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVEL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1907 EAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK08008 437 ENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNegETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1524-1913 |
2.27e-13 |
|
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: 75.57 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1524 RQTLTYRELNQRANRIAAALRA-NGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVML 1602
Cdd:cd17632 65 FETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 LQS----------------------------------------DRLESHMAGKRLFIEDIQLEAGISANNPEQQG-GPDS 1641
Cdd:cd17632 145 AVSaehldlaveavleggtpprlvvfdhrpevdahraalesarERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEpDDDP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1642 LAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMafSPEDRILLTASLGFDAMTF-----EVFGPLLNGACLYI---SDKE 1713
Cdd:cd17632 225 LALLIYTSGSTGTPKGAMYTERLVATFWLKVSS--IQDIRPPASITLNFMPMSHiagriSLYGTLARGGTAYFaaaSDMS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1714 TYLDS------------DRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLSRLILGGEALSpnhvnRVRNTAP---- 1777
Cdd:cd17632 303 TLFDDlalvrptelflvPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLA-----AVCGSAPlsae 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1778 ---------DLALWNGYGPTENTTFSTCFRIEH----EYKH-SIPigrpianSTAYIVNSRGRLQpmgviGELCVGGDGL 1843
Cdd:cd17632 378 mkafmesllDLDLHDGYGSTEAGAVILDGVIVRppvlDYKLvDVP-------ELGYFRTDRPHPR-----GELLVKTDTL 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 1844 ARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKI-RGYRIELGEIEAA------LRQI 1913
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVfaasplVRQI 516
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1515-1984 |
2.49e-13 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.44 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWML 1594
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 SDSN----------------AVMLLQSDRLESHM---------AGKRLFIEDIQLEAGISANNP-----------EQQGG 1638
Cdd:PLN03102 108 RHAKpkilfvdrsfeplareVLHLLSSEDSNLNLpvifiheidFPKRPSSEELDYECLIQRGEPtpslvarmfriQDEHD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYimyTSGSTGTPKGVMVEQRGVVRLVknsdmafspedrilLTASLGFDAMTFEVFG---PLL--NG--------- 1704
Cdd:PLN03102 188 PISLNY---TSGTTADPKGVVISHRGAYLST--------------LSAIIGWEMGTCPVYLwtlPMFhcNGwtftwgtaa 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1705 -----ACL-YISDKETYLDsdrlktfIQQNGITTLWLTSSLFNQLSEQNERTFSDLS---RLILGGEALSPNHVNRVRNT 1775
Cdd:PLN03102 251 rggtsVCMrHVTAPEIYKN-------IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSgpvHVLTGGSPPPAALVKKVQRL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1776 ApdLALWNGYGPTENTTfSTCF--------RIEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGV------IGELCVGGD 1841
Cdd:PLN03102 324 G--FQVMHAYGLTEATG-PVLFcewqdewnRLPENQQMELKARQGVSILGLADVDVKNKETQESVprdgktMGEIVIKGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1842 GLARGYFGRPELTKEKFvpnpftpGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAV 1921
Cdd:PLN03102 401 SIMKGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1922 IVRTGPSGHKELLAYMSLQ--AEMNIEKVRSLLSQQ----------LPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PLN03102 474 VAMPHPTWGETPCAFVVLEkgETTKEDRVDKLVTRErdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
602-952 |
2.83e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.13 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 602 DGGSLAYVIYTSGSTGTPKGVAVEHRQAA--AFLSGMQRQFPLTEDDVIV-LKSSFSFDAsiwqlfwWMIP------GAS 672
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLpVVPMFHVNA-------WGLPysapltGAK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 673 MyLLPqGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQveMETEEKRTSlakTLKRVFAGGEALAPQTAARFARSLpE 752
Cdd:PRK07008 247 L-VLP-GPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNH--MREAGLRFS---TLRRTVIGGSACPPAMIRTFEDEY-G 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 753 TAVIHGYGPTE-------ATVDAAFFRYDHEkDRERMRLPIGKPVPGARLYILDSEKAVQPI-GVA-GELYIAGAGVARG 823
Cdd:PRK07008 319 VEVIHAWGMTEmsplgtlCKLKWKHSQLPLD-EQRKLLEKQGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 824 YLNRPelteerflDDPFYRGerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAA------ 897
Cdd:PRK07008 398 YFRGD--------ASPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAciacah 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 898 ---------VVARTEGEET---ELYAYIEGqdqKTARtelgkrlpaYMMPSSFIEMREWPVTPSGKL 952
Cdd:PRK07008 468 pkwderpllVVVKRPGAEVtreELLAFYEG---KVAK---------WWIPDDVVFVDAIPHTATGKL 522
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2065-2384 |
3.18e-13 |
|
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: 76.05 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2065 APLIRKTERNIDQRPIEGEVPWTPVQRWFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGG 2144
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2145 QLQQFNRGIHGELYSLNIRDLSKTAQWEKLIEDEVADL-QRSIHLQTGPLLKAGLFNTMSGTYLFL-TIHHLVVDGVSWR 2222
Cdd:COG1020 81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEaLAPFDLLRGPLLRLLLLLLLLLLLLLLlALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2223 ILLEDLSAAYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRTVEKEKAAL--LPCEKPHSAADNIR-KT 2299
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLleLPTDRPRPAVQSYRgAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2300 ESFTLSEEDTHVLiHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRDHtlPELDisRTVGWFTTIYPVLID 2379
Cdd:COG1020 241 VSFRLPAELTAAL-RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELE--GLVGFFVNTLPLRVD 315
|
....*
gi 2040046167 2380 LHHAA 2384
Cdd:COG1020 316 LSGDP 320
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
971-1045 |
3.57e-13 |
|
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: 66.80 E-value: 3.57e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2040046167 971 APRTITEMKLAKLWEEVLKYGPA--GTRDHFFEQ-GGHSLKATALVSRIAKAFGVQVPLKEIFAKPTLEELAAVIQEL 1045
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDPEeiTPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2085-2391 |
3.57e-13 |
|
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: 74.41 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2085 PWTPVQRWFLAQHIEERqhfNQSVMLHSS-----EGFQEQPLRTALQHLVIHHDALRMTIIDDGGQ--LQQFNRGIHGEL 2157
Cdd:cd19536 3 PLSSLQEGMLFHSLLNP---GGSVYLHNYtytvgRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGqpVQVVHRQAQVPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2158 YSLNIRDLS-KTAQWEKLIEDEVA---DLQRSihlqtgPLLKAGLFNTMSGTYLFLTI--HHLVVDGVSWRILLEDLSAA 2231
Cdd:cd19536 80 TELDLTPLEeQLDPLRAYKEETKIrrfDLGRA------PLVRAALVRKDERERFLLVIsdHHSILDGWSLYLLVKEILAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2232 YSQAAAGQPVQLPrKTDSYQYFANRLAEYAESSKVIReqsYWRT-VEKEKAALLPCEKPHSAADNIRKTESFTLSEEDth 2310
Cdd:cd19536 154 YNQLLEYKPLSLP-PAQPYRDFVAHERASIQQAASER---YWREyLAGATLATLPALSEAVGGGPEQDSELLVSVPLP-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2311 VLIHKVNNAYNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRdhTLPELDISRTVGWFTTIYPVLIDL---------H 2381
Cdd:cd19536 228 VRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGR--SEETTGAERLLGLFLNTLPLRVTLseetvedllK 305
|
330
....*....|
gi 2040046167 2382 HAAEGELGLA 2391
Cdd:cd19536 306 RAQEQELESL 315
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
606-954 |
5.18e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 74.06 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 LAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSFDASIWQL-FWWMIPGASMYLLPQG-WEKD 683
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMNQYLMPTRlFIRR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 684 PALMTEAFTNEGVTTAHFIPAMANSFLDQVEMETEEKRTslAKTLKRVFAGGEALAPQTAARF-----ARSLPETAVIHG 758
Cdd:cd05908 188 PILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWD--LSSIRMILNGAEPIDYELCHEFldhmsKYGLKRNAILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 759 YGPTEATVDAAF---------FRYDHE-------------KDRERMR-LPIGKPVPGARLYILDSEKAVQPIGVAGELYI 815
Cdd:cd05908 266 YGLAEASVGASLpkaqspfktITLGRRhvthgepepevdkKDSECLTfVEVGKPIDETDIRICDEDNKILPDGYIGHIQI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 816 AGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLArWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVRE 895
Cdd:cd05908 346 RGKNVTPGYYNNPEATAKVFTDDGWLK------TGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEL 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 896 AAVVA----RTEGEETELYAYIEGQDQKTARTELGKRLPAYMMP------SSFIEMREWPVTPSGKLDR 954
Cdd:cd05908 419 GRVVAcgvnNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKrggwqiNEVLPIRRIPKTTSGKVKR 487
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1527-1889 |
6.50e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 74.49 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSN-AVMLLQS 1605
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEvSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1606 DRLESHMA-----------------------------GKRLFI-EDIQLEAGISANNPEQQggPDSLAYIMYTSGSTGTP 1655
Cdd:PLN02861 158 SKISSILSclpkcssnlktivsfgdvsseqkeeaeelGVSCFSwEEFSLMGSLDCELPPKQ--KTDICTIMYTSGTTGEP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1656 KGVMVEQRGVVRLVKNSDMAFSPEDRILLTASLGFDAMTF-EVFGPLLNGACLY---------------ISDKETYLDS- 1718
Cdd:PLN02861 236 KGVILTNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYLPLaHVYDQVIETYCISkgasigfwqgdirylMEDVQALKPTi 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 --------DRLKTFIQQNGITTLWLTSSLFNQ-------------------------LSEQNERTFSDLSRLILGGEALS 1765
Cdd:PLN02861 316 fcgvprvyDRIYTGIMQKISSGGMLRKKLFDFaynyklgnlrkglkqeeasprldrlVFDKIKEGLGGRVRLLLSGAAPL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1766 PNHVNRVRNTAPDLALWNGYGPTENTtfSTCF-RIEHEYKHSIPIGRPIANSTAYIVNsrgrLQPMGV-------IGELC 1837
Cdd:PLN02861 396 PRHVEEFLRVTSCSVLSQGYGLTESC--GGCFtSIANVFSMVGTVGVPMTTIEARLES----VPEMGYdalsdvpRGEIC 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 1838 VGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGR 1889
Cdd:PLN02861 470 LRGNTLFSGYHKRQDLTEEVLIDGWF-------HTGDIGEWQPNGAMKIIDR 514
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
606-887 |
8.28e-13 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 74.00 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 606 LAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFP-LTEDDVIV----LKSSFSFDASIWQLfwwmIPGASM-YLLP-- 677
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPkLGKNDVYLaylpLAHILELAAESVMA----AVGAAIgYGSPlt 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 678 ---------QGWEKD-----PALMTEaftnegvttahfIPAMANSFLDQVEMETEEKrTSLAKTL-----KR-------- 730
Cdd:PLN02387 328 ltdtsnkikKGTKGDasalkPTLMTA------------VPAILDRVRDGVRKKVDAK-GGLAKKLfdiayKRrlaaiegs 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 731 ---------------VF---------------AGGEALAPQTAaRFARSLPETAVIHGYGPTEATVDAAFFRYDhekDRE 780
Cdd:PLN02387 395 wfgawglekllwdalVFkkiravlggrirfmlSGGAPLSGDTQ-RFINICLGAPIGQGYGLTETCAGATFSEWD---DTS 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 781 RMRlpIGKPVPGARLYILDSEKAVQPIGVA----GELYIAGAGVARGYLNRPELTEERFLDDPfyRGERMYQTGDLARWL 856
Cdd:PLN02387 471 VGR--VGPPLPCCYVKLVSWEEGGYLISDKpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDE--RGMRWFYTGDIGQFH 546
|
330 340 350
....*....|....*....|....*....|..
gi 2040046167 857 PDGTVEWLGRMDGQVKIR-GYRIEPGEVEAAL 887
Cdd:PLN02387 547 PDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1525-1984 |
1.39e-12 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 72.84 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQ 1604
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 sdrleSHMAGKRLFIEDIQleagisannPEQQGG--PDSLAYImYTSGSTGTPKGVMVEQRGVVRLVKNSDMAF--SPED 1680
Cdd:cd05939 82 -----NLLDPLLTQSSTEP---------PSQDDVnfRDKLFYI-YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFgmRPED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1681 RILLTASLGFDAMTFEVFGP-LLNGACLYISdketyldsdrlKTFIQQNgittLWLTSSLFNQLSEQnerTFSDLSRLIL 1759
Cdd:cd05939 147 VVYDCLPLYHSAGGIMGVGQaLLHGSTVVIR-----------KKFSASN----FWDDCVKYNCTIVQ---YIGEICRYLL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1760 GGEALSPNHVNRVRntapdLALWNGYGPTENTTFSTCFRIEH--EYKHSIPIGRPIANSTAYI----VNSR--GRLQPMG 1831
Cdd:cd05939 209 AQPPSEEEQKHNVR-----LAVGNGLRPQIWEQFVRRFGIPQigEFYGATEGNSSLVNIDNHVgacgFNSRilPSVYPIR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1832 VI------GELCVGGDGLA------------------------RGYFGRPElTKEKFVPNPFTPGERMYRTGDLARWLKD 1881
Cdd:cd05939 284 LIkvdedtGELIRDSDGLCipcqpgepgllvgkiiqndplrrfDGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDEL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1882 GTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGP--SGHKELLAYMSLQAEMNIEKVRSLLSQQLPGF 1959
Cdd:cd05939 363 GYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPgvEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPY 442
|
490 500
....*....|....*....|....*
gi 2040046167 1960 MIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:cd05939 443 ARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
2083-2384 |
1.55e-12 |
|
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: 72.41 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2083 EVPWTPVQR--WFlaqhIEERQHFnqSVMLHSSEGFQEQP------LRTALQHLVIHHDALRMTII-DDGGQLQQFNRGI 2153
Cdd:cd19539 1 RIPLSFAQErlWF----IDQGEDG--GPAYNIPGAWRLTGpldveaLREALRDVVARHEALRTLLVrDDGGVPRQEILPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2154 HGElySLNIRDLS-KTAQWEKLIEDEVADLQRSI-HLQTGPLLKAGLFNTMSGT-YLFLTIHHLVVDGVSWRILLEDLSA 2230
Cdd:cd19539 75 GPA--PLEVRDLSdPDSDRERRLEELLRERESRGfDLDEEPPIRAVLGRFDPDDhVLVLVAHHTAFDAWSLDVFARDLAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2231 AYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYWRT-VEKEKAALLPCEKPHSAADNIRKTE-SFTLSEED 2308
Cdd:cd19539 153 LYAARRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRrLRGAEPTALPTDRPRPAGFPYPGADlRFELDAEL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 2309 THVLIHKVNNAYNTDTQdILLTAASLALCDWMGERKLRIAMEGHGRDHtlPELDisRTVGWFTTIYPVLIDLHHAA 2384
Cdd:cd19539 233 VAALRELAKRARSSLFM-VLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFE--STVGFFVNLLPLRVDVSDCA 303
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
484-898 |
1.61e-12 |
|
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: 72.71 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 484 FSGGILTYRELDQYTNQLAIRLKKK-GVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGAR 562
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 563 LLVTGP----------------GLSVSGFSGETLEVNLSSLRTEPAE--NEPV----CAHTDGGSLAYVIYTSGSTGTPK 620
Cdd:cd05938 81 VLVVAPelqeaveevlpalradGVSVWYLSHTSNTEGVISLLDKVDAasDEPVpaslRAHVTIKSPALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 621 GVAVEHRQAAAfLSGMQRQFPLTEDDVIVL-----KSSfsfdASIWQLFWWMIPGASMYLLP-----QGWEKdpalmtea 690
Cdd:cd05938 161 AARISHLRVLQ-CSGFLSLCGVTADDVIYItlplyHSS----GFLLGIGGCIELGATCVLKPkfsasQFWDD-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 691 FTNEGVTTAHFIPAMANSFLDQVEMETEekrtslaKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEATVDA-- 768
Cdd:cd05938 228 CRKHNVTVIQYIGELLRYLCNQPQSPND-------RDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFfn 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 769 ---------------------AFFRYDHEKDrERMRLPIGKPVPGARlyildsekavqpigvaGElyiAGAGVAR----- 822
Cdd:cd05938 301 ytgkigavgrvsylykllfpfELIKFDVEKE-EPVRDAQGFCIPVAK----------------GE---PGLLVAKitqqs 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 823 ---GYLNRPELTEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV 898
Cdd:cd05938 361 pflGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNV 439
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1511-2006 |
1.64e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.77 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVT-EDMPTEr 1589
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNfRQTPDE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1590 LEWMLSDSNA-VMLLQSD--------RLESHMAGKRLFIEDIQLEAGISANNPEQQGGP--------DSLAYIMYTSGST 1652
Cdd:PRK07470 96 VAYLAEASGArAMICHADfpehaaavRAASPDLTHVVAIGGARAGLDYEALVARHLGARvanaavdhDDPCWFFFTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1653 GTPKGVMVE--QRGVVRLVKNSDM--AFSPEDRILLTASLGFDAMTFEvfgpLLNGA-----CLYISDKetyLDSDRLKT 1723
Cdd:PRK07470 176 GRPKAAVLThgQMAFVITNHLADLmpGTTEQDASLVVAPLSHGAGIHQ----LCQVArgaatVLLPSER---FDPAEVWA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1724 FIQQNGITTLWLTSSLFNQLSEQ---NERTFSDLSRLILGGEALSPNHVNRVRNT-APDLALWNGYGP-TENTTFSTcfr 1798
Cdd:PRK07470 249 LVERHRVTNLFTVPTILKMLVEHpavDRYDHSSLRYVIYAGAPMYRADQKRALAKlGKVLVQYFGLGEvTGNITVLP--- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1799 iehEYKHSI---------PIGRPIANSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgerm 1869
Cdd:PRK07470 326 ---PALHDAedgpdarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1870 yRTGDLARWLKDGTIdYI-GRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMNIE 1946
Cdd:PRK07470 397 -RTGDLGHLDARGFL-YItGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARdgAPVDEA 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1947 KVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALpepettaintayappRNQLEER 2006
Cdd:PRK07470 475 ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV---------------REELEER 519
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1495-1878 |
2.11e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 72.60 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1495 QDYPkhETISRLFEYQAAKTPHAPAVIY-----DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGIL 1569
Cdd:PRK08180 35 GDYP--RRLTDRLVHWAQEAPDRVFLAErgadgGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1570 GILKAGGAYLPVtedmpterlewmlsdSNAVMLLQSD--RLeSHMAG----KRLFIEDIQLEAG------------ISAN 1631
Cdd:PRK08180 113 AAMYAGVPYAPV---------------SPAYSLVSQDfgKL-RHVLElltpGLVFADDGAAFARalaavvpadvevVAVR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1632 NPEQQG------------------------GPDSLAYIMYTSGSTGTPKGVMVEQRgvvRLVKNSDMafspedrilLTAS 1687
Cdd:PRK08180 177 GAVPGRaatpfaallatpptaavdaahaavGPDTIAKFLFTSGSTGLPKAVINTHR---MLCANQQM---------LAQT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1688 LGFDAMTFEV----------FG-------PLLNGACLYISD--------KETyLDSDRLktfIQqngiTTLWLT-----S 1737
Cdd:PRK08180 245 FPFLAEEPPVlvdwlpwnhtFGgnhnlgiVLYNGGTLYIDDgkptpggfDET-LRNLRE---IS----PTVYFNvpkgwE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1738 SLFNQLsEQN----ERTFSDLSRLILGGEALSPNHVNR-----VRNTAPDLALWNGYGPTENTTFSTC--FRIEheykHS 1806
Cdd:PRK08180 317 MLVPAL-ERDaalrRRFFSRLKLLFYAGAALSQDVWDRldrvaEATCGERIRMMTGLGMTETAPSATFttGPLS----RA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 1807 IPIGRPIANSTAYIVNSRGRLqpmgvigELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARW 1878
Cdd:PRK08180 392 GNIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF 450
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2005-2063 |
2.16e-12 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 64.12 E-value: 2.16e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 2005 ERLAVIWQEVLGV--EKVGIEDSFFELGGDSIKALQVSARL-GRFDLKITAGDLFRHPTIKE 2063
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLeEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
464-951 |
2.23e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 72.54 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 464 TLHSFFTRRAALSPNLPAVRFS-GGI-LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYV 541
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYRdQGLrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 542 PLDPDYPEERLRYMLADSGARLLVTGPGLSVSGFsgetLEVnLSSLRTEPAENEPVCAHTDGG-SLAYVI---------- 610
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCKALIAADGFKDSDY----VAM-LYELAPELATCEPGQLQSARLpELRRVIflgdekhpgm 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 611 ----------------------------------YTSGSTGTPKGVAVEHRQAA--AFLSGMQRQFplTEDDVIVlkssf 654
Cdd:PRK08315 172 lnfdellalgravddaelaarqatldpddpiniqYTSGTTGFPKGATLTHRNILnnGYFIGEAMKL--TEEDRLC----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 655 sfdasiwqlfwwmIP-------------------GASMYLLPQGWekDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEM 715
Cdd:PRK08315 245 -------------IPvplyhcfgmvlgnlacvthGATMVYPGEGF--DPLATLAAVEEERCTALYGVPTMFIAELDHPDF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 716 ET---EEKRTSlaktlkrVFAGgeALAP-QTAARFARSLPETAVIHGYGPTEAT-------VDAAFfrydhekdrERMRL 784
Cdd:PRK08315 310 ARfdlSSLRTG-------IMAG--SPCPiEVMKRVIDKMHMSEVTIAYGMTETSpvstqtrTDDPL---------EKRVT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 785 PIGKPVPGARLYILDSEK-AVQPIGVAGELYIAGAGVARGYLNRPELTEERFLDDPFyrgerMYqTGDLARWLPDGTVEW 863
Cdd:PRK08315 372 TVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-----MH-TGDLAVMDEEGYVNI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 864 LGRMDGQVkIR-GYRIEPGEVEAALRQIDGVREAAVVA---RTEGEetELYAYI---EGQDQKTA--RTELGKRLPAYMM 934
Cdd:PRK08315 446 VGRIKDMI-IRgGENIYPREIEEFLYTHPKIQDVQVVGvpdEKYGE--EVCAWIilrPGATLTEEdvRDFCRGKIAHYKI 522
|
570
....*....|....*....
gi 2040046167 935 PS--SFIEmrEWPVTPSGK 951
Cdd:PRK08315 523 PRyiRFVD--EFPMTVTGK 539
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1640-1984 |
2.40e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 71.23 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1640 DSLAYIMYTSGSTGTPKGVMV------------EQR-----------------GVVRLVKnSDMAFSpeDRILLTASLGF 1690
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLtaaaltasadatHDRlggpgqwllalpahhiaGLQVLVR-SVIAGS--EPVELDVSAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1691 DAMTFEVFGPLLNGACLYISDKETYLDsdrlktfiqqNGITTLWLTSSLfnqlseqnertfSDLSRLILGGEALSPNhvn 1770
Cdd:PRK07824 112 DPTALPRAVAELGGGRRYTSLVPMQLA----------KALDDPAATAAL------------AELDAVLVGGGPAPAP--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1771 rVRNTAPDLAL--WNGYGPTEntTFSTCFrieheYKhsipiGRPIANSTAYIVNSRGRLqpmgvigelcvGGDGLARGYF 1848
Cdd:PRK07824 167 -VLDAAAAAGInvVRTYGMSE--TSGGCV-----YD-----GVPLDGVRVRVEDGRIAL-----------GGPTLAKGYR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1849 GRPEltkekfvPNPFT-PGerMYRTGDLARwLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGP 1927
Cdd:PRK07824 223 NPVD-------PDPFAePG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 1928 S-GHKELLAYM-SLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK07824 293 RlGQRVVAAVVgDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
470-952 |
4.09e-12 |
|
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: 71.72 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 470 TRRAALSPNLPAVRFSGGIL------TYRELDQYTNQLAIRLK-KKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVP 542
Cdd:cd17632 43 QRATELVTDPATGRTTLRLLprfetiTYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 543 LDPDYPEERLRYMLADSGARLLVTGPG-------LSVSGFSGETLEV------------NLSSLRTEPAE---------- 593
Cdd:cd17632 123 LQAGASAAQLAPILAETEPRLLAVSAEhldlaveAVLEGGTPPRLVVfdhrpevdahraALESARERLAAvgipvttltl 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 594 ----------NEPVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLsgmqRQFPLTEDDVIVLKSSFSF------D 657
Cdd:cd17632 203 iavrgrdlppAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFW----LKVSSIQDIRPPASITLNFmpmshiA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 658 ASIWqLFWWMIPGASMYLLPqgwEKDPALMTEAFTNEGVTTAHFIP-------------------AMANSFLDQVEMETE 718
Cdd:cd17632 279 GRIS-LYGTLARGGTAYFAA---ASDMSTLFDDLALVRPTELFLVPrvcdmlfqryqaeldrrsvAGADAETLAERVKAE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 719 EKRTSLAKTLKRVFAGGEALAPQTAArFARSLPETAVIHGYGPTEA---TVDAAFFR---YDHekdrermRLpigKPVPG 792
Cdd:cd17632 355 LRERVLGGRLLAAVCGSAPLSAEMKA-FMESLLDLDLHDGYGSTEAgavILDGVIVRppvLDY-------KL---VDVPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 793 ARLYILDSEkavQPigvAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGD-LARWLPDgTVEWLGRMDGQV 871
Cdd:cd17632 424 LGYFRTDRP---HP---RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYR------TGDvMAELGPD-RLVYVDRRNNVL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 872 KI-RGYRIEPGEVEAA------LRQI----DGVRE--AAVVARTEGEetelyayIEGQDQKTARTELGKR---------L 929
Cdd:cd17632 491 KLsQGEFVTVARLEAVfaasplVRQIfvygNSERAylLAVVVPTQDA-------LAGEDTARLRAALAESlqriareagL 563
|
570 580
....*....|....*....|...
gi 2040046167 930 PAYMMPSSFIEMREwPVTPSGKL 952
Cdd:cd17632 564 QSYEIPRDFLIETE-PFTIANGL 585
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1511-1984 |
4.09e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 71.90 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIY------DRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTED 1584
Cdd:PRK10524 63 LAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1585 MPTERLEWMLSDSNAVMLLQSD-------------------RLESHMAGKRLFIE----DIQLEAGIS---ANNPEQQGG 1638
Cdd:PRK10524 143 FASHSLAARIDDAKPVLIVSADagsrggkvvpykplldeaiALAQHKPRHVLLVDrglaPMARVAGRDvdyATLRAQHLG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PD---------SLAYIMYTSGSTGTPKGVmveQRGV----VRLVKNSDMAF--SPEDRILLTASLGFD-AMTFEVFGPLL 1702
Cdd:PRK10524 223 ARvpvewlesnEPSYILYTSGTTGKPKGV---QRDTggyaVALATSMDTIFggKAGETFFCASDIGWVvGHSYIVYAPLL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1703 NGAC--LYisdkE---TYLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNERTF-----SDLSRLILGGEAL-SPNH--- 1768
Cdd:PRK10524 300 AGMAtiMY----EglpTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLrkhdlSSLRALFLAGEPLdEPTAswi 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1769 -----VNRVRN-----TA-PDLALWNGYGPTENTTFSTCF-------RIEHEYKhsipiGRPIANSTAYIVNSRGRLQPm 1830
Cdd:PRK10524 376 sealgVPVIDNywqteTGwPILAIARGVEDRPTRLGSPGVpmygynvKLLNEVT-----GEPCGPNEKGVLVIEGPLPP- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1831 GVIGElcVGGDglargyfgrpeltKEKFVPNPFTP-GERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAA 1909
Cdd:PRK10524 450 GCMQT--VWGD-------------DDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEES 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1910 LRQIDGVKEAAVI---------------VRTGPSGHKELLAYMSLQAEmniekVRSLLSQQLPGFMIPAHLVELAALPLT 1974
Cdd:PRK10524 515 ISSHPAVAEVAVVgvkdalkgqvavafvVPKDSDSLADREARLALEKE-----IMALVDSQLGAVARPARVWFVSALPKT 589
|
570
....*....|
gi 2040046167 1975 QNGKLDRRAL 1984
Cdd:PRK10524 590 RSGKLLRRAI 599
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1866-1991 |
8.36e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 70.07 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1866 GERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI 1945
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2040046167 1946 EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPEPETTA 1991
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1639-1986 |
9.23e-12 |
|
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: 70.21 E-value: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQRGVV---RLVKNSdMAFSPEDRIL----LTASLGFDAMTFevfGPLLNGAclyisd 1711
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVhnmFAILNS-TEWKTKDRILswmpLTHDMGLIAFHL---APLIAGM------ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1712 kETYLDSDRLktFIQQngiTTLWL---TSSLFNQLSEQN------ERTFS-------DLS--RLILGG------------ 1761
Cdd:cd05908 175 -NQYLMPTRL--FIRR---PILWLkkaSEHKATIVSSPNfgykyfLKTLKpekandwDLSsiRMILNGaepidyelchef 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1762 -EALSPNHVNRVrntapdlALWNGYGPTENTTFSTC-------FRIEHEYKHS-------------------IPIGRPIA 1814
Cdd:cd05908 249 lDHMSKYGLKRN-------AILPVYGLAEASVGASLpkaqspfKTITLGRRHVthgepepevdkkdsecltfVEVGKPID 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1815 NSTAYIVNSRGRLQPMGVIGELCVGGDGLARGYFGRPELTKEKFVPNPFTpgermyRTGDLArWLKDGTIDYIGRMDDQV 1894
Cdd:cd05908 322 ETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDII 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1895 KIRGYRIELGEIEAALRQIDGV---KEAAVIVRTGPSGHKELLAYMSLQAEMN-----IEKVRSLLSQQlPGFMIpAHLV 1966
Cdd:cd05908 395 FVNGQNVYPHDIERIAEELEGVelgRVVACGVNNSNTRNEEIFCFIEHRKSEDdfyplGKKIKKHLNKR-GGWQI-NEVL 472
|
410 420
....*....|....*....|
gi 2040046167 1967 ELAALPLTQNGKLDRRALPE 1986
Cdd:cd05908 473 PIRRIPKTTSGKVKRYELAQ 492
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1515-1983 |
1.20e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 70.02 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1515 PHAPaviyDRQTltYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAylpVTedM---PTERL- 1590
Cdd:PRK07768 24 PDAP----VRHT--WGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAS---LT--MlhqPTPRTd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 --EW---------MLSDSNAVM----LLQSDRLESHmAGKRLFIEDiqLEAGISANNPEQqgGPDSLAYIMYTSGSTGTP 1655
Cdd:PRK07768 93 laVWaedtlrvigMIGAKAVVVgepfLAAAPVLEEK-GIRVLTVAD--LLAADPIDPVET--GEDDLALMQLTSGSTGSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1656 KGVMVEQRGvvrLVKNSD-----MAFSPE-DRILLTASLGFD-AMTFEVFGPLLNGACLYISDKETYLDSdrlktfiqqn 1728
Cdd:PRK07768 168 KAVQITHGN---LYANAEamfvaAEFDVEtDVMVSWLPLFHDmGMVGFLTVPMYFGAELVKVTPMDFLRD---------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1729 giTTLWLT-----------------SSLFNQLSEQNERTFSDLSRL---ILGGEALSPNHVNR-----VRNTAPDLALWN 1783
Cdd:PRK07768 235 --PLLWAEliskyrgtmtaapnfayALLARRLRRQAKPGAFDLSSLrfaLNGAEPIDPADVEDlldagARFGLRPEAILP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1784 GYGPTENT---TFSTCFR---------------------IEHEYKHSIPIGRPIANSTAYIVNSRGRLQPMGVIGELCVG 1839
Cdd:PRK07768 313 AYGMAEATlavSFSPCGAglvvdevdadllaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1840 GDGLARGYfgrpeLTKEKFVPNPFTPGerMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEA 1919
Cdd:PRK07768 393 GESVTPGY-----LTMDGFIPAQDADG--WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1920 -AVIVRTGPSGHKELLAymsLQAEMN----IEKVRSLLSQqlpgfmIPA-------------HLVELAALPLTQNGKLDR 1981
Cdd:PRK07768 466 nAVAVRLDAGHSREGFA---VAVESNafedPAEVRRIRHQ------VAHevvaevgvrprnvVVLGPGSIPKTPSGKLRR 536
|
..
gi 2040046167 1982 RA 1983
Cdd:PRK07768 537 AN 538
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
605-957 |
1.36e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.92 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 605 SLAYVIYTSGSTGTPKGV------------AVEHRQA----------AAFLSGMQ---RQFpLTEDDVIVLKSSFSFDAS 659
Cdd:PRK07824 36 DVALVVATSGTTGTPKGAmltaaaltasadATHDRLGgpgqwllalpAHHIAGLQvlvRSV-IAGSEPVELDVSAGFDPT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 660 iwqlfwwMIPGASmyllpqgwekdpALMTEAFTNEGVTTAHFIPAMansfldqvemETEEKRTSLAkTLKRVFAGGEALA 739
Cdd:PRK07824 115 -------ALPRAV------------AELGGGRRYTSLVPMQLAKAL----------DDPAATAALA-ELDAVLVGGGPAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 740 PQTAARfARSLPETaVIHGYGPTEAtvdAAFFRYDhekdrermrlpiGKPVPGARLYILDsekavqpigvaGELYIAGAG 819
Cdd:PRK07824 165 APVLDA-AAAAGIN-VVRTYGMSET---SGGCVYD------------GVPLDGVRVRVED-----------GRIALGGPT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 820 VARGYLNRPElteerflDDPFYRgERMYQTGDLARwLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVV 899
Cdd:PRK07824 217 LAKGYRNPVD-------PDPFAE-PGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 900 ARTE---GEEteLYAYIEGQDQKTA-----RTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK07824 288 GLPDdrlGQR--VVAAVVGDGGPAPtlealRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
489-935 |
2.03e-11 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 68.99 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGARLLVTgp 568
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 569 glsvsgfsgETLEVNLSSLRTEPaenePVCAHTDGGSLAYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDV- 647
Cdd:cd05939 82 ---------NLLDPLLTQSSTEP----PSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 648 -------------------------IVLKSSFSfdASiwqLFWwmipgasmyllpqgweKDPAlmteaftNEGVTTAHFI 702
Cdd:cd05939 149 ydclplyhsaggimgvgqallhgstVVIRKKFS--AS---NFW----------------DDCV-------KYNCTIVQYI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 703 PAMANSFLDQVEMETEEKRtslaktlkRV-FAGGEALAPQTAARFARSLPETAVIHGYGPTEAT---------VDAAFF- 771
Cdd:cd05939 201 GEICRYLLAQPPSEEEQKH--------NVrLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNsslvnidnhVGACGFn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 772 -RYDH--------EKDRERMRLpigkpvpgarlyILDSEKAVQPI--GVAGELY---IAGAGVAR--GYLNRPElTEERF 835
Cdd:cd05939 273 sRILPsvypirliKVDEDTGEL------------IRDSDGLCIPCqpGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 836 LDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAV----VARTEGEE--TEL 909
Cdd:cd05939 340 ARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPGVEGRAgmAAI 419
|
490 500
....*....|....*....|....*.
gi 2040046167 910 YAYIEGQDQKTARTELGKRLPAYMMP 935
Cdd:cd05939 420 VDPERKVDLDRFSAVLAKSLPPYARP 445
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1639-1910 |
2.34e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 69.38 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQRGVVRLV------------KNSDMAFSPEDRIL-LTA---------SLGF-DAMTF 1695
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVagvmtvvpklgkNDVYLAYLPLAHILeLAAesvmaavgaAIGYgSPLTL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1696 ---------------EVFGPLLNGACLYIsdketyLDSDR---LKTFIQQNGittlwLTSSLFN-----QLSEQN----- 1747
Cdd:PLN02387 329 tdtsnkikkgtkgdaSALKPTLMTAVPAI------LDRVRdgvRKKVDAKGG-----LAKKLFDiaykrRLAAIEgswfg 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1748 ----ERTFSDL-----SRLILGGE---------ALSPNhVNRVRNTAPDLALWNGYGPTEN---TTFStcfriehEYKhS 1806
Cdd:PLN02387 398 awglEKLLWDAlvfkkIRAVLGGRirfmlsggaPLSGD-TQRFINICLGAPIGQGYGLTETcagATFS-------EWD-D 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1807 IPIGR---PIANSTAYIVN--SRGRL---QPMGViGELCVGGDGLARGYFGRPELTKEKFVPNpfTPGERMYRTGDLARW 1878
Cdd:PLN02387 469 TSVGRvgpPLPCCYVKLVSweEGGYLisdKPMPR-GEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQF 545
|
330 340 350
....*....|....*....|....*....|...
gi 2040046167 1879 LKDGTIDYIGRMDDQVKIR-GYRIELGEIEAAL 1910
Cdd:PLN02387 546 HPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1635-1902 |
2.60e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 69.36 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1635 QQGGPDSLAYIMYTSGSTGTPKGVMVEQR----GVVRLVKNSDMA-FSPE------------DRILLTASLgFDAMTFEV 1697
Cdd:PTZ00342 299 QNEDPDFITSIVYTSGTSGKPKGVMLSNKnlynTVVPLCKHSIFKkYNPKthlsylpishiyERVIAYLSF-MLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1698 FGPLLN--GACLYISDKETYLDSDRLKTFIQQNGITTL--------WLTSSLFNQLSEQNERTFS--------------- 1752
Cdd:PTZ00342 378 WSKDINyfSKDIYNSKGNILAGVPKVFNRIYTNIMTEInnlpplkrFLVKKILSLRKSNNNGGFSkflegithisskikd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1753 ----DLSRLILGGEALSPNhVNRVRNTAPDLALWNGYGPTENTtfSTCFRIEHEYKHSIPIGRPIANSTAYIVNSRGRLQ 1828
Cdd:PTZ00342 458 kvnpNLEVILNGGGKLSPK-IAEELSVLLNVNYYQGYGLTETT--GPIFVQHADDNNTESIGGPISPNTKYKVRTWETYK 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2040046167 1829 PMGVI--GELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermYRTGDLARWLKDGTIDYIGRMDDQVKI-RGYRIE 1902
Cdd:PTZ00342 535 ATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1513-1978 |
2.94e-11 |
|
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: 68.84 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1513 KTPHAPAVIY-----DRQTLTYRELNQRANRIAAALRANGVG------------SESVVALL---------TSRTPELAV 1566
Cdd:cd05943 80 ADADDPAAIYaaedgERTEVTWAELRRRVARLAAALRALGVKpgdrvagylpniPEAVVAMLatasigaiwSSCSPDFGV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1567 -GILG--------ILKA------GGAYLPVTEDMPTERLEwmLSDSNAVMLLQSDRLESHM----AGKRLFIEDIQleAG 1627
Cdd:cd05943 160 pGVLDrfgqiepkVLFAvdaytyNGKRHDVREKVAELVKG--LPSLLAVVVVPYTVAAGQPdlskIAKALTLEDFL--AT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1628 ISANNPE-QQGGPDSLAYIMYTSGSTGTPKGVMVEQRGVV-----RLVKNSDMafSPEDRILLTASLGFDAMTFEVFGpL 1701
Cdd:cd05943 236 GAAGELEfEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLlqhlkEHILHCDL--RPGDRLFYYTTCGWMMWNWLVSG-L 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1702 LNGACLYISD-KETYLDSDRLKTFIQQNGITTLWLTSSLFNQLSE--QNERTFSDLS--RLILG-GEALSPNHVNRV-RN 1774
Cdd:cd05943 313 AVGATIVLYDgSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKagLKPAETHDLSslRTILStGSPLKPESFDYVyDH 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1775 TAPDLALWNGYGPTEnttFSTCFRIEHEykhSIPIGR-----PIANSTAYIVNSRGRLQPmGVIGEL-CVGG-DGLARGY 1847
Cdd:cd05943 393 IKPDVLLASISGGTD---IISCFVGGNP---LLPVYRgeiqcRGLGMAVEAFDEEGKPVW-GEKGELvCTKPfPSMPVGF 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1848 FGRPELTK------EKFvpnpftPGerMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAV 1921
Cdd:cd05943 466 WNDPDGSRyraayfAKY------PG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLV 537
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 1922 IVRTGPSGHKELLAYMSLQAEMNI-----EKVRSLLSQQLPGFMIPAHLVELAALPLTQNGK 1978
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELddelrKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1644-1984 |
4.09e-11 |
|
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: 68.17 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1644 YIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMA-----FSPEDRILLTASLGFDAMTFEVFGPLLNGACLYIS---DKETY 1715
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAalgfgPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMekfDPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1716 LDsdrlktFIQQNGITTLWLTSSLFNQL-----SEQNERTFSDLSRLILGGEALSPNhvnrVRNTAPDL---ALWNGYGP 1787
Cdd:cd05929 209 LR------LIERYRVTFAQFVPTMFVRLlklpeAVRNAYDLSSLKRVIHAAAPCPPW----VKEQWIDWggpIIWEYYGG 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1788 TENTTFsTCFRIEHEYKHSIPIGRPIAnSTAYIVNSRGRLQPMGVIGEL-CVGGDGLArgYFGRPELTKEKFvpnpftpG 1866
Cdd:cd05929 279 TEGQGL-TIINGEEWLTHPGSVGRAVL-GKVHILDEDGNEVPPGEIGEVyFANGPGFE--YTNDPEKTAAAR-------N 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1867 ERMYRT-GDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAV--------------IVRTGPSG-H 1930
Cdd:cd05929 348 EGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvgvpdeelgqrvhaVVQPAPGAdA 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1931 KELLAymslqaemniEKVRSLLSQQLPGFMIPaHLVEL-AALPLTQNGKLDRRAL 1984
Cdd:cd05929 428 GTALA----------EELIAFLRDRLSRYKCP-RSIEFvAELPRDDTGKLYRRLL 471
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
602-957 |
4.71e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 68.24 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 602 DGGSLAYVIYTSGSTGTPKGVAVEHRQAA--AFLSGMQRQFPLTEDDViVLKSSFSFDASIWQLFwWMIPGASMYLLPQG 679
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSNVlhALMANNGDALGTSAADT-MLPVVPLFHANSWGIA-FSAPSMGTKLVMPG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 680 WEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQveMETEEKRTSlakTLKRVFAGGEAlAPQTAARfARSLPETAVIHGY 759
Cdd:PRK06018 253 AKLDGASVYELLDTEKVTFTAGVPTVWLMLLQY--MEKEGLKLP---HLKMVVCGGSA-MPRSMIK-AFEDMGVEVRHAW 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 760 GPTE----ATVDAAFFRYDHEKDRERM--RLPIGKPVPGARLYILDSEKAVQPI-GVA-GELYIAGAGVARGYLNrpelT 831
Cdd:PRK06018 326 GMTEmsplGTLAALKPPFSKLPGDARLdvLQKQGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYR----V 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 832 EERFLDDpfyrgERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVA--RTEGEETEL 909
Cdd:PRK06018 402 DGEILDD-----DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGvyHPKWDERPL 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 910 YAYIEGQDQKTARTEL-----GKrLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK06018 477 LIVQLKPGETATREEIlkymdGK-IAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
2083-2287 |
7.84e-11 |
|
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: 66.90 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2083 EVPWTPVQR--WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQFNRGIHGELYSL 2160
Cdd:cd19538 1 EIPLSFAQRrlWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2161 NIRDLSKTAQwEKLIEDEVadlQRSIHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQ 2239
Cdd:cd19538 81 EIKEVDEEEL-ESEINEAV---RYPFDLSEEPPFRATLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 2240 PVQLPRKTDSYQYFA----NRLAEYAESSKVIREQ-SYWrtveKEKAALLPCE 2287
Cdd:cd19538 157 APELAPLPVQYADYAlwqqELLGDESDPDSLIARQlAYW----KKQLAGLPDE 205
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1502-1986 |
8.81e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 67.04 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1502 TISRLFEYqaAKTPHAPAVIYDRQT------LTYRELNQRANRIAAALRANGVGSESVVALLT---SRTPELAVGILGIl 1572
Cdd:PRK07008 11 LISSLIAH--AARHAGDTEIVSRRVegdihrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSGS- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1573 kagGAYL-PVTEDMPTERLEWMLSDSN-AVMLLQS------DRLESHMAGKRLFI----------EDIQL---EAGISAN 1631
Cdd:PRK07008 88 ---GAVChTINPRLFPEQIAYIVNHAEdRYVLFDLtflplvDALAPQCPNVKGWVamtdaahlpaGSTPLlcyETLVGAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1632 NP--------EQQGgpdslAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSD----MAFSPEDRIL--------------LT 1685
Cdd:PRK07008 165 DGdydwprfdENQA-----SSLCYTSGTTGNPKGALYSHRSTVLHAYGAAlpdaMGLSARDAVLpvvpmfhvnawglpYS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1686 ASLGFDAMTFEvfGPLLNGACLYisdkeTYLDSDRLkTFiqQNGITTLWLtsSLFNQLSEQNERtFSDLSRLILGGEALS 1765
Cdd:PRK07008 240 APLTGAKLVLP--GPDLDGKSLY-----ELIEAERV-TF--SAGVPTVWL--GLLNHMREAGLR-FSTLRRTVIGGSACP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1766 PNHVNRVRNtAPDLALWNGYGPTENTTFSTCFRIEheYKHS-IPI----------GRPIANSTAYIVNSRGRLQPM-GV- 1832
Cdd:PRK07008 307 PAMIRTFED-EYGVEVIHAWGMTEMSPLGTLCKLK--WKHSqLPLdeqrkllekqGRVIYGVDMKIVGDDGRELPWdGKa 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1833 IGELCVGGDGLARGYFGRPEltkekfvpNPFTPGerMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQ 1912
Cdd:PRK07008 384 FGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 1913 IDGVKEAAVIVRTGPS-GHKELLAYMSLQ-AEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK07008 454 HPAVAEAACIACAHPKwDERPLLVVVKRPgAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1498-1984 |
8.93e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 67.01 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1498 PKHETISRLFEYQAAKtpHAPAVIYDRQTLTYRELNQRANRIAAALRAN-GVGSESVVALLTSRTPELAVgilgILKAG- 1575
Cdd:PRK07867 2 SSAPTVAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSL----LLGAAa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1576 -GAYLPVTEDmPTERLEWMLSD---SNAVMLL----QSDRLESHMAGKRLFIEDIQLEAGISANNPEQQ-----GGPDSL 1642
Cdd:PRK07867 76 lSGIVPVGLN-PTRRGAALARDiahADCQLVLtesaHAELLDGLDPGVRVINVDSPAWADELAAHRDAEppfrvADPDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1643 AYIMYTSGSTGTPKGVMVEQRGVVrlVKNSDMA----FSPEDRILLTASLGFDAMTFEVFGP-LLNGACLYISDK---ET 1714
Cdd:PRK07867 155 FMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAqrfgLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIALRRKfsaSG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1715 YLDSdrlktfIQQNGITTL-WLTSSLFNQLSEQNERTFSDLS-RLILGGEAlspnhvnrvrnTAPDLA---------LWN 1783
Cdd:PRK07867 233 FLPD------VRRYGATYAnYVGKPLSYVLATPERPDDADNPlRIVYGNEG-----------APGDIArfarrfgcvVVD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1784 GYGPTENTtfstcfrIEHEYKHSIP---IGRPIANSTAY-----------IVNSRGRLQPMGVIGELC-VGGDGLARGYF 1848
Cdd:PRK07867 296 GFGSTEGG-------VAITRTPDTPpgaLGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1849 GRPELTKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPS 1928
Cdd:PRK07867 369 NDPEADAERMR-------GGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPV 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1929 GHKELLAYMSLQ--AEMNIEKVRSLLSQQ--LPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK07867 442 VGDQVMAALVLApgAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1500-1984 |
9.00e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 67.36 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1500 HETISRLFEYQAakTPHAPAVIYDRQTLTYRE-LNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGilkAGGAY 1578
Cdd:PRK13388 2 RDTIAQLLRDRA--GDDTIAVRYGDRTWTWREvLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAA---AALGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1579 LPVTEDMPTERLEWMLSD----------SNAVMLLQSDRLEshMAGKRLFIED----IQLEAGISANNPEQQGGPDSLAY 1644
Cdd:PRK13388 77 YVLVGLNTTRRGAALAADirradcqllvTDAEHRPLLDGLD--LPGVRVLDVDtpayAELVAAAGALTPHREVDAMDPFM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1645 IMYTSGSTGTPKGVMVEQRGVVRLvknsdmAFSPEDRILLTAS-LGFDAM-------TFEVFGPLL-NGACLYISDKET- 1714
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFA------GRALTERFGLTRDdVCYVSMplfhsnaVMAGWAPAVaSGAAVALPAKFSa 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1715 --YLDSDRL--KTFIQQNGITTLWLTSSlfnqlSEQNERTFSDLsRLILGGEAlSPNHVNRVRNTApDLALWNGYGPTEN 1790
Cdd:PRK13388 229 sgFLDDVRRygATYFNYVGKPLAYILAT-----PERPDDADNPL-RVAFGNEA-SPRDIAEFSRRF-GCQVEDGYGSSEG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1791 TTFSTcfRIEHEYKHSIpiGRP-----IANSTAYIVNSRGRLQPMG-------VIGELC-VGGDGLARGYFGRPELTKEK 1857
Cdd:PRK13388 301 AVIVV--REPGTPPGSI--GRGapgvaIYNPETLTECAVARFDAHGallnadeAIGELVnTAGAGFFEGYYNNPEATAER 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1858 FvpnpftpgeR--MYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLA 1935
Cdd:PRK13388 377 M---------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMA 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1936 YMSLQAE--MNIEKVRSLLSQQ--LPGFMIPAHLVELAALPLTQNGKLDRRAL 1984
Cdd:PRK13388 448 ALVLRDGatFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1639-1921 |
1.07e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 67.35 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQR-------GVVRLVKNSDMAFSPEDRILLTASLG--FDAMTFEVFgpLLNGAC--- 1706
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNEsivtliaGVIRLLKSANAALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAigf 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1707 ------LYISD----KETYLDS-----DRLKTFIQQN----GITTLWLTSSLF-----NQLSEQNERTFSDLS------- 1755
Cdd:PLN02614 300 wrgdvkLLIEDlgelKPTIFCAvprvlDRVYSGLQKKlsdgGFLKKFVFDSAFsykfgNMKKGQSHVEASPLCdklvfnk 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1756 ---------RLILGGEALSPNHVNRVRNTAPDLALWNGYGPTENT--TFSTcfrIEHEYKHSIPIGRPIANstayiVNSR 1824
Cdd:PLN02614 380 vkqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCagTFVS---LPDELDMLGTVGPPVPN-----VDIR 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1825 GRLQP------MGVI--GELCVGGDGLARGYFGRPELTKEKFVpnpftpgERMYRTGDLARWLKDGTIDYIGRMDDQVKI 1896
Cdd:PLN02614 452 LESVPemeydaLASTprGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
|
330 340
....*....|....*....|....*.
gi 2040046167 1897 -RGYRIELGEIEAALRQIDGVKEAAV 1921
Cdd:PLN02614 525 sQGEYVAVENIENIYGEVQAVDSVWV 550
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1822-1986 |
1.29e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 66.56 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1822 NSRGRLQP-------MGVIGELCVGGDGLARGYFgrPEltkekFVPNPftpgeRMYRTGDLARWLKDGTIDYIGRMDDQV 1894
Cdd:PRK07445 283 NSSGQVLPhaqitipANQTGNITIQAQSLALGYY--PQ-----ILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1895 KIRGYRIELGEIEAALRQIDGVKEAAVIvrtG-PSGH-KELLA--YMSLQAEMNIEKVRSLLSQQLPGFMIPAHLVELAA 1970
Cdd:PRK07445 351 ITGGENVYPAEVEAAILATGLVQDVCVL---GlPDPHwGEVVTaiYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQ 427
|
170
....*....|....*.
gi 2040046167 1971 LPLTQNGKLDRRALPE 1986
Cdd:PRK07445 428 LPRNPQGKINRQQLQQ 443
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1528-1986 |
1.49e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.31 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1528 TYRELNQRANRIAAALRANGVGSESVVALL---TSRTPELAVGILGIlkaGGAYLPVTEDMPTERLEW---------MLS 1595
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWiinhaedrvVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1596 DSNAVMLLQ--SDRLES-----------HMAGKRLfIEDIQLEAGISANNPEQQGG---PDSLAYIMYTSGSTGTPKGVM 1659
Cdd:PRK06018 118 DLTFVPILEkiADKLPSveryvvltdaaHMPQTTL-KNAVAYEEWIAEADGDFAWKtfdENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1660 VEQRGVV---RLVKNSD-MAFSPEDRILLTASLgFDAMTFEVF-------------GPLLNGACLYisdkeTYLDSDRLk 1722
Cdd:PRK06018 197 YSHRSNVlhaLMANNGDaLGTSAADTMLPVVPL-FHANSWGIAfsapsmgtklvmpGAKLDGASVY-----ELLDTEKV- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1723 TFIQqnGITTLWLtssLFNQLSEQNERTFSDLSRLILGGEALsPNHVNRVRNTApDLALWNGYGPTENTTFSTCFRIEHE 1802
Cdd:PRK06018 270 TFTA--GVPTVWL---MLLQYMEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDM-GVEVRHAWGMTEMSPLGTLAALKPP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1803 Y---------KHSIPIGRPIANSTAYIVNSRGRLQPMG--VIGELCVGGDGLARGYF--GRPELTKEKFvpnpftpgerm 1869
Cdd:PRK06018 343 FsklpgdarlDVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYrvDGEILDDDGF----------- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1870 YRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQAEMNI--EK 1947
Cdd:PRK06018 412 FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETAtrEE 491
|
490 500 510
....*....|....*....|....*....|....*....
gi 2040046167 1948 VRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDRRALPE 1986
Cdd:PRK06018 492 ILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1527-1983 |
2.81e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 65.91 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1527 LTYRELNQRANRIAAALRAngVGS-ESVVALLTSRTPELAVGILGILKAGGAYLPVTE-DMP--TERLEWMLSDSNAVML 1602
Cdd:PRK07769 56 LTWSQFGARNRAVGARLQQ--VTKpGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDpAEPghVGRLHAVLDDCTPSAI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1603 LQSDrleSHMAGKRLFIED--------------IQLEAGISANNPEQQggPDSLAYIMYTSGSTGTPKGV---------- 1658
Cdd:PRK07769 134 LTTT---DSAEGVRKFFRArpakerprviavdaVPDEVGATWVPPEAN--EDTIAYLQYTSGSTRIPAGVqithlnlptn 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1659 ---MVE-------QRGVVRLVKNSDMAfspedriLLTAslgfdamtfeVFGPLLNGACLYISDKetyldsdrlkTFIQQN 1728
Cdd:PRK07769 209 vlqVIDalegqegDRGVSWLPFFHDMG-------LITV----------LLPALLGHYITFMSPA----------AFVRRP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1729 GittLWLtsslfNQLSEQNE---RTFS-----------------------DLSR---LILGGEALSPNHVNRVrNTA--- 1776
Cdd:PRK07769 262 G---RWI-----RELARKPGgtgGTFSaapnfafehaaarglpkdgepplDLSNvkgLLNGSEPVSPASMRKF-NEAfap 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1777 ---PDLALWNGYGPTENTTFSTCFRIEHEYK----------------------HSIP---IGRPIANSTAYIVNSR-GRL 1827
Cdd:PRK07769 333 yglPPTAIKPSYGMAEATLFVSTTPMDEEPTviyvdrdelnagrfvevpadapNAVAqvsAGKVGVSEWAVIVDPEtASE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1828 QPMGVIGELCVGGDGLARGYFGRPELTKEKF---VPNPFTP--------GERMYRTGDLARWLkDGTIdYI-GRMDDQVK 1895
Cdd:PRK07769 413 LPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEshaegapdDALWVRTGDYGVYF-DGEL-YItGRVKDLVI 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1896 IRGYR-----IELGEIEA--ALR------------QI----------------DGVKEAAVIV-RTGPSGHKellaymsL 1939
Cdd:PRK07769 491 IDGRNhypqdLEYTAQEAtkALRtgyvaafsvpanQLpqvvfddshaglkfdpEDTSEQLVIVaERAPGAHK-------L 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2040046167 1940 QAEMNIEKVRSLLSQQlPGFMI-PAHLVELAALPLTQNGKLDRRA 1983
Cdd:PRK07769 564 DPQPIADDIRAAIAVR-HGVTVrDVLLVPAGSIPRTSSGKIARRA 607
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
489-979 |
4.17e-10 |
|
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: 65.03 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAG-------GAYVPldpdyPEERLRymLADSGA 561
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA-----KELASR--IDDAKP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 562 RLLVTG-----PG------------LSVSGFSGE-TLEVNLSSLRTEP-------------AENEPV-CAHTDGGSLAYV 609
Cdd:cd05967 156 KLIVTAscgiePGkvvpykplldkaLELSGHKPHhVLVLNRPQVPADLtkpgrdldwsellAKAEPVdCVPVAATDPLYI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 610 IYTSGSTGTPKGVAvehR----QAAAFLSGMQRQFPLTEDDVivlkssfsfdasiwqlfWW------------------M 667
Cdd:cd05967 236 LYTSGTTGKPKGVV---RdnggHAVALNWSMRNIYGIKPGDV-----------------WWaasdvgwvvghsyivygpL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 668 IPGASMYL---LPQGWeKDPALMTEAFTNEGVTtAHFIPAMANSFLDQVEMETEEKRTSLAKTLKRVFAGGEALAPQTAA 744
Cdd:cd05967 296 LHGATTVLyegKPVGT-PDPGAFWRVIEKYQVN-ALFTAPTAIRAIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 745 rFARSLPETAVIHGYGPTE---ATVDAAFFRYDHekdrermrlPI-----GKPVPGARLYILDSEKAVQPIGVAGELYIA 816
Cdd:cd05967 374 -WAENTLGVPVIDHWWQTEtgwPITANPVGLEPL---------PIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 817 GAgVARGYLNRPELTEERFLDDPF--YRGerMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVR 894
Cdd:cd05967 444 LP-LPPGCLLTLWKNDERFKKLYLskFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVA 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 895 EAAVVA---RTEGEETELYAYIEGQDQKTA---RTELGK----RLPAYMMPSSFIEMREWPVTPSGKLDRKALPApdgAA 964
Cdd:cd05967 521 ECAVVGvrdELKGQVPLGLVVLKEGVKITAeelEKELVAlvreQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK---IA 597
|
570
....*....|....*
gi 2040046167 965 ERRVYTAPRTITEMK 979
Cdd:cd05967 598 DGEDYTIPSTIEDPS 612
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
979-1037 |
5.04e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 57.19 E-value: 5.04e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 979 KLAKLWEEVLKYGPA--GTRDHFFEQGGHSLKATALVSRIAKAFGVQVPLKEIFAKPTLEE 1037
Cdd:pfam00550 2 RLRELLAEVLGVPAEeiDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1511-1664 |
5.54e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 64.58 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1511 AAKTPHAPAVIYDRQTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGaylpVTEDMPTeRL 1590
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA----VLNTLNT-RL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1591 E-----WMLSDSNAVMLLqSDRLESHMAGKRL----------------------FIEDIQLEAGISANNPEQQGGP---- 1639
Cdd:PRK08162 103 DaasiaFMLRHGEAKVLI-VDTEFAEVAREALallpgpkplvidvddpeypggrFIGALDYEAFLASGDPDFAWTLpade 181
|
170 180
....*....|....*....|....*.
gi 2040046167 1640 -DSLAyIMYTSGSTGTPKGVMVEQRG 1664
Cdd:PRK08162 182 wDAIA-LNYTSGTTGNPKGVVYHHRG 206
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
787-967 |
6.05e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.25 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 787 GKPVPGARLYILDSEkavqpigvAGELYIAGAGVARGYLnrPELTEERflddpfyrgeRMYQTGDLARWLPDGTVEWLGR 866
Cdd:PRK07445 286 GQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQILDSQ----------GIFETDDLGYLDAQGYLHILGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 867 MDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTEGEETELYA--YIEGQDQKTA---RTELGKRLPAYMMPSSFIEM 941
Cdd:PRK07445 346 NSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTaiYVPKDPSISLeelKTAIKDQLSPFKQPKHWIPV 425
|
170 180
....*....|....*....|....*.
gi 2040046167 942 REWPVTPSGKLDRKALpaPDGAAERR 967
Cdd:PRK07445 426 PQLPRNPQGKINRQQL--QQIAVQRL 449
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
484-935 |
7.20e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 63.99 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 484 FSGGILTYRELDQYTNQLAIRLKK-KGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSGAR 562
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 563 LLVTgpglsvsgfsgetlevnlsslrtepaenepvcahtDGGSLAYVIYTSGSTGTPKGVAVEHRQ---AAAFLS-GMQR 638
Cdd:cd05937 81 FVIV-----------------------------------DPDDPAILIYTSGTTGLPKAAAISWRRtlvTSNLLShDLNL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 639 QFPLTEDDVIVLkssFSFDASIWQLFWWMIPGASMYLLP-----QGWekDPALMTEAftnegvTTAHFIPAMANsFLDQV 713
Cdd:cd05937 126 KNGDRTYTCMPL---YHGTAAFLGACNCLMSGGTLALSRkfsasQFW--KDVRDSGA------TIIQYVGELCR-YLLST 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 714 EMETEEKRTSLaktlkRVfAGGEALAPQTAARFaRSLPETAVIHG-YGPTEATV-------------------------- 766
Cdd:cd05937 194 PPSPYDRDHKV-----RV-AWGNGLRPDIWERF-RERFNVPEIGEfYAATEGVFaltnhnvgdfgagaighhglirrwkf 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 767 --DAAFFRYDHEKDRERM--------RLPIGKPvpGARLYildsekAVQPIGVAGelyiagagvARGYLNRPELTEERFL 836
Cdd:cd05937 267 enQVVLVKMDPETDDPIRdpktgfcvRAPVGEP--GEMLG------RVPFKNREA---------FQGYLHNEDATESKLV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 837 DDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVART----EGEETelYAY 912
Cdd:cd05937 330 RDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDGRAG--CAA 407
|
490 500 510
....*....|....*....|....*....|..
gi 2040046167 913 IEGQDQKTARTELG---------KRLPAYMMP 935
Cdd:cd05937 408 ITLEESSAVPTEFTksllaslarKNLPSYAVP 439
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
12-324 |
7.53e-10 |
|
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: 64.04 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 12 PLSFMQEGMLFHSLLDQESRAYFEQASFTINGSLDTERFQKSLDALIERYDIFRTAFIhKNVAKPRQVVLKERQSRLQFV 91
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFP-GDGGDVHQRILDADAARPELP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 92 DISHLDETAKETFVDQFEHDdkkkgFDLQTDPLMRVSILKRAHEQYHCIWSHHHILMDGWCFGIVMKEFLAIYKALGKEQ 171
Cdd:cd19546 85 VVPATEEELPALLADRAAHL-----FDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 172 LPDFEPVH-PFSKYIKWLMR--QDRKEAE-------AFWKTRLIDVKQTASLPKTSSSS---KGKLEQMAFTLSKEQTEG 238
Cdd:cd19546 160 APERAPLPlQFADYALWEREllAGEDDRDsligdqiAYWRDALAGAPDELELPTDRPRPvlpSRRAGAVPLRLDAEVHAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 239 LRKLALQAGATLNTVFQALWGIILQKINRCDDAVFGSVISgRPSDLEDVEKMVGLFINTIPVRVK-SGPESFLTLVSHLQ 317
Cdd:cd19546 240 LMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDlSGDPTFRELLGRVR 318
|
....*..
gi 2040046167 318 QESLKAE 324
Cdd:cd19546 319 EAVREAR 325
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1639-1980 |
9.34e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 64.60 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQRGvvrLVKN-----SDMAFSPEDRIlltaslgFDAM-TFEVFG-------PLLNGA 1705
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRN---LLANraqvaARIDFSPEDKV-------FNALpVFHSFGltgglvlPLLSGV 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1706 CLYIsdketY---LDSDRLKTFIQQNGITTLWLTSSLFNQLSeqneRT-----FSDLSRLILGGEALSPnhvnRVRNTAP 1777
Cdd:PRK06814 862 KVFL-----YpspLHYRIIPELIYDTNATILFGTDTFLNGYA----RYahpydFRSLRYVFAGAEKVKE----ETRQTWM 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1778 D---LALWNGYGPTENTTFstcfrieheykhsIPIGRPIANStayiVNSRGRLQP-------------MGviGELCVGGD 1841
Cdd:PRK06814 929 EkfgIRILEGYGVTETAPV-------------IALNTPMHNK----AGTVGRLLPgieyrlepvpgidEG--GRLFVRGP 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1842 GLARGYFgRPEltkekfvpNPFT---PGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQID-GVK 1917
Cdd:PRK06814 990 NVMLGYL-RAE--------NPGVlepPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWpDAL 1060
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1918 EAAVIVRTGPSGHKELLAYMSLQAEMNiEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGKLD 1980
Cdd:PRK06814 1061 HAAVSIPDARKGERIILLTTASDATRA-AFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
2085-2309 |
2.15e-09 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 62.39 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2085 PWTPVQR--WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRM-TIIDDGGQLQQFNrgihgELYSLN 2161
Cdd:cd19533 3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLrFTEEEGEPYQWID-----PYTPVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2162 IR--DLSKTAQWEKLIEDEV-ADLQRSIHLQTGPLLKAGLFNTMSGT-YLFLTIHHLVVDGVSWRILLEDLSAAYSQAAA 2237
Cdd:cd19533 78 IRhiDLSGDPDPEGAAQQWMqEDLRKPLPLDNDPLFRHALFTLGDNRhFWYQRVHHIVMDGFSFALFGQRVAEIYTALLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2238 GQPVQlPRKTDSYQYFANRLAEYAESSKVIREQSYWRtvekEKAALLPceKPHS--------AADNIRKTESFTLSEEDT 2309
Cdd:cd19533 158 GRPAP-PAPFGSFLDLVEEEQAYRQSERFERDRAFWT----EQFEDLP--EPVSlarrapgrSLAFLRRTAELPPELTRT 230
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
490-866 |
2.66e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 62.73 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 490 TYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPLDPDYPEERLRYMLADSG--------- 560
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEvsivfveek 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 561 --ARLLVTGPGLS-----VSGFSGETLEvnlsslRTEPAENEPVCAHT------------------DGGSLAYVIYTSGS 615
Cdd:PLN02614 161 kiSELFKTCPNSTeymktVVSFGGVSRE------QKEEAETFGLVIYAwdeflklgegkqydlpikKKSDICTIMYTSGT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 616 TGTPKGVAVEHRQAAAFLSGMQRQF-----PLTEDDVIV--LKSSFSFDASIWQLFwwMIPGASMYLlpqgWEKDPALMT 688
Cdd:PLN02614 235 TGDPKGVMISNESIVTLIAGVIRLLksanaALTVKDVYLsyLPLAHIFDRVIEECF--IQHGAAIGF----WRGDVKLLI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 689 EAFTNEGVTTAHFIPAMansfLDQVEMETEEK--------------------------------------------RTSL 724
Cdd:PLN02614 309 EDLGELKPTIFCAVPRV----LDRVYSGLQKKlsdggflkkfvfdsafsykfgnmkkgqshveasplcdklvfnkvKQGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 725 AKTLKRVFAGGEALAPQTAArFARSLPETAVIHGYGPTEATVdAAFFRYDHEKDrerMRLPIGKPVPGARLYiLDSEKAV 804
Cdd:PLN02614 385 GGNVRIILSGAAPLASHVES-FLRVVACCHVLQGYGLTESCA-GTFVSLPDELD---MLGTVGPPVPNVDIR-LESVPEM 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 805 QPIGVA----GELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGR 866
Cdd:PLN02614 459 EYDALAstprGEICIRGKTLFSGYYKREDLTKEVLIDGWLH-------TGDVGEWQPNGSMKIIDR 517
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
843-959 |
2.81e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.98 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 843 GERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVARTE---GEETELyAYI--EGQD 917
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDpvaGERVKA-KVIshEEID 367
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2040046167 918 QKTARTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKALPA 959
Cdd:PRK08308 368 PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
32-329 |
3.88e-09 |
|
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: 61.35 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 32 AYFEqasFTINGsLDTERFQKSLDALIERYDIFRTAFIHKNvakpRQVVLKERQS-RLQFVDISHLDETAKETFV----D 106
Cdd:cd19535 28 AYLE---FDGED-LDPDRLERAWNKLIARHPMLRAVFLDDG----TQQILPEVPWyGITVHDLRGLSEEEAEAALeelrE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 107 QFEH--DDKKKG--FDLQtdplmrVSILKRAHeqyhciwSHHHI-----LMDGWCFGIVMKEFLAIYKALGkEQLPDFEP 177
Cdd:cd19535 100 RLSHrvLDVERGplFDIR------LSLLPEGR-------TRLHLsidllVADALSLQILLRELAALYEDPG-EPLPPLEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 178 vhPFSKYIKW---LMRQDRKEAEAFWKTRLidvkqtASLP---------KTSSSSKGKLEQMAFTLSKEQTEGLRKLALQ 245
Cdd:cd19535 166 --SFRDYLLAeqaLRETAYERARAYWQERL------PTLPpapqlplakDPEEIKEPRFTRREHRLSAEQWQRLKERARQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 246 AGATLNTVFQAlwgiilqkinrcddaVFGSVISG---------------RPSDLEDVEKMVGLFINTIPVRVK-SGPESF 309
Cdd:cd19535 238 HGVTPSMVLLT---------------AYAEVLARwsgqprfllnltlfnRLPLHPDVNDVVGDFTSLLLLEVDgSEGQSF 302
|
330 340
....*....|....*....|
gi 2040046167 310 LTLVSHLQQESLKAEAYSYY 329
Cdd:cd19535 303 LERARRLQQQLWEDLDHSSY 322
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
607-957 |
7.74e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.95 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 607 AYVIYTSGSTGTPKGVAVEHRqaAAFLSGMQRqfpLTEDDVIVLK-SSFSFDASIWQLFWWMIPGASMY----LLPQGWE 681
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHR--SLYLQSLSL---RTTDSLAVTHgESFLCCVPIYHVLSWGVPLAAFMsgtpLVFPGPD 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 682 KDPALMTEAFTNEGVTTAHFIPAMANSFLDQVeMETEEKRTSlaktLKRVFAGGEALAPQT----AARFArslpeTAVIH 757
Cdd:PRK05620 259 LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHY-LKNPPERMS----LQEIYVGGSAVPPILikawEERYG-----VDVVH 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 758 GYGPTEATVDAAFFRYD---HEKDRERMRLPIGKPVPGARLYILDSEKAVQPIGV-AGELYIAGAGVARGYLNRPELTE- 832
Cdd:PRK05620 329 VWGMTETSPVGTVARPPsgvSGEARWAYRVSQGRFPASLEYRIVNDGQVMESTDRnEGEIQVRGNWVTASYYHSPTEEGg 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 833 ---------------ERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAA 897
Cdd:PRK05620 409 gaastfrgedvedanDRFTADGWLR------TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECA 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 898 VVA---RTEGEE----TELYAYIEgQDQKTA---RTELGKRLPAYMMPSSFIEMREWPVTPSGKLDRKAL 957
Cdd:PRK05620 483 VIGypdDKWGERplavTVLAPGIE-PTRETAerlRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1905-1978 |
8.13e-09 |
|
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: 54.47 E-value: 8.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 1905 EIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSL--QAEMNIEKVRSLLSQQLPGFMIPAHLVELAALPLTQNGK 1978
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLkpGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
489-951 |
1.06e-08 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 60.75 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAK-ESVVGVLADrSPEMVIAVLAVLKAGGAYVPLDPDYPE----ERL-----RYMLAD 558
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPgDRVAGYLPN-IPEAVVAMLATASIGAIWSSCSPDFGVpgvlDRFgqiepKVLFAV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 559 SGARL-------------LVTG-PGLS----VSGFSGETLE--------VNLSSLRTEPAENEPVCAHTDGGSLAYVIYT 612
Cdd:cd05943 178 DAYTYngkrhdvrekvaeLVKGlPSLLavvvVPYTVAAGQPdlskiakaLTLEDFLATGAAGELEFEPLPFDHPLYILYS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 613 SGSTGTPK-------GVAVEHRQAAAFlsgmqrQFPLTEDDVIvlkssFSFDASIWQLFWWMIP----GASMYLL--PQG 679
Cdd:cd05943 258 SGTTGLPKcivhgagGTLLQHLKEHIL------HCDLRPGDRL-----FYYTTCGWMMWNWLVSglavGATIVLYdgSPF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 680 WEKDPALMTEAfTNEGVTT----AHFIPAMANSFLDQVEmeteekRTSLAkTLKRVFAGGEALAPQTaarfarslpetav 755
Cdd:cd05943 327 YPDTNALWDLA-DEEGITVfgtsAKYLDALEKAGLKPAE------THDLS-SLRTILSTGSPLKPES------------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 756 ihgygpteatvdaafFRYDHEKDRERMRL-------------------------PIGKPVPGARLYILDsEKAVQPIGVA 810
Cdd:cd05943 386 ---------------FDYVYDHIKPDVLLasisggtdiiscfvggnpllpvyrgEIQCRGLGMAVEAFD-EEGKPVWGEK 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 811 GELYIAGAGVAR--GYLNRPEltEERFLDDPFYRGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALR 888
Cdd:cd05943 450 GELVCTKPFPSMpvGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVE 527
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 889 QIDGVREAAVVART-EGEETELYAYI---EGQD-----QKTARTELGKRLPAYMMPSSFIEMREWPVTPSGK 951
Cdd:cd05943 528 KIPEVEDSLVVGQEwKDGDERVILFVklrEGVElddelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2083-2307 |
1.27e-08 |
|
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: 59.97 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2083 EVPWTPVQR--WFLAQHIEERQHFNQSVMLHSSEGFQEQPLRTALQHLVIHHDALRMTIIDDGGQLQQ-----FNrgihg 2155
Cdd:cd20483 1 PRPMSTFQRrlWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQqvlddPS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2156 elYSLNIRDLSKTAQWEKLIEDEVADLQRS-IHLQTGPLLKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLEDLSAAYS 2233
Cdd:cd20483 76 --FHLIVIDLSEAADPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFaLVLASHHIAWDRGSSKSIFEQFTALYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2234 QAAAGQP---VQLPRktdsYQYfanrlAEYA-------ESSKVIREQSYWRTVEK---EKAALLPCEKPHSAADNI--RK 2298
Cdd:cd20483 154 ALRAGRDlatVPPPP----VQY-----IDFTlwhnallQSPLVQPLLDFWKEKLEgipDASKLLPFAKAERPPVKDyeRS 224
|
....*....
gi 2040046167 2299 TESFTLSEE 2307
Cdd:cd20483 225 TVEATLDKE 233
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1520-1981 |
2.25e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.39 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1520 VIYDRQTLTYR-----ELNQRANRIAAalRANGVGSESVVALLTSRTPELAVGILGILKAGGAY--LPVTEDMPTERlEW 1592
Cdd:PRK05851 20 VVLDRESGLWRrhpwpEVHGRAENVAA--RLLDRDRPGAVGLVGEPTVELVAAIQGAWLAGAAVsiLPGPVRGADDG-RW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1593 ---------------MLSDSNAVMLLQSdrleshmAGKRLFIEDIQLEAGISANNPEQQGGPDSLAYIMYTSGSTGTPKG 1657
Cdd:PRK05851 97 adatltrfagigvrtVLSHGSHLERLRA-------VDSSVTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1658 VMVEQRGVVR----LVKNSDMAfSPEDRILLTASLGFD-AMTFEVFGpLLNGACLYISDKETYLDSD-RLKTFIQQNGIT 1731
Cdd:PRK05851 170 AILSPGAVLSnlrgLNARVGLD-AATDVGCSWLPLYHDmGLAFLLTA-ALAGAPLWLAPTTAFSASPfRWLSWLSDSRAT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1732 TLWLTSSLFNQLSEQNER-TFSDLSRL---ILGGEALSPNHVNR-VRNTAP----DLALWNGYGPTEnttfSTC------ 1796
Cdd:PRK05851 248 LTAAPNFAYNLIGKYARRvSDVDLGALrvaLNGGEPVDCDGFERfATAMAPfgfdAGAAAPSYGLAE----STCavtvpv 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1797 ----FRIEH--------EYKHSIpIGRPIANSTAYIVNSRGRLQPMGV-IGELCVGGDGLARGYFGRPeltkekfvpnPF 1863
Cdd:PRK05851 324 pgigLRVDEvttddgsgARRHAV-LGNPIPGMEVRISPGDGAAGVAGReIGEIEIRGASMMSGYLGQA----------PI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1864 TPGErMYRTGDLArWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI-VRTGPSGHKELLAymsLQAE 1942
Cdd:PRK05851 393 DPDD-WFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVaVGTGEGSARPGLV---IAAE 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2040046167 1943 M---NIEKVRSLLSQQLPGF--MIPAHLVELA--ALPLTQNGKLDR 1981
Cdd:PRK05851 468 FrgpDEAGARSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKLRR 513
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1648-1981 |
2.74e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 58.62 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1648 TSGSTGTPKGVMVEQRGVVRLVKN-----SDMAFSPEDRILLTASLGFD--AMTFEvfgpllNGA----CLYISdkETYL 1716
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELfarslRAAGVRPGDRVQNAFGYGLFtgGLGLH------YGAerlgATVIP--AGGG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1717 DSDRLKTFIQQNGITTLWLTSSLFNQLSEQNER---TFSDLS--RLILGGEALSPNHVNRVRNTApDLALWNGYGPTEnt 1791
Cdd:COG1541 163 NTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEegiDPRDLSlkKGIFGGEPWSEEMRKEIEERW-GIKAYDIYGLTE-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1792 tfstcfrieheykhsipIGRPIANSTAYivnsrgrlQPMGVIGELCVggdglargYfgrPEL----TKEkfvpnPFTPGE 1867
Cdd:COG1541 240 -----------------VGPGVAYECEA--------QDGLHIWEDHF--------L---VEIidpeTGE-----PVPEGE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1868 R------------M----YRTGDLARWLKD----GT----IDYI-GRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVI 1922
Cdd:COG1541 279 EgelvvttltkeaMplirYRTGDLTRLLPEpcpcGRthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQI 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 1923 VRTGPSGHKELLAYMSLQAEMNIEKVRSLLSQQL---PGFMIPAHLVELAALPLTQnGKLDR 1981
Cdd:COG1541 359 VVDREGGLDELTVRVELAPGASLEALAEAIAAALkavLGLRAEVELVEPGSLPRSE-GKAKR 419
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1644-1981 |
3.05e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 59.37 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1644 YIMYTSGSTGTPKGVmVEQRG--VVRLVKN-SDMAFSPEDRILLT-ASLGFDAMTFEVFGPLLNGACLYISD----KETY 1715
Cdd:PTZ00237 258 YILYTSGTTGNSKAV-VRSNGphLVGLKYYwRSIIEKDIPTVVFShSSIGWVSFHGFLYGSLSLGNTFVMFEggiiKNKH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1716 LDSDRLKTfIQQNGITTLWLTSSLFNQLSE-----QNERTFSDLSRL---ILGGEALSPNHVNRVRNTAPDLALwNGYGP 1787
Cdd:PTZ00237 337 IEDDLWNT-IEKHKVTHTLTLPKTIRYLIKtdpeaTIIRSKYDLSNLkeiWCGGEVIEESIPEYIENKLKIKSS-RGYGQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1788 TEnttfSTCFRIeHEYKH-SIPI---GRPIANSTAYIVNSRGRLQPMGVIGELCVG---GDGLARGYFGRPELTKEKFvp 1860
Cdd:PTZ00237 415 TE----IGITYL-YCYGHiNIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLF-- 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1861 NPFtPGerMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSL- 1939
Cdd:PTZ00237 488 SKF-PG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLk 564
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1940 ------QAEMNIEK--VRSLLSQQLPGFMIPAHLVELAALPLTQNGKLDR 1981
Cdd:PTZ00237 565 qdqsnqSIDLNKLKneINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2121-2285 |
3.66e-08 |
|
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: 58.27 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2121 LRTALQHLVIHHDALRMTIIDDGgqLQQFNRGIHgeLYSLNIRDLSKTAQWEklIEDEVADL-QRSIH----LQTGPL-- 2193
Cdd:cd19535 42 LERAWNKLIARHPMLRAVFLDDG--TQQILPEVP--WYGITVHDLRGLSEEE--AEAALEELrERLSHrvldVERGPLfd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2194 LKAGLFNTmSGTYLFLTIHHLVVDGVSWRILLEDLSAAYsqaaAGQPVQLPRKTDSY-QYFANRLAEYAESSKviREQSY 2272
Cdd:cd19535 116 IRLSLLPE-GRTRLHLSIDLLVADALSLQILLRELAALY----EDPGEPLPPLELSFrDYLLAEQALRETAYE--RARAY 188
|
170
....*....|...
gi 2040046167 2273 WRtvekEKAALLP 2285
Cdd:cd19535 189 WQ----ERLPTLP 197
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
2085-2274 |
6.32e-08 |
|
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: 57.69 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2085 PWTPVQRWFLAqhIEERQHfnQSVMLHS----SEGFQEQPLRTALQHLVIHHDALRMTIIDDggqlqqfnrgIHGELYSL 2160
Cdd:cd19545 3 PCTPLQEGLMA--LTARQP--GAYVGQRvfelPPDIDLARLQAAWEQVVQANPILRTRIVQS----------DSGGLLQV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2161 NIRDLSKTAQWEKLIEDEVA-DLQRSIHLqTGPLLKAGLF-NTMSGTYLFLTIHHLVVDGVSWRILLEDLSAAYSQAAAG 2238
Cdd:cd19545 69 VVKESPISWTESTSLDEYLEeDRAAPMGL-GGPLVRLALVeDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVP 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 2040046167 2239 QPVQLPRktdsyqyfANRLAEYAESSKVireQSYWR 2274
Cdd:cd19545 148 QPPPFSR--------FVKYLRQLDDEAA---AEFWR 172
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1634-1991 |
1.12e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 57.41 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1634 EQQggPDSLAYIMYTSGSTGTPKGVM---------VEQrgvVRLVKNsdmaFSPEDRILLTASLgFDA--MTFEVFGPLL 1702
Cdd:PRK08043 361 KQQ--PEDAALILFTSGSEGHPKGVVhshksllanVEQ---IKTIAD----FTPNDRFMSALPL-FHSfgLTVGLFTPLL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1703 NGA--CLYISDketyLDSDRLKTFIQQNGITTLWLTSS-LFNQLSEQNERTFSDLSRLILGGEALSPNhvnrVRNTAPD- 1778
Cdd:PRK08043 431 TGAevFLYPSP----LHYRIVPELVYDRNCTVLFGTSTfLGNYARFANPYDFARLRYVVAGAEKLQES----TKQLWQDk 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1779 --LALWNGYGPTEnttfstCFRIeheykhsIPIGRPIA---NSTAYIV-NSRGRLQPMGVI---GELCVGGDGLARGYFg 1849
Cdd:PRK08043 503 fgLRILEGYGVTE------CAPV-------VSINVPMAakpGTVGRILpGMDARLLSVPGIeqgGRLQLKGPNIMNGYL- 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1850 RPELTKEKFVPNPFTP-GER---MYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRT 1925
Cdd:PRK08043 569 RVEKPGVLEVPTAENArGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKS 648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 1926 GPSgHKELLAYMSLQAEMNiekvRSLLSQQ-----LPGFMIPAHLVELAALPLTQNGKLD----RRALPEPETTA 1991
Cdd:PRK08043 649 DAS-KGEALVLFTTDSELT----REKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPDfvtlKSMVDEPEQHD 718
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1513-1979 |
1.45e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 57.11 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1513 KTPHAPAVIY-----DRQTLTYRELNQRANRIAAALRANGVGS------------ESVVALL---------TSRTPELAV 1566
Cdd:PRK03584 96 RRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgdrvaaylpnipETVVAMLataslgaiwSSCSPDFGV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1567 -GILG--------ILKA------GGAYLPVTEDMpTERLEWMLSDSNAVMLlqsDRLESHMAGKRlfIEDIQLEAGISAN 1631
Cdd:PRK03584 176 qGVLDrfgqiepkVLIAvdgyryGGKAFDRRAKV-AELRAALPSLEHVVVV---PYLGPAAAAAA--LPGALLWEDFLAP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1632 NPEQQGGPDSLA-----YIMYTSGSTGTPK-------GVMVEQRGVVRLvkNSDmaFSPEDRILLTASLGFDAMTFEVFG 1699
Cdd:PRK03584 250 AEAAELEFEPVPfdhplWILYSSGTTGLPKcivhghgGILLEHLKELGL--HCD--LGPGDRFFWYTTCGWMMWNWLVSG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1700 pLLNGACLYISD-KETYLDSDRLKTFIQQNGITTLWlTSSLFNQLSEQNE---RTFSDLSRL-ILG--GEALSPNHVNRV 1772
Cdd:PRK03584 326 -LLVGATLVLYDgSPFYPDPNVLWDLAAEEGVTVFG-TSAKYLDACEKAGlvpGETHDLSALrTIGstGSPLPPEGFDWV 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1773 -RNTAPDLALWNGYGPTEnttFSTCFrieheykhsiPIGRPIanSTAYivnsRGRLQPMG--------------VIGElc 1837
Cdd:PRK03584 404 yEHVKADVWLASISGGTD---ICSCF----------VGGNPL--LPVY----RGEIQCRGlgmaveawdedgrpVVGE-- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1838 VGgdglargyfgrpELTkekfVPNPFtP-----------GER-------MY----RTGDLARWLKDGTIDYIGRMDDQVK 1895
Cdd:PRK03584 463 VG------------ELV----CTKPF-PsmplgfwndpdGSRyrdayfdTFpgvwRHGDWIEITEHGGVVIYGRSDATLN 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1896 IRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSGHKELLAYMSLQ--AEMN---IEKVRSLLSQQL-PGFmIPAHLVELA 1969
Cdd:PRK03584 526 RGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAegVTLDdalRARIRTTIRTNLsPRH-VPDKIIAVP 604
|
570
....*....|
gi 2040046167 1970 ALPLTQNGKL 1979
Cdd:PRK03584 605 DIPRTLSGKK 614
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
607-953 |
1.46e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 57.28 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 607 AYVIYTSGSTGTPKGVAVEHR-------QAAAFLsgmqrqfPLTEDDVI--VLK--SSFSFDASiwqLFWWMIPGASMYL 675
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRnllanraQVAARI-------DFSPEDKVfnALPvfHSFGLTGG---LVLPLLSGVKVFL 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 676 LPQ--GWEKDPALM----------TEAFTNEGVTTAHfipamANSFldqvemeteekrtslaKTLKRVFAGGEALAPQT- 742
Cdd:PRK06814 866 YPSplHYRIIPELIydtnatilfgTDTFLNGYARYAH-----PYDF----------------RSLRYVFAGAEKVKEETr 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 743 ---AARFARSLPEtavihGYGPTE-ATVDA----AFFRYDhekdrermrlPIGKPVPG--ARLyildsEKaVQPIGVAGE 812
Cdd:PRK06814 925 qtwMEKFGIRILE-----GYGVTEtAPVIAlntpMHNKAG----------TVGRLLPGieYRL-----EP-VPGIDEGGR 983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 813 LYIAGAGVARGYL--NRPELTEERflddpfyrGERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQI 890
Cdd:PRK06814 984 LFVRGPNVMLGYLraENPGVLEPP--------ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAEL 1055
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 891 DGVREAAVVAR---TEGEETELYAyiegqDQKTA-RTEL-----GKRLPAYMMPSSFIEMREWPVTPSGKLD 953
Cdd:PRK06814 1056 WPDALHAAVSIpdaRKGERIILLT-----TASDAtRAAFlahakAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
787-913 |
1.48e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 57.07 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 787 GKPVPGARLYILDSEKAVQPIGVAGELYIAGA--GVARGYLNRPElteeRFLDDPFYRGERMYQTGDLARWLPDGTVEWL 864
Cdd:PRK00174 427 TRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWIT 502
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2040046167 865 GRMDGQVKIRGYRIEPGEVEAALRQIDGVREAAVVAR---TEGEetELYAYI 913
Cdd:PRK00174 503 GRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRpddIKGQ--GIYAFV 552
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1982-2065 |
3.06e-07 |
|
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: 50.33 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1982 RALPEPETTAIntayapprnqLEERLAVIWQEVLGV---EKVGIEDSFFELGGDSIKALQVSARLGR-FDLKITAGDLFR 2057
Cdd:smart00823 2 AALPPAERRRL----------LLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAaTGLRLPATLVFD 71
|
....*...
gi 2040046167 2058 HPTIKEAA 2065
Cdd:smart00823 72 HPTPAALA 79
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
882-951 |
7.61e-07 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 48.69 E-value: 7.61e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 882 EVEAALRQIDGVREAAVVARTEGEETE-LYAYI---EGQDQ--KTARTELGKRLPAYMMPSSFIEMREWPVTPSGK 951
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEaPVAFVvlkPGVELleEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
609-873 |
1.02e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 54.44 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 609 VIYTSGSTGTPKGVAVEHRQAAAFLSGMQ---RQF--PLTEDDVIV--LKSSFSFDASIWQLFWWmiPGAS--------- 672
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRGVDlfmEQFedKMTHDDVYLsfLPLAHILDRMIEEYFFR--KGASvgyyhgdln 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 673 ------MYL-------LPQGWEKDPALMTEAFTNEGVTTAHFIPAMANSFLDQVEMETEEKRTS--------------LA 725
Cdd:PLN02430 303 alrddlMELkptllagVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYSHKKASpmadflafrkvkakLG 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 726 KTLKRVFAGGEALAPQTAaRFARSLPETAVIHGYGPTEaTVDAAFFRYdheKDRERMRLPIGKPVPGARLYILD-SEKAV 804
Cdd:PLN02430 383 GRLRLLISGGAPLSTEIE-EFLRVTSCAFVVQGYGLTE-TLGPTTLGF---PDEMCMLGTVGAPAVYNELRLEEvPEMGY 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2040046167 805 QPIGV--AGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGRMDGQVKI 873
Cdd:PLN02430 458 DPLGEppRGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVLKIIDRKKNLIKL 521
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2066-2381 |
1.28e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.58 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2066 PLIRKTERNIDQRP-----IEGEVPWTPVQRWFLAQHIEERQ---HFNQsvMLHSSEGFQEQPLRTALQHLVIHHDALRM 2137
Cdd:PRK12316 4080 PLAGLDQARLDALPlplgeIEDIYPLSPMQQGMLFHSLYEQEagdYINQ--MRVDVQGLDVERFRAAWQAALDRHDVLRS 4157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2138 TIIDDGgQLQQFNRGIHGEL-YSLNIRDLSKTAQWEKLIEDEVA-DLQRSIHLQTGPLLKAGLFNTMSGT-YLFLTIHHL 2214
Cdd:PRK12316 4158 GFVWQG-ELGRPLQVVHKQVsLPFAELDWRGRADLQAALDALAAaERERGFDLQRAPLLRLVLVRTAEGRhHLIYTNHHI 4236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2215 VVDGVSWRILLEDLSAAYSQAAAGQPVQlpRKTDSYQYFANRLAEYAEsskvireqSYWRTvekEKAALlpcEKPHSAAD 2294
Cdd:PRK12316 4237 LMDGWSNSQLLGEVLERYSGRPPAQPGG--RYRDYIAWLQRQDAAASE--------AFWRE---QLAAL---DEPTRLAQ 4300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2295 NIRKTESFTLSEEDTHVlihKVNNAYNTD-----------TQDILLTAASLALCD-WMGERKLRIAMEGHGRDHTLPEld 2362
Cdd:PRK12316 4301 AIARADLRSANGYGEHV---RELDATATArlrefartqrvTLNTLVQAAWLLLLQrYTGQDTVAFGATVAGRPAELPG-- 4375
|
330
....*....|....*....
gi 2040046167 2363 ISRTVGWFTTIYPVLIDLH 2381
Cdd:PRK12316 4376 IEGQIGLFINTLPVIATPR 4394
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
489-866 |
1.65e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 53.69 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 489 LTYRELDQYTNQLAIRLKKKGVAKESVVGVLADRSPEMVIAVLAVLKAGGAYVPL-DP----------DYPEERLRYMLA 557
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLyDTlganavefiiNHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 558 DSGARLLVTGPG------------------------LSVSGFSGEtlevNLSSLRTEPAENEPVCAhtdgGSLAYVIYTS 613
Cdd:PLN02861 158 SKISSILSCLPKcssnlktivsfgdvsseqkeeaeeLGVSCFSWE----EFSLMGSLDCELPPKQK----TDICTIMYTS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 614 GSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIVLKSSFSF------------------DASIWqlFWwmiPGASMYL 675
Cdd:PLN02861 230 GTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEEDSYFSYlplahvydqvietyciskGASIG--FW---QGDIRYL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 676 L--------------PQGWEKDPALMTEAFTNEGVTTAH----------------FIPAMANSFLDQVEMEteEKRTSLA 725
Cdd:PLN02861 305 MedvqalkptifcgvPRVYDRIYTGIMQKISSGGMLRKKlfdfaynyklgnlrkgLKQEEASPRLDRLVFD--KIKEGLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 726 KTLKRVFAGGEALaPQTAARFARSLPETAVIHGYGPTEA-----TVDAAFFRydhekdrerMRLPIGKPVPG--ARLyil 798
Cdd:PLN02861 383 GRVRLLLSGAAPL-PRHVEEFLRVTSCSVLSQGYGLTEScggcfTSIANVFS---------MVGTVGVPMTTieARL--- 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2040046167 799 dseKAVQPIGV-------AGELYIAGAGVARGYLNRPELTEERFLDDPFYrgermyqTGDLARWLPDGTVEWLGR 866
Cdd:PLN02861 450 ---ESVPEMGYdalsdvpRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGEWQPNGAMKIIDR 514
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1525-1962 |
2.83e-06 |
|
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: 52.68 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRAN-GVGSESVVALLTSRTPELAVGILGILKAG--GAYLP--------------------- 1580
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakvlv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1581 --------VTEDMPTERLE----WMLSDsnavmllqsdrlESHMAGKRLFIEDIQLEAG--ISANNPEQQGGPDSLAYIm 1646
Cdd:cd05938 84 vapelqeaVEEVLPALRADgvsvWYLSH------------TSNTEGVISLLDKVDAASDepVPASLRAHVTIKSPALYI- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1647 YTSGSTGTPKGVMVEQRgvvRLVKNSDMAFS----PEDRILLTASL-GFDAMTFEVFGPLLNGACLYISDK--ETYLDSD 1719
Cdd:cd05938 151 YTSGTTGLPKAARISHL---RVLQCSGFLSLcgvtADDVIYITLPLyHSSGFLLGIGGCIELGATCVLKPKfsASQFWDD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1720 RLK---TFIQQNGITTLWLTsslfNQLSEQNERTFSdlSRLILGgEALSPNHVNRVRNTAPDLALWNGYGPTE-NTTF-- 1793
Cdd:cd05938 228 CRKhnvTVIQYIGELLRYLC----NQPQSPNDRDHK--VRLAIG-NGLRADVWREFLRRFGPIRIREFYGSTEgNIGFfn 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1794 -----STCFRIEHEYKHSIPI---------GRPIANSTAYIVNSrgrlqPMGVIGELcvggdgLAR--------GYFGRP 1851
Cdd:cd05938 301 ytgkiGAVGRVSYLYKLLFPFelikfdvekEEPVRDAQGFCIPV-----AKGEPGLL------VAKitqqspflGYAGDK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1852 ELTKEKFVPNPFTPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPsGHK 1931
Cdd:cd05938 370 EQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVP-GHE 448
|
490 500 510
....*....|....*....|....*....|....*
gi 2040046167 1932 ELLAYMSLQ----AEMNIEKVRSLLSQQLPGFMIP 1962
Cdd:cd05938 449 GRIGMAAVKlkpgHEFDGKKLYQHVREYLPAYARP 483
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
607-909 |
2.94e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.51 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 607 AYVIYTSGSTGTPKGVAVEHRQAAAFLSGMQRQFPLTEDDVIV--LKSSFSFDASIWQLFWwMIPGASMYLLPQGWEkdP 684
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMsfLPPFHAYGFNSCTLFP-LLSGVPVVFAYNPLY--P 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 685 ALMTEAFTNEGVTTAHFIPAmansFLDQVeMETEEKRTSLAKTLKRVFAGGEALAPQTAARFARSLPETAVIHGYGPTEA 764
Cdd:PRK06334 263 KKIVEMIDEAKVTFLGSTPV----FFDYI-LKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTEC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 765 TVDAAFFRYDHEKDRErmrlPIGKPVPGARLYILDSEKAVQ-PIGVAGELYIAGAGVARGYLNrpelteerflDDP---F 840
Cdd:PRK06334 338 SPVITINTVNSPKHES----CVGMPIRGMDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLG----------EDFgqgF 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 841 YR--GERMYQTGDLARWLPDGTVEWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVREAA-----VVARTEGEETEL 909
Cdd:PRK06334 404 VElgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADhagplVVCGLPGEKVRL 479
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
728-929 |
3.01e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.46 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 728 LKRVFAGGEALAPQTAARFARSLPETAVIHgYGPTEATVDAAFfrydhE-KDRERMRLPigkpvPGARLY-ILDSE--KA 803
Cdd:COG1541 205 LKKGIFGGEPWSEEMRKEIEERWGIKAYDI-YGLTEVGPGVAY-----EcEAQDGLHIW-----EDHFLVeIIDPEtgEP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 804 VQPiGVAGELYIAGagvargylnrpeLTEERFlddPFYRgermYQTGDLARWLPD----GT-----VEWLGRMDGQVKIR 874
Cdd:COG1541 274 VPE-GEEGELVVTT------------LTKEAM---PLIR----YRTGDLTRLLPEpcpcGRthpriGRILGRADDMLIIR 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2040046167 875 GYRIEPGEVEAALRQIDGVR-EAAVVARTEGEETELYAYIE---GQDQKTARTELGKRL 929
Cdd:COG1541 334 GVNVFPSQIEEVLLRIPEVGpEYQIVVDREGGLDELTVRVElapGASLEALAEAIAAAL 392
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2121-2307 |
4.44e-06 |
|
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: 51.93 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2121 LRTALQHLVIHHDALRMTIIDDGGQLQQFNRgiHGELYSLNIRDLSKtaqwekLIEDEVADLQRSI-----HLQTGPLLK 2195
Cdd:cd20484 41 FKQACQFVLEQHPILKSVIEEEDGVPFQKIE--PSKPLSFQEEDISS------LKESEIIAYLREKakepfVLENGPLMR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2196 AGLFnTMSGT--YLFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQPVQLPRKTDSYQYFANRLAEYAESSKVIREQSYW 2273
Cdd:cd20484 113 VHLF-SRSEQehFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYW 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 2040046167 2274 RtvEKEKAAL----LPCEKPHSAADNIR-KTESFTLSEE 2307
Cdd:cd20484 192 K--QQLSGTLpileLPADRPRSSAPSFEgQTYTRRLPSE 228
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
1648-1956 |
6.55e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 51.09 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1648 TSGSTGTPKGVMVEQRGVVRLVKNS----DMA-FSPEDRI-------LLTASLGFD-------AMTFEVFGpllngacly 1708
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVWAELVarclDAAgVTPGDRVqnaygygLFTGGLGFHygaerlgALVIPAGG--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1709 isdketyLDSDRLKTFIQQNGITTLWLTSSLFNQLSEQNER-----TFSDLSRLILGGEALSPNHVNRVRNtAPDLALWN 1783
Cdd:cd05913 157 -------GNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEegidpRELSLKVGIFGAEPWTEEMRKRIER-RLGIKAYD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1784 GYGPTENTTFSTCFriEHEYKHSIPIgrpiaNSTAYIVN----SRGRLQPMGVIGELCVggdglargyfgrPELTKEKFv 1859
Cdd:cd05913 229 IYGLTEIIGPGVAF--ECEEKDGLHI-----WEDHFIPEiidpETGEPVPPGEVGELVF------------TTLTKEAM- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1860 pnpftPGERmYRTGDLARwLKDGT---------IDYI-GRMDDQVKIRGYRIELGEIEAALRQIDGVKEAAVIVRTGPSG 1929
Cdd:cd05913 289 -----PLIR-YRTRDITR-LLPGPcpcgrthrrIDRItGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEH 361
|
330 340
....*....|....*....|....*..
gi 2040046167 1930 HKELLAYMSLQAEMNIEKVRSLLSQQL 1956
Cdd:cd05913 362 LDELTIKVEVRPEADDDEKLEALKQRL 388
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
980-1040 |
6.85e-06 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.47 E-value: 6.85e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 980 LAKLWEEVLKYGPAGTRDH---FFEQGGHSLKATALVSRIAKAFGVQVPLKEIFAKPTLEELAA 1040
Cdd:smart00823 17 VREQVAAVLGHAAAEAIDPdrpFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1525-1946 |
8.06e-06 |
|
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: 51.20 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1525 QTLTYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGILGILKAGGAYLPVTEDMPTERLEWMLSDSNAVMLLQ 1604
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1605 SDR-------------------------LESHMAGkrLF-----------IEDIQLEAGISANNPEQqggpdsLAYIMYT 1648
Cdd:cd05933 87 ENQkqlqkilqiqdklphlkaiiqykepLKEKEPN--LYswdefmelgrsIPDEQLDAIISSQKPNQ------CCTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1649 SGSTGTPKGVMVEQRGVV----RLVKNSDMAFSPEDRILLTASLGFD---AMTFEVFGPLLNGACLYISDKE----TYLD 1717
Cdd:cd05933 159 SGTTGMPKGVMLSHDNITwtakAASQHMDLRPATVGQESVVSYLPLShiaAQILDIWLPIKVGGQVYFAQPDalkgTLVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1718 S--------------------DRLKTFIQQNG----ITTLW-----LTSSLFNQLSEQNERTFSDLS-RLILGG--EALS 1765
Cdd:cd05933 239 TlrevrptafmgvprvwekiqEKMKAVGAKSGtlkrKIASWakgvgLETNLKLMGGESPSPLFYRLAkKLVFKKvrKALG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1766 PNHVNRVRN-TAP------------DLALWNGYGPTENTTFSTcfrieheykhsipigrpIANSTAYIVNSRGRLQPmGV 1832
Cdd:cd05933 319 LDRCQKFFTgAAPisretlefflslNIPIMELYGMSETSGPHT-----------------ISNPQAYRLLSCGKALP-GC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1833 -----------IGELCVGGDGLARGYFGRPELTKEKFvpnpftPGERMYRTGDLARWLKDGTIDYIGRMDDQVKIRGyri 1901
Cdd:cd05933 381 ktkihnpdadgIGEICFWGRHVFMGYLNMEDKTEEAI------DEDGWLHSGDLGKLDEDGFLYITGRIKELIITAG--- 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2040046167 1902 elGE------IEAALRQ-IDGVKEAAVIvrtgpsGHKE--LLAYMSLQAEMNIE 1946
Cdd:cd05933 452 --GEnvppvpIEDAVKKeLPIISNAMLI------GDKRkfLSMLLTLKCEVNPE 497
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
727-879 |
1.55e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 50.49 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 727 TLKRVFAGGEALAPQTAARFaRSLPETAVIHGYGPTEATvDAAFFRYDHEKDRERMRLPIGkpvPGARLYILDSE--KAV 804
Cdd:PTZ00342 462 NLEVILNGGGKLSPKIAEEL-SVLLNVNYYQGYGLTETT-GPIFVQHADDNNTESIGGPIS---PNTKYKVRTWEtyKAT 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2040046167 805 QPIGvAGELYIAGAGVARGYLNRPELTEERFLDDPFYRgermyqTGDLARWLPDGTVEWLGRMDGQVKI-RGYRIE 879
Cdd:PTZ00342 537 DTLP-KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFK------TGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2133-2285 |
1.72e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.43 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2133 DALRMTIIDDGGQLQQFnrgIHGELY--SLNIRDLSK----TAQWEKLIEdevADLQRSIHLQTG-PLLKAGLFNtMSGT 2205
Cdd:PRK10252 59 DTLRMRFTEDNGEVWQW---VDPALTfpLPEIIDLRTqpdpHAAAQALMQ---ADLQQDLRVDSGkPLVFHQLIQ-LGDN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2206 --YLFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQPVQLPRKTDsyqyFANRLAEYA---ESSKVIREQSYWRtvekEK 2280
Cdd:PRK10252 132 rwYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASPFTP----FADVVEEYQryrASEAWQRDAAFWA----EQ 203
|
....*
gi 2040046167 2281 AALLP 2285
Cdd:PRK10252 204 RRQLP 208
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
1092-1294 |
2.26e-05 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 49.32 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1092 LTGPLDRARLDEVFRQLIRRHESLRTSFETGADGEPVQRIHDDVPFQL--MELAAAEDfVRPFRL-QEAPLFRAALVKEA 1168
Cdd:PRK09294 30 LRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLLHPGIvvVDGDAARP-LPELQLdQGVSLLALDVVPDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1169 EESHLLLVdMHHIISDGVSVGTLIREFSELYASR--TLHPLRIQYKDYAVWQQAFKQGEAYNRQEAYWLKQLDGELPVLE 1246
Cdd:PRK09294 109 GGARVTLY-IHHSIADAHHSASLLDELWSRYTDVvtTGDPGPIRPQPAPQSLEAVLAQRGIRRQALSGAERFMPAMYAYE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 1247 LPaDNARPAVRSFAGD-----HVSFSLDADTSSGLYKIARDNGCTLYMVLLAA 1294
Cdd:PRK09294 188 LP-PTPTAAVLAKPGLpqavpVTRCRLSKAQTSSLAAFGRRHRLTVNALVSAA 239
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1528-1991 |
3.41e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.43 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1528 TYRELNQRANRIAAALRANGVGSESVVALLTSRTPELAVGilgiLKAGGAY----LPVTEDMPTERLEWML--------- 1594
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA----MEACAAHslicVPLYDTLGPGAVDYIVdhaeidfvf 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1595 -SDSNAVMLLQSD-----RLESHMAGKRLFIEDIQ--LEAGISA-----------NNPEQQGGPD--SLAYIMYTSGSTG 1653
Cdd:PLN02430 154 vQDKKIKELLEPDcksakRLKAIVSFTSVTEEESDkaSQIGVKTyswidflhmgkENPSETNPPKplDICTIMYTSGTSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1654 TPKGVMVEQRGVVRLVKNSDMAFSPEDrilltaslgfDAMTFE-VFGPLLNGAclYISDK--ETYL------------DS 1718
Cdd:PLN02430 234 DPKGVVLTHEAVATFVRGVDLFMEQFE----------DKMTHDdVYLSFLPLA--HILDRmiEEYFfrkgasvgyyhgDL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1719 DRLKTFIQQNGITTLWLTSSLFNQLSEQNERTFSDLS------------------------------------------- 1755
Cdd:PLN02430 302 NALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNprrrlifnalykyklawmnrgyshkkaspmadflafrkvkakl 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1756 ----RLIL-GGEALSPNHVNRVRNTAPDLALwNGYGPTENTTFSTcfrieheykhsipIGRP-----IANSTAYIVNSRG 1825
Cdd:PLN02430 382 ggrlRLLIsGGAPLSTEIEEFLRVTSCAFVV-QGYGLTETLGPTT-------------LGFPdemcmLGTVGAPAVYNEL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1826 RLQ--------PMGV--IGELCVGGDGLARGYFGRPELTKEKFVPNPFtpgermyRTGDLARWLKDGTIDYIGRMDDQVK 1895
Cdd:PLN02430 448 RLEevpemgydPLGEppRGEICVRGKCLFSGYYKNPELTEEVMKDGWF-------HTGDIGEILPNGVLKIIDRKKNLIK 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 1896 I-RGYRIELGEIEAALRQIDGVKEAAVIvrtGPSGHKELLAYMSLQAEmNIEKVRSLLsqqlpGFMIPahLVELAALPLt 1974
Cdd:PLN02430 521 LsQGEYVALEYLENVYGQNPIVEDIWVY---GDSFKSMLVAVVVPNEE-NTNKWAKDN-----GFTGS--FEELCSLPE- 588
|
570
....*....|....*..
gi 2040046167 1975 qngkLDRRALPEPETTA 1991
Cdd:PLN02430 589 ----LKEHILSELKSTA 601
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
2121-2275 |
5.11e-05 |
|
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: 48.19 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2121 LRTALQHLVIHHDALRmTII--DDGGQLQQFnrgihgelysLNIRDLSKTAQWEKLIEDEVADL-----QRSIHLQTGPL 2193
Cdd:cd19540 41 LRAALADVVARHESLR-TVFpeDDGGPYQVV----------LPAAEARPDLTVVDVTEDELAARlaeaaRRGFDLTAELP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2194 LKAGLFNTMSGTY-LFLTIHHLVVDGVSWRILLEDLSAAYSQAAAGQ-------PVQlprktdsYQYFA----NRLAEYA 2261
Cdd:cd19540 110 LRARLFRLGPDEHvLVLVVHHIAADGWSMAPLARDLATAYAARRAGRapdwaplPVQ-------YADYAlwqrELLGDED 182
|
170
....*....|....*
gi 2040046167 2262 ESSKVIREQ-SYWRT 2275
Cdd:cd19540 183 DPDSLAARQlAYWRE 197
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
2085-2380 |
1.67e-04 |
|
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: 46.54 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2085 PWTPVQRWFLAQHI---EERQHFNQSVmLHSSEGFQEQPLRTALQHLVIHHDALRMTII-DDGGQLQQFNRGIHGELYSL 2160
Cdd:cd19547 3 PLAPMQEGMLFRGLfwpDSDAYFNQNV-LELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDDLAPPWAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2161 ---NIRDLSKTAQW-EKLIEDEVAdlqRSIHLQTGPLLKAGLFNTMSGT-YLFLTIHHLVVDGVSWRILLEDLSAAYSQA 2235
Cdd:cd19547 82 ldwSGEDPDRRAELlERLLADDRA---AGLSLADCPLYRLTLVRLGGGRhYLLWSHHHILLDGWCLSLIWGDVFRVYEEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 2236 AAGQPVQL----PRKtDSYQYFANRLAEYAESSKvireqsYWRTVEKEkaaLLPceKPHSAADNIRKTESFTLSEEDTHV 2311
Cdd:cd19547 159 AHGREPQLspcrPYR-DYVRWIRARTAQSEESER------FWREYLRD---LTP--SPFSTAPADREGEFDTVVHEFPEQ 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2040046167 2312 LIHKVNNA---YNTDTQDILLTAASLALCDWMGERKLRIAMEGHGRDhtlPELDISR-TVGWFTTIYPVLIDL 2380
Cdd:cd19547 227 LTRLVNEAargYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP---PELEGSEhMVGIFINTIPLRIRL 296
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1640-1659 |
2.72e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 46.51 E-value: 2.72e-04
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1639-1681 |
5.41e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.48 E-value: 5.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2040046167 1639 PDSLAYIMYTSGSTGTPKGVMVEQRGVVRLVKNSDMA--FSPEDR 1681
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLStkFYPSDV 264
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
695-925 |
7.07e-03 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 41.46 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 695 GVTTAHFIPAMANSFLDQVEMETEEKRTSlakTLKRVFAGGEALAPQTAARFARSLPETAVIHgYGPTEATVDAAFFryD 774
Cdd:cd05913 170 GPTVLCCTPSYALYLAEEAEEEGIDPREL---SLKVGIFGAEPWTEEMRKRIERRLGIKAYDI-YGLTEIIGPGVAF--E 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 775 HEKDR-----ERMRLPIgkpvpgarlyILDSE--KAVqPIGVAGELYIAgagvargylnrpELTEERFlddPFYRgermY 847
Cdd:cd05913 244 CEEKDglhiwEDHFIPE----------IIDPEtgEPV-PPGEVGELVFT------------TLTKEAM---PLIR----Y 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2040046167 848 QTGDLARWLPD----GTV-----EWLGRMDGQVKIRGYRIEPGEVEAALRQIDGVR-EAAVVARTEGEETELYAYIEGQD 917
Cdd:cd05913 294 RTRDITRLLPGpcpcGRThrridRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGpHYQLILTRQEHLDELTIKVEVRP 373
|
....*...
gi 2040046167 918 QKTARTEL 925
Cdd:cd05913 374 EADDDEKL 381
|
|
| |
