|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-1412 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1108.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRN------LPALRIQYKDYAVWREGFKT 76
Cdd:PRK12467 1218 QPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSqgqslqLPALPIQYADYAVWQRQWMD 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 156
Cdd:PRK12467 1298 AGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYS 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 157 GQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRN 236
Cdd:PRK12467 1378 GQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHS 1457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 237 PVFDAMFILQNVEKQDI-DLREIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEA 315
Cdd:PRK12467 1458 PLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGL 1537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 316 LSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQKDIpFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTL 395
Cdd:PRK12467 1538 VADPERRLGELDLLDEAERRQILEGWNATHTGYPLARL-VHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRL 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 396 QNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELKHLISnSPESEMShI 474
Cdd:PRK12467 1617 IALGvGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLP-LPDGLRS-L 1694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 475 FLDDEGSFEE--SNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVrLLQIASFSFDVF 552
Cdd:PRK12467 1695 VLDQEDDWLEgySDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADV-VLQFTSFAFDVS 1773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 553 SGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQfKLPDLDILILGSDMVKAQDFK 632
Cdd:PRK12467 1774 VWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVE-HPLSLRRVVCGGEALEVEALR 1852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 633 TLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKG 712
Cdd:PRK12467 1853 PWLERLPDT-GLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARG 1931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 713 YHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQH 791
Cdd:PRK12467 1932 YLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD 2011
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 792 DKNGQAgLAAYIVPSD-----------VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPN-NVLSRP 859
Cdd:PRK12467 2012 GANGKQ-LVAYVVPTDpglvdddeaqvALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDaSELQQA 2090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 860 YTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCG--HITPLAS 937
Cdd:PRK12467 2091 YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAvaQEGDGTV 2170
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 938 QADQGPAEGEAELTPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQFNRG 1017
Cdd:PRK12467 2171 SIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGF-VQEDGGWSAMHRA 2249
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1018 INHKDHELFglyisdWTKASLERAHLdEKLAAEEtviQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRIL 1096
Cdd:PRK12467 2250 PEQERRPLL------WQVVVADKEEL-EALCEQA---QRSLDLEEGPLLRAVLATLPDGSQrLLLVIHHLVVDGVSWRIL 2319
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1097 LEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIenvPDKLQMNSDAAAF 1176
Cdd:PRK12467 2320 LEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDH---PQGGLQRRHAASV 2396
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1177 V--LSGDWTEKLLFETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILLdm 1254
Cdd:PRK12467 2397 TthLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKL-- 2474
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1255 gIPEPfedQLAYRIKTTKDMLRRVPNKGTGYGLLTHIG--ELRHK-----EPEVSFNYLGQFSEEKEVETFQLsyYQPRY 1327
Cdd:PRK12467 2475 -SPTA---SLATSIKTIKEQLRAVPNKGLGFGVLRYLGseAARQTlqalpVPRITFNYLGQFDGSFDAEKQAL--FVPSG 2548
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1328 EIAG-EREREYELD----INALITDGRLHVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKEL 1401
Cdd:PRK12467 2549 EFSGaEQSEEAPLGnwlsINGQVYGGELNLGWTFsQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGL 2628
|
1450
....*....|....*...
gi 1238238751 1402 TLS-------ALSSIEDL 1412
Cdd:PRK12467 2629 SQEqldrlpvAVGDIEDI 2646
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-1412 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1061.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 2 IKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVWREGFK 75
Cdd:PRK12316 152 LQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYatgaepGLPALPIQYADYALWQRSWL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 76 TGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRL 155
Cdd:PRK12316 232 EAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRY 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 156 SGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSR 235
Cdd:PRK12316 312 SGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSH 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 236 NPVFDAMFILQNVEKqDIDLRE----IKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEF 311
Cdd:PRK12316 392 SPLFQVMYNHQPLVA-DIEALDtvagLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 312 LHEALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFA-QKDIpfHRIFEAKAEENPEHIAVIDNETEISYRLLNERANR 390
Cdd:PRK12316 471 LRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPlQRGV--HRLFEEQVERTPEAPALAFGEETLDYAELNRRANR 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 391 LARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELKHLISNSpeS 469
Cdd:PRK12316 549 LAHALIERGvGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLA--A 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 470 EMSHIFLDDEGSFEE--SNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASF 547
Cdd:PRK12316 627 GVQVLDLDRPAAWLEgySEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGD-TVLQKTPF 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 548 SFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIipvmeyvyrnQFKLPD--------LDIL 619
Cdd:PRK12316 706 SFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSML----------QAFLQDedvasctsLRRI 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 620 ILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSfYETSMggECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVA 699
Cdd:PRK12316 776 VCSGEALPADAQEQVFAKLPQA-GLYNLYGPTEAAIDVT-HWTCV--EEGGDSVPIGRPIANLACYILDANLEPVPVGVL 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 700 GELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQT 779
Cdd:PRK12316 852 GELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 780 GLVREAAVAVQHDKNgqagLAAYIVPSDVNTN---ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPN-NV 855
Cdd:PRK12316 932 PWVREAAVLAVDGKQ----LVGYVVLESEGGDwreALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEaSV 1007
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 856 LSRPYTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHIT-P 934
Cdd:PRK12316 1008 AQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKaG 1087
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 935 LASQADQGPAEGEAELTPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQf 1014
Cdd:PRK12316 1088 QATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDGGWQQ- 1165
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1015 nrginhkdhelfgLYISDWTKASLERAHL--DEKLAAEETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGV 1091
Cdd:PRK12316 1166 -------------AYAAPQAGEVLWQRQAasEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQrLLLVIHHLVVDGV 1232
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1092 SWRILLEDLAAAYQQALEKkeiqLPPKTDSYLSYADGLTQIAESkqLLSEKTYWQTILDAHTAFLPKDienVPDKLQMN- 1170
Cdd:PRK12316 1233 SWRILLEDLQRAYADLDAD----LPARTSSYQAWARRLHEHAGA--RAEELDYWQAQLEDAPHELPCE---NPDGALENr 1303
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1171 -SDAAAFVLSGDWTEKLLFETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYP 1249
Cdd:PRK12316 1304 hERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFP 1383
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1250 ILLdmgipEPfEDQLAYRIKTTKDMLRRVPNKGTGYGLLTHIG--ELRHK-----EPEVSFNYLGQFSEEKEvetfQLSY 1322
Cdd:PRK12316 1384 VRL-----TP-AADLGESIKAIKEQLRAVPDKGIGYGLLRYLAgeEAAARlaalpQPRITFNYLGQFDRQFD----EAAL 1453
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1323 YQPRYEIAGEREREYE-----LDINALITDGRLHVKAVYTQ-VFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDF 1396
Cdd:PRK12316 1454 FVPATESAGAAQDPCAplanwLSIEGQVYGGELSLHWSFSReMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDF 1533
|
1450 1460
....*....|....*....|...
gi 1238238751 1397 SNKELT---LSALS----SIEDL 1412
Cdd:PRK12316 1534 PLAGLSqaqLDALPlpagEIADI 1556
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1412 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 975.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRN------LPALRIQYKDYAVWREGFKT 76
Cdd:PRK12316 2702 RPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMD 2781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 156
Cdd:PRK12316 2782 SGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYS 2861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 157 GQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRN 236
Cdd:PRK12316 2862 GQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHS 2941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 237 PVFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEAL 316
Cdd:PRK12316 2942 PLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMV 3021
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 317 STPETSLAQINILSDKEKQKIVFEFNKTQVEFAqKDIPFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQ 396
Cdd:PRK12316 3022 ENPQRSVDELAMLDAEERGQLLEAWNATAAEYP-LERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLI 3100
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 397 NRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELKhlisnSPESEMSHIF 475
Cdd:PRK12316 3101 ERGvGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLR-----LPLAQGVQVL 3175
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 476 LDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGD 555
Cdd:PRK12316 3176 DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGD-RVLQFTTFSFDVFVEE 3254
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 556 LARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVyrNQFKLPDLDILILGSDMVKAQdfktLT 635
Cdd:PRK12316 3255 LFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEE--DAHRCTSLKRIVCGGEALPAD----LQ 3328
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 636 DRFGQSMRIINSYGVTEATIDSSFYETSmggECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHH 715
Cdd:PRK12316 3329 QQVFAGLPLYNLYGPTEATITVTHWQCV---EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHN 3405
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 716 KPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAvqhDKNG 795
Cdd:PRK12316 3406 RPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL---AVDG 3482
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 796 QAgLAAYIVPSDVNTN---ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPNNVLSR-PYTAPVNDLQKTM 871
Cdd:PRK12316 3483 RQ-LVAYVVPEDEAGDlreALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQqDYVAPVNELERRL 3561
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 872 AYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHITPLASQA-DQGPAEGEAEL 950
Cdd:PRK12316 3562 AAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAvDQGPVSGETLL 3641
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 951 TPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrginHKDHELFGLYI 1030
Cdd:PRK12316 3642 LPIQQQFFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAE------HLPVELGGALL 3715
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1031 sdWtKASLERAHLDEKLAAEetvIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALE 1109
Cdd:PRK12316 3716 --W-RAELDDAEELERLGEE---AQRSLDLADGPLLRALLATLADGSQrLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQ 3789
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1110 KKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDienVPDKLQMNSDAAAFV--LSGDWTEKLL 1187
Cdd:PRK12316 3790 GEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSELPCD---HPQGALQNRHAASVQtrLDRELTRRLL 3866
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1188 FETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILLDMGIpepfedQLAYR 1267
Cdd:PRK12316 3867 QQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPVE------DLGAS 3940
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1268 IKTTKDMLRRVPNKGTGYGLLTHIGELRHKE-------PEVSFNYLGQFSEEKEVETfqlSYYQPRYEIAG-EREREYEL 1339
Cdd:PRK12316 3941 IKAIKEQLRAIPNKGIGFGLLRYLGDEESRRtlaglpvPRITFNYLGQFDGSFDEEM---ALFVPAGESAGaEQSPDAPL 4017
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1340 D----INALITDGRLHVKAVYT-QVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELTLS-------ALS 1407
Cdd:PRK12316 4018 DnwlsLNGRVYGGELSLDWTFSrEMFEEATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQArldalplPLG 4097
|
....*
gi 1238238751 1408 SIEDL 1412
Cdd:PRK12316 4098 EIEDI 4102
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4-1214 |
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: 961.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 4 PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN------NRNLPALRIQYKDYAVWREGFKTG 77
Cdd:COG1020 122 PFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLaayagaPLPLPPLPIQYADYALWQREWLQG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 78 DAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSG 157
Cdd:COG1020 202 EELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 158 QEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNP 237
Cdd:COG1020 282 QDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNP 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 238 VFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEALS 317
Cdd:COG1020 362 LFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 318 TPETSLAQINILSDKEKQKIVFEFNKTQVEFAQkDIPFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQN 397
Cdd:COG1020 442 DPDQPLGDLPLLTAAERQQLLAEWNATAAPYPA-DATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRA 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 398 RkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELKHLIsnsPESEMSHIF 475
Cdd:COG1020 521 L-GVGPgdLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL---PELGVPVLA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 476 LDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGD 555
Cdd:COG1020 597 LDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGD-RVLQFASLSFDASVWE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 556 LARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNqfkLPDLDILILGSDMVKAQDFKTLT 635
Cdd:COG1020 676 IFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWR 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 636 DRFGQsMRIINSYGVTEATIDSSFYETSmGGECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHH 715
Cdd:COG1020 753 ARLPG-ARLVNLYGPTETTVDSTYYEVT-PPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLN 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 716 KPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN 794
Cdd:COG1020 831 RPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAP 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 795 GQAGLAAYIVP---SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPNNVLSRPYTAPVNDLQKTM 871
Cdd:COG1020 911 GDKRLVAYVVPeagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEE 990
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 872 AYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHITPLASQADQGPAEGEAELT 951
Cdd:COG1020 991 AALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPL 1070
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 952 PIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQFNRginhkDHELFGLYIS 1031
Cdd:COG1020 1071 PLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEG-----PRLRLLVALA 1145
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1032 DWTKASLERAHLDEKLAAEETVIQSKMNVEKGPLLQAGLFKTAEGDHLLIALHHLVIDGVSWRILLEDLAAAYQQALEKK 1111
Cdd:COG1020 1146 AALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLA 1225
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1112 EIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQtildAHTAFLPKDIENVPDKLQMNSDAAAFVLSGDWTEKLLFETQ 1191
Cdd:COG1020 1226 AAAAALLALALLLALLALAALLALAALAALAAALL----ALALALLALALLLLALALLLPALARARAARTARALALLLLL 1301
|
1210 1220
....*....|....*....|...
gi 1238238751 1192 QAYGTDANELLLTALGMALSEWT 1214
Cdd:COG1020 1302 ALLLLLALALALLLLLLLLLALL 1324
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-1412 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 867.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELY----NNRNLP--ALRIQYKDYAVWREGFKT 76
Cdd:PRK05691 1832 QPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYeaflDDRESPlePLPVQYLDYSVWQRQWLE 1911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 156
Cdd:PRK05691 1912 SGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYS 1991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 157 GQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRN 236
Cdd:PRK05691 1992 GQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYN 2071
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 237 PVFDAMFILQNVE-KQDIDLREIKVR-PANFAHHISlFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHE 314
Cdd:PRK05691 2072 PLFQVMCNVQRWEfQQSRQLAGMTVEyLVNDARATK-FDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEA 2150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 315 ALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQkDIPFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLART 394
Cdd:PRK05691 2151 LLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARL-DQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARA 2229
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 395 LQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELKHLISNSPESEMSH 473
Cdd:PRK05691 2230 LRERGvGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARW 2309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 474 IFLDDEGSFE-ESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVtyqnfTHAALAWRQIYELDRKPVRL----LQIASFS 548
Cdd:PRK05691 2310 CLEDDAAALAaYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVV-----SHGEIAMHCQAVIERFGMRAddceLHFYSIN 2384
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 549 FDVFSGDLARTLTNGGTlIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPdLDILILGSDMVKA 628
Cdd:PRK05691 2385 FDAASERLLVPLLCGAR-VVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLP-VRMCITGGEALTG 2462
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 629 QDFKTLTDRFgQSMRIINSYGVTEATI---DSSFYETSMGGECTgdnVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIG 705
Cdd:PRK05691 2463 EHLQRIRQAF-APQLFFNAYGPTETVVmplACLAPEQLEEGAAS---VPIGRVVGARVAYILDADLALVPQGATGELYVG 2538
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 706 GAGVAKGYHHKPDLTQMKFTENPFVS-GERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE 784
Cdd:PRK05691 2539 GAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE 2618
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 785 AAVaVQHDKNGQAGLAAYIV-----PSDVNTNALRAA----LTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPNNV 855
Cdd:PRK05691 2619 AVV-LALDTPSGKQLAGYLVsavagQDDEAQAALREAlkahLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPE 2697
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 856 LSRP-YTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHITP 934
Cdd:PRK05691 2698 LNRQaYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATH 2777
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 935 L-ASQADQGPAEGEAELTPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHvIQ 1013
Cdd:PRK05691 2778 SeAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRF-SQADGR-WQ 2855
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1014 FNRGINHKDHELFGLYISDWTKAslerahldeklAAEETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVS 1092
Cdd:PRK05691 2856 AEYRAVTAQELLWQVTVADFAEC-----------AALFADAQRSLDLQQGPLLRALLVDGPQGQQrLLLAIHHLVVDGVS 2924
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1093 WRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIENvPDKLQMNSD 1172
Cdd:PRK05691 2925 WRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQ-GGNLNRHAQ 3003
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1173 AAAFVLSGDWTEKLLFETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILL 1252
Cdd:PRK05691 3004 TVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRL 3083
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1253 DmgiPEPFEDQ-LAYRIKTTKDMLRRVPNKGTGYGLLTHIGELRHKE-------PEVSFNYLGQFSEEKEVETFqlsyYQ 1324
Cdd:PRK05691 3084 T---PAPGDDAaRGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREamaalpqAPITFNYLGQFDQSFASDAL----FR 3156
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1325 PRYEIAGEREREY-----ELDINALITDGRLHVKAVYT-QVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSN 1398
Cdd:PRK05691 3157 PLDEPAGPAHDPDaplpnELSVDGQVYGGELVLRWTYSaERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPL 3236
|
1450 1460
....*....|....*....|.
gi 1238238751 1399 KELT---LSAL----SSIEDL 1412
Cdd:PRK05691 3237 AQLTqaqLDALpvpaAEIEDV 3257
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-1149 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 802.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 4 PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVWREGFKTG 77
Cdd:PRK12467 154 PFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 78 DAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSG 157
Cdd:PRK12467 234 GERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 158 QEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNP 237
Cdd:PRK12467 314 QSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 238 VFDAMFILQNV-----EKQDIDLREIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFL 312
Cdd:PRK12467 394 LFQVMFNHQNTatggrDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 313 HEALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQKDIpfHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLA 392
Cdd:PRK12467 474 EAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCV--HQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 393 RTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELKHLIsNSPESeM 471
Cdd:PRK12467 552 HVLIAAGvGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQL-PVPAG-L 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 472 SHIFLDDEGSFEESNCNLNLSPA--PEEPVYIIYTSGTTGAPKGVIVTYQ---NFTHAALAWRQIYELDrkpvRLLQIAS 546
Cdd:PRK12467 630 RSLCLDEPADLLCGYSGHNPEVAldPDNLAYVIYTSGSTGQPKGVAISHGalaNYVCVIAERLQLAADD----SMLMVST 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 547 FSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVMeyvyrnQFKLPDLDI----LILG 622
Cdd:PRK12467 706 FAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALL------QASRVALPRpqraLVCG 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 623 SDMVkAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGECTGdNVPIGSPLPNVHMYVLSQTDQIQPIGVAGEL 702
Cdd:PRK12467 780 GEAL-QVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG-NVPIGQPLANLGLYILDHYLNPVPVGVVGEL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 703 CIGGAGVAKGYHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGL 781
Cdd:PRK12467 858 YIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPG 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 782 VREAAVAVQhDKNGQAGLAAYIVPSDVNTNA--------LRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPN 853
Cdd:PRK12467 938 VREAVVLAQ-PGDAGLQLVAYLVPAAVADGAehqatrdeLKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPD 1016
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 854 -NVLSRPYTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARL-AAEGWSMTIRDLFRYSTIQELCGH 931
Cdd:PRK12467 1017 aSAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVrQRLGIQVPLRTLFEHQTLAGFAQA 1096
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 932 ITPLAsQADQGPAEGEAELTPIQRRFFGQVHAF---------HYHYNQSVMLFSEkgFNANALHLALRKITEHHDAIRMI 1002
Cdd:PRK12467 1097 VAAQQ-QGAQPALPDVDRDQPLPLSYAQERQWFlwqlepgsaAYHIPQALRLKGP--LDIEALERSFDALVARHESLRTT 1173
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1003 FqRDQNGHVIQfnrgINHKDHELfGLYISDWTKASLERAHLDEKLAAEetvIQSKMNVEKGPLLQAGLFKTAEGDHLLI- 1081
Cdd:PRK12467 1174 F-VQEDGRTRQ----VIHPVGSL-TLEEPLLLAADKDEAQLKVYVEAE---ARQPFDLEQGPLLRVGLLRLAADEHVLVl 1244
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 1082 ALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL 1149
Cdd:PRK12467 1245 TLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQL 1312
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
367-849 |
0e+00 |
|
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: 797.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGvAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAA 525
Cdd:cd17650 81 EDSGAKLLLTQ--------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVMEY 605
Cdd:cd17650 123 HAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 606 VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHMY 685
Cdd:cd17650 203 VYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 686 VLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGY 765
Cdd:cd17650 283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 766 RIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD-VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAAtLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 1238238751 845 DRNAL 849
Cdd:cd17650 443 DRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-1159 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 668.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 4 PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVW-REGFKT 76
Cdd:PRK05691 780 PFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWqRQWLAQ 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDAYKtQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 156
Cdd:PRK05691 860 GEAAR-QLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYS 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 157 GQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSrn 236
Cdd:PRK05691 939 GQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQG-- 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 237 pVFDAMFilqnvEKQDIDLREIKVRPANFAHHI------SLFDITLIATE-ISGSICCEMEFSTEVFLKATIERWADHFI 309
Cdd:PRK05691 1017 -LFQVMF-----NHQQRDLSALRRLPGLLAEELpwhsreAKFDLQLHSEEdRNGRLTLSFDYAAELFDAATIERLAEHFL 1090
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 310 EFLHEALSTPETSLAQINILSDKEKQKIVfEFNKTQVEFAQKDIPfhRIFEAKAEENPEHIAVIDNETEISYRLLNERAN 389
Cdd:PRK05691 1091 ALLEQVCEDPQRALGDVQLLDAAERAQLA-QWGQAPCAPAQAWLP--ELLNEQARQTPERIALVWDGGSLDYAELHAQAN 1167
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 390 RLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRelkHLISNSPE 468
Cdd:PRK05691 1168 RLAHYLRDKGvGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS---HLLERLPQ 1244
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 469 SE-MSHIFLDdegsfeesncNLNLSPAPEEP----------VYIIYTSGTTGAPKGVIVtyqnfTHAALA----WRQ-IY 532
Cdd:PRK05691 1245 AEgVSAIALD----------SLHLDSWPSQApglhlhgdnlAYVIYTSGSTGQPKGVGN-----THAALAerlqWMQaTY 1309
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 533 ELDRKPVrLLQIASFSFDVFSGDLARTLTNGGTLIVC-PDETRlEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQF 611
Cdd:PRK05691 1310 ALDDSDV-LMQKAPISFDVSVWECFWPLITGCRLVLAgPGEHR-DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAAC 1387
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 612 KlpDLDILILGSDMVKAQdfktLTDRFGQSM---RIINSYGVTEATIDSSFYETSMGgecTGDNVPIGSPLPNVHMYVLS 688
Cdd:PRK05691 1388 T--SLRRLFSGGEALPAE----LRNRVLQRLpqvQLHNRYGPTETAINVTHWQCQAE---DGERSPIGRPLGNVLCRVLD 1458
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 689 QTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFV-SGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRI 767
Cdd:PRK05691 1459 AELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRV 1538
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 768 ETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP--SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLD 845
Cdd:PRK05691 1539 EPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLD 1618
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 846 RNALPAPnNVLSRPYTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARL-AAEGWSMTIRDLFRYST 924
Cdd:PRK05691 1619 RRALPEP-VWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTrQACDVELPLRALFEASE 1697
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 925 IQELCGHITPLASQAD---QGPAEGEAELTPI-----QRR--FFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITE 994
Cdd:PRK05691 1698 LGAFAEQVARIQAAGErnsQGAIARVDRSQPVplsysQQRmwFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALIL 1777
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 995 HHDAIRMIFQRDqNGHVIQfnrginhKDHELFGLYIsDWT-----KASLERAHLdEKLAAEETviQSKMNVEKGPLLQAG 1069
Cdd:PRK05691 1778 RHETLRTTFPSV-DGVPVQ-------QVAEDSGLRM-DWQdfsalPADARQQRL-QQLADSEA--HQPFDLERGPLLRAC 1845
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1070 LFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTI 1148
Cdd:PRK05691 1846 LVKAAEREHyFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQ 1925
|
1210
....*....|...
gi 1238238751 1149 L-DAHTAF-LPKD 1159
Cdd:PRK05691 1926 LgNEHPLLeLPAD 1938
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1265 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 658.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPALRIQYKDYAVWREGFKTGDAykt 82
Cdd:PRK12316 1659 KGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAAS--- 1735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 83 qEAYWLKQLeGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDII 162
Cdd:PRK12316 1736 -EAFWKEQL-AALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVA 1813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 163 VGSPIAGRPHK--DLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELvdklELTRDMSRNPVFD 240
Cdd:PRK12316 1814 FGATVAGRPAElpGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDI----QRWAGQGGEALFD 1889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 241 AMFILQNVE-----KQDIDLREIKVRPANfaHHISLFDITLiATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEA 315
Cdd:PRK12316 1890 SLLVFENYPvaealKQGAPAGLVFGRVSN--HEQTNYPLTL-AVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQM 1966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 316 LSTPETSLAQINILSDKEKQKIVFEFNKTQvEFAQKDIPFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTL 395
Cdd:PRK12316 1967 AEDAQAALGELALLDAGERQRILADWDRTP-EAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRL 2045
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 396 QNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRelkHLISNSP-ESEMSH 473
Cdd:PRK12316 2046 RARGvGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR---HLLERLPlPAGVAR 2122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 474 IFLDDEGSFEES-NCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTyqnftHAALAWR-----QIYELDRKPvRLLQIASF 547
Cdd:PRK12316 2123 LPLDRDAEWADYpDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVS-----HGALVAHcqaagERYELSPAD-CELQFMSF 2196
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 548 SFDVFSGDLARTLTNGGTLIVCPDETRLePAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQfKLPDLDILILGSDMVK 627
Cdd:PRK12316 2197 SFDGAHEQWFHPLLNGARVLIRDDELWD-PEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG-RPPAVRVYCFGGEAVP 2274
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 628 AQDFkTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGA 707
Cdd:PRK12316 2275 AASL-RLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGE 2353
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 708 GVAKGYHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA 786
Cdd:PRK12316 2354 GLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAV 2433
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 787 VAVQHDKNGQAgLAAYIVPSDVNTN---ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPN-NVLSRPYTA 862
Cdd:PRK12316 2434 VVAQDGASGKQ-LVAYVVPDDAAEDllaELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDvSQLRQAYVA 2512
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 863 PVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARL-AAEGWSMTIRDLFRYSTIQELCGHITPL-ASQA- 939
Cdd:PRK12316 2513 PQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVrQDLGLEVPLRILFERPTLAAFAASLESGqTSRAp 2592
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 940 DQGPAEGEAEL----TPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQFN 1015
Cdd:PRK12316 2593 VLQKVTRVQPLplshAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRF-VEVGEQTRQVI 2671
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1016 RGINHKDHELFglyisdWTKASLERAhLDEKLAAEetvIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWR 1094
Cdd:PRK12316 2672 LPNMSLRIVLE------DCAGVADAA-IRQRVAEE---IQRPFDLARGPLLRVRLLALDGQEHvLVITQHHIVSDGWSMQ 2741
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1095 ILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIENVPDKLQMNSDAA 1174
Cdd:PRK12316 2742 VMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGAR 2821
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1175 AFVLSGDWTEKLLFETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREghvpNIDISRTVGWFTSIYPILLDM 1254
Cdd:PRK12316 2822 LDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN----RAETERLIGFFVNTQVLRAQV 2897
|
1290
....*....|.
gi 1238238751 1255 GIPEPFEDQLA 1265
Cdd:PRK12316 2898 DAQLAFRDLLG 2908
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-954 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 645.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 5 FDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPALRIQYKDYAVWregFKTGDAYKTqE 84
Cdd:PRK12316 4207 FDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPAQPGGRYRDYIAW---LQRQDAAAS-E 4282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 85 AYWLKQLEGELPVLDLPADHARPPVRSFAG-DKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIV 163
Cdd:PRK12316 4283 AFWREQLAALDEPTRLAQAIARADLRSANGyGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAF 4362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 164 GSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELvdklELTRDMSRNPVFDA 241
Cdd:PRK12316 4363 GATVAGRPAelPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEI----QRWAGQGGEALFDS 4438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 242 MFILQN------VEKQ-DIDLREIKVRpanfAHHISLFDITLiatEISGSICCEMEFS--TEVFLKATIERWADHFIEFL 312
Cdd:PRK12316 4439 LLVFENypvseaLQQGaPGGLRFGEVT----NHEQTNYPLTL---AVGLGETLSLQFSydRGHFDAATIERLARHLTNLL 4511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 313 HEALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQKDIpFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLA 392
Cdd:PRK12316 4512 EAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRC-VHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLA 4590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 393 RTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRelkHLISNSPESE- 470
Cdd:PRK12316 4591 HALIARGvGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS---HLLQRLPIPDg 4667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 471 MSHIFLDDEGSFE---ESNCNLNLspAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASF 547
Cdd:PRK12316 4668 LASLALDRDEDWEgfpAHDPAVRL--HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD-RVLQFMSF 4744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 548 SFDVFSGDLARTLTNGGTLIVCPDETRLePAEIYKIIKSQRITVMESTPALIIPVMEYvYRNQFKLPDLDILILGSDMVk 627
Cdd:PRK12316 4745 SFDGSHEGLYHPLINGASVVIRDDSLWD-PERLYAEIHEHRVTVLVFPPVYLQQLAEH-AERDGEPPSLRVYCFGGEAV- 4821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 628 AQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGA 707
Cdd:PRK12316 4822 AQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE 4901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 708 GVAKGYHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA 786
Cdd:PRK12316 4902 GVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 787 VAVQHDKNGQAgLAAYIVPSDVN-----------TNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPN-N 854
Cdd:PRK12316 4982 VIAQEGAVGKQ-LVGYVVPQDPAladadeaqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDaS 5060
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 855 VLSRPYTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQELcghiT 933
Cdd:PRK12316 5061 LLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLAAF----V 5136
|
970 980
....*....|....*....|.
gi 1238238751 934 PLASQADQGPAEGEAELTPIQ 954
Cdd:PRK12316 5137 ELAAAAGSGDDEKFDDLEELL 5157
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
367-849 |
5.40e-180 |
|
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: 541.35 E-value: 5.40e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYI 444
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-ERGVGPGdlVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 445 LRDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHA 524
Cdd:cd05930 80 LEDSGAKLVLTD--------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 525 ALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVME 604
Cdd:cd05930 122 LLWMQEAYPLTPGD-RVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 605 YVYRNQFklPDLDILILGSDMVKAQDFKTLTDRFGQsMRIINSYGVTEATIDSSFYETSMGGECtGDNVPIGSPLPNVHM 684
Cdd:cd05930 201 ELELAAL--PSLRLVLVGGEALPPDLVRRWRELLPG-ARLVNLYGPTEATVDATYYRVPPDDEE-DGRVPIGRPIPNTRV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 685 YVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKING 764
Cdd:cd05930 277 YVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 765 YRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLN 841
Cdd:cd05930 357 YRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEggeLDEEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
....*...
gi 1238238751 842 GKLDRNAL 849
Cdd:cd05930 437 GKVDRKAL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-967 |
1.82e-177 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 588.28 E-value: 1.82e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 5 FDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPALRIQYKDYAVWregFKTGDAyKTQE 84
Cdd:PRK12467 2751 FDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQPPPAREGRYRDYIAW---LQAQDA-EASE 2826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 85 AYWLKQL----EGELPVLDLPADHARPpvRSFAGDKvSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQED 160
Cdd:PRK12467 2827 AFWKEQLaaleEPTRLARALYPAPAEA--VAGHGAH-YLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDT 2903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 161 IIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFeelvdkLELTRDMSR--N 236
Cdd:PRK12467 2904 VCFGATVAGRPAqlRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPL------ADIQRWAGQggE 2977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 237 PVFDAMFILQNV-------EKQDIDLREIKVRpanfAHHISLFDITLiATEISGSICCEMEFSTEVFLKATIERWADHFI 309
Cdd:PRK12467 2978 ALFDSILVFENYpisealkQGAPSGLRFGAVS----SREQTNYPLTL-AVGLGDTLELEFSYDRQHFDAAAIERLAESFD 3052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 310 EFLHEALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQkDIPFHRIFEAKAEENPEHIAVIDNETEISYRLLNERAN 389
Cdd:PRK12467 3053 RLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPS-ERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRAN 3131
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 390 RLA-RTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQrelKHLISNSPE 468
Cdd:PRK12467 3132 RLAhRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ---AHLLEQLPA 3208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 469 SEMSHIFLDDEGSFE-ESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASF 547
Cdd:PRK12467 3209 PAGDTALTLDRLDLNgYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAND-RVLLFMSF 3287
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 548 SFDVFSGDLARTLTNGGTLIVCPDETRlEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQfkLPDLDILILGSDMVK 627
Cdd:PRK12467 3288 SFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAGGAD--CASLDIYVFGGEAVP 3364
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 628 AQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGA 707
Cdd:PRK12467 3365 PAAFEQVKRKLKPR-GLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV 3443
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 708 GVAKGYHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA 786
Cdd:PRK12467 3444 GLARGYHQRPSLTAERFVADPFsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAV 3523
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 787 VAVQHDKNGQAgLAAYIVPSDVNTN---ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPNNVLSRPYTAP 863
Cdd:PRK12467 3524 VLARDGAGGKQ-LVAYVVPADPQGDwreTLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAP 3602
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 864 VNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARL-AAEGWSMTIRDLFRYSTIQELCGHItplasqadQG 942
Cdd:PRK12467 3603 RSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIrQSLGLKLSLRDLMSAPTIAELAGYS--------PL 3674
|
970 980
....*....|....*....|....*
gi 1238238751 943 PAEGEAELTPIQRRFFGQVHAFHYH 967
Cdd:PRK12467 3675 GDVPVNLLLDLNRLETGFPALFCRH 3699
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
357-852 |
6.00e-170 |
|
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: 516.88 E-value: 6.00e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLR-EKGVGPdtIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQRELKHLISNSPESEMshifLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGV 514
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDL----LDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 515 IVTYQNFTHAALAWRQIYELDRKpVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMES 594
Cdd:cd17655 156 MIEHRGVVNLVEWANKVIYQGEH-LRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 595 TPALiipVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSmGGECTGDNVP 674
Cdd:cd17655 235 TPAH---LKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYE-PETDQQVSVP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 675 IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLG 754
Cdd:cd17655 311 IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 755 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPS-DVNTNALRAALTKELPAYMIPAYLIPL 833
Cdd:cd17655 391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEkELPVAQLREFLARELPDYMIPSYFIKL 470
|
490
....*....|....*....
gi 1238238751 834 VNMPLTLNGKLDRNALPAP 852
Cdd:cd17655 471 DEIPLTPNGKVDRKALPEP 489
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
947-1383 |
3.25e-169 |
|
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: 512.57 E-value: 3.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 947 EAELTPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDqNGHVIQFNRGInhkDHELF 1026
Cdd:cd19534 1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRRE-DGGWQQRIRGD---VEELF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1027 GLYISDWTKASLErahldEKLAAEETVIQSKMNVEKGPLLQAGLFK-TAEGDHLLIALHHLVIDGVSWRILLEDLAAAYQ 1105
Cdd:cd19534 77 RLEVVDLSSLAQA-----AAIEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1106 QALEKKEIQLPPKTdSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDienvPDKLQMNSDAAAFVLSGDWTEK 1185
Cdd:cd19534 152 QALAGEPIPLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKD----PEQTYGDARTVSFTLDEEETEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1186 LLFETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDISRTVGWFTSIYPILLDMGIPEPFEDQla 1265
Cdd:cd19534 227 LLQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDT-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1266 yrIKTTKDMLRRVPNKGTGYGLLTHIGELR------HKEPEVSFNYLGQFSEEKEVETFQLSYY-QPRYEIAGEREREYE 1338
Cdd:cd19534 305 --LKRVKEQLRRIPNKGIGYGILRYLTPEGtkrlafHPQPEISFNYLGQFDQGERDDALFVSAVgGGGSDIGPDTPRFAL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1238238751 1339 LDINALITDGRLHVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHC 1383
Cdd:cd19534 383 LDINAVVEGGQLVITVSYsRNMYHEETIQQLADSYKEALEALIEHC 428
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
3-319 |
4.03e-155 |
|
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: 475.31 E-value: 4.03e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVWREGFKT 76
Cdd:cd19531 105 RPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlagrpsPLPPLPIQYADYAVWQREWLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 156
Cdd:cd19531 185 GEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 157 GQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRN 236
Cdd:cd19531 265 GQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAHQDLPFEKLVEALQPERDLSRS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 237 PVFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEAL 316
Cdd:cd19531 345 PLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIV 424
|
...
gi 1238238751 317 STP 319
Cdd:cd19531 425 ADP 427
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
357-849 |
1.42e-146 |
|
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: 455.12 E-value: 1.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLR-AAGVGPgdVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQRELKHLISNSPESEMShifldDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGV 514
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVI-----DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 515 IVTYQNFTHAAL--AWRQIYELDRkpvrLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVM 592
Cdd:cd12117 155 AVTHRGVVRLVKntNYVTLGPDDR----VLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 593 ESTPALIipvmeyvyrNQfkLPDLDI--------LILGSDMVKAQDFKTLTDRFGqSMRIINSYGVTEATIDSSFYETSm 664
Cdd:cd12117 231 WLTAALF---------NQ--LADEDPecfaglreLLTGGEVVSPPHVRRVLAACP-GLRLVNGYGPTENTTFTTSHVVT- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 665 GGECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACW 744
Cdd:cd12117 298 ELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARW 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 745 LPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPS-DVNTNALRAALTKELPA 823
Cdd:cd12117 378 LPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEgALDAAELRAFLRERLPA 457
|
490 500
....*....|....*....|....*.
gi 1238238751 824 YMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd12117 458 YMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
6-946 |
3.27e-140 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 462.98 E-value: 3.27e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 6 DLSQA-------PLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRN---------LPALRIQYKDYAV 69
Cdd:PRK10252 107 DLQQDlrvdsgkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLrgeptpaspFTPFADVVEEYQR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 70 WREGfktgDAYKTQEAYWLKQLEGELPVLDLPAdhARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYT 149
Cdd:PRK10252 187 YRAS----EAWQRDAAFWAEQRRQLPPPASLSP--APLPGRSASADILRLKLEFTDGAFRQLAAQASGVQRPDLALALVA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 150 AFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVdklel 229
Cdd:PRK10252 261 LWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIV----- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 230 tRDMSR----NPVFDAMFILQNVEKQdIDLREIKVRpanfAHHIS---LFDITL-IATEISGSICCEMEFSTEVFLKATI 301
Cdd:PRK10252 336 -RDSGRaagdEPLFGPVLNIKVFDYQ-LDFPGVQAQ----THTLAtgpVNDLELaLFPDEHGGLSIEILANPQRYDEATL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 302 ERWADHFIEFLHEALSTPETSLAQINILSDKEKQKIvFEFNKTQVEFAqkDIPFHRIFEAKAEENPEHIAVIDNETEISY 381
Cdd:PRK10252 410 IAHAERLKALIAQFAADPALLCGDVDILLPGEYAQL-AQVNATAVEIP--ETTLSALVAQQAAKTPDAPALADARYQFSY 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 382 RLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELK 460
Cdd:PRK10252 487 REMREQVVALANLLRERGvKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQL 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 461 HLISNSPESEmshiFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTyqnftHAALAWRQIYELDRKPV- 539
Cdd:PRK10252 567 PRFADVPDLT----SLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVG-----QTAIVNRLLWMQNHYPLt 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 540 ---RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMEstpalIIPVMEYVYRNQfklPDL 616
Cdd:PRK10252 638 addVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTH-----FVPSMLAAFVAS---LTP 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 617 DILILGSDMVKaQDFKT-------LTDRFGQ--SMRIINSYGVTEATIDSSFYETS--MGGECTGDNVPIGSPLPNVHMY 685
Cdd:PRK10252 710 EGARQSCASLR-QVFCSgealpadLCREWQQltGAPLHNLYGPTEAAVDVSWYPAFgeELAAVRGSSVPIGYPVWNTGLR 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 686 VLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGY 765
Cdd:PRK10252 789 ILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQ 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 766 RIETEEIESVLLQTGLVREAA----VAVQHDKNGQAG--LAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNM 836
Cdd:PRK10252 869 RIELGEIDRAMQALPDVEQAVthacVINQAAATGGDArqLVGYLVSQSglpLDTSALQAQLRERLPPHMVPVVLLQLDQL 948
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 837 PLTLNGKLDRNALPAPNNVLSRPYTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAARLAAE-GWSMT 915
Cdd:PRK10252 949 PLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQfARQVT 1028
|
970 980 990
....*....|....*....|....*....|.
gi 1238238751 916 IRDLFRYSTIQELCghiTPLASQADQGPAEG 946
Cdd:PRK10252 1029 PGQVMVASTVAKLA---TLLDAEEDESRRLG 1056
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
367-850 |
8.19e-140 |
|
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: 435.14 E-value: 8.19e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGvGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFthAA 525
Cdd:cd17652 81 ADARPALLLTT--------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGL--AN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LAWRQIYELDRKP-VRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALI--IPV 602
Cdd:cd17652 121 LAAAQIAAFDVGPgSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALaaLPP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 603 MEyvyrnqfkLPDLDILILGSDMVKAQdfktLTDRFGQSMRIINSYGVTEATIDSsfyeTSMGGECTGDNVPIGSPLPNV 682
Cdd:cd17652 201 DD--------LPDLRTLVVAGEACPAE----LVDRWAPGRRMINAYGPTETTVCA----TMAGPLPGGGVPPIGRPVPGT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 683 HMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLGRMDYQVK 761
Cdd:cd17652 265 RVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 762 INGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPL 838
Cdd:cd17652 345 IRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPgaaPTAAELRAHLAERLPGYMVPAAFVVLDALPL 424
|
490
....*....|..
gi 1238238751 839 TLNGKLDRNALP 850
Cdd:cd17652 425 TPNGKLDRRALP 436
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
945-1402 |
1.89e-137 |
|
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: 429.45 E-value: 1.89e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 945 EGEAELTPIQRR--FFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQFNRgiNHKD 1022
Cdd:pfam00668 2 QDEYPLSPAQKRmwFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVIL--EERP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1023 HELFGLYISDWTKASLERAhldEKLAAEETvIQSKMNVEKGPLLQAGLFK-TAEGDHLLIALHHLVIDGVSWRILLEDLA 1101
Cdd:pfam00668 80 FELEIIDISDLSESEEEEA---IEAFIQRD-LQSPFDLEKGPLFRAGLFRiAENRHHLLLSMHHIIVDGVSLGILLRDLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1102 AAYQQALEKKEIQLPPKTDsYLSYADGLTQIAESKQLLSEKTYWQTILD---AHTAFLPKDIENVPDKLQMNSDAAAFvl 1178
Cdd:pfam00668 156 DLYQQLLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEgelPVLQLPKDYARPADRSFKGDRLSFTL-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1179 sGDWTEKLLFETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPE 1258
Cdd:pfam00668 233 -DEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR----PSPDIERMVGMFVNTLPLRIDPKGGK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1259 PFedqlAYRIKTTKDMLRRV-PNKGTGYGLLTHIGELRHKE-------PEVSF-NYLGQFSEEkevETFQLSYYQPRYEI 1329
Cdd:pfam00668 308 TF----SELIKRVQEDLLSAePHQGYPFGDLVNDLRLPRDLsrhplfdPMFSFqNYLGQDSQE---EEFQLSELDLSVSS 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 1330 AGEREREYELDINALITDGRLHVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELT 1402
Cdd:pfam00668 381 VIEEEAKYDLSLTASERGGGLTIKIDYnTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
3-338 |
1.02e-135 |
|
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: 424.82 E-value: 1.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELY----NNRNLPALRIQ-YKDYAVWREGFKTG 77
Cdd:pfam00668 109 SPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqqllKGEPLPLPPKTpYKDYAEWLQQYLQS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 78 DAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSG 157
Cdd:pfam00668 189 EDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 158 QEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNP 237
Cdd:pfam00668 269 QDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHP 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 238 VFDAMFILQNVEKQDI-----DLREIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFL 312
Cdd:pfam00668 349 LFDPMFSFQNYLGQDSqeeefQLSELDLSVSSVIEEEAKYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELL 428
|
330 340
....*....|....*....|....*.
gi 1238238751 313 HEALSTPETSLAQINILSDKEKQKIV 338
Cdd:pfam00668 429 EQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
359-850 |
6.00e-135 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 424.45 E-value: 6.00e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 359 FEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYP 437
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARgVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 438 KARIEYILRDSGADILLLQRELKHLISNSPESEMShifLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVT 517
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTL---LDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 518 YQNFTHAaLAW-RQIYELDRkPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTP 596
Cdd:cd17651 158 HRSLANL-VAWqARASSLGP-GARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 597 ALIIPVMEYVYRNQFKLPDL-DILILGSDMVKAQDFKTLTDRFGqSMRIINSYGVTEATIDSSfYETSMGGECTGDNVPI 675
Cdd:cd17651 236 VALRALAEHGRPLGVRLAALrYLLTGGEQLVLTEDLREFCAGLP-GLRLHNHYGPTETHVVTA-LSLPGDPAAWPAPPPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLGR 755
Cdd:cd17651 314 GRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 756 MDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAALTKELPAYMIPAYLIP 832
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGdpeAPVDAAELRAALATHLPEYMVPSAFVL 473
|
490
....*....|....*...
gi 1238238751 833 LVNMPLTLNGKLDRNALP 850
Cdd:cd17651 474 LDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
367-849 |
1.24e-134 |
|
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: 422.10 E-value: 1.24e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGvGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAA 525
Cdd:cd17643 81 ADSGPSLLLTD--------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LAWRQIYELDRKPVRLLqIASFSFDvFS-GDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVME 604
Cdd:cd17643 123 AATQRWFGFNEDDVWTL-FHSYAFD-FSvWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 605 YVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFG-QSMRIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVH 683
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGlDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 684 MYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVS-GERLYRTGDRACWLPNGTIRLLGRMDYQVKI 762
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 763 NGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLT 839
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDgaaADIAELRALLKELLPDYMVPARYVPLDALPLT 440
|
490
....*....|
gi 1238238751 840 LNGKLDRNAL 849
Cdd:cd17643 441 VNGKLDRAAL 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
356-849 |
8.76e-134 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 421.30 E-value: 8.76e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 356 HRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGvGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQRELKHlisnSPESEMSHIFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGV 514
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAA----RLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 515 IVTyqnftHAALAWRQIYELDRKPV----RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRIT 590
Cdd:cd17646 157 MVT-----HAGIVNRLLWMQDEYPLgpgdRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 591 VMESTPALIIPVMEYVYRNQfkLPDLDILILGSDMVKAQdfktLTDRFGQ--SMRIINSYGVTEATIDSSFYETSmgGEC 668
Cdd:cd17646 232 TCHFVPSMLRVFLAEPAAGS--CASLRRVFCSGEALPPE----LAARFLAlpGAELHNLYGPTEAAIDVTHWPVR--GPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 669 TGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNG 748
Cdd:cd17646 304 ETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 749 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPS----DVNTNALRAALTKELPAY 824
Cdd:cd17646 384 ALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAagaaGPDTAALRAHLAERLPEY 463
|
490 500
....*....|....*....|....*
gi 1238238751 825 MIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd17646 464 MVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
367-850 |
2.24e-132 |
|
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: 416.00 E-value: 2.24e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGvGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQRelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAA 525
Cdd:cd17649 81 EDSGAGLLLTHH-------------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LAWRQIYELdRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPAliipvmey 605
Cdd:cd17649 124 QATAERYGL-TPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPA-------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 606 vYRNQFKL----------PDLDILILGSDmvkAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGECTGDNVPI 675
Cdd:cd17649 195 -YLQQLAEeadrtgdgrpPSLRLYIFGGE---ALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLG 754
Cdd:cd17649 271 GRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 755 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQhDKNGQAGLAAYIVPSDVNTNA-----LRAALTKELPAYMIPAY 829
Cdd:cd17649 351 RVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPelraqLRTALRASLPDYMVPAH 429
|
490 500
....*....|....*....|.
gi 1238238751 830 LIPLVNMPLTLNGKLDRNALP 850
Cdd:cd17649 430 LVFLARLPLTPNGKLDRKALP 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
380-787 |
3.73e-131 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 410.89 E-value: 3.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 380 SYRLLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQR 457
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPgdRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 458 ELKHLISNSPeSEMSHIFLDDEGSFEESNCN--LNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELD 535
Cdd:TIGR01733 81 ALASRLAGLV-LPVILLDPLELAALDDAPAPppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 536 RKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQR-ITVMESTPALIIPVMEyvyRNQFKLP 614
Cdd:TIGR01733 160 PDD-RVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAA---ALPPALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 615 DLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHMYVLSQTDQIQ 694
Cdd:TIGR01733 236 SLRLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 695 PIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFV--SGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEI 772
Cdd:TIGR01733 315 PVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEI 394
|
410
....*....|....*
gi 1238238751 773 ESVLLQTGLVREAAV 787
Cdd:TIGR01733 395 EAALLRHPGVREAVV 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-939 |
2.57e-129 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 445.00 E-value: 2.57e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 5 FDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN------NRNLPALRiQYKDYAVW--REGFKT 76
Cdd:PRK05691 3364 FDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTalgegrEAQLPVPP-RYRDYIGWlqRQDLAQ 3442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GdayktqEAYWLKQLEG-ELPVLdLPADhaRPPVRSFAGDKVSFT-------LDQEVASGLHKLARENGSTLYMVLLAAY 148
Cdd:PRK05691 3443 A------RQWWQDNLRGfERPTP-IPSD--RPFLREHAGDSGGMVvgdcytrLDAADGARLRELAQAHQLTVNTFAQAAW 3513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 149 TAFLSRLSGQEDIIVGSPIAGRP--HKDLEPILGMFVNTLALRTR-PEGGKP--FVQYLQEVRETALEAFEHQDYPfeeL 223
Cdd:PRK05691 3514 ALVLRRYSGDRDVLFGVTVAGRPvsMPQMQRTVGLFINSIALRVQlPAAGQRcsVRQWLQGLLDSNMELREYEYLP---L 3590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 224 VDKLELTRDMSRNPVFDAMFILQN--VEKQDIDLreikvrpanfAHHislfditLIATEISG---------SIC------ 286
Cdd:PRK05691 3591 VAIQECSELPKGQPLFDSLFVFENapVEVSVLDR----------AQS-------LNASSDSGrthtnfpltAVCypgddl 3653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 287 -CEMEFSTEVFLKATIERWADHFIEFLHEALSTPETSLAQINILSDKEKQKIVFEFNKTQVEFAQkDIPFHRIFEAKAEE 365
Cdd:PRK05691 3654 gLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPL-EQSYVRLFEAQVAA 3732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 366 NPEHIAVIDNETEISYRLLNERANRLARTL-QNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYI 444
Cdd:PRK05691 3733 HPQRIAASCLDQQWSYAELNRAANRLGHALrAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRI 3812
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 445 LRDSGADILLL---QRELKH-LISNSPESEMSHIFL-DDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQ 519
Cdd:PRK05691 3813 IELSRTPVLVCsaaCREQARaLLDELGCANRPRLLVwEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQR 3892
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 520 NFTHAALAWRQIYELDRKPVrLLQIASFSFDV----FsgdLARTLTnGGTLIVCPDETRLEPAEIYKIIKSQRITVMEST 595
Cdd:PRK05691 3893 GMLNNQLSKVPYLALSEADV-IAQTASQSFDIsvwqF---LAAPLF-GARVEIVPNAIAHDPQGLLAHVQAQGITVLESV 3967
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 596 PALIIPVMEyvyRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsMRIINSYGVTEATIDSSFYETSMGGEcTGDNVPI 675
Cdd:PRK05691 3968 PSLIQGMLA---EDRQALDGLRWMLPTGEAMPPELARQWLQRYPQ-IGLVNAYGPAECSDDVAFFRVDLAST-RGSYLPI 4042
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPF-VSGERLYRTGDRACWLPNGTIRLLG 754
Cdd:PRK05691 4043 GSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVG 4122
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 755 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAgLAAYIVPSDVNTN------ALRAALTKELPAYMIPA 828
Cdd:PRK05691 4123 RIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKH-LVGYLVPHQTVLAqgalleRIKQRLRAELPDYMVPL 4201
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 829 YLIPLVNMPLTLNGKLDRNALPAPN--NVLSRPYTAPVNDLQKTMAYIWEDVLSMSRVGIHDSFFELGGDSIKALQVAAR 906
Cdd:PRK05691 4202 HWLWLDRLPLNANGKLDRKALPALDigQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASR 4281
|
970 980 990
....*....|....*....|....*....|....
gi 1238238751 907 L-AAEGWSMTIRDLFRYSTIQELCGHITPLASQA 939
Cdd:PRK05691 4282 VqKALQRNVPLRAMFECSTVEELAEYIEGLAGSA 4315
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
356-850 |
4.55e-129 |
|
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: 407.59 E-value: 4.55e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 356 HRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:cd17644 3 HQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGvKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGV 514
Cdd:cd17644 83 NYPQERLTYILEDAQISVLLTQ--------------------------------------PENLAYVIYTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 515 IVTYQ---NFTHAALAWRQIYELDRkpvrLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITV 591
Cdd:cd17644 125 MIEHQslvNLSHGLIKEYGITSSDR----VLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 592 MESTPALIIPVMEYVYRNQFKLPD-LDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGECTG 670
Cdd:cd17644 201 LSLPPAYWHLLVLELLLSTIDLPSsLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 671 DNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVS--GERLYRTGDRACWLPNG 748
Cdd:cd17644 281 TSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 749 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAALTKELPAYM 825
Cdd:cd17644 361 NIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPhyeESPSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....*
gi 1238238751 826 IPAYLIPLVNMPLTLNGKLDRNALP 850
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
367-849 |
3.77e-126 |
|
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: 399.74 E-value: 3.77e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARgVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQRELKH-LISNSPESEmsHIFLDDEGSFEesncNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHA 524
Cdd:cd12116 81 EDAEPALVLTDDALPDrLPAGLPVLL--LALAAAAAAPA----APRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 525 ALAWRQiyELDRKPV-RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVM 603
Cdd:cd12116 155 LHSMRE--RLGLGPGdRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 604 EYVYRNqfkLPDLDILILGsdmvKAQDfKTLTDRF-GQSMRIINSYGVTEATIDSSFyeTSMGGECTGdnVPIGSPLPNV 682
Cdd:cd12116 233 DAGWQG---RAGLTALCGG----EALP-PDLAARLlSRVGSLWNLYGPTETTIWSTA--ARVTAAAGP--IPIGRPLANT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 683 HMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFV-SGERLYRTGDRACWLPNGTIRLLGRMDYQVK 761
Cdd:cd12116 301 QVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 762 INGYRIETEEIESVLLQTGLVREAAVAVQHDkNGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPL 838
Cdd:cd12116 381 IRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAgaaPDAAALRAHLRATLPAYMVPSAFVRLDALPL 459
|
490
....*....|.
gi 1238238751 839 TLNGKLDRNAL 849
Cdd:cd12116 460 TANGKLDRKAL 470
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
367-850 |
2.74e-125 |
|
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: 398.00 E-value: 2.74e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGvKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQRELKhlisNSPESEMSHIFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAa 525
Cdd:cd17656 82 LDSGVRVVLTQRHLK----SKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVM-E 604
Cdd:cd17656 157 LHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFsE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 605 YVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRiiNSYGVTEATIDSSfYETSMGGECTgDNVPIGSPLPNVHM 684
Cdd:cd17656 237 REFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLH--NHYGPSETHVVTT-YTINPEAEIP-ELPPIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 685 YVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKING 764
Cdd:cd17656 313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 765 YRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVP-SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGK 843
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMeQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
....*..
gi 1238238751 844 LDRNALP 850
Cdd:cd17656 473 VDRKALP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
356-850 |
2.68e-118 |
|
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: 377.67 E-value: 2.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 356 HRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNrKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRG-KGVKPddQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHYPKARIEYILRDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKG 513
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILLTN--------------------------------------PDDLAYVIYTSGSTGLPKG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 514 VIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVme 593
Cdd:cd17645 122 VMIEHHNLVNLCEWHRPYFGVTPAD-KSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITI-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 594 stPALIIPVMEyvyrnQFKLPD---LDILILGSDMVKAQDFKtltdrfgqSMRIINSYGVTEATIDSSFYETsmggECTG 670
Cdd:cd17645 199 --SFLPTGAAE-----QFMQLDnqsLRVLLTGGDKLKKIERK--------GYKLVNNYGPTENTVVATSFEI----DKPY 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 671 DNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTI 750
Cdd:cd17645 260 ANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 751 RLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV-PSDVNTNALRAALTKELPAYMIPAY 829
Cdd:cd17645 340 EFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTaPEEIPHEELREWLKNDLPDYMIPTY 419
|
490 500
....*....|....*....|.
gi 1238238751 830 LIPLVNMPLTLNGKLDRNALP 850
Cdd:cd17645 420 FVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
356-849 |
7.02e-112 |
|
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: 361.47 E-value: 7.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 356 HRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:cd05918 2 HDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGvGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLlqrelkhlisnspesemshiflddegsfeesncnlnlSPAPEEPVYIIYTSGTTGAPKGV 514
Cdd:cd05918 82 SHPLQRLQEILQDTGAKVVL-------------------------------------TSSPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 515 IVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEpaEIYKIIKSQRITVMES 594
Cdd:cd05918 125 VIEHRALSTSALAHGRALGLTSES-RVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 595 TP---ALIIPVmeyvyrnqfKLPDLDILILGSDMVKAQDfktlTDRFGQSMRIINSYGVTEATIDSSFYETSMGGECTgd 671
Cdd:cd05918 202 TPsvaRLLDPE---------DVPSLRTLVLGGEALTQSD----VDTWADRVRLINAYGPAECTIAATVSPVVPSTDPR-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 672 NvpIGSPLPnVHMYVLSQ--TDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENP-------FVSGERLYRTGDRA 742
Cdd:cd05918 267 N--IGRPLG-ATCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 743 CWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ---TGLVREAAVAVQHDKNGQAGLAAYIVPSDVNTN-------- 811
Cdd:cd05918 344 RYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQslpGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGsgdgdslf 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1238238751 812 ------------ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05918 424 lepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
367-850 |
3.00e-111 |
|
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: 359.02 E-value: 3.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYI 444
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDdlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 445 LRDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHA 524
Cdd:cd17648 81 LEDTGARVVITN--------------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 525 ALAWRQIYEL-DRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIipvM 603
Cdd:cd17648 123 RTSLSERYFGrDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVL---Q 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 604 EYVYRnqfKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINSYGVTEATIDS--SFYETSMGGECTgdnvpIGSPLPN 681
Cdd:cd17648 200 QYDLA---RLPHLKRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNhkRFFPGDQRFDKS-----LGRPVRN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 682 VHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGE--------RLYRTGDRACWLPNGTIRLL 753
Cdd:cd17648 270 TKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 754 GRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN-----GQAGLAAYIVPSD--VNTNALRAALTKELPAYMI 826
Cdd:cd17648 350 GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPghVPESDLLSFLRAKLPRYMV 429
|
490 500
....*....|....*....|....
gi 1238238751 827 PAYLIPLVNMPLTLNGKLDRNALP 850
Cdd:cd17648 430 PARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
357-849 |
1.86e-110 |
|
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: 355.85 E-value: 1.86e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTL-QNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLlQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 YPKARIEYILRDSGADILLlqrelkhlisnspesemshiflddegsfeesnCNlnlsPAPEEPVYIIYTSGTTGAPKGVI 515
Cdd:cd17653 81 LPSARIQAILRTSGATLLL--------------------------------TT----DSPDDLAYIIFTSGSTGIPKGVM 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 516 VTYQNFTHAALAWRqiYELDRKP-VRLLQIASFSFDVFSGDLARTLTNGGTLIVcpdetRLEPAEIYKIIKSqrITVMES 594
Cdd:cd17653 125 VPHRGVLNYVSQPP--ARLDVGPgSRVAQVLSIAFDACIGEIFSTLCNGGTLVL-----ADPSDPFAHVART--VDALMS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 595 TPALI--IPVMEYvyrnqfklPDLDILILGSDMVKAqdfkTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGgectgDN 672
Cdd:cd17653 196 TPSILstLSPQDF--------PNLKTIFLGGEAVPP----SLLDRWSPGRRLYNAYGPTECTISSTMTELLPG-----QP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 673 VPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRL 752
Cdd:cd17653 259 VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 753 LGRMDYQVKINGYRIETEEIESVLLQT-GLVREAAvAVQHDKNgqagLAAYIVPSDVNTNALRAALTKELPAYMIPAYLI 831
Cdd:cd17653 339 LGREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAA-AIVVNGR----LVAFVTPETVDVDGLRSELAKHLPSYAVPDRII 413
|
490
....*....|....*...
gi 1238238751 832 PLVNMPLTLNGKLDRNAL 849
Cdd:cd17653 414 ALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
367-849 |
8.10e-109 |
|
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: 353.11 E-value: 8.10e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTL-QNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALkAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQRELKHLisNSPESEMSHIFLDDEGSFEEsncNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAA 525
Cdd:cd12114 81 ADAGARLVLTDGPDAQL--DVAVFDVLILDLDALAAPAP---PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LAWRQIYELDRKPvRLLQIASFSFD--VFsgDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPALIIPVM 603
Cdd:cd12114 156 LDINRRFAVGPDD-RVLALSSLSFDlsVY--DIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 604 EYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETsmgGECTGD--NVPIGSPLPN 681
Cdd:cd12114 233 DVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDA-RLISLGGATEASIWSIYHPI---DEVPPDwrSIPYGRPLAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 682 VHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPfvSGERLYRTGDRACWLPNGTIRLLGRMDYQVK 761
Cdd:cd12114 309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 762 INGYRIETEEIESVLLQTGLVReAAVAVQHDKNGQAGLAAYIVP-SDVNT---NALRAALTKELPAYMIPAYLIPLVNMP 837
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVA-RAVVVVLGDPGGKRLAAFVVPdNDGTPiapDALRAFLAQTLPAYMIPSRVIALEALP 465
|
490
....*....|..
gi 1238238751 838 LTLNGKLDRNAL 849
Cdd:cd12114 466 LTANGKVDRAAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
356-849 |
4.47e-106 |
|
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: 344.30 E-value: 4.47e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 356 HRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:cd12115 2 HDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGvGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQrelkhlisnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGV 514
Cdd:cd12115 82 AYPPERLRFILEDAQARLVLTD--------------------------------------PDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 515 IVTYQNfTHAALAW-RQIYELDrKPVRLLQIASFSFD--VFsgDLARTLTNGGTLIVCPDETRL--EPAEiykiiksQRI 589
Cdd:cd12115 124 AIEHRN-AAAFLQWaAAAFSAE-ELAGVLASTSICFDlsVF--ELFGPLATGGKVVLADNVLALpdLPAA-------AEV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 590 TVMESTPALIIPVMEyvyrnQFKLP-DLDILILGSDMVKAQDFKTLTDRfGQSMRIINSYGVTEATIDSSFYETSMGGEc 668
Cdd:cd12115 193 TLINTVPSAAAELLR-----HDALPaSVRVVNLAGEPLPRDLVQRLYAR-LQVERVVNLYGPSEDTTYSTVAPVPPGAS- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 669 tgDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNG 748
Cdd:cd12115 266 --GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 749 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKELPAYM 825
Cdd:cd12115 344 LLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPgaaGLVEDLRRHLGTRLPAYM 423
|
490 500
....*....|....*....|....
gi 1238238751 826 IPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd12115 424 VPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
363-849 |
1.32e-103 |
|
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: 337.68 E-value: 1.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKPT-VAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARI 441
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDpVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 442 EYILRDSGADILLLqrelkhlisnspesemshiflddegsfeesncnlnlspAPEEPVYIIYTSGTTGAPKGVIVTYQNF 521
Cdd:cd05945 81 REILDAAKPALLIA--------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 522 tHAALAWrqiyELDRKPV----RLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPA 597
Cdd:cd05945 123 -VSFTNW----MLSDFPLgpgdVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 598 LIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYE---TSMGGEctgDNVP 674
Cdd:cd05945 198 FAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVTYIEvtpEVLDGY---DRLP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 675 IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPfvsGERLYRTGDRACWLPNGTIRLLG 754
Cdd:cd05945 274 IGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 755 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD----VNTNALRAALTKELPAYMIPAYL 830
Cdd:cd05945 351 RLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgaeaGLTKAIKAELAERLPPYMIPRRF 430
|
490
....*....|....*....
gi 1238238751 831 IPLVNMPLTLNGKLDRNAL 849
Cdd:cd05945 431 VYLDELPLNANGKIDRKAL 449
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
355-851 |
4.54e-98 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 322.53 E-value: 4.54e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 355 FHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPI 432
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPgdRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 433 DAHYPKARIEYILRDSGADILLLqrelkhlisnspesemshiflddegsfeesncnlnlspapeepVYIIYTSGTTGAPK 512
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT-------------------------------------------ALILYTSGTTGRPK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 513 GVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFDV-FSGDLARTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITV 591
Cdd:COG0318 117 GVMLTHRNLLANAAAIAAALGLTPGD-VVLVALPLFHVFgLTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 592 MESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMGGECTGd 671
Cdd:COG0318 193 LFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPGERRPG- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 672 nvPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTEnpfvsgeRLYRTGDRACWLPNGTIR 751
Cdd:COG0318 270 --SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-------GWLRTGDLGRLDEDGYLY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 752 LLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNALRAALTKELPAYMIP 827
Cdd:COG0318 341 IVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVvGVPDEKWGER-VVAFVVLrpgAELDAEELRAFLRERLARYKVP 419
|
490 500
....*....|....*....|....
gi 1238238751 828 AYLIPLVNMPLTLNGKLDRNALPA 851
Cdd:COG0318 420 RRVEFVDELPRTASGKIDRRALRE 443
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
4-319 |
2.12e-95 |
|
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: 314.36 E-value: 2.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 4 PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVW-REGFkt 76
Cdd:cd19540 101 GFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARragrapDWAPLPVQYADYALWqRELL-- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDA------YKTQEAYWLKQLEGeLP-VLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYT 149
Cdd:cd19540 179 GDEddpdslAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 150 AFLSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLEL 229
Cdd:cd19540 258 VLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPFERLVEALNP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 230 TRDMSRNPVFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFDITLIATE------ISGSICCEMEFSTEVFLKATIER 303
Cdd:cd19540 338 PRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGLTGELEYATDLFDRSTAER 417
|
330
....*....|....*.
gi 1238238751 304 WADHFIEFLHEALSTP 319
Cdd:cd19540 418 LADRFVRVLEAVVADP 433
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
359-762 |
1.53e-92 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 305.78 E-value: 1.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 359 FEAKAEENPEHIAVIDNETE-ISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHY 436
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGvGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 437 PKARIEYILRDSGADILLLQRELKHLISNSPESEMSHI----------FLDDEGSFEESNCNLNL-----SPAPEEPVYI 501
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVklvlvldrdpVLKEEPLPEEAKPADVPpppppPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 502 IYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPV---RLLQIASFSFDV-FSGDLARTLTNGGTLIVCPDETRLEP 577
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpddRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 578 AEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINSYGVTEATIDS 657
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG--ALVNGYGLTETTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 658 SFYETSMGGECTGDnvPIGSPLPNVHMYVLSQ-TDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTEnpfvsgERLY 736
Cdd:pfam00501 319 TTPLPLDEDLRSLG--SVGRPLPGTEVKIVDDeTGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
|
410 420
....*....|....*....|....*.
gi 1238238751 737 RTGDRACWLPNGTIRLLGRMDYQVKI 762
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
356-849 |
3.78e-89 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 299.12 E-value: 3.78e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 356 HRIFEAkAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKPT-VAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:PRK04813 6 ETIEEF-AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSpIIVFGHMSPEMLATFLGAVKAGHAYIPVDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQRELKHLISNSP---ESEMSHIFLDDEgSFEESNCnlnlsPAPEEPVYIIYTSGTTGAP 511
Cdd:PRK04813 85 SSPAERIEMIIEVAKPSLIIATEELPLEILGIPvitLDELKDIFATGN-PYDFDHA-----VKGDDNYYIIFTSGTTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 512 KGVIVTYQN---FTHAALawrQIYELDRKPVRLLQiASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQR 588
Cdd:PRK04813 159 KGVQISHDNlvsFTNWML---EDFALPEGPQFLNQ-APYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 589 ITVMESTPALI-IPVMEYVYrNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGE 667
Cdd:PRK04813 235 INVWVSTPSFAdMCLLDPSF-NEEHLPNLTHFLFCGEELPHKTAKKLLERFPSA-TIYNTYGPTEATVAVTSIEITDEML 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 668 CTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTEnpfVSGERLYRTGDRAcWLPN 747
Cdd:PRK04813 313 DQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAG-YLED 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 748 GTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREaAVAVQHDKNGQA-GLAAYIVPSDVN-------TNALRAALTK 819
Cdd:PRK04813 389 GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVES-AVVVPYNKDHKVqYLIAYVVPKEEDferefelTKAIKKELKE 467
|
490 500 510
....*....|....*....|....*....|
gi 1238238751 820 ELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK04813 468 RLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
356-849 |
1.00e-86 |
|
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: 292.43 E-value: 1.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 356 HRIFEAkAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRKGP-KPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:TIGR01734 4 EAIQAF-AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPkKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQRELKhliSNSPESEMshIFLDDEGSFEESNCNLNLSPA--PEEPVYIIYTSGTTGAPK 512
Cdd:TIGR01734 83 SIPSERIEMIIEAAGPELVIHTAELS---IDAVGTQI--ITLSALEQAETSGGPVSFDHAvkGDDNYYIIYTSGSTGNPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 513 GVIVTYQN---FTHAALawrQIYELDRKPVRLLQiASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRI 589
Cdd:TIGR01734 158 GVQISHDNlvsFTNWML---ADFPLSEGKQFLNQ-APFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 590 TVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFgQSMRIINSYGVTEATIDSSFYETSMGGECT 669
Cdd:TIGR01734 234 NVWVSTPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERF-PKATIYNTYGPTEATVAVTSVKITQEILDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 670 GDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTenpFVSGERLYRTGDRACwLPNGT 749
Cdd:TIGR01734 313 YPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGT-ITDGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 750 IRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQ-AGLAAYIVPSDVN-------TNALRAALTKEL 821
Cdd:TIGR01734 389 LFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPETEDfekefqlTKAIKKELKKSL 468
|
490 500
....*....|....*....|....*...
gi 1238238751 822 PAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:TIGR01734 469 PAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
4-319 |
9.90e-85 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 284.16 E-value: 9.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 4 PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVWREGFKTG 77
Cdd:cd19538 101 PFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELAPLPVQYADYALWQQELLGD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 78 DAYKT-----QEAYWLKQLEGeLPV-LDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAF 151
Cdd:cd19538 181 ESDPDsliarQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAAL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 152 LSRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTR 231
Cdd:cd19538 260 LTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAYEHQDIPFERLVEALNPTR 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 232 DMSRNPVFDAMFILQNVEKQDIDLREIkvrPANFAHH---ISLFDITL-----IATEISGSICCEMEFSTEVFLKATIER 303
Cdd:cd19538 340 SRSRHPLFQIMLALQNTPQPSLDLPGL---EAKLELRtvgSAKFDLTFelreqYNDGTPNGIEGFIEYRTDLFDHETIEA 416
|
330
....*....|....*.
gi 1238238751 304 WADHFIEFLHEALSTP 319
Cdd:cd19538 417 LAQRYLLLLESAVENP 432
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
87-952 |
7.38e-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: 280.80 E-value: 7.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 87 WLKQLEGeLPVLDLPADHARPPVRSFAGDKVSFTLDQEVAsglhklARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSp 166
Cdd:TIGR03443 2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 167 iagRPHKDLEPilgmfvntLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPVFdamFILQ 246
Cdd:TIGR03443 74 ---SSNKSGRP--------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPL---FRLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 247 NVEKQDIDLReikvrpaNFAHHiSLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEALSTPETSLAQI 326
Cdd:TIGR03443 140 FQDAPDNQQT-------TYSTG-STTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 327 NILSDKEKQkiVFEFNKTQVEFAQKDIPFHRIFEAKAEENPEHIAVIDNET---------EISYRLLNERANRLARTLQN 397
Cdd:TIGR03443 212 SLITPSQKS--LLPDPTKDLDWSGFRGAIHDIFADNAEKHPDRTCVVETPSfldpssktrSFTYKQINEASNILAHYLLK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 398 rKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKAR-IEYI----------LRDSGAdillLQRELKHLIS 464
Cdd:TIGR03443 290 -TGIKRgdVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYLsvakpralivIEKAGT----LDQLVRDYID 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 465 NSPE--SEMSHIFLDDEGSFE----ESNCNLNLSP-------------APEEPVYIIYTSGTTGAPKGVIvtyqnFTHAA 525
Cdd:TIGR03443 365 KELElrTEIPALALQDDGSLVggslEGGETDVLAPyqalkdtptgvvvGPDSNPTLSFTSGSEGIPKGVL-----GRHFS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LA----WR-QIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPAL-- 598
Cdd:TIGR03443 440 LAyyfpWMaKRFGLSEND-KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMgq 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 599 --------IIPVMeyvyRNQFKLPDldILIlGSDMVKAQdfkTLtdrfGQSMRIINSYGVTEATIDSSFYE-TSMGGECT 669
Cdd:TIGR03443 519 llsaqattPIPSL----HHAFFVGD--ILT-KRDCLRLQ---TL----AENVCIVNMYGTTETQRAVSYFEiPSRSSDST 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 670 -----GDNVPIGSPLPNVHMYVLSQTDQIQPIGVA--GELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGE--------- 733
Cdd:TIGR03443 585 flknlKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldken 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 734 -------------RLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLA 800
Cdd:TIGR03443 665 nkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLV 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 801 AYIVP-----------SDVNTNA------------------LRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPA 851
Cdd:TIGR03443 745 SYIVPqdksdeleefkSEVDDEEssdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPF 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 852 PNNV-------LSRPYTAP--VNDLQKTMAYIWEDVLSM--SRVGIHDSFFELGGDSI----------KALQVAARLAAe 910
Cdd:TIGR03443 825 PDTAqlaavakNRSASAADeeFTETEREIRDLWLELLPNrpATISPDDSFFDLGGHSIlatrmifelrKKLNVELPLGL- 903
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*
gi 1238238751 911 gwsmtirdLFRYSTIQELCGHITPLAS---QADQGPAEGEAELTP 952
Cdd:TIGR03443 904 --------IFKSPTIKGFAKEVDRLKKgeeLADEGDSEIEEEETV 940
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
4-319 |
3.52e-68 |
|
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: 236.51 E-value: 3.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 4 PFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVWREGFKTG 77
Cdd:cd19539 106 GFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARrkgpaaPLPELRQQYKEYAAWQREALAA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 78 DAYKTQEAYWLKQLEGeLPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSG 157
Cdd:cd19539 186 PRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 158 QEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNP 237
Cdd:cd19539 265 QTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELPVDRDAGRHP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 238 VFDAMFILQNVEKQDIDLR-EIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEAL 316
Cdd:cd19539 345 LVQIVFQVTNAPAGELELAgGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLL 424
|
...
gi 1238238751 317 STP 319
Cdd:cd19539 425 ANP 427
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
1263-1409 |
1.61e-61 |
|
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: 207.13 E-value: 1.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1263 QLAYRIKTTKDMLRRVPNKGTGYGLLTHIGELRHK-----EPEVSFNYLGQFSEEKEVETFQLSYYQPRYEIAGEREREY 1337
Cdd:TIGR01720 1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKlaaspQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRPY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 1338 ELDINALITDGRLHVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHCSQKKAREKTLSDFSNKELTLSALSSI 1409
Cdd:TIGR01720 81 ALEINAMIEDGELTLTWSYpTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
497-845 |
2.35e-59 |
|
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: 207.91 E-value: 2.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 497 EPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVrLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLE 576
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDV-FLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 577 PAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATID 656
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 657 SSFYETSMGGECTGDnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQmkftenpFVSGERLY 736
Cdd:cd04433 155 VATGPPDDDARKPGS---VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA-------AVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 737 RTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNA 812
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVvGVPDPEWGER-VVAVVVLrpgADLDAEE 303
|
330 340 350
....*....|....*....|....*....|...
gi 1238238751 813 LRAALTKELPAYMIPAYLIPLVNMPLTLNGKLD 845
Cdd:cd04433 304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3-319 |
3.99e-58 |
|
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: 207.55 E-value: 3.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELY-------NNRNLPALRIqYKDYAVWREGFK 75
Cdd:cd20484 101 EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqallqgkQPTLASSPAS-YYDFVAWEQDML 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 76 TGDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRL 155
Cdd:cd20484 180 AGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRY 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 156 SGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSR 235
Cdd:cd20484 260 TGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPRSQAN 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 236 NPVFDAMFILQNVeKQDIDLREIKVRPANF--------AHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADH 307
Cdd:cd20484 340 SPVFQVAFFYQNF-LQSTSLQQFLAEYQDVlsiefvegIHQEGEYELVLEVYEQEDRFTLNIKYNPDLFDASTIERMMEH 418
|
330
....*....|..
gi 1238238751 308 FIEFLHEALSTP 319
Cdd:cd20484 419 YVKLAEELIANP 430
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
355-851 |
7.88e-58 |
|
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: 209.25 E-value: 7.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 355 FHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRkGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPI 432
Cdd:TIGR03098 2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGL-GLARGerVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 433 DAHYPKARIEYILRDSGADILLLQRELKHLISNSPES--EMSHIFLDDEGS-------FEESNC---NLNLSPA------ 494
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGchDLRTLIIVGDPAhaseghpGEEPASwpkLLALGDAdpphpv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 -PEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELdRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVcpdET 573
Cdd:TIGR03098 161 iDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLEN-RPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVL---HD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 574 RLEPAEIYKIIKSQRITVMESTPaliiPVMEYVYRNQFKLPDLDILIL----GSDMVKAQdFKTLTDRFGQSmRIINSYG 649
Cdd:TIGR03098 237 YLLPRDVLKALEKHGITGLAAVP----PLWAQLAQLDWPESAAPSLRYltnsGGAMPRAT-LSRLRSFLPNA-RLFLMYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 650 VTEAtidssFYETSMGGECTgDNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTEN 727
Cdd:TIGR03098 311 LTEA-----FRSTYLPPEEV-DRRPdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 728 P-FVSGERLYRT----GDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAA 801
Cdd:TIGR03098 385 PpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfGVPDPTLGQA-IVL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 802 YIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPA 851
Cdd:TIGR03098 464 VVTPPGgeeLDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2-312 |
3.04e-56 |
|
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: 201.87 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 2 IKPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN-----NRNLPALRIQYKDYAVWREGFKT 76
Cdd:cd19066 103 QTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDaaerqKPTLPPPVGSYADYAAWLEKQLE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 156
Cdd:cd19066 183 SEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARESGTTPTQLLLAAFALALKRLT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 157 GQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRN 236
Cdd:cd19066 263 ASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEHQRVPFIELVRHLGVVPEAPKH 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 237 PVFDAMFILQNVEKQDIDLREIKVRPANFAHHI-SLFDITLIATEIS-GSICCEMEFSTEVFLKATIERWADHFIEFL 312
Cdd:cd19066 343 PLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEgTVFDLDLEASEDPdGDLLLRLEYSRGVYDERTIDRFAERYMTAL 420
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
3-312 |
2.11e-52 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. 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: 190.93 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNN-------RNLPALRIQYKDYAVWREGFK 75
Cdd:cd20483 103 QELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlragrdlATVPPPPVQYIDFTLWHNALL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 76 TGDAYKTQEAYWLKQLEGELPVLD-LP-ADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLS 153
Cdd:cd20483 183 QSPLVQPLLDFWKEKLEGIPDASKlLPfAKAERPPVKDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLY 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 154 RLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDM 233
Cdd:cd20483 263 RYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPFDYIVDALDVPRST 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 234 SRNPVFDAMFILQ------NVEKQDIDLREIK---VRPAnfahhislFDITLIATEI-SGSICCEMEFSTEVFLKATIER 303
Cdd:cd20483 343 SHFPIGQIAVNYQvhgkfpEYDTGDFKFTDYDhydIPTA--------CDIALEAEEDpDGGLDLRLEFSTTLYDSADMER 414
|
....*....
gi 1238238751 304 WADHFIEFL 312
Cdd:cd20483 415 FLDNFVTFL 423
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
950-1383 |
1.10e-51 |
|
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: 188.77 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 950 LTPIQRRFFgqvhaFHY-------HYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDqNGHVIQFNRGinhkD 1022
Cdd:cd19066 4 LSPMQRGMW-----FLKklatdpsAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLD----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1023 HELFGLYISDWTKASLERAHLDEKLAAeetVIQSKMNVEKGPLLQAGLFKTA-EGDHLLIALHHLVIDGVSWRILLEDLA 1101
Cdd:cd19066 74 TVRFRIEIIDLRNLADPEARLLELIDQ---IQQTIYDLERGPLVRVALFRLAdERDVLVVAIHHIIVDGGSFQILFEDIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1102 AAYQQALEKKEIqLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIENVPDKLQMNSDAAA-FVLSG 1180
Cdd:cd19066 151 SVYDAAERQKPT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLeFFLRS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1181 DWTEKLLfETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPF 1260
Cdd:cd19066 230 EETKRLR-EVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDTSPDATF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1261 EdqlaYRIKTTKDMLRRVPNKGTGYG--LLTHIGELR----HKEPEVSFNYLGQFSEEKEVETFQLSyyqpRYEIAGERE 1334
Cdd:cd19066 305 P----ELLKRTKEQSREAIEHQRVPFieLVRHLGVVPeapkHPLFEPVFTFKNNQQQLGKTGGFIFT----TPVYTSSEG 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1238238751 1335 REYELDINALI-TDGRLHVKAVY-TQVFSKHSIECFMDRFHRHLIETIEHC 1383
Cdd:cd19066 377 TVFDLDLEASEdPDGDLLLRLEYsRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
357-849 |
1.25e-50 |
|
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: 186.61 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGvQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 YPKARIEYILRDSGADILLLQRELKHLISNSPESEMSHIflddegsfeesncnlnlsPAPEEPVYIIYTSGTTGAPKGVI 515
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA------------------LTPEDVAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 516 VTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLT--NGGTLIVCPdetRLEPAEIYKIIKSQRITVME 593
Cdd:cd05936 145 LTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPlaLGATIVLIP---RFRPIGVLKEIRKHRVTIFP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 594 STPALIIPVMEYVYRNQFKLPDLDILILGSD--MVK-AQDFKTLTDrfgqsMRIINSYGVTeatidssfyETSMGGEC-- 668
Cdd:cd05936 222 GVPTMYIALLNAPEFKKRDFSSLRLCISGGAplPVEvAERFEELTG-----VPIVEGYGLT---------ETSPVVAVnp 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 669 -TGDNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLtqmkfTENPFVSGerLYRTGDRACWL 745
Cdd:cd05936 288 lDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE-----TAEAFVDG--WLRTGDIGYMD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 746 PNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAgLAAYIVPSD---VNTNALRAALTKEL 821
Cdd:cd05936 361 EDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGEA-VKAFVVLKEgasLTEEEIIAFCREQL 439
|
490 500
....*....|....*....|....*...
gi 1238238751 822 PAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05936 440 AGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
3-141 |
9.66e-50 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 176.77 E-value: 9.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR------NLPALRIQYKDYAVWREGFKT 76
Cdd:COG4908 99 RPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALlegeppPLPELPIQYADYAAWQRAWLQ 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 77 GDAYKTQEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLY 141
Cdd:COG4908 179 SEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKAHGATVN 243
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
5-243 |
3.16e-49 |
|
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: 181.12 E-value: 3.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 5 FDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPALRIQYKDYAVW-REGFKTGdAYKTQ 83
Cdd:cd19532 103 YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQYLDFAARqRQDYESG-ALDED 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 84 EAYWLKQLEGE---LPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQED 160
Cdd:cd19532 182 LAYWKSEFSTLpepLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 161 IIVGspI--AGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRDMSRNPV 238
Cdd:cd19532 262 ICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPL 339
|
....*
gi 1238238751 239 FDAMF 243
Cdd:cd19532 340 FQVFI 344
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
377-852 |
1.01e-48 |
|
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: 182.72 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 377 TEISYRLLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARieyilrdsgADIL 453
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKtgiKRGD--VVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR---------QNIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 454 LLQRELKHLISnspesemshifLDDEGSFEESNCNLNLSpapeepvyiiYTSGTTGAPKGVIvtyqnFTHAALAwrqiYE 533
Cdd:cd17647 88 LGVAKPRGLIV-----------IRAAGVVVGPDSNPTLS----------FTSGSEGIPKGVL-----GRHFSLA----YY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 534 LDRKPVRLLQIASFSFDVFSG--------DLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPAliipvMEY 605
Cdd:cd17647 138 FPWMAKRFNLSENDKFTMLSGiahdpiqrDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPA-----MGQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 606 VYRNQF--KLPDLDILILGSDMVKAQDFKTLtDRFGQSMRIINSYGVTEATIDSSFYE-TSMGGECT-----GDNVPIGS 677
Cdd:cd17647 213 LLTAQAttPFPKLHHAFFVGDILTKRDCLRL-QTLAENVRIVNMYGTTETQRAVSYFEvPSRSSDPTflknlKDVMPAGR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 678 PLPNVHMYVLSQTD--QIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVSGE---------------------- 733
Cdd:cd17647 292 GMLNVQLLVVNRNDrtQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprd 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 734 RLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVN---- 809
Cdd:cd17647 372 RLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKpdde 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 810 --------------------------TNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAP 852
Cdd:cd17647 452 sfaqedvpkevstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
370-849 |
6.91e-48 |
|
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: 178.05 E-value: 6.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 370 IAVIDNETEISYRLLNERANRLARTLQNRKGPKP-TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDS 448
Cdd:cd17654 8 IDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEErAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 449 GADILLLQRELkhliSNSPESEMShiflddegsfEESNCNLnlsPAPEEPVYIIYTSGTTGAPKGVIVTYQ----NFTHA 524
Cdd:cd17654 88 HVSYLLQNKEL----DNAPLSFTP----------EHRHFNI---RTDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 525 ALawrqiyELDRKPVRLLQIASF-SFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKII-KSQRITVMESTPALI--I 600
Cdd:cd17654 151 RS------LFNITSEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFrrF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 601 PVMEYVYRNQFKLPDLDILILG-----SDMVkaqdFKTLTDRFGQSmRIINSYGVTEATIDSSFYETSMGGEctgdNVPI 675
Cdd:cd17654 225 GSQSIKSTVLSATSSLRVLALGgepfpSLVI----LSSWRGKGNRT-RIFNIYGITEVSCWALAYKVPEEDS----PVQL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 GSPLPNVHMYVLSQTDQIQpigvAGELCIGGagVAKGYHHKPDLTQMKFTenpfvsgerLYRTGDRaCWLPNGTIRLLGR 755
Cdd:cd17654 296 GSPLLGTVIEVRDQNGSEG----TGQVFLGG--LNRVCILDDEVTVPKGT---------MRATGDF-VTVKDGELFFLGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 756 MDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNgqagLAAYIVPSDVNTNALRAALTKELPAYMIPAYLIPLVN 835
Cdd:cd17654 360 KDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR----LIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDK 435
|
490
....*....|....
gi 1238238751 836 MPLTLNGKLDRNAL 849
Cdd:cd17654 436 LPLTSHGKVDKSEL 449
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
363-849 |
3.35e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 177.79 E-value: 3.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKA 439
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAAlgiGKGDR--VAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 440 RIEYILRDSGADILLLQRE--------------LKHLISNSPESEMSHIflDDEGSFEE---SNCNLNLSPA--PEEPVY 500
Cdd:PRK07656 93 EAAYILARGDAKALFVLGLflgvdysattrlpaLEHVVICETEEDDPHT--EKMKTFTDflaAGDPAERAPEvdPDDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 IIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFsFDVF---SGDLArTLTNGGTLIVCPdetRLEP 577
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGD-RYLAANPF-FHVFgykAGVNA-PLMRGATILPLP---VFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 578 AEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMrIINSYGVTEAT--- 654
Cdd:PRK07656 245 DEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDI-VLTGYGLSEASgvt 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 655 ----IDSSFyetsmggectgDNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENP 728
Cdd:PRK07656 324 tfnrLDDDR-----------KTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 729 FvsgerLYrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGlAAYIVP-- 805
Cdd:PRK07656 393 W-----LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAViGVPDERLGEVG-KAYVVLkp 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1238238751 806 -SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK07656 466 gAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
3-319 |
9.71e-47 |
|
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: 173.93 E-value: 9.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN------NRNLPALRiQYKDYAVWREGFKT 76
Cdd:cd19543 106 RGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalgegqPPSLPPVR-PYRDYIAWLQRQDK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 77 GDAyktqEAYWLKQLEG--ELPVldLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSR 154
Cdd:cd19543 185 EAA----EAYWREYLAGfeEPTP--LPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 155 LSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELvdkleLTRD 232
Cdd:cd19543 259 YSGRDDVVFGTTVSGRPAelPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHEYVPLYEI-----QAWS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 233 MSRNPVFDAMFILQN--------VEKQDIDLREIKVRPANFAHhislFDITLIATEiSGSICCEMEFSTEVFLKATIERW 304
Cdd:cd19543 334 EGKQALFDHLLVFENypvdesleEEQDEDGLRITDVSAEEQTN----YPLTVVAIP-GEELTIKLSYDAEVFDEATIERL 408
|
330
....*....|....*
gi 1238238751 305 ADHFIEFLHEALSTP 319
Cdd:cd19543 409 LGHLRRVLEQVAANP 423
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
361-1265 |
1.90e-46 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 184.60 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 361 AKAEENPEHIAVI------DNETEISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIda 434
Cdd:PRK05691 17 RRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 hYP--------KARIEYILRDSGADILLLQRELKhlisnSPESEMSHIFLDDEgsfEESNCNLNLSPA-----------P 495
Cdd:PRK05691 95 -YPpesarrhhQERLLSIIADAEPRLLLTVADLR-----DSLLQMEELAAANA---PELLCVDTLDPAlaeawqepalqP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 496 EEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKP----VRLLQ-------IASFSFDVFSGD--------- 555
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPddviVSWLPlyhdmglIGGLLQPIFSGVpcvlmspay 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 556 -LARTL-------TNGGTLIVCPDETrlepaeiYKIIkSQRItvmeSTPALiipvmeyvyrNQFKLPDLDILILGSDMVK 627
Cdd:PRK05691 246 fLERPLrwleaisEYGGTISGGPDFA-------YRLC-SERV----SESAL----------ERLDLSRWRVAYSGSEPIR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 628 AQDFKTLTDRFG----QSMRIINSYGVTEATIdssFYETSMGGECT-----------------GDNVPI---GSPLPNVH 683
Cdd:PRK05691 304 QDSLERFAEKFAacgfDPDSFFASYGLAEATL---FVSGGRRGQGIpaleldaealarnraepGTGSVLmscGRSQPGHA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 684 MYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENpfvSGERLYRTGDRAcWLPNGTIRLLGRMDYQVKI 762
Cdd:PRK05691 381 VLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH---DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 763 NGYRIETEEIESVL------LQTGlvREAAVAVQHDKNGQAGLAAYI-------VPSDVNTNALRAALT---KELPAymi 826
Cdd:PRK05691 457 RGHNLYPQDIEKTVerevevVRKG--RVAAFAVNHQGEEGIGIAAEIsrsvqkiLPPQALIKSIRQAVAeacQEAPS--- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 827 payLIPLVN---MPLTLNGKLDRNA---------------LPAPNNVLSRPYTAPVNDLQKTMAYIWEDVLSMSRVGIHD 888
Cdd:PRK05691 532 ---VVLLLNpgaLPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADD 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 889 SFFELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQELCGHITPLasQADQGPAEGEAELTP---------IQRR-- 956
Cdd:PRK05691 609 HFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVARQ--LAGGGAAQAAIARLPrgqalpqslAQNRlw 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 957 FFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQrDQNGHVIQfnRGINHKDHELFGLYISDWTKA 1036
Cdd:PRK05691 687 LLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFY-ERDGVALQ--RIDAQGEFALQRIDLSDLPEA 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1037 SLE-RAhldekLAAEETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQ 1114
Cdd:PRK05691 764 EREaRA-----AQIREEEARQPFDLEKGPLLRVTLVRLDDEEHqLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAE 838
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1115 LPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAF-LPKDienVPDKLQMNSDAAAFVLS-GDWTEKLLFETQ 1191
Cdd:PRK05691 839 LAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLgDEQPVLeLATD---HPRSARQAHSAARYSLRvDASLSEALRGLA 915
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 1192 QAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPFEDQLA 1265
Cdd:PRK05691 916 QAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR----PRLETQGLVGFFINTQVLRAQLDGRLPFTALLA 985
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
363-846 |
2.61e-46 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 173.18 E-value: 2.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARI 441
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALgVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 442 EYILRDSGAdilllqrelkhlisnspesemsHIFLDDegsfeesncnlnlspapeePVYIIYTSGTTGAPKGVIVTYQNF 521
Cdd:cd17631 85 AYILADSGA----------------------KVLFDD-------------------LALLMYTSGTTGRPKGAMLTHRNL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 522 THAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALIIP 601
Cdd:cd17631 124 LWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 602 VMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRfgqSMRIINSYGVTEAT-----IDSSFYETSMGGectgdnvpIG 676
Cdd:cd17631 201 LLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GVKFVQGYGMTETSpgvtfLSPEDHRRKLGS--------AG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 677 SPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLtqmkfTENPFVSGerLYRTGDRACWLPNGTIRLLGRM 756
Cdd:cd17631 270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEA-----TAAAFRDG--WFHTGDLGRLDEDGYLYIVDRK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 757 DYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAyIVPSDVNT---NALRAALTKELPAYMIPAYLIP 832
Cdd:cd17631 343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAViGVPDEKWGEAVVAV-VVPRPGAEldeDELIAHCRERLARYKIPKSVEF 421
|
490
....*....|....
gi 1238238751 833 LVNMPLTLNGKLDR 846
Cdd:cd17631 422 VDALPRNATGKILK 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
370-849 |
2.00e-45 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 170.93 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 370 IAVIDNETEISYRLLNERANRLARTLQNRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRD 447
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGKDLRGdrVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 448 SGADILLlqrelkhlisnspesemshiflddegsfeesncnlnlspapeEPVYIIYTSGTTGAPKGVIVTYQNFTH--AA 525
Cdd:cd05941 83 SEPSLVL------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAAnvRA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 L--AWRQiyeldRKPVRLLQIASFsFDV---FSGDLArTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALII 600
Cdd:cd05941 121 LvdAWRW-----TEDDVLLHVLPL-HHVhglVNALLC-PLFAGASVEFLP---KFDPKEVAISRLMPSITVFMGVPTIYT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 601 PVMEYvYRNQFKLPDLDI---------LILGSDMVKAQDFKTLTDRFGQsmRIINSYGVTEatidssfyeTSMGGEC--T 669
Cdd:cd05941 191 RLLQY-YEAHFTDPQFARaaaaerlrlMVSGSAALPVPTLEEWEAITGH--TLLERYGMTE---------IGMALSNplD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 670 GDNVP--IGSPLPNVHMYVLSQ-TDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLP 746
Cdd:cd05941 259 GERRPgtVGMPLPGVQARIVDEeTGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 747 NGTIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPSD----VNTNALRAALTKE 820
Cdd:cd05941 333 DGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAViGVPDPDWGER-VVAVVVLRAgaaaLSLEELKEWAKQR 411
|
490 500
....*....|....*....|....*....
gi 1238238751 821 LPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05941 412 LAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
950-1199 |
4.02e-43 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 157.89 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 950 LTPIQRRFFgqvhaFHY----HYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFqRDQNGHVIQFNRginhkDHEL 1025
Cdd:COG4908 1 LSPAQKRFL-----FLEpgsnAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRF-VEEDGEPVQRID-----PDAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1026 FGLYISDWTK-ASLERAHLDEKLAAEEtvIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAA 1103
Cdd:COG4908 70 LPLEVVDLSAlPEPEREAELEELVAEE--ASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1104 YQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAF-LPKDIENvPDKLQMNSDAAAFVLSGD 1181
Cdd:COG4908 148 YAALLEGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLaGAPPVLeLPTDRPR-PAVQTFRGATLSFTLPAE 226
|
250
....*....|....*...
gi 1238238751 1182 WTEKLLfETQQAYGTDAN 1199
Cdd:COG4908 227 LTEALK-ALAKAHGATVN 243
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
386-849 |
1.01e-42 |
|
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: 163.38 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 386 ERANRLARTLQNRKGPKP--TVAVLAKRSiDAIVGVLAVMKAGG----VYIPIDAHYPKARIEYILRDSGADILLLQR-- 457
Cdd:cd05922 1 LGVSAAASALLEAGGVRGerVVLILPNRF-TYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAga 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 458 --ELKHLISNSPESEMshiFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQ---IY 532
Cdd:cd05922 80 adRLRDALPASPDPGT---VLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEylgIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 533 ELDRKPVRLlqiaSFSFDVFSGDLARTLTNGGTLIVCPDEtrLEPAEIYKIIKSQRITVMESTPALIiPVMEYVYRNQFK 612
Cdd:cd05922 157 ADDRALTVL----PLSYDYGLSVLNTHLLRGATLVLTNDG--VLDDAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 613 LPDLDILILGSDMVKAQDFKTLTDRFgQSMRIINSYGVTEATIDSSFYETSMGGECTGDnvpIGSPLPNVHMYVLSQTDQ 692
Cdd:cd05922 230 LPSLRYLTQAGGRLPQETIARLRELL-PGAQVYVMYGQTEATRRMTYLPPERILEKPGS---IGLAIPGGEFEILDDDGT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 693 IQPIGVAGELCIGGAGVAKGYHHKPdltqmKFTENPFVSGERLYrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEI 772
Cdd:cd05922 306 PTPPGEPGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEI 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238751 773 ESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05922 380 EAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
355-849 |
1.08e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 161.51 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 355 FHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPI 432
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR-ALGVKKgdRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 433 DAHYPKARIEYILRDSGADILLLQREL-KHLISNSPESEMSH--IFLDDEGSFEESNCNLNLS------------PAPEE 497
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEFvPLLAAILPQLPTVRtvIVEGDGPAAPLAPEVGEYEellaaasdtfdfPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 498 --PVYIIYTSGTTGAPKGVIVTYQN-FTH--AALAWRQIYELDRKPVRLLQIASFSFDVFsgdLARTLTnGGTLIVcPDe 572
Cdd:PRK06187 167 ndAAAMLYTSGTTGHPKGVVLSHRNlFLHslAVCAWLKLSRDDVYLVIVPMFHVHAWGLP---YLALMA-GAKQVI-PR- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 573 tRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILG-SDMVKA--QDFKtltDRFGqsMRIINSYG 649
Cdd:PRK06187 241 -RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGgAALPPAllREFK---EKFG--IDLVQGYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 650 VTEA--TIDSSFYETSMGGECTgdnVPI--GSPLPNVHMYVLSQTDQIQP--IGVAGELCIGGAGVAKGYHHKPDLtqmk 723
Cdd:PRK06187 315 MTETspVVSVLPPEDQLPGQWT---KRRsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEA---- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 724 fTENPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAY 802
Cdd:PRK06187 388 -TAETIDGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAViGVPDEKWGERPVAVV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1238238751 803 IVPSDVNTNA--LRAALTKELPAYMIPA--YLIPlvNMPLTLNGKLDRNAL 849
Cdd:PRK06187 465 VLKPGATLDAkeLRAFLRGRLAKFKLPKriAFVD--ELPRTSVGKILKRVL 513
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
376-850 |
1.95e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 158.61 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 376 ETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILL 454
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGiRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 LqrelkhlisnspesemshiflddegsfeesncnlnlspapeEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYEL 534
Cdd:cd05934 81 V-----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 535 DRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPAliipVMEYVYRnQFKLP 614
Cdd:cd05934 120 GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGA----MLSYLLA-QPPSP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 615 DlD----ILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTeatidssfyETSMG--GECTGDNVP--IGSPLPNVHMYV 686
Cdd:cd05934 192 D-DrahrLRAAYGAPNPPELHEEFEERFG--VRLLEGYGMT---------ETIVGviGPRDEPRRPgsIGRPAPGYEVRI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 687 LSQTDQIQPIGVAGELCI---GGAGVAKGYHHKPDLTQMKFtENPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKIN 763
Cdd:cd05934 260 VDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW------FHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 764 GYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV---PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLT 839
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVvAVPDEVGEDE-VKAVVVlrpGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKT 411
|
490
....*....|.
gi 1238238751 840 LNGKLDRNALP 850
Cdd:cd05934 412 PTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
374-807 |
4.32e-41 |
|
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: 158.92 E-value: 4.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 374 DNETEISYRLLNERANRLARTLQNRKGPKP-TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADI 452
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGdVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 453 LL--------LQRELKHLIS-------NSPESEMSHI--FLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVI 515
Cdd:cd05911 86 IFtdpdglekVKEAAKELGPkdkiivlDDKPDGVLSIedLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 516 VTYQNFT-HAALAWRQIYELDRKPVRLLqiASFSFDVFSGDLA--RTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVM 592
Cdd:cd05911 166 LSHRNLIaNLSQVQTFLYGNDGSNDVIL--GFLPLYHIYGLFTtlASLLNGATVIIMP---KFDSELFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 593 ESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEatidssfyetsMGGECT--- 669
Cdd:cd05911 241 YLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNA-TIKQGYGMTE-----------TGGILTvnp 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 670 -GDNVP--IGSPLPNVHM-YVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWL 745
Cdd:cd05911 309 dGDDKPgsVGRLLPNVEAkIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 746 PNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAGlAAYIVPSD 807
Cdd:cd05911 383 EDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIgIPDEVSGELP-RAYVVRKP 444
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
363-849 |
2.30e-40 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 158.74 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVI-----DNETEISYRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:COG0365 19 AEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRAL-GVKKgdRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 Y-PKArIEYILRDSGADILL-------------LQRELKHLISNSPESEmsHIFL--------DDEG--SFEE--SNCNL 489
Cdd:COG0365 98 FgAEA-LADRIEDAEAKVLItadgglrggkvidLKEKVDEALEELPSLE--HVIVvgrtgadvPMEGdlDWDEllAAASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 490 NLSPAP---EEPVYIIYTSGTTGAPKGVIvtyqnFTHAALAWRQIYEldrkpvrllqiASFSFDVFSGDL----ART--- 559
Cdd:COG0365 175 EFEPEPtdaDDPLFILYTSGTTGKPKGVV-----HTHGGYLVHAATT-----------AKYVLDLKPGDVfwctADIgwa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 560 ----------LTNGGTLIVCPD-ETRLEPAEIYKIIKSQRITVMESTPALIIPVMEY--VYRNQFKLPDLDILILGSDMV 626
Cdd:COG0365 239 tghsyivygpLLNGATVVLYEGrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 627 KAQDFKTLTDRFGqsMRIINSYGVTEatidssfyetsMGGeCTGDNVP--------IGSPLPNVHMYVLSQTDQIQPIGV 698
Cdd:COG0365 319 NPEVWEWWYEAVG--VPIVDGWGQTE-----------TGG-IFISNLPglpvkpgsMGKPVPGYDVAVVDEDGNPVPPGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 699 AGELCIGGA--GVAKGYHHKPDLTQMKFtenpFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVL 776
Cdd:COG0365 385 EGELVIKGPwpGMFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESAL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 777 LQTGLVREAAV-AVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:COG0365 461 VSHPAVAEAAVvGVPDEIRGQV-VKAFVVlkpgvePSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
370-849 |
6.02e-40 |
|
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: 155.93 E-value: 6.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 370 IAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDS 448
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAALGiKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 449 GADILLLQRElkhliSNSPESEMSH----------------IFLDDEGS-----FEESNCNLNLSPAPEEPVYIIYTSGT 507
Cdd:cd05926 86 GSKLVLTPKG-----ELGPASRAASklglailelaldvgvlIRAPSAESlsnllADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 508 TGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTlIVCPDetRLEPAEIYKIIKSQ 587
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGS-VVLPP--RFSASTFWPDVRDY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 588 RITVMESTPALI-IPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTEATidssfyetsmgG 666
Cdd:cd05926 238 NATWYTAVPTIHqILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPV--LEAYGMTEAA-----------H 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 667 ECTGDNVPIGSPLP-------NVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTG 739
Cdd:cd05926 305 QMTSNPLPPGPRKPgsvgkpvGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 740 DRACWLPNGTIRLLGRmdyqVK--IN--GYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTN 811
Cdd:cd05926 379 DLGYLDADGYLFLTGR----IKelINrgGEKISPLEVDGVLLSHPAVLEAVAfGVPDEKYGEE-VAAAVVLregASVTEE 453
|
490 500 510
....*....|....*....|....*....|....*...
gi 1238238751 812 ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05926 454 ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
358-849 |
1.11e-39 |
|
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: 155.22 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALR-ALGVKREerVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 YPKARIEYILRDSGADILLLQREL---------------KHLI------SNSPESEMSHIFLDDEGSFEESNCNlnlspa 494
Cdd:cd05959 88 LTPDDYAYYLEDSRARVVVVSGELapvlaaaltksehtlVVLIvsggagPEAGALLLAELVAAEAEQLKPAATH------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 PEEPVYIIYTSGTTGAPKGVIVTYQNFTHAA-LAWRQIYELdRKPVRLLQIASFSFDVFSGD-LARTLTNGGTLIVCPDe 572
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAeLYARNVLGI-REDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMPE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 573 tRLEPAEIYKIIKSQRITVMESTPALiipvmeyvYRNQFKLPD--------LDILILGSDMVKAQDFKTLTDRFGqsMRI 644
Cdd:cd05959 240 -RPTPAAVFKRIRRYRPTVFFGVPTL--------YAAMLAAPNlpsrdlssLRLCVSAGEALPAEVGERWKARFG--LDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 645 INSYGVTEA-------TIDSSFYETSmggectgdnvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKP 717
Cdd:cd05959 309 LDGIGSTEMlhiflsnRPGRVRYGTT------------GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 718 DLTQMKFtenpfvSGErLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQA 797
Cdd:cd05959 377 DKTRDTF------QGE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLT 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 798 GLAAYIVP------SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05959 450 KPKAFVVLrpgyedSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
3-319 |
1.14e-39 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 153.29 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYN----NRNLPA------LRIQYKDYAvwre 72
Cdd:cd19533 103 KPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTallkGRPAPPapfgsfLDLVEEEQA---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 73 gFKTGDAYKTQEAYWLKQLEGELPVLDLpADHARPPVRSFAGDKVSFTLDQEVAsgLHKLARENGSTLYMVLLAAYTAFL 152
Cdd:cd19533 179 -YRQSERFERDRAFWTEQFEDLPEPVSL-ARRAPGRSLAFLRRTAELPPELTRT--LLEAAEAHGASWPSFFIALVAAYL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 153 SRLSGQEDIIVGSPIAGRPHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRD 232
Cdd:cd19533 255 HRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 233 msRNPVFDamfILQNVEKQDIDLREIKV--RPANFAHHISL-FDITLIATEISGSICCEMEFSTEVFLKATIERWADHFI 309
Cdd:cd19533 335 --LHPLFG---PTVNYMPFDYGLDFGGVvgLTHNLSSGPTNdLSIFVYDRDDESGLRIDFDANPALYSGEDLARHQERLL 409
|
330
....*....|
gi 1238238751 310 EFLHEALSTP 319
Cdd:cd19533 410 RLLEEAAADP 419
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
3-319 |
3.24e-38 |
|
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: 149.55 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR---NLP---ALRIQYKDYAVW-REGFK 75
Cdd:cd19546 103 HLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregRAPeraPLPLQFADYALWeRELLA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 76 TGDAYKT----QEAYWLKQLEGELPVLDLPADHARPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAF 151
Cdd:cd19546 183 GEDDRDSligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAML 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 152 LSRLSGQEDIIVGSPIAGRPHK-DLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELT 230
Cdd:cd19546 263 LTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 231 RDMSRNPVFDAMFILQNVEKQDIDLREI---KVRPANFAHHISLFDITLIATEISGS------ICCEMEFSTEVFLKATI 301
Cdd:cd19546 343 PSADRHPVFQVALDVRDDDNDPWDAPELpglRTSPVPLGTEAMELDLSLALTERRNDdgdpdgLDGSLRYAADLFDRATA 422
|
330
....*....|....*...
gi 1238238751 302 ERWADHFIEFLHEALSTP 319
Cdd:cd19546 423 AALARRLVRVLEQVAADP 440
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
358-845 |
5.53e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 147.72 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHY 436
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGlGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 437 PKARIEYILRDSGADILLLQRE--------------LKHLIS--NSPESEMSHIFLDDEGSFEESNCNLNLSPAPEEPVY 500
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREfaprvaevlprlpkLRTLVVveDGSGNDLLPGAVDYEDALAAGSPERDFGERSPDDLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 IIYTSGTTGAPKGVIvtyqnfthaalaWRQ---------------------IYELDRK-----PVRLL----------QI 544
Cdd:PRK07798 168 LLYTGGTTGMPKGVM------------WRQedifrvllggrdfatgepiedEEELAKRaaagpGMRRFpapplmhgagQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 545 ASFSfdvfsgdlarTLTNGGTlIVCPDETRLEPAEIYKIIKSQRITVMEST-PALIIP-VMEYVYRNQFKLPDLDILILG 622
Cdd:PRK07798 236 AAFA----------ALFSGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPlLDALEARGPYDLSSLFAIASG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 623 ----SDMVKAQdfktLTDRFGQSMrIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSplpnvHMYVLS-QTDQIQP-I 696
Cdd:PRK07798 305 galfSPSVKEA----LLELLPNVV-LTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP-----RTVVLDeDGNPVEPgS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 697 GVAGELCIGGAgVAKGYHHKPDLTQMKFTEnpfVSGERLYRTGDRACWLPNGTIRLLGRmDYQVkIN--GYRIETEEIES 774
Cdd:PRK07798 375 GEIGWIARRGH-IPLGYYKDPEKTAETFPT---IDGVRYAIPGDRARVEADGTITLLGR-GSVC-INtgGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 775 VLLQTGLVREAAVA-VQHDKNGQAgLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLD 845
Cdd:PRK07798 449 ALKAHPDVADALVVgVPDERWGQE-VVAVVQLREgarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
352-849 |
1.71e-35 |
|
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: 142.47 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 352 DIPFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVyi 430
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGiRPGDRVVVQLPNVAEFVVLFFALLRLGAV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 431 PIDAhYPKARieyilrdsgadilllQRELKHLISnspESEMSHIFLDDE-GSFEESNCNLNLSPAPEEPVYIIYTSGTTG 509
Cdd:cd05920 92 PVLA-LPSHR---------------RSELSAFCA---HAEAVAYIVPDRhAGFDHRALARELAESIPEVALFLLSGGTTG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 510 APKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQI-ASFSFDVFSGDLARTLTNGGTLIVCPDEtrlEPAEIYKIIKSQR 588
Cdd:cd05920 153 TPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLpAAHNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 589 ITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMGGEC 668
Cdd:cd05920 230 VTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLG--CTLQQVFGMAEGLLNYTRLDDPDEVII 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 669 TGDNVPIgSPLPNVHmyVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLPNG 748
Cdd:cd05920 308 HTQGRPM-SPDDEIR--VVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 749 TIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQAgLAAYIVPSD--VNTNALRAALTK-ELPAY 824
Cdd:cd05920 379 YLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAvVAMPDELLGER-SCAFVVLRDppPSAAQLRRFLRErGLAAY 457
|
490 500
....*....|....*....|....*
gi 1238238751 825 MIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05920 458 KLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
360-849 |
3.34e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 141.92 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 360 EAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYP 437
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKgeRIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 438 KARIEYILRDSGADILLLQRELKHLI-SNSPESEMSH-IFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVI 515
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMAlSMQKVSYVQRvISITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 516 VTYQNfthaaLAWRQIYEL-------DRKPVRLLQ------IASFSFDvfsgdlarTLTNGGTLIVcPDetRLEPAEIYK 582
Cdd:PRK06839 169 LTQEN-----MFWNALNNTfaidltmHDRSIVLLPlfhiggIGLFAFP--------TLFAGGVIIV-PR--KFEPTKALS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 583 IIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGS---DMVKAQDFKTLTDRFGQsmriinSYGVTEaTIDSSF 659
Cdd:PRK06839 233 MIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcPEELMREFIDRGFLFGQ------GFGMTE-TSPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 660 yetsMGGECTGDNVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLtqmkfTENPFVSGerLYR 737
Cdd:PRK06839 306 ----MLSEEDARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDA-----TEETIQDG--WLC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 738 TGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAYIV-PSDVNTNA-LR 814
Cdd:PRK06839 375 TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVvGRQHVKWGEIPIAFIVKkSSSVLIEKdVI 454
|
490 500 510
....*....|....*....|....*....|....*
gi 1238238751 815 AALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK06839 455 EHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
380-849 |
3.97e-35 |
|
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: 140.28 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 380 SYRLLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQ 456
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAqgiRSGS--RVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 457 RELKhlisnspESEMSHIFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDR 536
Cdd:TIGR01923 79 SLLE-------EKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 537 KPVRLLQIASFSFDVFSGdLARTLTNGGTL-IVCPDetrlepAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQfklpD 615
Cdd:TIGR01923 152 DDNWLLSLPLYHISGLSI-LFRWLIEGATLrIVDKF------NQLLEMIANERVTHISLVPTQLNRLLDEGGHNE----N 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 616 LDILILGSDMVKAQDFKTLTDrfgQSMRIINSYGVTEATIDSSFYETSMggecTGDNVPIGSPLPNVHMYvLSQTDQIQp 695
Cdd:TIGR01923 221 LRKILLGGSAIPAPLIEEAQQ---YGLPIYLSYGMTETCSQVTTATPEM----LHARPDVGRPLAGREIK-IKVDNKEG- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 696 igvAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESV 775
Cdd:TIGR01923 292 ---HGEIMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 776 LLQTGLVREAAV-AVQHDKNGQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:TIGR01923 362 LYQHPGIQEAVVvPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
371-849 |
3.12e-34 |
|
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: 137.59 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 371 AVIDNETEISYRLLNERANRLARTLQNR-KGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSG 449
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLgVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 450 ADILLLQRElkhlisnspesemshiflddegsfeesncnlnlspapeEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAW- 528
Cdd:cd05919 83 ARLVVTSAD--------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMa 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 529 RQIYELdRKPVRLLQIASFSFDVFSGD-LARTLTNGGTLIVCPdeTRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVY 607
Cdd:cd05919 125 REALGL-TPGDRVFSSAKMFFGYGLGNsLWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 608 RNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTE-------ATIDSSFYETSmggectgdnvpiGSPLP 680
Cdd:cd05919 202 GSPDALRSLRLCVSAGEALPRGLGERWMEHFG--GPILDGIGATEvghiflsNRPGAWRLGST------------GRPVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 681 NVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENpfvsgerLYRTGDRACWLPNGTIRLLGRMDYQV 760
Cdd:cd05919 268 GYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 761 KINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVNTN------ALRAALTKELPAYMIPAYLIPLV 834
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPqeslarDIHRHLLERLSAHKVPRRIAFVD 420
|
490
....*....|....*
gi 1238238751 835 NMPLTLNGKLDRNAL 849
Cdd:cd05919 421 ELPRTATGKLQRFKL 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
380-849 |
4.85e-34 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 136.70 E-value: 4.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 380 SYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGAdilllq 456
Cdd:cd05972 2 SFRELKRESAKAANVLAKlglRKGDR--VAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 457 relKHLISNSpesemshiflddegsfeesncnlnlspapEEPVYIIYTSGTTGAPKGVIVTyqnftHAAlawrqiyeldr 536
Cdd:cd05972 74 ---KAIVTDA-----------------------------EDPALIYFTSGTTGLPKGVLHT-----HSY----------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 537 kPVRLLQIASFSFDVFSGDLART-----------------LTNGGTLIVCpDETRLEPAEIYKIIKSQRITVMESTPAli 599
Cdd:cd05972 106 -PLGHIPTAAYWLGLRPDDIHWNiadpgwakgawssffgpWLLGATVFVY-EGPRFDAERILELLERYGVTSFCGPPT-- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 600 ipvmeyVYR-------NQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATI---DSSFYETSMGGect 669
Cdd:cd05972 182 ------AYRmlikqdlSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG--LPIRDGYGQTETGLtvgNFPDMPVKPGS--- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 670 gdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCI--GGAGVAKGYHHKPDLTQMKFTENpfvsgerLYRTGDRACWLPN 747
Cdd:cd05972 251 -----MGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDED 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 748 GTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKE 820
Cdd:cd05972 319 GYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAvVGSPDPVRGEV-VKAFVVltsgyePSEELAEELQGHVKKV 397
|
490 500 510
....*....|....*....|....*....|
gi 1238238751 821 LPAYMIPaYLIPLV-NMPLTLNGKLDRNAL 849
Cdd:cd05972 398 LAPYKYP-REIEFVeELPKTISGKIRRVEL 426
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
353-849 |
1.03e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 137.32 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 353 IPFHrifeakAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIP 431
Cdd:PRK06145 8 IAFH------ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGiGQGDVVALLMKNSAAFLELAFAASYLGAVFLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 432 IDAHYPKARIEYILRDSGADILLLQRELkhliSNSPESEMSHIFLDDEGSFEESN-------CNLNLSPAPEEPVYIIYT 504
Cdd:PRK06145 82 INYRLAADEVAYILGDAGAKLLLVDEEF----DAIVALETPKIVIDAAAQADSRRlaqggleIPPQAAVAPTDLVRLMYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 505 SGTTGAPKGVIVTYQNFthaalAWR---QIYELD-RKPVRLLQIASFsFDVFSGDLA--RTLTNGGTLIVcpdETRLEPA 578
Cdd:PRK06145 158 SGTTDRPKGVMHSYGNL-----HWKsidHVIALGlTASERLLVVGPL-YHVGAFDLPgiAVLWVGGTLRI---HREFDPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 579 EIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEATIDSS 658
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRA-RYIDAYGLTETCSGDT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 659 FYETSMGGECTGDNvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlyRT 738
Cdd:PRK06145 308 LMEAGREIEKIGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 739 GDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDVNT---NALRA 815
Cdd:PRK06145 378 GDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATltlEALDR 457
|
490 500 510
....*....|....*....|....*....|....
gi 1238238751 816 ALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK06145 458 HCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
368-849 |
2.38e-33 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 136.61 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 368 EHIAVIDNETEI------------SYRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:cd12119 3 EHAARLHGDREIvsrthegevhryTYAEVAERARRLANALRRL-GVKPgdRVATLAWNTHRHLELYYAVPGMGAVLHTIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHYPKARIEYILRDSGADILLLQREL--------------KHLISNSPESEMSHIFLDDEGSFEESncnlnlsPAPEEPV 499
Cdd:cd12119 82 PRLFPEQIAYIINHAEDRVVFVDRDFlplleaiaprlptvEHVVVMTDDAAMPEPAGVGVLAYEEL-------LAAESPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 500 Y------------IIYTSGTTGAPKGVIVTY-QNFTHA-ALAWRQIYELDRKPVRLLqIASFsFDVFSGDLARTLTNGGT 565
Cdd:cd12119 155 YdwpdfdentaaaICYTSGTTGNPKGVVYSHrSLVLHAmAALLTDGLGLSESDVVLP-VVPM-FHVNAWGLPYAAAMVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 566 LIVCPDEtRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFgqsMRII 645
Cdd:cd12119 233 KLVLPGP-YLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERG---VRVI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 646 NSYGVTE----ATIDSSFYETSMGGECTGDNVPI--GSPLPNVHMYVLSQTDQIQPI-GVA-GELCIGGAGVAKGYHHKP 717
Cdd:cd12119 309 HAWGMTEtsplGTVARPPSEHSNLSEDEQLALRAkqGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKND 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 718 DLTQmKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQ 796
Cdd:cd12119 389 EESE-ALTEDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAViGVPHPKWGE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238751 797 AGLAaYIVP---SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd12119 462 RPLA-VVVLkegATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
359-849 |
7.65e-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: 134.56 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 359 FEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLqNRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHY 436
Cdd:cd05923 9 RAASRAPDACAIADPARGLRLTYSELRARIEAVAARL-HARGLRPGqrVAVVLPNSVEAVIALLALHRLGAVPALINPRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 437 PKARIEYILRDSGADILLLQrELKHLISNSPESEMSHIFLDDEGSFEEsNCNLNLSPA-----PEEPVYIIYTSGTTGAP 511
Cdd:cd05923 88 KAAELAELIERGEMTAAVIA-VDAQVMDAIFQSGVRVLALSDLVGLGE-PESAGPLIEdpprePEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 512 KGVIVTyqnftHAALAWRQIYELDRKPVR------------LLQIASFsFDVFSGDLArtltnGGTLIVCPDETRlePAE 579
Cdd:cd05923 166 KGAVIP-----QRAAESRVLFMSTQAGLRhgrhnvvlglmpLYHVIGF-FAVLVAALA-----LDGTYVVVEEFD--PAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 580 IYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILIL-GSDMVKaqdfkTLTDRFGQSM--RIINSYGVTEAtID 656
Cdd:cd05923 233 ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFaGATMPD-----AVLERVNQHLpgEKVNIYGTTEA-MN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 657 SSFYEtsmggectgdNVPIGSPL-PNVHMYV-----LSQTDQIQPIGVAGELCIGGAGVA--KGYHHKPDLTQMKFTEnp 728
Cdd:cd05923 307 SLYMR----------DARTGTEMrPGFFSEVrivriGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 729 fvsgeRLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPSD 807
Cdd:cd05923 375 -----GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVViGVADERWGQS-VTACVVPRE 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1238238751 808 VNTNALRA---ALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05923 449 GTLSADELdqfCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
380-851 |
9.41e-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: 133.40 E-value: 9.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 380 SYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRE 458
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGvGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 459 LKHLISnspesemshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKP 538
Cdd:cd05969 82 LYERTD------------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 539 VRLLQ-----IASFSFDVFSgdlarTLTNGGTLIVcpDETRLEPAEIYKIIKSQRITVMESTPALIIPVMEY--VYRNQF 611
Cdd:cd05969 132 IYWCTadpgwVTGTVYGIWA-----PWLNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdELARKY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 612 KLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATidssfyeTSMGGECTGDNVPIGS---PLPNVHMYVLS 688
Cdd:cd05969 205 DLSSLRFIHSVGEPLNPEAIRWGMEVFG--VPIHDTWWQTETG-------SIMIANYPCMPIKPGSmgkPLPGVKAAVVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 689 QTDQIQPIGVAGELCI--GGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDRACWlpngtirLLGRMDYQVKINGYR 766
Cdd:cd05969 276 ENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFW-------FVGRADDIIKTSGHR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 767 IETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV------PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTL 840
Cdd:cd05969 349 VGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfePSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|.
gi 1238238751 841 NGKLDRNALPA 851
Cdd:cd05969 429 SGKIMRRVLKA 439
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
380-844 |
9.51e-33 |
|
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: 133.27 E-value: 9.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 380 SYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRE 458
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGvGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 459 LKhliSNSPESEmshiflddegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKP 538
Cdd:cd05903 83 FR---QFDPAAM------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 539 VRLLQIASFSFDVFSGDLARTLTNGGTLIVCpdeTRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDI 618
Cdd:cd05903 136 VFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 619 LILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTE-ATIDSSFYETSMGGECTGDnvpiGSPLPNVHMYVLSQTDQIQPIG 697
Cdd:cd05903 213 FVCGGATVPRSLARRAAELLG--AKVCSAYGSTEcPGAVTSITPAPEDRRLYTD----GRPLPGVEIKVVDDTGATLAPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 698 VAGELCIGGAGVAKGYHHKPDLTqmkFTENPfvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLL 777
Cdd:cd05903 287 VEGELLSRGPSVFLGYLDRPDLT---ADAAP----EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238238751 778 QTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAALTKE-LPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:cd05903 360 GHPGVIEAAVVALPDERLGERACAVVVTKSgalLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
3-242 |
2.03e-32 |
|
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: 131.15 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQAPLFRaqiVKISDeRHLLLVdMHHIISDGVSVNILIREFGELYNNRNLPALRIQYKDYAVWRegfKTGDAykT 82
Cdd:cd19537 91 RPFDLEREDPIR---VFISP-DTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWS---RPASP--E 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 83 QEAYWLKQLEGeLPVLDLPAdhaRPPVRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQEDII 162
Cdd:cd19537 161 DLDFWSEYLSG-LPLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 163 VGSPIAGRPHKDLEPILGMFVNTLALRTR--PEGGKPFVQYLQEVRETALEAFEHQdYPFEELVDKLELTRDMSRNPVFD 240
Cdd:cd19537 237 LGAPYLNRTSEEDMETVGLFLEPLPIRIRfpSSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFD 315
|
..
gi 1238238751 241 AM 242
Cdd:cd19537 316 VM 317
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2-252 |
1.49e-31 |
|
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: 129.11 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 2 IKPFDLSQAPLFRAQIVKISDERHLLLV-DMHHIISDGVSVNILIREFGELYNNR-------NLPALriQYKDYAVWREG 73
Cdd:cd19536 103 IRRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNQLleykplsLPPAQ--PYRDFVAHERA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 74 FKTGDAYktqEAYWLKQLEG-ELPVLdlpadharPPVRSFAGDKVSFTLDQEVASGL----HKLARENGSTLYMVLLAAY 148
Cdd:cd19536 181 SIQQAAS---ERYWREYLAGaTLATL--------PALSEAVGGGPEQDSELLVSVPLpvrsRSLAKRSGIPLSTLLLAAW 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 149 TAFLSRLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPEGGkPFVQYLQEVRETALEAFEHQDYPFEelvdk 226
Cdd:cd19536 250 ALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQELESLSHEQVPLA----- 323
|
250 260
....*....|....*....|....*.
gi 1238238751 227 lELTRDMSRNPVFDAMFILQNVEKQD 252
Cdd:cd19536 324 -DIQRCSEGEPLFDSIVNFRHFDLDF 348
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
366-852 |
2.72e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 130.49 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 366 NPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIdahYPKARIE-- 442
Cdd:PRK06188 25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGlGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL---HPLGSLDdh 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 443 -YILRDSGADIL-------------LLQR--ELKHLISNSPeSEMSHIFLDDEGSFEESNcnlnLSPA--PEEPVYIIYT 504
Cdd:PRK06188 102 aYVLEDAGISTLivdpapfveralaLLARvpSLKHVLTLGP-VPDGVDLLAAAAKFGPAP----LVAAalPPDIAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 505 SGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFDvfSGDL-ARTLTNGGTLIVCPdetRLEPAEIYKI 583
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADP-RFLMCTPLSHA--GGAFfLPTLLRGGTVIVLA---KFDPAEVLRA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 584 IKSQRITVmestpALIIPVMEYVYRNQFKLPD-----LDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTEA----- 653
Cdd:PRK06188 251 IEEQRITA-----TFLVPTMIYALLDHPDLRTrdlssLETVYYGASPMSPVRLAEAIERFGPIF--AQYYGQTEApmvit 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 654 ---TIDSSFYETSMGGECtgdnvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFtenpfv 730
Cdd:PRK06188 324 ylrKRDHDPDDPKRLTSC-------GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 731 SGERLyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---S 806
Cdd:PRK06188 391 RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAViGVPDEKWGEA-VTAVVVLrpgA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1238238751 807 DVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAP 852
Cdd:PRK06188 469 AVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
495-849 |
2.80e-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: 126.62 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 PEEPVYIIYTSGTTGAPKGVIVTYQN------FTHAALAWRqiyELDRK--PVRLLQIasfsFDVFSGDLArTLTNGGTl 566
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNivnngyFIGERLGLT---EQDRLciPVPLFHC----FGSVLGVLA-CLTHGAT- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 567 IVCPDETrLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKtltdrfgqsmRIIN 646
Cdd:cd05917 72 MVFPSPS-FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMK----------RVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 647 SYGVTEATIDSSFYETSMGGECTGDNVPI-------GSPLPNVHMYVLSQTDQIQP-IGVAGELCIGGAGVAKGYHHKPD 718
Cdd:cd05917 141 VMNMKDVTIAYGMTETSPVSTQTRTDDSIekrvntvGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 719 LTqmkfteNPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQA 797
Cdd:cd05917 221 KT------AEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVgVPDERYGEE 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 798 gLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05917 295 -VCAWIRLKEgaeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
378-849 |
3.28e-31 |
|
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: 127.85 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 378 EISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADill 454
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAAlgvRKGDR--VALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 lqrelkhlisnspesemshifLDDEGSfeesncnlnlspapeepvyIIYTSGTTGAPKGVIVTYQNFTHAALAWRQ---I 531
Cdd:cd05912 76 ---------------------LDDIAT-------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALnlgL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 532 YELDR--KPVRLLQIASFSFdvfsgdLARTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALIIPVMEyVYRN 609
Cdd:cd05912 116 TEDDNwlCALPLFHISGLSI------LMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLE-ILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 610 QFKlPDLDILILGSDMVKAQDFKTLTDRfgqSMRIINSYGVTE-----ATIDSSFYETSMGGectgdnvpIGSPLPNVHm 684
Cdd:cd05912 186 GYP-NNLRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTEtcsqiVTLSPEDALNKIGS--------AGKPLFPVE- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 685 yvLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlyRTGDRACWLPNGTIRLLGRMDYQVKING 764
Cdd:cd05912 253 --LKIEDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 765 YRIETEEIESVLLQTGLVREAAVAVQHDKN-GQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGK 843
Cdd:cd05912 324 ENIYPAEIEEVLLSHPAIKEAGVVGIPDDKwGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
|
....*.
gi 1238238751 844 LDRNAL 849
Cdd:cd05912 404 LLRHEL 409
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
378-849 |
6.60e-31 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 127.60 E-value: 6.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 378 EISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILL 454
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNkgvRKGDR--VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 LQRELkhlisnspesemshiflddegsfeesncnlnlspapEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYEL 534
Cdd:cd05935 79 VGSEL------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 535 DRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCpdeTRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLP 614
Cdd:cd05935 123 TPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 615 DLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEAtidssFYETSMGGECTGDNVPIGSPLPNVHMYVLSQTDQIQ 694
Cdd:cd05935 200 SLKVLTGGGAPMPPAVAEKLLKLTG--LRFVEGYGLTET-----MSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 695 -PIGVAGELCIGGAGVAKGYHHKPDLTQMKFTEnpfVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIE 773
Cdd:cd05935 273 lPPNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 774 SVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSDvntnALRAALTKE---------LPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:cd05935 350 AKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRP----EYRGKVTEEdiiewareqMAAYKYPREVEFVDELPRSASGKI 425
|
....*
gi 1238238751 845 DRNAL 849
Cdd:cd05935 426 LWRLL 430
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
371-807 |
1.20e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 127.41 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 371 AVIDNETEISYRLLNERANRLARtlqnRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGA 450
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAE----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 451 DILLlqrelkhliSNSPES--EMSHIFLDDEG----SFEEsncnlnlsPAPEEPVYIIYTSGTTGAPKGVIVTYQ----N 520
Cdd:PRK07787 94 QAWL---------GPAPDDpaGLPHVPVRLHArswhRYPE--------PDPDAPALIVYTSGTTGPPKGVVLSRRaiaaD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 521 FTHAALAWRQIYElD----------------------RKPVRLLQIASFSFDVFsgdlARTLTNGGTLI---------VC 569
Cdd:PRK07787 157 LDALAEAWQWTAD-DvlvhglplfhvhglvlgvlgplRIGNRFVHTGRPTPEAY----AQALSEGGTLYfgvptvwsrIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 570 PDEtrlepaEIYKIIKSQRITVMESTPaliipvmeyvyrnqfkLPdldililgsdmvkAQDFKTLTDRFGQsmRIINSYG 649
Cdd:PRK07787 232 ADP------EAARALRGARLLVSGSAA----------------LP-------------VPVFDRLAALTGH--RPVERYG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 650 VTEATIDSSfyeTSMGGECTGDNVpiGSPLPNVHMYVLSQTDQIQPIGVA--GELCIGGAGVAKGYHHKPDLTQMKFTEN 727
Cdd:PRK07787 275 MTETLITLS---TRADGERRPGWV--GLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTAD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 728 PFvsgerlYRTGDRACWLPNGTIRLLGRMDYQ-VKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP 805
Cdd:PRK07787 350 GW------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVvGVPDDDLGQR-IVAYVVG 422
|
..
gi 1238238751 806 SD 807
Cdd:PRK07787 423 AD 424
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
359-849 |
1.48e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 127.62 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 359 FEAKAEenPEHIAVID--NETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:PRK09088 3 FHARLQ--PQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGcVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 YPKARIEYILRDSGADILLLQrelKHLISNSPESEMSHIFLDdegSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVI 515
Cdd:PRK09088 81 LSASELDALLQDAEPRLLLGD---DAVAAGRTDVEDLAAFIA---SADALEPADTPSIPPERVSLILFTSGTSGQPKGVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 516 VTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPDetrLEPAEIYKIIKSQRITVmesT 595
Cdd:PRK09088 155 LSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNG---FEPKRTLGRLGDPALGI---T 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 596 PALIIPVMEYVYRNQfklPDLD--------ILILGSDMVKAQDFKTLTDrfgQSMRIINSYGVTEA-TIdssfyeTSMGG 666
Cdd:PRK09088 229 HYFCVPQMAQAFRAQ---PGFDaaalrhltALFTGGAPHAAEDILGWLD---DGIPMVDGFGMSEAgTV------FGMSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 667 ECTGDNVPIGS---PLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTenpfvsGERLYRTGDRAC 743
Cdd:PRK09088 297 DCDVIRAKAGAagiPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT------GDGWFRTGDIAR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 744 WLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN-GQAGLAAyIVPSD---VNTNALRAALTK 819
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLA-IVPADgapLDLERIRSHLST 449
|
490 500 510
....*....|....*....|....*....|
gi 1238238751 820 ELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK09088 450 RLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
11-319 |
3.23e-30 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 124.73 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 11 PLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPAlRIQYKDYAVWREGFKTGDAYktqeAYWLKQ 90
Cdd:cd19542 105 PPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPFSDYISYLQSQSQEESL----QYWRKY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 91 LEGELPVLDLPADHARPPVRsfagdkvsfTLDQEVASG--LHKLARENGSTLYMVLLAAYTAFLSRLSGQEDIIVGSPIA 168
Cdd:cd19542 180 LQGASPCAFPSLSPKRPAER---------SLSSTRRSLakLEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 169 GR--PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPFEELVDKLELTRdmsRNPVFDAMFILQ 246
Cdd:cd19542 251 GRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWP---SGTLFNTLVSYQ 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 247 NVE-KQDIDLREIKVRPANFAHHISLFDITLIATEISGSICCEMEFSTEVFLKATIERWADHFIEFLHEALSTP 319
Cdd:cd19542 328 NFEaSPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
367-849 |
3.95e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 126.23 E-value: 3.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRKGPK-PTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKgDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQRELKH--------LISNSPESEMSHIFLDDEGSFEESncnlnlspapeepVYIIYTSGTTGAPKGVIVT 517
Cdd:PRK03640 96 DDAEVKCLITDDDFEAklipgisvKFAELMNGPKEEAEIQEEFDLDEV-------------ATIMYTSGTTGKPKGVIQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 518 YQNFTHAALAWRQ---IYELDR--KPVRLLQIASFSFdvfsgdLARTLTNGGTLIVcpdETRLEPAEIYKIIKSQRITVM 592
Cdd:PRK03640 163 YGNHWWSAVGSALnlgLTEDDCwlAAVPIFHISGLSI------LMRSVIYGMRVVL---VEKFDAEKINKLLQTGGVTII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 593 ESTPA----LIIPVMEYVYRNQFKLpdldILILGSDMVKAqdfkTLTDRFGQSMRIINSYGVTE-----ATIDSSFYETS 663
Cdd:PRK03640 234 SVVSTmlqrLLERLGEGTYPSSFRC----MLLGGGPAPKP----LLEQCKEKGIPVYQSYGMTEtasqiVTLSPEDALTK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 664 MGGectgdnvpIGSPLPNVHMYVLSQTDQIQPiGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlyRTGDRAC 743
Cdd:PRK03640 306 LGS--------AGKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 744 WLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAGLAAYIVPSDVNTNALRAALTKELP 822
Cdd:PRK03640 370 LDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVgVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLA 449
|
490 500
....*....|....*....|....*..
gi 1238238751 823 AYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK03640 450 KYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
347-849 |
5.05e-30 |
|
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: 126.80 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 347 EFAQK--------DIPFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAI 416
Cdd:COG1021 11 EFAARyreagywrGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPgdRVVVQLPNVAEFV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 417 VGVLAVMKAGGvyIPIDAhYPKAR---IEYILRDSGA------------DILLLQRELKhliSNSPEseMSHIFLDDE-G 480
Cdd:COG1021 90 IVFFALFRAGA--IPVFA-LPAHRraeISHFAEQSEAvayiipdrhrgfDYRALARELQ---AEVPS--LRHVLVVGDaG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 481 SF-------EESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQI-ASFSFDVF 552
Cdd:COG1021 162 EFtsldallAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALpAAHNFPLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 553 S-GDLArTLTNGGTLIVCPDetrLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDF 631
Cdd:COG1021 242 SpGVLG-VLYAGGTVVLAPD---PSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 632 KTLTDRFGqsMRIINSYGVTEATIDssfyetsmggeCTGDNVP-------IGSPL-PNVHMYVLSQTDQIQPIGVAGELC 703
Cdd:COG1021 318 RRVRPALG--CTLQQVFGMAEGLVN-----------YTRLDDPeevilttQGRPIsPDDEVRIVDEDGNPVPPGEVGELL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 704 IGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRmdyqVK--IN--GYRIETEEIESVLLQT 779
Cdd:COG1021 385 TRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGR----AKdqINrgGEKIAAEEVENLLLAH 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 780 GLVREAA-VAVQHDKNGQAgLAAYIVPSD--VNTNALRAAL-TKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:COG1021 455 PAVHDAAvVAMPDEYLGER-SCAFVVPRGepLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
377-845 |
2.25e-29 |
|
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: 123.98 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 377 TEISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGgvYIPIDAHYPKA--RIEYILRDSGADILL 454
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGlrELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 LQRE----LKHLISNSPESEMSHIFLDD---------------EGSFEESNCNLNLSPA---PEEPVYIIYTSGTTGAPK 512
Cdd:cd05909 84 TSKQfiekLKLHHLFDVEYDARIVYLEDlrakiskadkckaflAGKFPPKWLLRIFGVApvqPDDPAVILFTSGSEGLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 513 GVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASF-SFDvFSGDLARTLTNGGTLIVCPDEtrLEPAEIYKIIKSQRITV 591
Cdd:cd05909 164 GVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFhSFG-LTGCLWLPLLSGIKVVFHPNP--LDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 592 MESTPALiipVMEYV-YRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMggectg 670
Cdd:cd05909 241 LLGTPTF---LRGYArAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG--IRILEGYGTTECSPVISVNTPQS------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 671 DNVP--IGSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQmkftenpFVSGERLYRTGDRACWLPN 747
Cdd:cd05909 310 PNKEgtVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 748 GTIRLLGRMDYQVKINGYRIETEEIESVLLQ--TGLVREAAVAVQHDKNGQAgLAAYIVPSDVNTNALRAALTK-ELPAY 824
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSEilPEDNEVAVVSVPDGRKGEK-IVLLTTTTDTDPSSLNDILKNaGISNL 461
|
490 500
....*....|....*....|.
gi 1238238751 825 MIPAYLIPLVNMPLTLNGKLD 845
Cdd:cd05909 462 AKPSYIHQVEEIPLLGTGKPD 482
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
354-849 |
6.11e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 123.60 E-value: 6.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 354 PFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYI 430
Cdd:PRK06710 25 PLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKlgvEKGDR--VAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 431 PIDAHYPKARIEYILRDSGADILL----------------------------------------LQRELKHLISNSPESE 470
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsatkiehvivtriadflpfpknllypfVQKKQSNLVVKVSESE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 471 MSHIFLDDEgsfEESNCNLNLSPAPEEPVYII-YTSGTTGAPKGVIVTYQNFTHAALAWRQ-IYELDRKPVRLLQIASFs 548
Cdd:PRK06710 183 TIHLWNSVE---KEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEGEEVVLGVLPF- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 549 FDVF--SGDLARTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSD-- 624
Cdd:PRK06710 259 FHVYgmTAVMNLSIMQGYKMVLIP---KFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSApl 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 625 MVKAQD-FKTLTdrfgqSMRIINSYGVTEAT--IDSSF-YETSMGGEctgdnvpIGSPLPNVHMYVLS-QTDQIQPIGVA 699
Cdd:PRK06710 336 PVEVQEkFETVT-----GGKLVEGYGLTESSpvTHSNFlWEKRVPGS-------IGVPWPDTEAMIMSlETGEALPPGEI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 700 GELCIGGAGVAKGYHHKPDltqmkftENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQT 779
Cdd:PRK06710 404 GEIVVKGPQIMKGYWNKPE-------ETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 780 GLVREAAVAVQHDKNGQAGLAAYIV---PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVlkeGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
363-844 |
8.46e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 122.73 E-value: 8.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKA 439
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDlglKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 440 RIEYILRDSGADILLLQRELKHLISNSPESEMSHIFL--------DDEGSF--------EESNCNLNLSPAPEEPVYIIY 503
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLIlslvlggrEAPGGWldfadwaeAGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 504 TSGTTGAPKGVIVtyqnfTHAALAWRQI-------YELDRKPVRLLQI-ASFSFDVFSG-DLARTLTNggTLIVCPDetr 574
Cdd:PRK08316 179 TSGTESLPKGAML-----THRALIAEYVscivagdMSADDIPLHALPLyHCAQLDVFLGpYLYVGATN--VILDAPD--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 575 lePAEIYKIIKSQRITVMESTPALIIPVMEYvyrnqfklPDLDILILGSdMVKAQ---------DFKTLTDRFGQsMRII 645
Cdd:PRK08316 249 --PELILRTIEAERITSFFAPPTVWISLLRH--------PDFDTRDLSS-LRKGYygasimpveVLKELRERLPG-LRFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 646 NSYGVTE----ATIDSSFYETSMGGECtgdnvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQ 721
Cdd:PRK08316 317 NCYGQTEiaplATVLGPEEHLRRPGSA-------GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 722 MKFTENPFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLA 800
Cdd:PRK08316 390 EAFRGGWFHSGDLGVMDEE-------GYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAViGLPDPKWIEA-VT 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1238238751 801 AYIVP---SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:PRK08316 462 AVVVPkagATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
355-849 |
9.37e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 122.29 E-value: 9.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 355 FHRIFEAKAEenPEHIAV-IDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPI 432
Cdd:PRK07514 6 FDALRAAFAD--RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGvKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 433 DAHYPKARIEYILRDSGADILLLQRELKHLISNSPESE-MSHIF-LDDEGSFEESNCNLNLSP-------APEEPVYIIY 503
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAgAPHVEtLDADGTGSLLEAAAAAPDdfetvprGADDLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 504 TSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRL----------LQIASFSfdvfsgdlarTLTNGGTLIVCPdet 573
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIhalpifhthgLFVATNV----------ALLAGASMIFLP--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 574 RLEPAEIYKIIKsqRITVMESTPALiipvmeyvYRNQFKLPDLD--------ILILGSDMVKAQDFKTLTDRFGQsmRII 645
Cdd:PRK07514 231 KFDPDAVLALMP--RATVMMGVPTF--------YTRLLQEPRLTreaaahmrLFISGSAPLLAETHREFQERTGH--AIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 646 NSYGVTEATIDSSF-YEtsmggectGDNVP--IGSPLPNVHMYVL-SQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQ 721
Cdd:PRK07514 299 ERYGMTETNMNTSNpYD--------GERRAgtVGFPLPGVSLRVTdPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 722 MKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLA 800
Cdd:PRK07514 371 EEFRADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAViGVPHPDFGEGVTA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1238238751 801 AyIVPS---DVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK07514 445 V-VVPKpgaALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
376-849 |
2.30e-28 |
|
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: 121.62 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 376 ETEISYRLLNERANRLARTLQNRKGPKPTVAVLA-KRSIDAIVGVLAVMKAGGVYIP--IDAHYP-----KARIEYILRD 447
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQfDDNEDFIPAFWACVLAGFVPAPltVPPTYDepnarLRKLRHIWQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 448 SGADILLLQRELKHLISnsPESEMSHIFLDDEGSFEESNCNLNLSPA----PEEPVYIIYTSGTTGAPKGVIVTYQNFTH 523
Cdd:cd05906 117 LGSPVVLTDAELVAEFA--GLETLSGLPGIRVLSIEELLDTAADHDLpqsrPDDLALLMLTSGSTGFPKAVPLTHRNILA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 524 AALAWRQIYELDRKPVRLLQIAsfsFD-----VFSGDLARTLtnGGTLIVCPDETRL-EPAEIYKIIKSQRITVMEStP- 596
Cdd:cd05906 195 RSAGKIQHNGLTPQDVFLNWVP---LDhvgglVELHLRAVYL--GCQQVHVPTEEILaDPLRWLDLIDRYRVTITWA-Pn 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 597 ---ALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQ---DFKTLTDRFG-QSMRIINSYGVTE----ATIDSSFYETSMG 665
Cdd:cd05906 269 fafALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKtirRLLRLLEPYGlPPDAIRPAFGMTEtcsgVIYSRSFPTYDHS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 666 GECTgdNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRAcWL 745
Cdd:cd05906 349 QALE--FVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 746 PNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE---AAVAVQHDKNGQAGLAAYIVPSDVNTNAL-------RA 815
Cdd:cd05906 420 DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEELAIFFVPEYDLQDALsetlraiRS 499
|
490 500 510
....*....|....*....|....*....|....*..
gi 1238238751 816 ALTKEL---PAYMIPaylIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05906 500 VVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
363-849 |
3.30e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 121.69 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARI 441
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGvGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 442 EYILRDSGADILLLQRELKHLI-SNSPESEMSHIF-------LDDEGSFE---------------------ESNCNLNL- 491
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLAPVVeQVRAETSLRHVIvtsladvLPAEPTLPlpdslraprlaaagaidllpaLRACTAPVp 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 492 --SPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQI-YELDRKPVRLlqiaSFsFDVF--SGD---LARTLTNG 563
Cdd:PRK06178 203 lpPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVaVVGGEDSVFL----SF-LPEFwiAGEnfgLLFPLFSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 564 GTLIVCpdeTRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLdililgsDMVKAQDF-KTLTDRFGQSM 642
Cdd:PRK06178 278 ATLVLL---ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSL-------RQVRVVSFvKKLNPDYRQRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 643 RIIN-------SYGVTEA----TIDSSFYETSMggECTGDNVPIGSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVA 710
Cdd:PRK06178 348 RALTgsvlaeaAWGMTEThtcdTFTAGFQDDDF--DLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 711 KGYHHKPDLTQmkfteNPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQ 790
Cdd:PRK06178 426 KGYWNKPEATA-----EALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGR 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 791 HDKN-GQAGLaAYIVP---SDVNTNALRAALTKELPAYMIPAylIPLVN-MPLTLNGKLDRNAL 849
Cdd:PRK06178 499 PDPDkGQVPV-AFVQLkpgADLTAAALQAWCRENMAVYKVPE--IRIVDaLPMTATGKVRKQDL 559
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
357-805 |
2.43e-27 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 119.05 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVIDNE----TEISYRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYI 430
Cdd:COG1022 15 DLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLAL-GVKPgdRVAILSDNRPEWVIADLAILAAGAVTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 431 PIDAHYPKARIEYILRDSGADILLLQRE-----LKHLISNSPESEmsHIFLDDEGSFEESNCNLNL-------------- 491
Cdd:COG1022 94 PIYPTSSAEEVAYILNDSGAKVLFVEDQeqldkLLEVRDELPSLR--HIVVLDPRGLRDDPRLLSLdellalgrevadpa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 492 -------SPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLL-----QIASFSFDVFSgdlart 559
Cdd:COG1022 172 elearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSflplaHVFERTVSYYA------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 560 LTNGGTLIVCPDETRLEPA-------------EIY-KIIKSQRITVMESTP----------ALIIPVMEYVYRNQ----- 610
Cdd:COG1022 246 LAAGATVAFAESPDTLAEDlrevkptfmlavpRVWeKVYAGIQAKAEEAGGlkrklfrwalAVGRRYARARLAGKspsll 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 611 --FKLPDLDILIlgsdmvkaqdFKTLTDRFGQSMRIINS-----------------------YGVTEATIDSSFYetsmg 665
Cdd:COG1022 326 lrLKHALADKLV----------FSKLREALGGRLRFAVSggaalgpelarffralgipvlegYGLTETSPVITVN----- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 666 geCTGDNVP--IGSPLPNVhmyvlsqtdQIQpIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRAC 743
Cdd:COG1022 391 --RPGDNRIgtVGPPLPGV---------EVK-IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 744 WLPNGTIRLLGRMDYQVKI-NGYRIETEEIESVLLQTGLVREAAVaVQHDKNgqaGLAAYIVP 805
Cdd:COG1022 453 LDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVV-VGDGRP---FLAALIVP 511
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
377-831 |
7.34e-27 |
|
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: 115.77 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 377 TEISYRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILl 454
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIAL-GVEPgdRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 lqrelkhlisnspesemshiFLDDegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYEL 534
Cdd:cd05907 82 --------------------FVED----------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 535 DRKPVRLlqiasfSFDVFSGDLART------LTNGGTLIVCPDETRLEPAeiykiIKSQRITVMESTPAliipVMEYVYr 608
Cdd:cd05907 126 TEGDRHL------SFLPLAHVFERRaglyvpLLAGARIYFASSAETLLDD-----LSEVRPTVFLAVPR----VWEKVY- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 609 nqfklpdldiliLGSDMVKAQDFK-TLTDR-FGQSMR-----------------------IINSYGVTE--ATIDSSFYE 661
Cdd:cd05907 190 ------------AAIKVKAVPGLKrKLFDLaVGGRLRfaasggaplpaellhffralgipVYEGYGLTEtsAVVTLNPPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 662 TSMGGECtgdnvpiGSPLPNVHmyvlsqtdqIQpIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDR 741
Cdd:cd05907 258 DNRIGTV-------GKPLPGVE---------VR-IADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 742 ACWLPNGTIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVREAAVAvqhdKNGQAGLAAYIVPsdvNTNALRAALTKE 820
Cdd:cd05907 315 GEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI----GDGRPFLVALIVP---DPEALEAWAEEH 387
|
490
....*....|.
gi 1238238751 821 LPAYMIPAYLI 831
Cdd:cd05907 388 GIAYTDVAELA 398
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
497-849 |
1.15e-26 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 112.42 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 497 EPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLL-----QIASFSFdvfsgdLARTLTNGGTLIVcPD 571
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLslplyHVGGLAI------LVRSLLAGAELVL-LE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 572 ETRLEPAEIykiiKSQRITVMESTPALIIPVMEYVYRNQfKLPDLDILILGSDMVKAQDFKTLTDRfgqSMRIINSYGVT 651
Cdd:cd17630 74 RNQALAEDL----APPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAADR---GIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 652 EATidSSFYETSMGGECTGDNvpiGSPLPNVhmyvlsqtdQIQpIGVAGELCIGGAGVAKGYHHKPdltqmkfTENPFvS 731
Cdd:cd17630 146 ETA--SQVATKRPDGFGRGGV---GVLLPGR---------ELR-IVEDGEIWVGGASLAMGYLRGQ-------LVPEF-N 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 732 GERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAYIVPSDVNT 810
Cdd:cd17630 203 EDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVvGVPDEELGQRPVAVIVGRGPADP 282
|
330 340 350
....*....|....*....|....*....|....*....
gi 1238238751 811 NALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
364-844 |
1.34e-26 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 116.91 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 364 EENPEHIAVIDNETE------ISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:cd17634 64 RENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDlgvKKGDR--VAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGADILLLQRE---------LKHLISNSPESEMSH----IFLDDEGSFEESNCNLNL---------S 492
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDDALNPNVTSvehvIVLKRTGSDIDWQEGRDLwwrdliakaS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PA-------PEEPVYIIYTSGTTGAPKGVIVTYQNFthaalawrqiyeldrkPVRLLQIASFSFDVFSGDLARTLTN--- 562
Cdd:cd17634 222 PEhqpeamnAEDPLFILYTSGTTGKPKGVLHTTGGY----------------LVYAATTMKYVFDYGPGDIYWCTADvgw 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 563 --GGTLIV-----CPDETRL--------EPAEIYKIIKSQRITVMESTPALIIPVM----EYVYRnqFKLPDLDILILGS 623
Cdd:cd17634 286 vtGHSYLLygplaCGATTLLyegvpnwpTPARMWQVVDKHGVNILYTAPTAIRALMaagdDAIEG--TDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 624 DMVKAQDFKTLTDRFGQSMR-IINSYGVTEATidssfyetsmGGECTgdNVPIGSPL---------PNVHMYVLSQTDQI 693
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEKCpVVDTWWQTETG----------GFMIT--PLPGAIELkagsatrpvFGVQPAVVDNEGHP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 694 QPIGVAGELCIGGA--GVAKGYHHKPDltqmKFTENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEE 771
Cdd:cd17634 432 QPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 772 IESVLLQTGLVREAA-VAVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:cd17634 508 IESVLVAHPKVAEAAvVGIPHAIKGQA-PYAYVVlnhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
351-804 |
2.71e-26 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 115.02 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 351 KDIPFHRIFEAKAEENPEHIAVIDNET--EISYRLLNERANRLARTLQNRKG-PKPTVAVLAKRSIDAIVGVLAVMKAGG 427
Cdd:cd05904 3 TDLPLDSVSFLFASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGrKGDVVLLLSPNSIEFPVAFLAVLSLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 428 VYIPIDAHYPKARIEYILRDSGADILLLQRELKH---------LISNSPESEMSHIFLDDEGSFEESNCNLNLSPapEEP 498
Cdd:cd05904 83 VVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEklaslalpvVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQ--DDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 499 VYIIYTSGTTGAPKGVIVTYQNFThAALA---WRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRL 575
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLI-AMVAqfvAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMP---RF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 576 EPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSdmvkAQDFKTLTDRFGQ---SMRIINSYGVTE 652
Cdd:cd05904 237 DLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGA----APLGKELIEAFRAkfpNVDLGQGYGMTE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 653 ATIDSsfyeTSMGGECtGDNVPIGSP---LPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTEnp 728
Cdd:cd05904 313 STGVV----AMCFAPE-KDRAKYGSVgrlVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK-- 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238751 729 fvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA-VQHDKNGQAGlAAYIV 804
Cdd:cd05904 386 ----EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIpYPDEEAGEVP-MAFVV 457
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
376-813 |
1.03e-25 |
|
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: 112.54 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 376 ETEISYRLLNERANRLARTLQ-NRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSgadill 454
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKiNGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 lqrelkhlisnspesEMSHIFLDDEgsfeesncnlnlspapEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQiYEL 534
Cdd:cd05914 79 ---------------EAKAIFVSDE----------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE-VVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 535 DRKPVRLLQIASFSfDVF--SGDLARTLTNGGTLIVCpdeTRLEPAeiyKIIKSQRITVmesTPALIIPV---MEYVYRN 609
Cdd:cd05914 127 LGKGDKILSILPLH-HIYplTFTLLLPLLNGAHVVFL---DKIPSA---KIIALAFAQV---TPTLGVPVplvIEKIFKM 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 610 QfKLPDLDI--------LILGSDMVKAQDFKTLTDRFGQSMRIINS-----------------------YGVTEAT--ID 656
Cdd:cd05914 197 D-IIPKLTLkkfkfklaKKINNRKIRKLAFKKVHEAFGGNIKEFVIggakinpdveeflrtigfpytigYGMTETApiIS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 657 SSFYETSMGGECtgdnvpiGSPLPNVHMyvlsQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlY 736
Cdd:cd05914 276 YSPPNRIRLGSA-------GKVIDGVEV----RIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------F 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 737 RTGDRACWLPNGTIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKngqAGLAAYIVPSDVNTNAL 813
Cdd:cd05914 339 HTGDLGKIDAEGYLYIRGRKkEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKK---LVALAYIDPDFLDVKAL 413
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
355-849 |
1.41e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 112.91 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 355 FHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIP 431
Cdd:PRK06164 12 LASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAqgvRRGDR--VAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 432 IDAHYPKARIEYILRDSGADILLLQRELKHL--------ISNSPESEMSHIFLDDEGSFE------------------ES 485
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGFKGIdfaailaaVPPDALPPLRAIAVVDDAADAtpapapgarvqlfalpdpAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 486 NCNLNLSPAPEEPVYIIYT-SGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVrLLQIASFS--FDvFSGDLArTLTN 562
Cdd:PRK06164 170 PAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAV-LLAALPFCgvFG-FSTLLG-ALAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 563 GGTLIVCPdetRLEPAEIYKIIKSQRIT-VMESTPAliipvmeyvYRNQFKLPDldililgsdmvKAQDFKTLtDRFG-- 639
Cdd:PRK06164 247 GAPLVCEP---VFDAARTARALRRHRVThTFGNDEM---------LRRILDTAG-----------ERADFPSA-RLFGfa 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 640 ---------------QSMRIINSYGVTEA-------TIDSSFYETSMGGectgdNVPIgSPLPNVHMyVLSQTDQIQPIG 697
Cdd:PRK06164 303 sfapalgelaalaraRGVPLTGLYGSSEVqalvalqPATDPVSVRIEGG-----GRPA-SPEARVRA-RDPQDGALLPDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 698 VAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLL 777
Cdd:PRK06164 376 ESGEIEIRAPSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALE 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 778 QTGLVREA-AVAVQHDknGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNG---KLDRNAL 849
Cdd:PRK06164 450 ALPGVAAAqVVGATRD--GKTVPVAFVIPTDgasPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
363-849 |
3.62e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 111.02 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIE 442
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 443 YILRDSGADILLLQRELKHLISnspESEMSHIFLDD--EGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQN 520
Cdd:PRK07638 91 ERLAISNADMIVTERYKLNDLP---DEEGRVIEIDEwkRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 521 FTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALIi 600
Cdd:PRK07638 168 WLHSFDCNVHDFHMKRED-SVLIAGTLVHSLFLYGAISTLYVGQTVHLMR---KFIPNQVLDKLETENISVMYTVPTML- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 601 pvmEYVYR-NQFKLPDLDILILGSDMVKAQDfKTLTDRFgQSMRIINSYGVTEAtidsSFYETSMGGECTGDNVPIGSPL 679
Cdd:PRK07638 243 ---ESLYKeNRVIENKMKIISSGAKWEAEAK-EKIKNIF-PYAKLYEFYGASEL----SFVTALVDEESERRPNSVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 680 PNVhmyvlsqtdQIQPIGVAGELCIGGAgVAKGYHHKPdltqMKFTEnpFVSGERLYRTGDRACWLP---------NGTI 750
Cdd:PRK07638 314 HNV---------QVRICNEAGEEVQKGE-IGTVYVKSP----QFFMG--YIIGGVLARELNADGWMTvrdvgyedeEGFI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 751 RLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAayIVPSDVNTNALRAALTKELPAYMIPAY 829
Cdd:PRK07638 378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVViGVPDSYWGEKPVA--IIKGSATKQQLKSFCLQRLSSFKIPKE 455
|
490 500
....*....|....*....|
gi 1238238751 830 LIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK07638 456 WHFVDEIPYTNSGKIARMEA 475
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
354-805 |
3.66e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 111.98 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 354 PFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIP 431
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKgdRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 432 IDAHYPKARIEYILRDSGADIL-----LLQR--------ELKHLISN------SPESEMS-HIFLDDEGSFE-------- 483
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAivgseLAPKvapavgnlRLRHVIVAqysdylPAEPEIAvPAWLRAEPPLQalapggvv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 484 --ESNCNLNLSPAPEEPVY-----IIYTSGTTGAPKGVIVTYQNFTHAALA---WRQiyeLDRKPVRLLQIASFSFDVFS 553
Cdd:PRK08314 171 awKEALAAGLAPPPHTAGPddlavLPYTSGTTGVPKGCMHTHRTVMANAVGsvlWSN---STPESVVLAVLPLFHVTGMV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 554 GDLARTLTNGGTLIVCPDETRLEPAEiykIIKSQRITVMESTPALIIPVMEYVYRNQFklpDLDILIL----GSDMVKAQ 629
Cdd:PRK08314 248 HSMNAPIYAGATVVLMPRWDREAAAR---LIERYRVTHWTNIPTMVVDFLASPGLAER---DLSSLRYigggGAAMPEAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 630 DFKtLTDRFGqsMRIINSYGVTEaTIdsSFyetsmggecTGDNVP-------IGSPLPNVHMYVLS-QTDQIQPIGVAGE 701
Cdd:PRK08314 322 AER-LKELTG--LDYVEGYGLTE-TM--AQ---------THSNPPdrpklqcLGIPTFGVDARVIDpETLEELPPGEVGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 702 LCIGGAGVAKGYHHKPDLTQMKFTEnpfVSGERLYRTGDracwlpngtirlLGRMD---Y-----QVK--IN--GYRIET 769
Cdd:PRK08314 387 IVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGD------------LGRMDeegYffitdRLKrmINasGFKVWP 451
|
490 500 510
....*....|....*....|....*....|....*..
gi 1238238751 770 EEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP 805
Cdd:PRK08314 452 AEVENLLYKHPAIQEACViATPDPRRGET-VKAVVVL 487
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
5-218 |
3.71e-25 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 110.27 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 5 FDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNR--NLPALRIQYKDYAVWREGFKtGDAYKT 82
Cdd:cd19535 106 LDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPgePLPPLELSFRDYLLAEQALR-ETAYER 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 83 QEAYWLKQLEG-----ELPVLDLPADHARPPVRSFagdkvSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLSG 157
Cdd:cd19535 185 ARAYWQERLPTlppapQLPLAKDPEEIKEPRFTRR-----EHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSG 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 158 QEDIIVGSPIAGRP--HKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDY 218
Cdd:cd19535 260 QPRFLLNLTLFNRLplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSY 322
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
377-849 |
1.30e-24 |
|
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: 108.67 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 377 TEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADIL 453
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEiglEKGDR--VGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 454 LlqrelkhlisnspesemshiflddegsfeesncnlnlSPAPEEPVYIIYTSGTTGAPKGVIvtyqnftHAalawrqiye 533
Cdd:cd05971 83 V-------------------------------------TDGSDDPALIIYTSGTTGPPKGAL-------HA--------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 534 lDRKPVRLLQIASFSFDVF--SGDLARTLTN----GGTL------------IVCPDETRLEPAEIYKIIKSQRITvMEST 595
Cdd:cd05971 110 -HRVLLGHLPGVQFPFNLFprDGDLYWTPADwawiGGLLdvllpslyfgvpVLAHRMTKFDPKAALDLMSRYGVT-TAFL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 596 PALIIPVMEYVYrNQFKLPDLDILILGS--DMVKAQDFKTLTDRFGQSmrIINSYGVTEATIdssfyetsMGGECTG--- 670
Cdd:cd05971 188 PPTALKMMRQQG-EQLKHAQVKLRAIATggESLGEELLGWAREQFGVE--VNEFYGQTECNL--------VIGNCSAlfp 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 671 -DNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIggagvakgyhHKPDLTQM-------KFTENPFVSGerLYRTGDRA 742
Cdd:cd05971 257 iKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAV----------ELPDPVAFlgywnnpSATEKKMAGD--WLLTGDLG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 743 CWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV------PSDVNTNALRAA 816
Cdd:cd05971 325 RKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgetPSDALAREIQEL 404
|
490 500 510
....*....|....*....|....*....|...
gi 1238238751 817 LTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05971 405 VKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
358-849 |
1.91e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 109.46 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNrKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAA-AGVKRgdRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 YPKARIEYILRDSGADILLLQRELKHLISNSPESEMS--HIFLDDEGSFEESNCNLNLSP-------------APEEPVY 500
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPlpAVWLLDAPASVSVPAGWSTAPlppldapapaaavQPGDTAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 IIYTSGTTGAPKGVIVtyqnfTHAALAWRQIY-----ELDRKPVRLLQIASFSFDVFSGdLARTLTNGGTLIVcpdETRL 575
Cdd:PRK06155 185 ILYTSGTTGPSKGVCC-----PHAQFYWWGRNsaedlEIGADDVLYTTLPLFHTNALNA-FFQALLAGATYVL---EPRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 576 EPAEIYKIIKSQRITVmestpALIIPVMEYVYRNQFKLPD-----LDILILGSdmVKAQDFKTLTDRFGqsMRIINSYGV 650
Cdd:PRK06155 256 SASGFWPAVRRHGATV-----TYLLGAMVSILLSQPARESdrahrVRVALGPG--VPAALHAAFRERFG--VDLLDGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 651 TEAtidssfyetsmggectgdNVPIGSPL------------PNVHMYVLSQTDQIQPIGVAGELCIGGA---GVAKGYHH 715
Cdd:PRK06155 327 TET------------------NFVIAVTHgsqrpgsmgrlaPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 716 KPDLTqmkftenpfVSGER--LYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDK 793
Cdd:PRK06155 389 MPEKT---------VEAWRnlWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSE 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 794 NGQAGLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK06155 460 LGEDEVMAAVVLRDgtaLEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
498-846 |
2.18e-24 |
|
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: 105.57 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 498 PVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFDVFSGDLARTLTNGGTLIVcpdETRLEP 577
Cdd:cd17633 2 PFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGED-AILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 578 AEIYKIIKSQRITVMESTPALIipvmEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEAT-ID 656
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTML----QALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKA-NLIEFYGTSELSfIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 657 SSFYETSMGGEctgdnvPIGSPLPNVHMYVLSQTDqiqpiGVAGELCIggagvakgyhhKPDLTQMKFTENPFVSGERLY 736
Cdd:cd17633 153 YNFNQESRPPN------SVGRPFPNVEIEIRNADG-----GEIGKIFV-----------KSEMVFSGYVRGGFSNPDGWM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 737 RTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAYIVPSdVNTNALRA 815
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVvGIPDARFGEIAVALYSGDK-LTYKQLKR 289
|
330 340 350
....*....|....*....|....*....|.
gi 1238238751 816 ALTKELPAYMIPAYLIPLVNMPLTLNGKLDR 846
Cdd:cd17633 290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
493-846 |
2.61e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 109.32 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PAPEEPVYIIYTSGTTGAPKGVIVTYQN-FTHAA--LAWrqIYELDRKPVRLLQIASFsFDVFSGDLARTLTN--GGTLI 567
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNlFANAAqgKAW--VPGLGDGPERVLAALPM-FHAYGLTLCLTLAVsiGGELV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 568 VCPdetRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINS 647
Cdd:PRK05605 293 LLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGG--LLVEG 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 648 YGVTEatidssfyeTS---MGGECTGDNVP--IGSPLPNVHMYVLSQTD--QIQPIGVAGELCIGGAGVAKGYHHKPDLT 720
Cdd:PRK05605 368 YGLTE---------TSpiiVGNPMSDDRRPgyVGVPFPDTEVRIVDPEDpdETMPDGEEGELLVRGPQVFKGYWNRPEET 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 721 QMKFTENpfvsgerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLA 800
Cdd:PRK05605 439 AKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVV 511
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1238238751 801 AYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDR 846
Cdd:PRK05605 512 AAVVLEPgaaLDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
378-849 |
5.81e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 107.16 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 378 EISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVyipidahyPkarieyILRDSGADIll 454
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAygiRRGMR--AVLMVPPGPDFFALTFALFKAGAV--------P------VLIDPGMGR-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 lqRELKH-LISNSPESemshiFLDDegsfeesncnlnlsPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYE 533
Cdd:cd05910 64 --KNLKQcLQEAEPDA-----FIGI--------------PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 534 LDRKPVRLlqiASFS-FDVFSGDLARTltnggTLIVCPDETR---LEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRN 609
Cdd:cd05910 123 IRPGEVDL---ATFPlFALFGPALGLT-----SVIPDMDPTRparADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 610 QFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMRIINSYGVTEA----TIDSSFYETSMGGECT-GDNVPIGSPLPNVHM 684
Cdd:cd05910 195 GITLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlpvsSIGSRELLATTTAATSgGAGTCVGRPIPGVRV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 685 YVLSQTDQ---------IQPIGVAGELCIGGAGVAKGYHHKPDLTqmKFTENPFVSGERLYRTGDRACWLPNGTIRLLGR 755
Cdd:cd05910 275 RIIEIDDEpiaewddtlELPRGEIGEITVTGPTVTPTYVNRPVAT--ALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 756 MDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAY------IVPSDVNTNALRAALTKELPAYMIPAY 829
Cdd:cd05910 353 KAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVeplpgtITPRARLEQELRALAKDYPHTQRIGRF 432
|
490 500
....*....|....*....|.
gi 1238238751 830 LI-PLVNMPLTLNGKLDRNAL 849
Cdd:cd05910 433 LIhPSFPVDIRHNAKIFREKL 453
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
378-849 |
7.11e-24 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 107.46 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 378 EISYRLLNERANRLAR---TLQNRKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILL 454
Cdd:PRK08008 37 RYSYLELNEEINRTANlfySLGIRKGDK--VALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 LQRELKHL---ISNSPESEMSHIFLDDEGSFEESN------------CNLNLSPA--PEEPVYIIYTSGTTGAPKGVIVT 517
Cdd:PRK08008 115 TSAQFYPMyrqIQQEDATPLRHICLTRVALPADDGvssftqlkaqqpATLCYAPPlsTDDTAEILFTSGTTSRPKGVVIT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 518 YQNFTHAAL--AWRQiyELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVcpdetrLE---PAEIYKIIKSQRITVM 592
Cdd:PRK08008 195 HYNLRFAGYysAWQC--ALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL------LEkysARAFWGQVCKYRATIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 593 ESTPALI-----IPVMEyvYRNQFKLPDLDILILGSDMVKaQDFKTltdRFGqsMRIINSYGVTeatidssfyETSMG-- 665
Cdd:PRK08008 267 ECIPMMIrtlmvQPPSA--NDRQHCLREVMFYLNLSDQEK-DAFEE---RFG--VRLLTSYGMT---------ETIVGii 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 666 GECTGDN---VPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGG-AG--VAKGYHHKPDLTQMKFTENPFVsgerlyRTG 739
Cdd:PRK08008 330 GDRPGDKrrwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYYLDPKATAKVLEADGWL------HTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 740 DRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD---VNTNALRAA 816
Cdd:PRK08008 404 DTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgetLSEEEFFAF 483
|
490 500 510
....*....|....*....|....*....|...
gi 1238238751 817 LTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK08008 484 CEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
357-823 |
7.32e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 107.68 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVID----------NETEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVM 423
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAagiGRGMR--AVLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 424 KAGGVYIPIDAHYPKARIEYILRDSGAD------------ILLL--QRELKHLISNSPESEMSHIFLDdegSFEESNCNL 489
Cdd:PRK09274 88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDafigipkahlarRLFGwgKPSVRRLVTVGGRLLWGGTTLA---TLLRDGAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 490 NLSPA---PEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLlqiASFS-FDVFSGDLartltnGGT 565
Cdd:PRK09274 165 PFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL---PTFPlFALFGPAL------GMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 566 LIVCP-DETR---LEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQS 641
Cdd:PRK09274 236 SVIPDmDPTRpatVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 642 MRIINSYGVTEA----TIDSS--FYETSMGGECtGDNVPIGSPLPNVHMYVLSQTD----QIQ-----PIGVAGELCIGG 706
Cdd:PRK09274 316 AEILTPYGATEAlpisSIESReiLFATRAATDN-GAGICVGRPVDGVEVRIIAISDapipEWDdalrlATGEIGEIVVAG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 707 AGVAKGYHHKPDLTQM-KFTEnpfVSGERLYRTGDrACWL-PNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLV-R 783
Cdd:PRK09274 395 PMVTRSYYNRPEATRLaKIPD---GQGDVWHRMGD-LGYLdAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkR 470
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1238238751 784 EAAVAVqhdKNGQAGLAAYIVPSDVNTNALRAALTKELPA 823
Cdd:PRK09274 471 SALVGV---GVPGAQRPVLCVELEPGVACSKSALYQELRA 507
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
358-849 |
4.77e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 105.35 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVI--DNETEISYRLLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:PRK05852 21 LVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLT-RSGLLPgdRVALRMGSNAEFVVALLAASRADLVVVPLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHYPKARIEYILRDSGADILLLQRELKH------------LISNSPESEMSH----IFLDDEGSFE-ESNCNLNLSPape 496
Cdd:PRK05852 100 PALPIAEQRVRSQAAGARVVLIDADGPHdraepttrwwplTVNVGGDSGPSGgtlsVHLDAATEPTpATSTPEGLRP--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 497 EPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVcPDETRLE 576
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLL-PARGRFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 577 PAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQF--KLPDLDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTEAT 654
Cdd:PRK05852 256 AHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSgrKPAALRFIRSCSAPLTAETAQALQTEFAAPV--VCAFGMTEAT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 655 IDSSfyETSMGGECTGDNvPIGSPLP-----NVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPF 729
Cdd:PRK05852 334 HQVT--TTQIEGIGQTEN-PVVSTGLvgrstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 730 vsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPSD- 807
Cdd:PRK05852 411 -------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfGVPDQLYGEA-VAAVIVPREs 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1238238751 808 --VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK05852 483 apPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
371-849 |
6.63e-23 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 103.71 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 371 AVIDNETEISYRLLNERANRLARTLQNRKGPKPTVAVLAkRSIDAIVGV---LAVMKAGGVYIPIDAHYPKARIEYILRD 447
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLL-RGSNSPELVacwFGIQKAGAIAVATMPLLRPKELAYILDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 448 SgadilllqrelkhlisnspesEMSHIFLDDEGSFEESNCNLNlspapeepvyiiYTSGTTGAPKGVIVTYQNFTHAALA 527
Cdd:cd05958 82 A---------------------RITVALCAHALTASDDICILA------------FTSGTTGAPKATMHFHRDPLASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 528 W-RQIYELdRKPVRLLQIASFSFDV-FSGDLARTLTNGGTLIVCPDETrlePAEIYKIIKSQRITVMESTPALIIPVMEY 605
Cdd:cd05958 129 YaVNVLRL-REDDRFVGSPPLAFTFgLGGVLLFPFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 606 VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATidsSFYETSMGGECTGDNVpiGSPLPNVHMY 685
Cdd:cd05958 205 PDAAGPDLSSLRKCVSAGEALPAALHRAWKEATG--IPIIDGIGSTEMF---HIFISARPGDARPGAT--GKPVPGYEAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 686 VLSQTDQIQPIGVAGELCIGGagvAKGYHHKPDLTQMKftenpFVSGERLYrTGDRACWLPNGTIRLLGRMDYQVKINGY 765
Cdd:cd05958 278 VVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRT-----YVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 766 RIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV------PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLT 839
Cdd:cd05958 349 NIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgviPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRT 428
|
490
....*....|
gi 1238238751 840 LNGKLDRNAL 849
Cdd:cd05958 429 ATGKLQRFAL 438
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
363-848 |
2.12e-22 |
|
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: 103.09 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAV--IDNETE----ISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPidAHY 436
Cdd:cd05931 3 AAARPDRPAYtfLDDEGGreetLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP--LPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 437 PK-----ARIEYILRDSGADILL----LQRELKHLISNSPESEMSHIFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGT 507
Cdd:cd05931 81 PTpgrhaERLAAILADAGPRVVLttaaALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 508 TGAPKGVIVTYQNFTHAALAWRQIYELDRKPVrllqIAS---FSFD--VFSGDLArTLTNGGTLIVCPDETRL-EPAEIY 581
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAYGLDPGDV----VVSwlpLYHDmgLIGGLLT-PLYSGGPSVLMSPAAFLrRPLRWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 582 KIIKSQRITVmesTPAliiP------VMEYVYRNQfkLPDLD-----ILILGSDMVKAQDFKTLTDRFG------QSMRi 644
Cdd:cd05931 236 RLISRYRATI---SAA---PnfaydlCVRRVRDED--LEGLDlsswrVALNGAEPVRPATLRRFAEAFApfgfrpEAFR- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 645 iNSYGVTEATIDSSFYETSMGGECTGDN---------------------VPIGSPLPNVHMYVL-SQTDQIQPIGVAGEL 702
Cdd:cd05931 307 -PSYGLAEATLFVSGGPPGTGPVVLRVDrdalagravavaaddpaarelVSCGRPLPDQEVRIVdPETGRELPDGEVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 703 CIGGAGVAKGYHHKPDLTQMKF------TENPFVsgerlyRTGDRAcWLPNGTIRLLGRMDYQVKINGYRIETEEIE-SV 775
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFgalaatDEGGWL------RTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEaTA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 776 LLQTGLVRE---AAVAVQHDKNGQAGLAAYIVPSDVNT------NALRAALTKElpaYMIPAYLIPLVN---MPLTLNGK 843
Cdd:cd05931 459 EEAHPALRPgcvAAFSVPDDGEERLVVVAEVERGADPAdlaaiaAAIRAAVARE---HGVAPADVVLVRpgsIPRTSSGK 535
|
....*
gi 1238238751 844 LDRNA 848
Cdd:cd05931 536 IQRRA 540
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
496-846 |
2.40e-22 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 100.03 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 496 EEPVYIIYTSGTTGAPKGVIVTYQNFThAALAWRQIYEL----DRKPVRLLQIAsfsfdvFSGDLARTLT---NGGTLIV 568
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFF-AVPDILQKEGLnwvvGDVTYLPLPAT------HIGGLWWILTcliHGGLCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 569 CPDETRLEpaEIYKIIKSQRITVMESTPALIIP-VMEYVYRNQFkLPDLDILILGSDMVKAQDfKTLTDRFGQSmRIINS 647
Cdd:cd17635 74 GGENTTYK--SLFKILTTNAVTTTCLVPTLLSKlVSELKSANAT-VPSLRLIGYGGSRAIAAD-VRFIEATGLT-NTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 648 YGVTEATiDSSFYETSMGGECTGdnvPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTEN 727
Cdd:cd17635 149 YGLSETG-TALCLPTDDDSIEIN---AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 728 PFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPSD 807
Cdd:cd17635 225 WVNTGDLGERRED-------GFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1238238751 808 V-NTNALRA---ALTKELPAYMIPAYLIPLVNMPLTLNGKLDR 846
Cdd:cd17635 298 ElDENAIRAlkhTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
374-805 |
5.34e-22 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 101.28 E-value: 5.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 374 DNETEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGA 450
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSlgvKAGEK--VALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 451 DILLLQrelkhlisNSPESEMShiflddegsfeesncnlnlspapeepvyIIYTSGTTGAPKGVIVTYQNFTHAAlawRQ 530
Cdd:cd17640 79 VALVVE--------NDSDDLAT----------------------------IIYTSGTTGNPKGVMLTHANLLHQI---RS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 531 IYELDRKPV--RLLQI--------ASFSFDVFSGDLARTLTNGGTLIvcPDETRLEPaeiykiiksqriTVMESTPALII 600
Cdd:cd17640 120 LSDIVPPQPgdRFLSIlpiwhsyeRSAEYFIFACGCSQAYTSIRTLK--DDLKRVKP------------HYIVSVPRLWE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 601 PVMEYVYRNQFKLPDLDILILGSdMVKAQDFKTL----------TDRFGQS--MRIINSYGVTeatidssfyETSMGGEC 668
Cdd:cd17640 186 SLYSGIQKQVSKSSPIKQFLFLF-FLSGGIFKFGisgggalpphVDTFFEAigIEVLNGYGLT---------ETSPVVSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 669 --TGDNV--PIGSPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRAC 743
Cdd:cd17640 256 rrLKCNVrgSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGW 329
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 744 WLPNGTIRLLGRM-DYQVKINGYRIETEEIESVLLQTGLVrEAAVAVQHDkngQAGLAAYIVP 805
Cdd:cd17640 330 LTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSPFI-EQIMVVGQD---QKRLGALIVP 388
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
367-849 |
7.58e-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: 100.84 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRS---IDAIVGVLAvmkAGGVYIPIDAHYPKARIE 442
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGiSRGDTVAVLAPNTpamYELHFGVPM---AGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 443 YILRDSGADILLLQRELKH---LISNSPESEMshiflddegsfeesncnlnLSPAPE-EPVYIIYTSGTTGAPKGVIVT- 517
Cdd:cd12118 95 FILRHSEAKVLFVDREFEYedlLAEGDPDFEW-------------------IPPADEwDPIALNYTSGTTGRPKGVVYHh 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 518 ---YQNFTHAALAWrqiyELDRKPVRLLQIASFSFDVFSGDLARTlTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMES 594
Cdd:cd12118 156 rgaYLNALANILEW----EMKQHPVYLWTLPMFHCNGWCFPWTVA-AVGGTNVCLR---KVDAKAIYDLIEKHKVTHFCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 595 TPALIIPVMEYVYRNQFKLPD-LDILILGSdmvkAQDFKTLTDRFGQSMRIINSYGVTEATIDSSFYETSMGGEctgdnv 673
Cdd:cd12118 228 APTVLNMLANAPPSDARPLPHrVHVMTAGA----PPPAAVLAKMEELGFDVTHVYGLTETYGPATVCAWKPEWD------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 674 piGSPLPN---------VHMYVLSQTDQIQPIGV---------AGELCIGGAGVAKGYHHKPDLtqmkfTENPFVSGerL 735
Cdd:cd12118 298 --ELPTEErarlkarqgVRYVGLEEVDVLDPETMkpvprdgktIGEIVFRGNIVMKGYLKNPEA-----TAEAFRGG--W 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 736 YRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV---PSDVNTN 811
Cdd:cd12118 369 FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVvARPDEKWGEV-PCAFVElkeGAKVTEE 447
|
490 500 510
....*....|....*....|....*....|....*...
gi 1238238751 812 ALRAALTKELPAYMIPAYLIpLVNMPLTLNGKLDRNAL 849
Cdd:cd12118 448 EIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVL 484
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
363-844 |
9.21e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 101.27 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQNR---KGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKA 439
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARgvrKGDR--ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 440 RIEYILRDSGADILLLQREL-KHL-ISNSPESEMSHIFLDDEGSFEES-----NCNLNLSPAP-----EEPVYIIYTSGT 507
Cdd:PRK07470 95 EVAYLAEASGARAMICHADFpEHAaAVRAASPDLTHVVAIGGARAGLDyealvARHLGARVANaavdhDDPCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 508 TGAPKGVIVTYQNFT-----HAALAWRQIYELDRKPV-----------RLLQIAsfsfdvfsgdlartltNGGTLIVCPD 571
Cdd:PRK07470 175 TGRPKAAVLTHGQMAfvitnHLADLMPGTTEQDASLVvaplshgagihQLCQVA----------------RGAATVLLPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 572 EtRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILIL-GSDMVKAqDFKTLTDRFGQSmrIINSYGV 650
Cdd:PRK07470 239 E-RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYaGAPMYRA-DQKRALAKLGKV--LVQYFGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 651 TEATIDSSFYETSMGGECTGDNVPIGS-PLPNVHMYVLSQTDQIQPI--GVAGELCIGGAGVAKGYHHKPDLTQMKFTEN 727
Cdd:PRK07470 315 GEVTGNITVLPPALHDAEDGPDARIGTcGFERTGMEVQIQDDEGRELppGETGEICVIGPAVFAGYYNNPEANAKAFRDG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 728 PFvsgerlyRTGDracwlpngtirlLGRMDYQ--VKING-----Y-----RIETEEIESVLLQTGLVREAAV-AVQHDKN 794
Cdd:PRK07470 395 WF-------RTGD------------LGHLDARgfLYITGrasdmYisggsNVYPREIEEKLLTHPAVSEVAVlGVPDPVW 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 795 GQAGLAAyIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:PRK07470 456 GEVGVAV-CVARDgapVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
344-851 |
1.29e-21 |
|
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: 101.03 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 344 TQVEFAQKDIPFHRIF-----------EAKAEENPEHIAVIDNETE------ISYRLLNERANRLA---RTLQNRKGPKp 403
Cdd:cd05968 40 YQTLDLSGGKPWAAWFvggrmniveqlLDKWLADTRTRPALRWEGEdgtsrtLTYGELLYEVKRLAnglRALGVGKGDR- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 404 tVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILL-------------LQRELKHLISNSPESE 470
Cdd:cd05968 119 -VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItadgftrrgrevnLKEEADKACAQCPTVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 471 ----MSHIFLDDEGS---------FEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFthaalawrqiyeldrk 537
Cdd:cd05968 198 kvvvVRHLGNDFTPAkgrdlsydeEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGF---------------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 538 PVRLLQIASFSFDVFSGDLAR----------------TLTNGGTLIV---CPDETrlEPAEIYKIIKSQRITVMESTPAL 598
Cdd:cd05968 262 PLKAAQDMYFQFDLKPGDLLTwftdlgwmmgpwlifgGLILGATMVLydgAPDHP--KADRLWRMVEDHEITHLGLSPTL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 599 IIPVMEYvyrnqfklpdldililGSDMVKAQDFKtltdrfgqSMRIINSYGvteATID----SSFYETSMGGEC-----T 669
Cdd:cd05968 340 IRALKPR----------------GDAPVNAHDLS--------SLRVLGSTG---EPWNpepwNWLFETVGKGRNpiinyS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 670 GD---------NVPI--------GSPLPNVHMYVLSqtDQIQPI-GVAGELCIGGA--GVAKGYHHKPDltqmKFTENPF 729
Cdd:cd05968 393 GGteisggilgNVLIkpikpssfNGPVPGMKADVLD--ESGKPArPEVGELVLLAPwpGMTRGFWRDED----RYLETYW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 730 VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE-AAVAVQHDKNGQAgLAAYIV---- 804
Cdd:cd05968 467 SRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEsAAIGVPHPVKGEA-IVCFVVlkpg 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1238238751 805 --PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPA 851
Cdd:cd05968 546 vtPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
660-940 |
2.62e-21 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 95.97 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 660 YETSMGGECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGElcIGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTG 739
Cdd:COG3433 5 TPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGE--GGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 740 DRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQH----DKNGQAGLAAYIVPSDVNTNALRA 815
Cdd:COG3433 83 DDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAalrgAGVGLLLIVGAVAALDGLAAAAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 816 ALTKELPAYMIPAYLIPLVNMPLTLNGKL-DRNALPAPNNVLSRPYTAPVNDLQKTMAY-----IWEDVLSMS--RVGIH 887
Cdd:COG3433 163 AALDKVPPDVVAASAVVALDALLLLALKVvARAAPALAAAEALLAAASPAPALETALTEeelraDVAELLGVDpeEIDPD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 888 DSFFELGGDSIKALQVAARLAAEGWSMTIRDLFRYSTIQELCGHITPLASQAD 940
Cdd:COG3433 243 DNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
371-852 |
3.53e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 99.00 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 371 AVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSG 449
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGvRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 450 ADILLLQRELKH------------LISNSPESEMSHIFLDDEG--------SFEE--SNCNLNLSPAPEEPVYIIYTSGT 507
Cdd:PRK12406 84 ARVLIAHADLLHglasalpagvtvLSVPTPPEIAAAYRISPALltppagaiDWEGwlAQQEPYDGPPVPQPQSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 508 TGAPKGV---IVTYQNFTHAALAWRQIYELDRKPVRLL-----QIASFSFDVFSGDLartltnGGTLIVCPdetRLEPAE 579
Cdd:PRK12406 164 TGHPKGVrraAPTPEQAAAAEQMRALIYGLKPGIRALLtgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 580 IYKIIKSQRITVMESTPALIIPVM---EYVyRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmrIINSYGVTeatid 656
Cdd:PRK12406 235 LLQLIERHRITHMHMVPTMFIRLLklpEEV-RAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV--IYEYYGST----- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 657 ssfyETSMGGECTGD---NVP--IGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAK-GYHHKPDltqmKFTEnpfV 730
Cdd:PRK12406 307 ----ESGAVTFATSEdalSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPE----KRAE---I 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 731 SGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN-GQAgLAAYIVP---S 806
Cdd:PRK12406 376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEfGEA-LMAVVEPqpgA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1238238751 807 DVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAP 852
Cdd:PRK12406 455 TLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
363-849 |
6.36e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 98.67 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNE-TEISYRLLNERANRLARTLQNrKGPKPTVAV---LAKRSIDAIVgVLAVMKAGGVYIPIDAHYPK 438
Cdd:PRK06087 33 ARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLA-KGIEPGDRVafqLPGWCEFTII-YLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 439 ARIEYILRDSGAD----------------ILLLQRELKHLI------SNSPESE---MSHIFLDDEGSFEESNCNLNlsp 493
Cdd:PRK06087 111 AELVWVLNKCQAKmffaptlfkqtrpvdlILPLQNQLPQLQqivgvdKLAPATSslsLSQIIADYEPLTTAITTHGD--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 494 apeEPVYIIYTSGTTGAPKGVIVTYQN--FTHAA------LAWRQIYELdrkPVRLLQIASFsfdvFSGDLARTLTNGGT 565
Cdd:PRK06087 188 ---ELAAVLFTSGTEGLPKGVMLTHNNilASERAycarlnLTWQDVFMM---PAPLGHATGF----LHGVTAPFLIGARS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 566 LIvcpdETRLEPAEIYKIIKSQRIT-VMESTPaLIIPVMEYVYRNQFKLPDLDILILGSDMVKAqdfKTLTDRFGQSMRI 644
Cdd:PRK06087 258 VL----LDIFTPDACLALLEQQRCTcMLGATP-FIYDLLNLLEKQPADLSALRFFLCGGTTIPK---KVARECQQRGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 645 INSYGVTEatidSSFYETSMGGECTGDNVPI-GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMK 723
Cdd:PRK06087 330 LSVYGSTE----SSPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 724 FTEnpfvsgERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYI 803
Cdd:PRK06087 406 LDE------EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1238238751 804 VPSD-VNTNALRAAL----TKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK06087 480 VLKApHHSLTLEEVVaffsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
359-846 |
6.56e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 98.69 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 359 FEAKAEENPEHIAVIDNETEI--SYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:PRK12583 24 FDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGvQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 YPKARIEYILRDSGADIL-------------LLQRELKHLISNSPEsEMSH---------IFLDDEG-----SFEE---- 484
Cdd:PRK12583 104 YRASELEYALGQSGVRWVicadafktsdyhaMLQELLPGLAEGQPG-ALACerlpelrgvVSLAPAPppgflAWHElqar 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 485 ----SNCNLNLSPA---PEEPVYIIYTSGTTGAPKGVIVTYQN------FTHAALAwrqIYELDR--KPVRLLQiasfSF 549
Cdd:PRK12583 183 getvSREALAERQAsldRDDPINIQYTSGTTGFPKGATLSHHNilnngyFVAESLG---LTEHDRlcVPVPLYH----CF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 550 DVFSGDLArTLTNGGTLIVCPDEtrLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQ 629
Cdd:PRK12583 256 GMVLANLG-CMTVGACLVYPNEA--FDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 630 DFKTLTDRFGQSMRIInSYGVTEATIDSsfYETsmggeCTGDNVP-----IGSPLPNVHMYVLSQTDQIQPIGVAGELCI 704
Cdd:PRK12583 333 VMRRVMDEMHMAEVQI-AYGMTETSPVS--LQT-----TAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 705 GGAGVAKGYHHKPDLTQMKFTENPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE 784
Cdd:PRK12583 405 RGYSVMKGYWNNPEATAESIDEDGWM------HTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238751 785 AAV-AVQHDKNGQAgLAAYIV--PSD-VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDR 846
Cdd:PRK12583 479 VQVfGVPDEKYGEE-IVAWVRlhPGHaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
359-852 |
1.41e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.52 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 359 FEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKP-TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYP 437
Cdd:PRK13382 49 FAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPrVVGIMCRNHRGFVEALLAANRIGADILLLNTSFA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 438 KARIEYILRDSGADILLLQRELKHLI----SNSPESEMSHIFLDDEGS-----FEESNCNLNLSPAPEEPVYIIYTSGTT 508
Cdd:PRK13382 129 GPALAEVVTREGVDTVIYDEEFSATVdralADCPQATRIVAWTDEDHDltvevLIAAHAGQRPEPTGRKGRVILLTSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 509 GAPKGvivTYQNFTHAALAWRQIyeLDRKPVRLLQ---IAS-------FSFDVFSGDLARTLTNggtlivcpdETRLEPA 578
Cdd:PRK13382 209 GTPKG---ARRSGPGGIGTLKAI--LDRTPWRAEEptvIVApmfhawgFSQLVLAASLACTIVT---------RRRFDPE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 579 EIYKIIKSQRITVMESTPALIIPVMEYV--YRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmrIINSYGVTEAtid 656
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV--IYNNYNATEA--- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 657 ssfyetSMGGECTGDNV-----PIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDltqmKFTENPFVS 731
Cdd:PRK13382 350 ------GMIATATPADLraapdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST----KDFHDGFMA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 732 gerlyrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVPSD--- 807
Cdd:PRK13382 420 ------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAViGVDDEQYGQR-LAAFVVLKPgas 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1238238751 808 VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAP 852
Cdd:PRK13382 493 ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
503-849 |
2.88e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 96.81 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 503 YTSGTTGAPKGVIVTYQNF------THAALA---------WRQIYELDRKPVRLLQIASFSFD----VFSGdlartltNG 563
Cdd:PRK12492 214 YTGGTTGLAKGAMLTHGNLvanmlqVRACLSqlgpdgqplMKEGQEVMIAPLPLYHIYAFTANcmcmMVSG-------NH 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 564 GTLIVCPdetRLEPAEIyKIIKSQRITVMESTPALIIPVMEYvyrNQFKLPDLDILIL----GSDMVKA--QDFKTLTdr 637
Cdd:PRK12492 287 NVLITNP---RDIPGFI-KELGKWRFSALLGLNTLFVALMDH---PGFKDLDFSALKLtnsgGTALVKAtaERWEQLT-- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 638 fgqSMRIINSYGVTEAtidSSFYETSMGGECTGDNVpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKP 717
Cdd:PRK12492 358 ---GCTIVEGYGLTET---SPVASTNPYGELARLGT-VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQP 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 718 DLTQmkftenPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE-AAVAVQHDKNGQ 796
Cdd:PRK12492 431 EATA------EALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANcAAIGVPDERSGE 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 797 AgLAAYIVPSD--VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK12492 505 A-VKLFVVARDpgLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
358-846 |
4.44e-20 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 96.03 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVI-----DNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIP 431
Cdd:cd05970 22 VVDAMAKEYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGiGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 432 IDAHYPKARIEYILRDSGADILL------LQRELKHLISNSPESEMSHIFLDD--EG--SFEESNCNL---------NLS 492
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVaiaednIPEEIEKAAPECPSKPKLVWVGDPvpEGwiDFRKLIKNAspdferptaNSY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PAPEEPVYIIYTSGTTGAPKGVivtYQNFTHaalawrqiyeldrkPVRLLQIASFSFDVFSGDLARTLTN---------- 562
Cdd:cd05970 182 PCGEDILLVYFSSGTTGMPKMV---EHDFTY--------------PLGHIVTAKYWQNVREGGLHLTVADtgwgkavwgk 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 563 ------GGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPAliipvmeyVYR-------NQFKLPDLDILILGSDMVKAQ 629
Cdd:cd05970 245 iygqwiAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPT--------IYRfliredlSRYDLSSLRYCTTAGEALNPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 630 DFKTLTDRFGqsMRIINSYGVTEATIDS---SFYETSMGGectgdnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGG 706
Cdd:cd05970 317 VFNTFKEKTG--IKLMEGFGQTETTLTIatfPWMEPKPGS--------MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 707 A-----GVAKGYHHKPDLTQMKFTENpfvsgerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGL 781
Cdd:cd05970 387 SkgkpvGLFGGYYKDAEKTAEVWHDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238238751 782 VREAAV-AVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDR 846
Cdd:cd05970 460 VLECAVtGVPDPIRGQV-VKATIVlakgyePSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
950-1380 |
8.18e-20 |
|
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: 93.81 E-value: 8.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 950 LTPIQRRFFgqvhaFHYHYNQSV------MLFSEKG-FNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrgINHKD 1022
Cdd:cd19543 4 LSPMQEGML-----FHSLLDPGSgayveqMVITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQ----VVLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1023 HELfGLYISDWTKAS-LERAHLDEKLAAEEtviQSK-MNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLED 1099
Cdd:cd19543 75 RKL-PWRELDLSHLSeAEQEAELEALAEED---RERgFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1100 LAAAYQQALEKKEIQLPPkTDSYLSYADGLTQ--IAESKQllsektYWQTILDAHTAF--LPKDIENVPDKLQMNsDAAA 1175
Cdd:cd19543 151 LFAIYAALGEGQPPSLPP-VRPYRDYIAWLQRqdKEAAEA------YWREYLAGFEEPtpLPKELPADADGSYEP-GEVS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1176 FVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDisRTVGWFTSIYPILLDMG 1255
Cdd:cd19543 223 FELSAELTARLQ-ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIE--TMVGLFINTLPVRVRLD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1256 IPEPF--------EDQLA---------YRIKTTKDMlrrvpnkgtGYGLLTHIgelrhkepeVSF-NY--LGQFSEEKEV 1315
Cdd:cd19543 300 PDQTVlellkdlqAQQLElreheyvplYEIQAWSEG---------KQALFDHL---------LVFeNYpvDESLEEEQDE 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238751 1316 ETFQLSyyqpryEIAGEREREYELDINAlITDGRLHVKAVY-TQVFSKHSIECFMDRFhRHLIETI 1380
Cdd:cd19543 362 DGLRIT------DVSAEEQTNYPLTVVA-IPGEELTIKLSYdAEVFDEATIERLLGHL-RRVLEQV 419
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
492-849 |
1.19e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 95.76 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 492 SPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASF-SFDvFSGDLARTLTNGGTLIVCP 570
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFhSFG-LTVTLWLPLLEGIKVVYHP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 571 DETrlEPAEIYKIIKSQRITVMESTPALIipvMEYVyRNQFKLPD----LDILILGSDMVK---AQDFKtltDRFGqsMR 643
Cdd:PRK08633 857 DPT--DALGIAKLVAKHRATILLGTPTFL---RLYL-RNKKLHPLmfasLRLVVAGAEKLKpevADAFE---EKFG--IR 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 644 IINSYGVTEAT--IDSSFYETsmggECTGDNVPIGS-------PLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGY 713
Cdd:PRK08633 926 ILEGYGATETSpvASVNLPDV----LAADFKRQTGSkegsvgmPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 714 HHKPDLTQMKFTEnpfVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGY-----RIEtEEIeSVLLQTGLVREAAVA 788
Cdd:PRK08633 1002 LGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEmvplgAVE-EEL-AKALGGEEVVFAVTA 1076
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238238751 789 VQHDKNGQAgLAAYIVPSDVNTNALRAALTK-ELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK08633 1077 VPDEKKGEK-LVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
374-787 |
1.93e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 94.19 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 374 DNETEISYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPI-DAHYPKA---RIEyilr 446
Cdd:PRK04319 69 SRKEKYTYKELKELSNKFANVLKElgvEKGDR--VFIFMPRIPELYFALLGALKNGAIVGPLfEAFMEEAvrdRLE---- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 447 DSGADIL-----LLQR-------ELKHLISNSPESEMSHIFLDDEGSFEESNCNLNLSP-APEEPVYIIYTSGTTGAPKG 513
Cdd:PRK04319 143 DSEAKVLittpaLLERkpaddlpSLKHVLLVGEDVEEGPGTLDFNALMEQASDEFDIEWtDREDGAILHYTSGSTGKPKG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 514 VI-VTYQNFTHAALAWrqiYELDRKPVrllqiasfsfDVF-----SGDLART-------LTNGGTLIVcpDETRLEPAEI 580
Cdd:PRK04319 223 VLhVHNAMLQHYQTGK---YVLDLHED----------DVYwctadPGWVTGTsygifapWLNGATNVI--DGGRFSPERW 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 581 YKIIKSQRITVMESTPALIIPVMEyvyrnqfklpdldiliLGSDMVKAQDFKTLtdrfgqsmRIINSYG----------- 649
Cdd:PRK04319 288 YRILEDYKVTVWYTAPTAIRMLMG----------------AGDDLVKKYDLSSL--------RHILSVGeplnpevvrwg 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 650 --VTEATIDSSFYETSMGGE--CTGDNVPI-----GSPLPNVHMYVLSQTDQIQPIGVAGELCI--GGAGVAKGYHHKPD 718
Cdd:PRK04319 344 mkVFGLPIHDNWWMTETGGImiANYPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 719 ltqmKFtENPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV 787
Cdd:PRK04319 424 ----KY-ESYFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
501-844 |
2.05e-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: 91.02 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 IIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELdRKPVRLLQIASF--SFDVFSGDLArTLTNGGTLIvcPDETrLEPA 578
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADL-TEDDRYLIINPFfhTFGYKAGIVA-CLLTGATVV--PVAV-FDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 579 EIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqSMRIINSYGVTEAtidss 658
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELG-FETVLTAYGLTEA----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 659 fyetSMGGEC-TGDNV-----PIGSPLPNVHMyvlsqtdqiqPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVsg 732
Cdd:cd17638 154 ----GVATMCrPGDDAetvatTCGRACPGFEV----------RIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWL-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 733 erlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGlAAYIV---PSDV 808
Cdd:cd17638 218 ----HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAViGVPDERMGEVG-KAFVVarpGVTL 292
|
330 340 350
....*....|....*....|....*....|....*.
gi 1238238751 809 NTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:cd17638 293 TEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
363-849 |
2.24e-19 |
|
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: 94.24 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVI------DNETEISYRLLNERANRLARTLQN---RKG----------PKPTVAVLAKRSIDAIVGVL--- 420
Cdd:TIGR02188 67 LEARPDKVAIIwegdepGEVRKITYRELHREVCRFANVLKSlgvKKGdrvaiympmiPEAAIAMLACARIGAIHSVVfgg 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 421 ----------------AVMKA-----GGVYIPIDAHYPKArieyiLRDSGADI---LLLQRelkhliSNSPESEMSH--- 473
Cdd:TIGR02188 147 fsaealadrindagakLVITAdeglrGGKVIPLKAIVDEA-----LEKCPVSVehvLVVRR------TGNPVVPWVEgrd 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 474 IFLDDEGSFEESNCnlnlSPAP---EEPVYIIYTSGTTGAPKGVIVT---YqnFTHAALAWRqiYELDRKPvrllqiasf 547
Cdd:TIGR02188 216 VWWHDLMAKASAYC----EPEPmdsEDPLFILYTSGSTGKPKGVLHTtggY--LLYAAMTMK--YVFDIKD--------- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 548 sFDVF--SGDLART----------LTNGGTLIV------CPDETRlepaeIYKIIKSQRITVMESTPALIIPVMEYvyrn 609
Cdd:TIGR02188 279 -GDIFwcTADVGWItghsyivygpLANGATTVMfegvptYPDPGR-----FWEIIEKHKVTIFYTAPTAIRALMRL---- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 610 qfklpdldililGSDMVKAQDFKTLtdrfgqsmRIINS------------Y----GVTEATIDSSFYETSMGGECTgdnV 673
Cdd:TIGR02188 349 ------------GDEWVKKHDLSSL--------RLLGSvgepinpeawmwYykvvGKERCPIVDTWWQTETGGIMI---T 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 674 PI--------GS---PLPNVHMYVLSQTDQIQPI-GVAGELCIGGA--GVAKGYHHKPDltqmKFTENPFVSGERLYRTG 739
Cdd:TIGR02188 406 PLpgatptkpGSatlPFFGIEPAVVDEEGNPVEGpGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPGYYFTG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 740 DRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV------PSDVNTNA 812
Cdd:TIGR02188 482 DGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVvGIPDDIKGQA-IYAFVTlkdgyePDDELRKE 560
|
570 580 590
....*....|....*....|....*....|....*..
gi 1238238751 813 LRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:TIGR02188 561 LRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLL 597
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
379-849 |
2.90e-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: 341277 [Multi-domain] Cd Length: 437 Bit Score: 92.58 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPI-DAHYPKArIEYILRDSGADILLLQ 456
Cdd:cd05973 1 LTFGELRALSARFANALQELGvGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLfTAFGPKA-IEHRLRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 457 RELKHLISNSPESEMShiflddegsfeesncnlnlspapeepvyiiyTSGTTGAPKGVIVTYQnfthAALAWR--QIYEL 534
Cdd:cd05973 80 AANRHKLDSDPFVMMF-------------------------------TSGTTGLPKGVPVPLR----ALAAFGayLRDAV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 535 DRKP-VRLLQIAS--FSFDVFSGDLARTLTNGGTLIVcpdETRLEPAEIYKIIKSQRITVMESTPAliipvmeyVYRnqf 611
Cdd:cd05973 125 DLRPeDSFWNAADpgWAYGLYYAITGPLALGHPTILL---EGGFSVESTWRVIERLGVTNLAGSPT--------AYR--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 612 klpdldILILGSDMVKAqdfktltdRFGQSMRIINSYG------VTE-------ATIDSSFYETSMG-----GECTGDNV 673
Cdd:cd05973 191 ------LLMAAGAEVPA--------RPKGRLRRVSSAGepltpeVIRwfdaalgVPIHDHYGQTELGmvlanHHALEHPV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 674 PIGS---PLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVA----KGYHHKPDltqmkftenPFVSGeRLYRTGDRACWLP 746
Cdd:cd05973 257 HAGSagrAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDT---------PAIDG-GYYLTGDTVEFDP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 747 NGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV--PSDVNTNALRAALT----KE 820
Cdd:cd05973 327 DGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrGGHEGTPALADELQlhvkKR 406
|
490 500
....*....|....*....|....*....
gi 1238238751 821 LPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05973 407 LSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
951-1380 |
3.72e-19 |
|
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: 91.60 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 951 TPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIF-QRDQNGHVIQfnrgINHKDHELFGLY 1029
Cdd:cd19542 5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQ----VVLKSLDPPIEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1030 ISDWTKA--SLERAHLDEKLAAEEtviqskmnvekgPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQ 1106
Cdd:cd19542 81 VETDEDSldALTRDLLDDPTLFGQ------------PPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAYNG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1107 ALekkeiqLPPKTD--SYLSYADGLTQiAESKQllsektYWQTILDAHTAFLPKDIenvpdklqmnSDAAAFVLSGDWTE 1184
Cdd:cd19542 149 QL------LPPAPPfsDYISYLQSQSQ-EESLQ------YWRKYLQGASPCAFPSL----------SPKRPAERSLSSTR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1185 KLLFETQQAYG----TDANeLLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDisRTVGWFTSIypilldmgipepf 1260
Cdd:cd19542 206 RSLAKLEAFCAslgvTLAS-LFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGID--DIVGPCINT------------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1261 edqLAYRIK-----TTKDMLRRV--------PNKGTGYGLLTHIGELRHKEPEvsFNYLGQFSEEKEVETFQLSYYQPRY 1327
Cdd:cd19542 270 ---LPVRVKldpdwTVLDLLRQLqqqylrslPHQHLSLREIQRALGLWPSGTL--FNTLVSYQNFEASPESELSGSSVFE 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 1328 EIAGEREREYELDINALITDGRLHVKAVY-TQVFSKHSIECFMDRFhRHLIETI 1380
Cdd:cd19542 345 LSAAEDPTEYPVAVEVEPSGDSLKVSLAYsTSVLSEEQAEELLEQF-DDILEAL 397
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
4-215 |
4.76e-19 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 91.34 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 4 PFDLSQAPLFRAQIVKISD-ERHLLLVDMHHIISDGVSVNILIREFGELYNNR--NLPALrIQYKDY-AVWREGFKTGDA 79
Cdd:cd19544 104 RLDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRaaALPPP-VPYRNFvAQARLGASQAEH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 80 yktqEAYWLKQL----EGELP--VLDLPADHARPpvrsfagDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLS 153
Cdd:cd19544 183 ----EAFFREMLgdvdEPTAPfgLLDVQGDGSDI-------TEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVLA 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238751 154 RLSGQEDIIVGSPIAGRPH--KDLEPILGMFVNTLALRTRPeGGKPFVQYLQEVRE--TALEAFEH 215
Cdd:cd19544 252 RCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLRVRL-GGRSVREAVRQTHArlAELLRHEH 316
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
379-849 |
1.75e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 90.98 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQ 456
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHTDLKPgdRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 457 RELKHLISNS-PESEMSHIFLDDEG-------------------------------------------SFEESNcnlnls 492
Cdd:PRK05677 130 ANMAHLAEKVlPKTGVKHVIVTEVAdmlpplkrllinavvkhvkkmvpayhlpqavkfndalakgagqPVTEAN------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIY--------ELDRKPVRLLQIASFSFDVfsgdLARTLT-NG 563
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMgsnlnegcEILIAPLPLYHIYAFTFHC----MAMMLIgNH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 564 GTLIVCPdetRLEPAEIyKIIKSQRITVMESTPALIIPVMeyvyrNQFKLPDLDI----LILGSDMV----KAQDFKTLT 635
Cdd:PRK05677 280 NILISNP---RDLPAMV-KELGKWKFSGFVGLNTLFVALC-----NNEAFRKLDFsalkLTLSGGMAlqlaTAERWKEVT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 636 drfgqSMRIINSYGVTEATIDSSFyeTSMGGECTGDnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHH 715
Cdd:PRK05677 351 -----GCAICEGYGMTETSPVVSV--NPSQAIQVGT---IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQ 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 716 KPDLTQMKFTENPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ-TGLVREAAVAVQHDKN 794
Cdd:PRK05677 421 RPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAlPGVLQCAAIGVPDEKS 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 795 GQAgLAAYIVP---SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK05677 495 GEA-IKVFVVVkpgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
358-755 |
2.40e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 90.88 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVIDNE------TEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYI 430
Cdd:PRK12582 54 LLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGlDPGRPVMILSGNSIEHALMTLAAMQAGVPAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 431 PIDAHYP-----KARIEY---------ILRDSGAdilLLQRELKHL---------ISNSPESEMShIFLDD------EGS 481
Cdd:PRK12582 134 PVSPAYSlmshdHAKLKHlfdlvkprvVFAQSGA---PFARALAALdlldvtvvhVTGPGEGIAS-IAFADlaatppTAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 482 FEESNCNLNlspaPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQI--YELDRKPVRLLQIASFSfDVFSGDLA-- 557
Cdd:PRK12582 210 VAAAIAAIT----PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLrpREPDPPPPVSLDWMPWN-HTMGGNANfn 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 558 RTLTNGGTLIVcpDETRLEPAEIYKIIKSQR---ITVMESTP---ALIIPVMEY---VYRNQFKlpDLDILILG----SD 624
Cdd:PRK12582 285 GLLWGGGTLYI--DDGKPLPGMFEETIRNLReisPTVYGNVPagyAMLAEAMEKddaLRRSFFK--NLRLMAYGgatlSD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 625 MV--KAQDFKTLTDrfGQSMRIINSYGVTEA--TIDSSFYETSMGGEctgdnvpIGSPLPNVHMYVLsqtdqiqPIGVAG 700
Cdd:PRK12582 361 DLyeRMQALAVRTT--GHRIPFYTGYGATETapTTTGTHWDTERVGL-------IGLPLPGVELKLA-------PVGDKY 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 701 ELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWL----PNGTIRLLGR 755
Cdd:PRK12582 425 EVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddPEKGLIFDGR 477
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
934-1380 |
3.18e-18 |
|
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: 91.46 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 934 PLASQADQGPAEGEAELTPIQRRFFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRdqngHVIQ 1013
Cdd:COG1020 6 AAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRT----RAGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1014 FNRGINHKDHELFGLYISDWTKASLERAHLDEKLAAEEtviQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVS 1092
Cdd:COG1020 82 PVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEA---LAPFDLLRGPLLRLLLLLLLLLLLlLLLALHHIISDGLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1093 WRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL--DAHTAFLPKDIENvPDKLQMN 1170
Cdd:COG1020 159 DGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLagLPPLLELPTDRPR-PAVQSYR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1171 SDAAAFVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHvpniDISRTVGWFTSIYPI 1250
Cdd:COG1020 238 GARVSFRLPAELTAALR-ALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP----ELEGLVGFFVNTLPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1251 LLDMGIPEPFEDQLAyRIKTTK-----------DMLRRV--PNKGTGYGLLThigelrhkepEVSFNYLGQFSEEKEVET 1317
Cdd:COG1020 313 RVDLSGDPSFAELLA-RVRETLlaayahqdlpfERLVEElqPERDLSRNPLF----------QVMFVLQNAPADELELPG 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 1318 FQLSYYQPRYEIAgererEYELDINALITDGRLHVKAVY-TQVFSKHSIECFMDRFhRHLIETI 1380
Cdd:COG1020 382 LTLEPLELDSGTA-----KFDLTLTVVETGDGLRLTLEYnTDLFDAATIERMAGHL-VTLLEAL 439
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
7-318 |
3.90e-18 |
|
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: 88.91 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 7 LSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNIL----IREFGELYNNR--NLPALRiQYKDYAVW-REGFKTGDa 79
Cdd:cd19547 110 LADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIwgdvFRVYEELAHGRepQLSPCR-PYRDYVRWiRARTAQSE- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 80 ykTQEAYWLKQLEgEL---PVLDLPADharppvRSFAGDKVSFTLDQEVASGLHKLARENGSTLYMVLLAAYTAFLSRLS 156
Cdd:cd19547 188 --ESERFWREYLR-DLtpsPFSTAPAD------REGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 157 GQEDIIVGSPIAGRPHK--DLEPILGMFVNTLALRTRPEGGKPFVQYLQEV-RETALEAfEHQDYPFEELVDKLELTRdM 233
Cdd:cd19547 259 GARDVVHGLTIAGRPPEleGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIhRDLATTA-AHGHVPLAQIKSWASGER-L 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 234 SRNPVFDAMFILQNVEKQDIDLREIKVRPANF-AHHISLFDITLIATEISgSICCEMEFSTEVFLKATIERWADHFiEFL 312
Cdd:cd19547 337 SGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLhAQEKTEYPIGLIVLPLQ-KLAFHFNYDTTHFTRAQVDRFIEVF-RLL 414
|
....*.
gi 1238238751 313 HEALST 318
Cdd:cd19547 415 TEQLCR 420
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
496-845 |
4.71e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 87.82 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 496 EEPVYIIYTSGTTGAPKGVIvtyqnfthaalaWRQiyelDRKPVRLLQIASFSFDVFSGD-------------------- 555
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVM------------WRQ----EDIFRMLMGGADFGTGEFTPSedahkaaaaaagtvmfpapp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 556 --------LARTLTNGGTLIVCPDEtRLEPAEIYKIIKSQRITVMEST-PALIIPVMEYVYR-NQFKLPDLDILILG--- 622
Cdd:cd05924 67 lmhgtgswTAFGGLLGGQTVVLPDD-RFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDaGPYDLSSLFAISSGgal 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 623 -SDMVKAQDFKTLTDrfgqsMRIINSYGVTEATIDSSFYETSMGGEcTGDNVPIGSPLpnvhmYVLSQTDQIQPIGVAGE 701
Cdd:cd05924 146 lSPEVKQGLLELVPN-----ITLVDAFGSSETGFTGSGHSAGSGPE-TGPFTRANPDT-----VVLDDDGRVVPPGSGGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 702 LCIGGAG-VAKGYHHKPDLTQMKFTEnpfVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTG 780
Cdd:cd05924 215 GWIARRGhIPLGYYGDEAKTAETFPE---VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 781 LVREAAVAVQHD-KNGQ--AGLAAYIVPSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLD 845
Cdd:cd05924 292 AVYDVLVVGRPDeRWGQevVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
379-821 |
9.65e-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: 88.43 E-value: 9.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLqnRK---GPKPTVAVLAKRSIDAIVGVLAVMKAGgvyIPIDAHYPKarieyiLRDSGadilll 455
Cdd:cd17639 6 MSYAEVWERVLNFGRGL--VElglKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAT------LGEDA------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 456 qreLKHLISnspESEMSHIFLDdegsfeesncnlnlsPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQ-IYEL 534
Cdd:cd17639 69 ---LIHSLN---ETECSAIFTD---------------GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrVPEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 535 DRKPVRLL------QIASFSFD---VFSGDL-----ARTLTNGGTLIVCPDETRLEPaeiykiiksqriTVMESTPAlii 600
Cdd:cd17639 128 LGPDDRYLaylplaHIFELAAEnvcLYRGGTigygsPRTLTDKSKRGCKGDLTEFKP------------TLMVGVPA--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 601 pVMEYVYRN--------------------QFKLPDLDILI---LGSDMVkaqdFKTL---------------------TD 636
Cdd:cd17639 193 -IWDTIRKGvlaklnpmgglkrtlfwtayQSKLKALKEGPgtpLLDELV----FKKVraalggrlrymlsggaplsadTQ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 637 RFGQSM--RIINSYGVTE----ATIDSSF-YETSMggectgdnvpIGSPLPNVHMYVLS------QTDQIQPigvAGELC 703
Cdd:cd17639 268 EFLNIVlcPVIQGYGLTEtcagGTVQDPGdLETGR----------VGPPLPCCEIKLVDweeggySTDKPPP---RGEIL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 704 IGGAGVAKGYHHKPDLTQMKFTenpfvsGERLYRTGDRACWLPNGTIRLLGRMDYQVKI-NGYRIETEEIESVLLQTGLV 782
Cdd:cd17639 335 IRGPNVFKGYYKNPEKTKEAFD------GDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRSNPLV 408
|
490 500 510
....*....|....*....|....*....|....*....
gi 1238238751 783 REAAVAVQHDKNGQAGLaayIVPsdvNTNALRAALTKEL 821
Cdd:cd17639 409 NNICVYADPDKSYPVAI---VVP---NEKHLTKLAEKHG 441
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
363-844 |
1.05e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 88.30 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARI 441
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGvGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 442 EYILRDSGADILL--------------LQRELKHLISNSPESEMSHIFLDDEgsFEESNCNLNLSPAPEE-PVYIIYTSG 506
Cdd:PRK07786 107 AFLVSDCGAHVVVteaalapvatavrdIVPLLSTVVVAGGSSDDSVLGYEDL--LAEAGPAHAPVDIPNDsPALIMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 507 TTGAPKGVIVTYQNFTHAALAWRQIYELDRKP------VRLLQIASFsfdvfsGDLARTLTNGGTLIVCPDETrLEPAEI 580
Cdd:PRK07786 185 TTGRPKGAVLTHANLTGQAMTCLRTNGADINSdvgfvgVPLFHIAGI------GSMLPGLLLGAPTVIYPLGA-FDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 581 YKIIKSQRItvmesTPALIIPVM-EYVYRNQFKLP-DLDILILGSDMVKAQDfkTLTDRFGQSMriinsygvTEATIDSS 658
Cdd:PRK07786 258 LDVLEAEKV-----TGIFLVPAQwQAVCAEQQARPrDLALRVLSWGAAPASD--TLLRQMAATF--------PEAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 659 FYETSMGG-ECT--GDNV-----PIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFV 730
Cdd:PRK07786 323 FGQTEMSPvTCMllGEDAirklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 731 SGErLYRTGDracwlpNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQ-HDKNGQAGLAAYIVPSD-- 807
Cdd:PRK07786 403 SGD-LVRQDE------EGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRaDEKWGEVPVAVAAVRNDda 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 1238238751 808 -VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:PRK07786 476 aLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
352-849 |
1.50e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 88.15 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 352 DIPFHRI-FEAKAEE-NPEHIAVIDNETEISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGV-LAVMKAGGV 428
Cdd:PLN03102 11 NVPLTPItFLKRASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMhFAVPMAGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 429 YIPIDAHYPKARIEYILRDSGADILLLQRELKHLISNSPE---SEMSH-----IFLDD-----EGSFEESNCNLNL---S 492
Cdd:PLN03102 91 LNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHllsSEDSNlnlpvIFIHEidfpkRPSSEELDYECLIqrgE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PAP------------EEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFS---GDLA 557
Cdd:PLN03102 171 PTPslvarmfriqdeHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTftwGTAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 558 RTLTNggtliVCpdETRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQ-FKLPDLDILILGSDMVKAQDFKtlTD 636
Cdd:PLN03102 251 RGGTS-----VC--MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLsPRSGPVHVLTGGSPPPAALVKK--VQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 637 RFGqsMRIINSYGVTEATIDSSFYETSmggectgDNvpiGSPLPNVHMYVLSQTDQIQPIGVA----------------- 699
Cdd:PLN03102 322 RLG--FQVMHAYGLTEATGPVLFCEWQ-------DE---WNRLPENQQMELKARQGVSILGLAdvdvknketqesvprdg 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 700 ---GELCIGGAGVAKGYHHKPdltqmKFTENPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVL 776
Cdd:PLN03102 390 ktmGEIVIKGSSIMKGYLKNP-----KATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 777 LQTGLVREAA-VAVQHDKNGQAGLAAYIVPSDVNTNALRAA--LTKE----------LPAYMIPAYLIPLVNMPLTLNGK 843
Cdd:PLN03102 463 YKYPKVLETAvVAMPHPTWGETPCAFVVLEKGETTKEDRVDklVTRErdlieycrenLPHFMCPRKVVFLQELPKNGNGK 542
|
....*.
gi 1238238751 844 LDRNAL 849
Cdd:PLN03102 543 ILKPKL 548
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
364-863 |
1.69e-17 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 88.14 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 364 EENPEHIAVI------DNETEISYRLLNERANRLARTLQN---RKG----------PKPTVAVLAKRSIDAIVGVLAvmk 424
Cdd:cd05967 62 AGRGDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRKlgvVKGdrviiympmiPEAAIAMLACARIGAIHSVVF--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 425 aGGVYIP-----IDAHYPK------------ARIEYI------LRDSG---ADILLLQRELKHLISNSPEsemshifldd 478
Cdd:cd05967 139 -GGFAAKelasrIDDAKPKlivtascgiepgKVVPYKplldkaLELSGhkpHHVLVLNRPQVPADLTKPG---------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 479 eGSFEESNCNLNLSPAP------EEPVYIIYTSGTTGAPKGVIVTyqNFTHA-ALAW--RQIYELdrKPVRLLQIAS--- 546
Cdd:cd05967 208 -RDLDWSELLAKAEPVDcvpvaaTDPLYILYTSGTTGKPKGVVRD--NGGHAvALNWsmRNIYGI--KPGDVWWAASdvg 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 547 ----FSFDVFSgdlarTLTNGGTLIVC---PDETRlEPAEIYKIIKSQRITVMESTPALI--I----PVMEYVyrNQFKL 613
Cdd:cd05967 283 wvvgHSYIVYG-----PLLHGATTVLYegkPVGTP-DPGAFWRVIEKYQVNALFTAPTAIraIrkedPDGKYI--KKYDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 614 PDLDILILGSDMVKAQDFKTLTDRFGQSmrIINSYGVTEATidssfyeTSMGGECTG-DNVPI-----GSPLPNVHMYVL 687
Cdd:cd05967 355 SSLRTLFLAGERLDPPTLEWAENTLGVP--VIDHWWQTETG-------WPITANPVGlEPLPIkagspGKPVPGYQVQVL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 688 SQTDQIQPIGVAGELCIGGA---GVAKGYHHKPDLTQMK-FTENPFVsgerlYRTGDRACWLPNGTIRLLGRMDYQVKIN 763
Cdd:cd05967 426 DEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLyLSKFPGY-----YDTGDAGYKDEDGYLFIMGRTDDVINVA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 764 GYRIETEEIESVLLQTGLVREAAVAVQHDK-NGQAGLAAYIVPSDVN------TNALRAALTKELPAYMIPAYLIPLVNM 836
Cdd:cd05967 501 GHRLSTGEMEESVLSHPAVAECAVVGVRDElKGQVPLGLVVLKEGVKitaeelEKELVALVREQIGPVAAFRLVIFVKRL 580
|
570 580
....*....|....*....|....*..
gi 1238238751 837 PLTLNGKLDRNALPAPNNvlSRPYTAP 863
Cdd:cd05967 581 PKTRSGKILRRTLRKIAD--GEDYTIP 605
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
947-1276 |
1.75e-17 |
|
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: 86.66 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 947 EAELTPIQRR--FFGQVHAFHYHYNQSVMLFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnRGINHKDHE 1024
Cdd:cd19539 1 RIPLSFAQERlwFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQ--EILPPGPAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1025 LFGLYISDWTKaslERAHLDEKLAAEetVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAA 1103
Cdd:cd19539 79 LEVRDLSDPDS---DRERRLEELLRE--RESRGFDLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1104 YQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAFLPKDIEnVPDKLQMNSDAAAFVLSGDW 1182
Cdd:cd19539 154 YAARRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLrGAEPTALPTDRP-RPAGFPYPGADLRFELDAEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1183 TEKLlfeTQQAYGTDAN--ELLLTALGMALSEWTGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPF 1260
Cdd:cd19539 233 VAAL---RELAKRARSSlfMVLLAAYCVLLRRYTGQTDIVVGTPVAGR----NHPRFESTVGFFVNLLPLRVDVSDCATF 305
|
330
....*....|....*.
gi 1238238751 1261 EDQLAYRIKTTKDMLR 1276
Cdd:cd19539 306 RDLIARVRKALVDAQR 321
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
349-854 |
1.89e-17 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 87.76 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 349 AQKDIP---FHRIFEaKAEENPEHIAV--IDNETEISYRLLNERANRLARTLQNRKGPKPT-VAVLAKRSIDAIVGVLAV 422
Cdd:PRK05857 8 AMPQLPstvLDRVFE-QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSrVLVISDNGPETYLSVLAC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 423 MKAGGVYIPIDAHYPKARIEYILRDSGADILLLQRELKHLISNSPE--SEMSHIFLDDEGSFEESNCNL-------NLSP 493
Cdd:PRK05857 87 AKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEalHSIPVIAVDIAAVTRESEHSLdaaslagNADQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 494 APEEPVYIIYTSGTTGAPKGVIVTYQNF-------THAALAWRQ--IYELDRKPVRLLQIASFSFdvfsgdLARTLTNGG 564
Cdd:PRK05857 167 GSEDPLAMIFTSGTTGEPKAVLLANRTFfavpdilQKEGLNWVTwvVGETTYSPLPATHIGGLWW------ILTCLMHGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 565 TLIVCPDETrlepAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTdrfGQSMRI 644
Cdd:PRK05857 241 LCVTGGENT----TSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIE---ATGVRT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 645 INSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHMYVLSQ------TDQIQPIGVAGELCIGGAGVAKGYHHKPD 718
Cdd:PRK05857 314 AQVYGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATdgigptAPGAGPSASFGTLWIKSPANMLGYWNNPE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 719 LTQMKFTENPFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAG 798
Cdd:PRK05857 394 RTAEVLIDGWVNTGDLLERRED-------GFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAL 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 799 LAAYIVPS-DVNTNALR-------AALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPAPNN 854
Cdd:PRK05857 467 VGLAVVASaELDESAARalkhtiaARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAAT 530
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
354-851 |
2.16e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 87.29 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 354 PFHRIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKPT--VAVLAKRSIDAIVGVLAVMKAGGVYIP 431
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLL-ALGVRAGdgVAVLARNHRGFVLALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 432 IDAHYPKARIEYILRDSGADILLLQRELKHLIS-----------------NSPESEMSHIFLDD--EGSFEESncnlnlS 492
Cdd:PRK07788 129 LNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSalppdlgrlrawggnpdDDEPSGSTDETLDDliAGSSTAP------L 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PAPEEPV-YIIYTSGTTGAPKGVIVTyqnfTHAALA-WRQIyeLDRKPVRLLQIASFSFDVFSG------DLARTLtnGG 564
Cdd:PRK07788 203 PKPPKPGgIVILTSGTTGTPKGAPRP----EPSPLApLAGL--LSRVPFRAGETTLLPAPMFHAtgwahlTLAMAL--GS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 565 TLIVcpdETRLEPAEIYKIIKSQRITVMestpaLIIPVMeyvYRNQFKLPD----------LDILI-----LGSDMVKAq 629
Cdd:PRK07788 275 TVVL---RRRFDPEATLEDIAKHKATAL-----VVVPVM---LSRILDLGPevlakydtssLKIIFvsgsaLSPELATR- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 630 dfktLTDRFGQsmRIINSYGVTE---ATI----DSSFYETSMGgectgdNVPIGsplpnVHMYVLSQTDQIQPIGVAGEL 702
Cdd:PRK07788 343 ----ALEAFGP--VLYNLYGSTEvafATIatpeDLAEAPGTVG------RPPKG-----VTVKILDENGNEVPRGVVGRI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 703 CIGGAGVAKGYHHKPDltqmKFTENPFVSgerlyrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLV 782
Cdd:PRK07788 406 FVGNGFPFEGYTDGRD----KQIIDGLLS------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDV 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 783 REAAV-AVQHDKNGQAgLAAYIVPSD---VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALPA 851
Cdd:PRK07788 476 VEAAViGVDDEEFGQR-LRAFVVKAPgaaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
363-849 |
2.24e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 86.85 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKAR 440
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFA-QQGVVEgsGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 441 IEYILRDSGADILLlqrelkhlisnsPESEMSHIFLDDEGSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQN 520
Cdd:PRK09029 92 LEELLPSLTLDFAL------------VLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 521 ftHAALAwrqiyeldrkpVRLLQIASFS-----------FDVfSGD--LARTLTNGGTLIVcPDETRLEPAeiykiiksq 587
Cdd:PRK09029 160 --HLASA-----------EGVLSLMPFTaqdswllslplFHV-SGQgiVWRWLYAGATLVV-RDKQPLEQA--------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 588 ritVMESTPALIIP--VMEYVYRNQFKLPDLDILiLGSDMVKAqdfkTLTDRFGQsmRIINS---YGVTEA--TI----- 655
Cdd:PRK09029 216 ---LAGCTHASLVPtqLWRLLDNRSEPLSLKAVL-LGGAAIPV----ELTEQAEQ--QGIRCwcgYGLTEMasTVcakra 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 656 DSSfyetsmggectgDNVpiGSPLPNvHMYVLsqtdqiqpigVAGELCIGGAGVAKGYHHKPDLTqmkftenPFVSGERL 735
Cdd:PRK09029 286 DGL------------AGV--GSPLPG-REVKL----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 736 YRTGDRACWLpNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKN-GQAGLAAYIVPSDVNTNALR 814
Cdd:PRK09029 334 FATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfGQRPVAVVESDSEAAVVNLA 412
|
490 500 510
....*....|....*....|....*....|....*....
gi 1238238751 815 AALTKELPAYMIP-AYLIplvnMPLTL-NG--KLDRNAL 849
Cdd:PRK09029 413 EWLQDKLARFQQPvAYYL----LPPELkNGgiKISRQAL 447
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
379-942 |
3.37e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 87.39 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVyIPIDAHYPKARIEYIL--RDSGADILLLQ 456
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGV-MAFLANPELHRDDHALaaRNTEPALVVTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 457 RELKHLISNSPESEMSHIFLDDEgsfeesncnlNLSPAPEEPV------YIIYTSGTTGAPKGVIVTYQN-FTHAALAWR 529
Cdd:PRK06060 110 DALRDRFQPSRVAEAAELMSEAA----------RVAPGGYEPMggdalaYATYTSGTTGPPKAAIHRHADpLTFVDAMCR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 530 QIYELDRKPVRLLQIASFsfdvFSGDLART----LTNGGTLIVCPD----------ETRLEPAEIYKIiksqritvmest 595
Cdd:PRK06060 180 KALRLTPEDTGLCSARMY----FAYGLGNSvwfpLATGGSAVINSApvtpeaaailSARFGPSVLYGV------------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 596 PALIIPVMEYVYRNQFKlpDLDILILGSDMVKAQDFKTLTDRFGqSMRIINSYGVTEatIDSSFYETSMGGECTGDnvpI 675
Cdd:PRK06060 244 PNFFARVIDSCSPDSFR--SLRCVVSAGEALELGLAERLMEFFG-GIPILDGIGSTE--VGQTFVSNRVDEWRLGT---L 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 GSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDltqmkftenPFVSGERLYRTGDRACWLPNGTIRLLGR 755
Cdd:PRK06060 316 GRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 756 MDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIVPS-------DVNTNALRAALTKeLPAYMIPA 828
Cdd:PRK06060 387 ADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATsgatidgSVMRDLHRGLLNR-LSAFKVPH 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 829 YLIPLVNMPLTLNGKLDRNALPApnnvlsrpytapvndlQKTMAYIWEDVLSMSRvgiHDSFFELGGDSIKALQVAARLA 908
Cdd:PRK06060 466 RFAVVDRLPRTPNGKLVRGALRK----------------QSPTKPIWELSLTEPG---SGVRAQRDDLSASNMTIAGGND 526
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1238238751 909 AEgwsMTIRDlfRYSTIQE---------LCGHITPLASQADQG 942
Cdd:PRK06060 527 GG---ATLRE--RLVALRQerqrlvvdaVCAEAAKMLGEPDPW 564
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
340-849 |
4.08e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 86.58 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 340 EFNKTQVEFAQK--------DIPFHRIFEAKAEenPEHIAVIDNETEISYRLLNERANRLARTLQnRKGPKP--TVAVLA 409
Cdd:PRK10946 4 PFTRWPEEFARRyrekgywqDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLR-RQGIKPgdTALVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 410 KRSIDAIVGVLAVMKAGGVyiPIDAHYPKARIE---YILRDSGAdILLLQRE---------LKHLISNSPESEMShIFLD 477
Cdd:PRK10946 81 GNVAEFYITFFALLKLGVA--PVNALFSHQRSElnaYASQIEPA-LLIADRQhalfsdddfLNTLVAEHSSLRVV-LLLN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 478 DEGSF------EESNCNLNLSPAPEEPVYIIYTSG-TTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQI-ASFSF 549
Cdd:PRK10946 157 DDGEHslddaiNHPAEDFTATPSPADEVAFFQLSGgSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALpAAHNY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 550 DVFS-GDLArTLTNGGTLIVCPDEtrlEPAEIYKIIKSQRITVMESTPALIIPVMEYV----YRNQfkLPDLDILILG-- 622
Cdd:PRK10946 237 PMSSpGALG-VFLAGGTVVLAPDP---SATLCFPLIEKHQVNVTALVPPAVSLWLQAIaeggSRAQ--LASLKLLQVGga 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 623 --SDMVKAQDFKTLTDR----FGQSMRIINsYGVTEATIDSSFyeTSMGgectgdnVPIGsplPNVHMYVLSQTDQIQPI 696
Cdd:PRK10946 311 rlSETLARRIPAELGCQlqqvFGMAEGLVN-YTRLDDSDERIF--TTQG-------RPMS---PDDEVWVADADGNPLPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 697 GVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVL 776
Cdd:PRK10946 378 GEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 777 LQTGLVREAA-VAVQHDKNGQAGlAAYIVPsdvnTNALRA-ALTKELPAYMIPAYLIP-----LVNMPLTLNGKLDRNAL 849
Cdd:PRK10946 452 LRHPAVIHAAlVSMEDELMGEKS-CAFLVV----KEPLKAvQLRRFLREQGIAEFKLPdrvecVDSLPLTAVGKVDKKQL 526
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
357-843 |
6.60e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.02 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVIDNETEI--SYRLLNERANRLARTLQN---RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIP 431
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLAlgiEKGDR--VGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 432 IDAHYPKARIEYILRDSGADILLLQR----------------ELKHLISNSPESEM-----SHIFLDDEG-----SFEES 485
Cdd:PRK08315 98 INPAYRLSELEYALNQSGCKALIAADgfkdsdyvamlyelapELATCEPGQLQSARlpelrRVIFLGDEKhpgmlNFDEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 486 ncnLNLSPA--------------PEEPVYIIYTSGTTGAPKGVIVTY-------------QNFTHAalawrqiyelDRK- 537
Cdd:PRK08315 178 ---LALGRAvddaelaarqatldPDDPINIQYTSGTTGFPKGATLTHrnilnngyfigeaMKLTEE----------DRLc 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 538 -PVRLlqiasfsFDVFS---GDLArTLTNGGTlIVCPDEtRLEPAEIYKIIKSQRITVMESTPALIIPVMEyvyrnqfkL 613
Cdd:PRK08315 245 iPVPL-------YHCFGmvlGNLA-CVTHGAT-MVYPGE-GFDPLATLAAVEEERCTALYGVPTMFIAELD--------H 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 614 PDLDILilgsdmvkaqDFKTLtdRFG---------QSM-RIINSYGVTEATIDSSFYETSMGGECTGDNVPI-------G 676
Cdd:PRK08315 307 PDFARF----------DLSSL--RTGimagspcpiEVMkRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLekrvttvG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 677 SPLPNVHMYVLS-QTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQmkftenpfvsgerlyRTGDRACWLPNGTirlLGR 755
Cdd:PRK08315 375 RALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTA---------------EAIDADGWMHTGD---LAV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 756 MD---YqVKINGyRIET-----------EEIESVLLQTGLVREAAVA-VQHDKNGQAgLAAYIVP---SDVNTNALRAAL 817
Cdd:PRK08315 437 MDeegY-VNIVG-RIKDmiirggeniypREIEEFLYTHPKIQDVQVVgVPDEKYGEE-VCAWIILrpgATLTEEDVRDFC 513
|
570 580
....*....|....*....|....*.
gi 1238238751 818 TKELPAYMIPAYLIPLVNMPLTLNGK 843
Cdd:PRK08315 514 RGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
490-850 |
6.92e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.05 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 490 NLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDrkpvrllQIASFS----FDVfSGDLA--RTLTNG 563
Cdd:PRK07445 114 GILPNLETGWIMIPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQ-------QVNSFCvlplYHV-SGLMQfmRSFLTG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 564 GTLIVCPdetrlepaeiYKIIKSQRIT---VMESTPALIIPVMEYVYRN------QFKLpdldILILGsdmvkAQDFKTL 634
Cdd:PRK07445 186 GKLVILP----------YKRLKSGQELppnPSDFFLSLVPTQLQRLLQLrpqwlaQFRT----ILLGG-----APAWPSL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 635 TD--RFgQSMRIINSYGVTEAtidSSFYETSMGGECTGDNVPIGSPLPNVHMYVLSQTdqiqpigvAGELCIGGAGVAKG 712
Cdd:PRK07445 247 LEqaRQ-LQLRLAPTYGMTET---ASQIATLKPDDFLAGNNSSGQVLPHAQITIPANQ--------TGNITIQAQSLALG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 713 YHhkPDltqmkFTENPfvsgeRLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHD 792
Cdd:PRK07445 315 YY--PQ-----ILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPD 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 793 KN-GQAGLAAYI-VPSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNALP 850
Cdd:PRK07445 383 PHwGEVVTAIYVpKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
358-849 |
7.55e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 85.84 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNR---KGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDA 434
Cdd:PRK07059 28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRglaKGAR--VAIMMPNVLQYPVAIAAVLRAGYVVVNVNP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 435 HYPKARIEYILRDSGAD-ILLLQR------------ELKHLISNS-----------------------PESEM-SHIFLD 477
Cdd:PRK07059 106 LYTPRELEHQLKDSGAEaIVVLENfattvqqvlaktAVKHVVVASmgdllgfkghivnfvvrrvkkmvPAWSLpGHVRFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 478 D---EGSfeesncNLNLSP---APEEPVYIIYTSGTTGAPKGVIVTYQNFTHAAL---AWRQ-IYELDRKPVRLLQIAS- 546
Cdd:PRK07059 186 DalaEGA------RQTFKPvklGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeAWLQpAFEKKPRPDQLNFVCAl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 547 -----FSFDVFSgdlARTLTNGGTLIVCPDetrlePAEIYKIIKSqritvMESTPALIIPVMEYVYRNQFKLPDLDILil 621
Cdd:PRK07059 260 plyhiFALTVCG---LLGMRTGGRNILIPN-----PRDIPGFIKE-----LKKYQVHIFPAVNTLYNALLNNPDFDKL-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 622 gsdmvkaqDFKTLTDRFGQSMR----------------IINSYGVTEaTIDSSFYETSMGGECTGDnvpIGSPLPNVHMY 685
Cdd:PRK07059 325 --------DFSKLIVANGGGMAvqrpvaerwlemtgcpITEGYGLSE-TSPVATCNPVDATEFSGT---IGLPLPSTEVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 686 VLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGY 765
Cdd:PRK07059 393 IRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 766 RIETEEIESVL-LQTGLVREAAVAVQHDKNGQAgLAAYIVPSDVNTNA--LRAALTKELPAYMIPAYLIPLVNMPLTLNG 842
Cdd:PRK07059 467 NVYPNEIEEVVaSHPGVLEVAAVGVPDEHSGEA-VKLFVVKKDPALTEedVKAFCKERLTNYKRPKFVEFRTELPKTNVG 545
|
....*..
gi 1238238751 843 KLDRNAL 849
Cdd:PRK07059 546 KILRREL 552
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
363-846 |
1.32e-16 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 85.31 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVI------DNETEISYRLLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:cd05966 63 LKERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSlgvKKGD--RVAIYMPMIPELVIAMLACARIGAVHSVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHY-PKA---RIEyilrDSGADILL-----LQRE------------------------LKHLISNSPESEMSHIFLDDEG 480
Cdd:cd05966 141 AGFsAESladRIN----DAQCKLVItadggYRGGkviplkeivdealekcpsvekvlvVKRTGGEVPMTEGRDLWWHDLM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 481 SFEESNCnlnlSPAP---EEPVYIIYTSGTTGAPKGVIVT---YqnFTHAALAWRqiYELDRKPVrllqiasfsfDVF-- 552
Cdd:cd05966 217 AKQSPEC----EPEWmdsEDPLFILYTSGSTGKPKGVVHTtggY--LLYAATTFK--YVFDYHPD----------DIYwc 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 553 SGDLART----------LTNGGTLIVC------PDETRLepaeiYKIIKSQRITVMESTPALIIPVMEYvyrnqfklpdl 616
Cdd:cd05966 279 TADIGWItghsyivygpLANGATTVMFegtptyPDPGRY-----WDIVEKHKVTIFYTAPTAIRALMKF----------- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 617 dililGSDMVKAQDFKTLtdrfgqsmRIINSYGvtEAtIDSS----FYETSMGGEC----------TGDNV--PI----- 675
Cdd:cd05966 343 -----GDEWVKKHDLSSL--------RVLGSVG--EP-INPEawmwYYEVIGKERCpivdtwwqteTGGIMitPLpgatp 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 ---GS---PLPNVHMYVLSQTDQIQPIGVAGELCIGGA--GVAKGYHHKPDltqmKFTENPFVSGERLYRTGDRACWLPN 747
Cdd:cd05966 407 lkpGSatrPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDED 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 748 GTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIV------PSDVNTNALRAALTKE 820
Cdd:cd05966 483 GYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVvGRPHDIKGEA-IYAFVTlkdgeePSDELRKELRKHVRKE 561
|
570 580
....*....|....*....|....*.
gi 1238238751 821 LPAYMIPAYLIPLVNMPLTLNGKLDR 846
Cdd:cd05966 562 IGPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
981-1223 |
1.45e-16 |
|
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: 83.94 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 981 NANALHLALRKITEHHDAIRMIFqRDQNGHVIQFnrgINhkDHELFGLYISDWTKASLERAHLD-EKLAAEEtvIQSKMN 1059
Cdd:cd19531 37 DVAALERALNELVARHEALRTTF-VEVDGEPVQV---IL--PPLPLPLPVVDLSGLPEAEREAEaQRLAREE--ARRPFD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1060 VEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPktdsyLS--YAD-------GL 1129
Cdd:cd19531 109 LARGPLLRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPP-----LPiqYADyavwqreWL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1130 TQIAESKQLlsekTYWQTIL-DAHTAF-LPKDIEnVPDKLQMNSDAAAFVLSGDWTEKL----------LFETqqaygtd 1197
Cdd:cd19531 184 QGEVLERQL----AYWREQLaGAPPVLeLPTDRP-RPAVQSFRGARVRFTLPAELTAALralarregatLFMT------- 251
|
250 260
....*....|....*....|....*.
gi 1238238751 1198 anelLLTALGMALSEWTGHDQIVIST 1223
Cdd:cd19531 252 ----LLAAFQVLLHRYSGQDDIVVGT 273
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
363-849 |
1.85e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 84.29 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNET--EISYRLLNERANRLARTLQNrKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPK 438
Cdd:PRK13390 7 AQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYD-AGLRTgdVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 439 ARIEYILRDSGADILLLQRELKHLISNS-PESEMSHIF---LDDEGSFEESNCNLNlSPAPEEP--VYIIYTSGTTGAPK 512
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKVgADLPLRLSFggeIDGFGSFEAALAGAG-PRLTEQPcgAVMLYSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 513 GVivtyqnftHAALAWRQIyelDRKPVRLLQIASFSFDVFSGDL---------ARTL-------TNGGTLIVCpdeTRLE 576
Cdd:PRK13390 165 GI--------QPDLPGRDV---DAPGDPIVAIARAFYDISESDIyyssapiyhAAPLrwcsmvhALGGTVVLA---KRFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 577 PAEIYKIIKSQRITVMESTPALIIPVMEY--VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSmrIINSYGVTEA- 653
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLLKLdaDVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI--VYEYYSSTEAh 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 654 ---TIDSS---FYETSMGGECTGDnvpigsplpnvhMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLT-QMKFTE 726
Cdd:PRK13390 309 gmtFIDSPdwlAHPGSVGRSVLGD------------LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTaAAQHPA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 727 NPFVSgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQ-----AGLA 800
Cdd:PRK13390 377 HPFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAViGVPDPEMGEqvkavIQLV 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1238238751 801 AYIVPSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK13390 452 EGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
501-849 |
2.50e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 82.40 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 IIYTSGTTGAPKGVIVTYQNF------THAALA----WrqiyeldrkpvrLL-----QIASFSFdvfsgdLARTLTNGGT 565
Cdd:PRK07824 40 VVATSGTTGTPKGAMLTAAALtasadaTHDRLGgpgqW------------LLalpahHIAGLQV------LVRSVIAGSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 566 LIVCPDETRLEPAEIYKIIKS----QRITVMesTPALIIPVMEYVYRNQfKLPDLDILILGSDMVKAQDFKTLTDrfgQS 641
Cdd:PRK07824 102 PVELDVSAGFDPTALPRAVAElgggRRYTSL--VPMQLAKALDDPAATA-ALAELDAVLVGGGPAPAPVLDAAAA---AG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 642 MRIINSYGVTEatidssfyeTSmgGECTGDnvpiGSPLPNVHMYVlsqtdqiqpigVAGELCIGGAGVAKGYHHKPDltq 721
Cdd:PRK07824 176 INVVRTYGMSE---------TS--GGCVYD----GVPLDGVRVRV-----------EDGRIALGGPTLAKGYRNPVD--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 722 mkfteNPFVSGERLYRTGDrACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLA 800
Cdd:PRK07824 227 -----PDPFAEPGWFRTDD-LGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVfGLPDDRLGQRVVA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1238238751 801 AYIV---PSDVnTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK07824 301 AVVGdggPAPT-LEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
950-1329 |
3.30e-16 |
|
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: 82.88 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 950 LTPIQRRFFgqvhaFHYHYN--QSVMLFS----EKG-FNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrgINHKD 1022
Cdd:cd19536 4 LSSLQEGML-----FHSLLNpgGSVYLHNytytVGRrLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQ----VVHRQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1023 HELFGLYISDWtkasleraHLDEKLAA-----EETVIQsKMNVEKGPLLQAGLFKTAEGDH--LLIALHHLVIDGVSWRI 1095
Cdd:cd19536 75 AQVPVTELDLT--------PLEEQLDPlraykEETKIR-RFDLGRAPLVRAALVRKDERERflLVISDHHSILDGWSLYL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1096 LLEDLAAAYQQALEKKEIQLPPKtdsyLSYADGLTQIAESKQLLSEKTYWQTIL-DAHTAFLPKDIENVPDKLQMNSDaa 1174
Cdd:cd19536 146 LVKEILAVYNQLLEYKPLSLPPA----QPYRDFVAHERASIQQAASERYWREYLaGATLATLPALSEAVGGGPEQDSE-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1175 afVLSGDWTEKLLFETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDisRTVGWFTSIYPILLDM 1254
Cdd:cd19536 220 --LLVSVPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1255 GIpEPFEDQLayriKTTKDML------RRVP-----NKGTGYGLLTHIGELRHKepEVSFNYLGQFSEEKEVETFQLSYY 1323
Cdd:cd19536 296 SE-ETVEDLL----KRAQEQEleslshEQVPladiqRCSEGEPLFDSIVNFRHF--DLDFGLPEWGSDEGMRRGLLFSEF 368
|
....*.
gi 1238238751 1324 QPRYEI 1329
Cdd:cd19536 369 KSNYDV 374
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
357-830 |
3.76e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.77 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 357 RIFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNR---KGpkPTVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:PRK08279 41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARgvgKG--DVVALLMENRPEYLAAWLGLAKLGAVVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHYPKARIEYILRDSGADILLLQRELKHLISNSPES---EMSHIFLDDEGSFEES---NCNLNLSPAP------------ 495
Cdd:PRK08279 119 TQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADlarPPRLWVAGGDTLDDPEgyeDLAAAAAGAPttnpasrsgvta 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 496 EEPVYIIYTSGTTGAPKGVIVT-------YQNFTH---------------------------------AALAWRQIYELD 535
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMShmrwlkaMGGFGGllrltpddvlycclplyhntggtvawssvlaagATLALRRKFSAS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 536 R--KPVRLLQIASFsfdVFSGDLARTLTNggtlivCPDetrlEPAEiykiiKSQRITVMestpaliipvmeyvyrnqfkl 613
Cdd:PRK08279 279 RfwDDVRRYRATAF---QYIGELCRYLLN------QPP----KPTD-----RDHRLRLM--------------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 614 pdldiliLGSDMvKAQDFKTLTDRFGQsMRIINSYGVTEATIdsSFYETsmggectgDNVP--IG-SPLPNVHMYVLSQT 690
Cdd:PRK08279 320 -------IGNGL-RPDIWDEFQQRFGI-PRILEFYAASEGNV--GFINV--------FNFDgtVGrVPLWLAHPYAIVKY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 691 DQI--QPI------------GVAGELC--IGGAGVAKGYhHKPDLTQMKFTENPFVSGERLYRTGDRACWLPNGTIRLLG 754
Cdd:PRK08279 381 DVDtgEPVrdadgrcikvkpGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 755 RM-D-YQVKinGYRIETEEIESVLLQTGLVREAAV-AVQ-HDKNGQAGLAAyIVPSDVNT---NALRAALTKELPAYMIP 827
Cdd:PRK08279 460 RLgDtFRWK--GENVATTEVENALSGFPGVEEAVVyGVEvPGTDGRAGMAA-IVLADGAEfdlAALAAHLYERLPAYAVP 536
|
...
gi 1238238751 828 AYL 830
Cdd:PRK08279 537 LFV 539
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
379-805 |
4.58e-16 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 83.03 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLQNRKGPKPT---VAVLAKRSIDAIVGVLAVMKAGGVYIPI-DAHYPKArIEYILRDSGADILL 454
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPAPasfVGIYSINRPEWIISELACYAYSLVTVPLyDTLGPEA-IEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 LQRELKhlisnspesemshIFLDDEgsFEESNCNLNLS---PAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALA---- 527
Cdd:cd05927 85 CDAGVK-------------VYSLEE--FEKLGKKNKVPpppPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvfki 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 528 WRQIYELDRKPV------------RLLQIASFSFDV----FSGDLaRTLTNggtlivcpDETRLEPA----------EIY 581
Cdd:cd05927 150 LEILNKINPTDVyisylplahifeRVVEALFLYHGAkigfYSGDI-RLLLD--------DIKALKPTvfpgvprvlnRIY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 582 KIIKSQritvMESTPALIIPVMEYVYRNQ---------FKLPDLDILIlgsdmvkaqdFKTLTDRFGQSMRIINS----- 647
Cdd:cd05927 221 DKIFNK----VQAKGPLKRKLFNFALNYKlaelrsgvvRASPFWDKLV----------FNKIKQALGGNVRLMLTgsapl 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 648 -------------------YGVTEatidssfyeTSMGGECT--GDNVP--IGSPLPNVHM---------YVLSQTDQiqp 695
Cdd:cd05927 287 spevleflrvalgcpvlegYGQTE---------CTAGATLTlpGDTSVghVGGPLPCAEVklvdvpemnYDAKDPNP--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 696 igvAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRmdyqvKIN------GYRIET 769
Cdd:cd05927 355 ---RGEVCIRGPNVFSGYYKDPEKTAEALDEDGW------LHTGDIGEWLPNGTLKIIDR-----KKNifklsqGEYVAP 420
|
490 500 510
....*....|....*....|....*....|....*.
gi 1238238751 770 EEIESVLLQTGLVREAAVavqHDKNGQAGLAAYIVP 805
Cdd:cd05927 421 EKIENIYARSPFVAQIFV---YGDSLKSFLVAIVVP 453
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
367-851 |
4.92e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 83.12 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 367 PEHIAVIDNETEISYRLLNERANRLARTL-QNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYIL 445
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLtRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 446 RDSGADILLLQRELKHLISNSPESemshIFLDDEGSFEESNCNLNLSPAPEEPVyIIYTSGTTGAPKGVIVTYQnFTHAA 525
Cdd:PRK13383 129 RAHHISTVVADNEFAERIAGADDA----VAVIDPATAGAEESGGRPAVAAPGRI-VLLTSGTTGKPKGVPRAPQ-LRSAV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 526 LAWRQIyeLDRKPVRLLQIASFSFDVFS----GDLARTLTNGGTLIV---CPDETRLEPAEIYkiiKSQRITVMESTPAL 598
Cdd:PRK13383 203 GVWVTI--LDRTRLRTGSRISVAMPMFHglglGMLMLTIALGGTVLThrhFDAEAALAQASLH---RADAFTAVPVVLAR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 599 IIPVMEYVyRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQSMriINSYGVTEATIDSsfyeTSMGGECTGDNVPIGSP 678
Cdd:PRK13383 278 ILELPPRV-RARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDIL--YNGYGSTEVGIGA----LATPADLRDAPETVGKP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 679 LPNVHMYVLSQTDqiQPIG--VAGELCIGGAGVAKGYHHKPDltqmkfteNPFVSGerLYRTGDRACWLPNGTIRLLGRM 756
Cdd:PRK13383 351 VAGCPVRILDRNN--RPVGprVTGRIFVGGELAGTRYTDGGG--------KAVVDG--MTSTGDMGYLDNAGRLFIVGRE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 757 DYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNALRAALTKELPAYMIPAYLIP 832
Cdd:PRK13383 419 DDMIISGGENVYPRAVENALAAHPAVADNAViGVPDERFGHR-LAAFVVLhpgSGVDAAQLRDYLKDRVSRFEQPRDINI 497
|
490
....*....|....*....
gi 1238238751 833 LVNMPLTLNGKLDRNALPA 851
Cdd:PRK13383 498 VSSIPRNPTGKVLRKELPG 516
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
354-849 |
1.15e-15 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 81.80 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 354 PFHRIFEAKAEEN-----------PEHIAVID--NETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGV 419
Cdd:cd17642 7 PFYPLEDGTAGEQlhkamkryasvPGTIAFTDahTGVNYSYAEYLEMSVRLAEALKKYGlKQNDRIAVCSENSLQFFLPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 420 LAVMKAGGVYIPIDAHY-----------PKARIEYILRDSGADILLLQRELKH----LISNSPESEMSHIFLDdegSFEE 484
Cdd:cd17642 87 IAGLFIGVGVAPTNDIYnereldhslniSKPTIVFCSKKGLQKVLNVQKKLKIiktiIILDSKEDYKGYQCLY---TFIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 485 SNCNLNLSPAPEEPV---------YIIYTSGTTGAPKGVIVTYQN----FTHAalawRQ-IYELDRKP-VRLLQIASF-- 547
Cdd:cd17642 164 QNLPPGFNEYDFKPPsfdrdeqvaLIMNSSGSTGLPKGVQLTHKNivarFSHA----RDpIFGNQIIPdTAILTVIPFhh 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 548 SFDVFSgdLARTLTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVK 627
Cdd:cd17642 240 GFGMFT--TLGYLICGFRVVLMY---KFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 628 AQDFKTLTDRFGQSMrIINSYGVTEATidSSFYETSmggecTGDNVP--IGSPLPNVHMYVLS-QTDQIQPIGVAGELCI 704
Cdd:cd17642 315 KEVGEAVAKRFKLPG-IRQGYGLTETT--SAILITP-----EGDDKPgaVGKVVPFFYAKVVDlDTGKTLGPNERGELCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 705 GGAGVAKGYHHKPDLTQMKFTENPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE 784
Cdd:cd17642 387 KGPMIMKGYVNNPEATKALIDKDGWL------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFD 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 785 AAVA-VQHDKNGQAGLAAYIVPSDVNTN---ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd17642 461 AGVAgIPDEDAGELPAAVVVLEAGKTMTekeVMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
377-615 |
2.42e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 80.72 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 377 TEISYRLLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADIL 453
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRAlglREGD--VVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 454 LLQREL----KHLISNSPEsEMSHIFLDDEG-----SFEESncnlnLSPAPEEPV-------YIIYTSGTTGAPKGVIvt 517
Cdd:PRK08276 88 IVSAALadtaAELAAELPA-GVPLLLVVAGPvpgfrSYEEA-----LAAQPDTPIadetagaDMLYSSGTTGRPKGIK-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 518 yqnfthaalawRQIYELDRKPVRLLQIASFSFDVFSGDLARTL------------------TNGGTLIVCPdetRLEPAE 579
Cdd:PRK08276 160 -----------RPLPGLDPDEAPGMMLALLGFGMYGGPDSVYLspaplyhtaplrfgmsalALGGTVVVME---KFDAEE 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1238238751 580 IYKIIKSQRITVMEstpalIIPVMeyvYRNQFKLPD 615
Cdd:PRK08276 226 ALALIERYRVTHSQ-----LVPTM---FVRMLKLPE 253
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
377-849 |
3.38e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 80.69 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 377 TEISYR----LLNERANRLARTLQNRKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADI 452
Cdd:PRK08751 49 KTITYReadqLVEQFAAYLLGELQLKKGDR--VALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 453 LLLQ----RELKHLISNSPESEMSHIFLDDEGSFEES---------------NCNLN-------------------LSPA 494
Cdd:PRK08751 127 LVVIdnfgTTVQQVIADTPVKQVITTGLGDMLGFPKAalvnfvvkyvkklvpEYRINgairfrealalgrkhsmptLQIE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 PEEPVYIIYTSGTTGAPKGVIVTYQNFT---HAALAWRQIYE--LDRKPVRLLQIASFSFDVFSGDLARTLTNGGT--LI 567
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmQQAHQWLAGTGklEEGCEVVITALPLYHIFALTANGLVFMKIGGCnhLI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 568 VCPDETRlepaEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVK---AQDFKTLTdrfgqSMRI 644
Cdd:PRK08751 287 SNPRDMP----GFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQrsvAERWKQVT-----GLTL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 645 INSYGVTEATIDSSFYETSMggecTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQmkf 724
Cdd:PRK08751 358 VEAYGLTETSPAACINPLTL----KEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETA--- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 725 tenPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVL-LQTGLVREAAVAVQHDKNGQAgLAAYI 803
Cdd:PRK08751 431 ---KVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIaMMPGVLEVAAVGVPDEKSGEI-VKVVI 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1238238751 804 VPSDVNTNA--LRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK08751 507 VKKDPALTAedVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
497-787 |
4.58e-15 |
|
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: 78.11 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 497 EPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLArTLTNGGTLIVCPdetRLE 576
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLA-TFHAGGTNVFVR---RVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 577 PAEIYKIIKSQRITvmestPALIIP--VMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTD-RFGQSMRiinSYGVTEA 653
Cdd:cd17636 77 AEEVLELIEAERCT-----HAFLLPptIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTsPWGRKPG---GYGQTEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 654 TIDSSFYetSMGGECTGDNvpiGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTenpfvSGe 733
Cdd:cd17636 149 MGLATFA--ALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-----GG- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238751 734 rLYRTGDRACWLPNGTIRLLG---RMdyqVKINGYRIETEEIESVLLQTGLVREAAV 787
Cdd:cd17636 218 -WHHTNDLGRREPDGSLSFVGpktRM---IKSGAENIYPAEVERCLRQHPAVADAAV 270
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
359-849 |
1.21e-14 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 78.56 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 359 FEAKAEENPEHIAVID------NETEISYRLLNERANRLARTLqNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYI 430
Cdd:PRK13295 30 LDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGL-ARLGVGRgdVVSCQLPNWWEFTVLYLACSRIGAVLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 431 PIDAHYPKARIEYILRDSGADILL----------------LQRELKHLisnspesemSHIFL---DDEGSFEESNCN--- 488
Cdd:PRK13295 109 PLMPIFRERELSFMLKHAESKVLVvpktfrgfdhaamarrLRPELPAL---------RHVVVvggDGADSFEALLITpaw 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 489 ----------LNLSPAPEEPVYIIYTSGTTGAPKGVIVTyqnfthAALAWRQIYELdrkPVRLlqiasfsfDVFSGD--- 555
Cdd:PRK13295 180 eqepdapailARLRPGPDDVTQLIYTSGTTGEPKGVMHT------ANTLMANIVPY---AERL--------GLGADDvil 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 556 LARTLTN------GGTLIVCPDETRL-----EPAEIYKIIKSQRIT-VMESTPALIiPVMEYVYRNQFKLPDLDILILGS 623
Cdd:PRK13295 243 MASPMAHqtgfmyGLMMPVMLGATAVlqdiwDPARAAELIRTEGVTfTMASTPFLT-DLTRAVKESGRPVSSLRTFLCAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 624 DMVKAQDFKTLTDRFGQSmrIINSYGVTE---ATIdssfyeTSMGGEctgDNVPI---GSPLPNVHMYVLSQTDQIQPIG 697
Cdd:PRK13295 322 APIPGALVERARAALGAK--IVSAWGMTEngaVTL------TKLDDP---DERASttdGCPLPGVEVRVVDADGAPLPAG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 698 VAGELCIGGAGVAKGYHHKPDLTQMkftenpfvSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLL 777
Cdd:PRK13295 391 QIGRLQVRGCSNFGGYLKRPQLNGT--------DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLY 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238751 778 QTGLVREAAVAVQHDKNGQAGLAAYIVP---SDVNTNALRAAL-TKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK13295 463 RHPAIAQVAIVAYPDERLGERACAFVVPrpgQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
378-756 |
2.12e-14 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 77.89 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 378 EISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIdahYPKA---RIEYILRDSGADIL 453
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGlEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTLnpdTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 454 LLQR-----ELKHLISNSPESEMShiFLDDEGSFEESNCNL---------NLSPAPEEPVYIIYTSGTTGAPKGVIVTYQ 519
Cdd:cd05932 83 FVGKlddwkAMAPGVPEGLISISL--PPPSAANCQYQWDDLiaqhppleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 520 NFTHAALAwrQIYELDRKPV-RLL------QIASFSFdVFSGDLArtltnGGTLIVCPDETRLEPAEiykiIKSQRITVM 592
Cdd:cd05932 161 SFAWAAQA--GIEHIGTEENdRMLsylplaHVTERVF-VEGGSLY-----GGVLVAFAESLDTFVED----VQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 593 ESTPALIIPVMEYVYRnqfKLP--DLDILI----------------LGSDMVK---------AQDFKTLTDRFGqsMRII 645
Cdd:cd05932 229 FSVPRLWTKFQQGVQD---KIPqqKLNLLLkipvvnslvkrkvlkgLGLDQCRlagcgsapvPPALLEWYRSLG--LNIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 646 NSYGVTEatidSSFYETSmggectgdNVP-------IGSPLPNVHMyvlsqtdqiqPIGVAGELCIGGAGVAKGYHHKPD 718
Cdd:cd05932 304 EAYGMTE----NFAYSHL--------NYPgrdkigtVGNAGPGVEV----------RISEDGEILVRSPALMMGYYKDPE 361
|
410 420 430
....*....|....*....|....*....|....*...
gi 1238238751 719 LTQMKFTENPFVsgerlyRTGDRACWLPNGTIRLLGRM 756
Cdd:cd05932 362 ATAEAFTADGFL------RTGDKGELDADGNLTITGRV 393
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
503-849 |
8.31e-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: 74.82 E-value: 8.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 503 YTSGTTGAPKgvIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSG--DLARTLTNGGTLIVCPDETRLEPA-- 578
Cdd:cd05944 9 HTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSvvTLLTPLASGAHVVLAGPAGYRNPGlf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 579 -EIYKIIKSQRITVMESTPALIIPVMEyVYRNQfKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDS 657
Cdd:cd05944 87 dNFWKLVERYRITSLSTVPTVYAALLQ-VPVNA-DISSLRFAMSGAAPLPVELRARFEDATG--LPVVEGYGLTEATCLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 658 SfyetsmggeCTGDNVP-----IGSPLPNVHMYVL---SQTDQIQPIGV--AGELCIGGAGVAKGYhhkpdlTQMKFTEN 727
Cdd:cd05944 163 A---------VNPPDGPkrpgsVGLRLPYARVRIKvldGVGRLLRDCAPdeVGEICVAGPGVFGGY------LYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 728 PFVsGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYI--VP 805
Cdd:cd05944 228 AFV-ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqlKP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1238238751 806 -SDVNTNALRAALTKELPAY-MIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05944 307 gAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
980-1157 |
9.87e-14 |
|
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: 75.19 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 980 FNANALHLALRKITEHHDAIRM-IFQRDQNGHVIQfnrGINHKdhelfglyisdwTKASLERAHLDEKLAAEETV--IQS 1056
Cdd:cd19532 36 LDVARLERAVRAVGQRHEALRTcFFTDPEDGEPMQ---GVLAS------------SPLRLEHVQISDEAEVEEEFerLKN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1057 -KMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQAlekkeiQLPPKTDSYLSYADGLTQIAE 1134
Cdd:cd19532 101 hVYDLESGETMRIVLLSLSPTEHyLIFGYHHIAMDGVSFQIFLRDLERAYNGQ------PLLPPPLQYLDFAARQRQDYE 174
|
170 180
....*....|....*....|...
gi 1238238751 1135 SKQLLSEKTYWQTILDAHTAFLP 1157
Cdd:cd19532 175 SGALDEDLAYWKSEFSTLPEPLP 197
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
358-804 |
2.82e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 74.49 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAeeNPEHIAVIDNET--EISYRLLNERANRLARTLQNRKGPK--PTVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:PLN02574 46 IFSHHN--HNGDTALIDSSTgfSISYSELQPLVKSMAAGLYHVMGVRqgDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHYPKARIEYILRDSGADILLLQRE-------LKHLISNSPESemshiFLDDEGSFEESNCNLNLSPAPE---EPVY--- 500
Cdd:PLN02574 124 PSSSLGEIKKRVVDCSVGLAFTSPEnveklspLGVPVIGVPEN-----YDFDSKRIEFPKFYELIKEDFDfvpKPVIkqd 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 ----IIYTSGTTGAPKGVIVTYQNFTH-----------------------AALAWRQIYELDRKPVRLLQIasfsfdvfs 553
Cdd:PLN02574 199 dvaaIMYSSGTTGASKGVVLTHRNLIAmvelfvrfeasqyeypgsdnvylAALPMFHIYGLSLFVVGLLSL--------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 554 gdlartltnGGTLIVCpdeTRLEPAEIYKIIKSQRITVMESTPaliiPVMEYVYR-------NQFKlpDLDILILGSdmv 626
Cdd:PLN02574 270 ---------GSTIVVM---RRFDASDMVKVIDRFKVTHFPVVP----PILMALTKkakgvcgEVLK--SLKQVSCGA--- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 627 kAQDFKTLTDRFGQSM---RIINSYGVTEAT-IDSSFYETsmggECTGDNVPIGSPLPNVHMYVLS-QTDQIQPIGVAGE 701
Cdd:PLN02574 329 -APLSGKFIQDFVQTLphvDFIQGYGMTESTaVGTRGFNT----EKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 702 LCIGGAGVAKGYHHKPDLTQMKFTENPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGL 781
Cdd:PLN02574 404 LWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPE 477
|
490 500
....*....|....*....|...
gi 1238238751 782 VREAAVAVQHDKNGQAGLAAYIV 804
Cdd:PLN02574 478 IIDAAVTAVPDKECGEIPVAFVV 500
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
949-1264 |
3.75e-13 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 73.29 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 949 ELTPIQRRFF---------GQV--HAfhyhYNQsvmlFSEKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQfnrg 1017
Cdd:cd19535 3 PLTDVQYAYWigrqddqelGGVgcHA----YLE----FDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1018 inhkDHELFGLYISDWTKASLERAhlDEKLAAE-ETVIQSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRI 1095
Cdd:cd19535 71 ----EVPWYGITVHDLRGLSEEEA--EAALEELrERLSHRVLDVERGPLFDIRLSLLPEGRTrLHLSIDLLVADALSLQI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1096 LLEDLAAAYQQAlekkEIQLPPKTDSYLSYadgLTQIAESKQLLSE--KTYWQTILDAhtafLP--------KDienvPD 1165
Cdd:cd19535 145 LLRELAALYEDP----GEPLPPLELSFRDY---LLAEQALRETAYEraRAYWQERLPT----LPpapqlplaKD----PE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1166 KLqmnsDAAAFV-----LS-GDWteKLLFETQQAYGTDANELLLTALGMALSEWTGHDQIVIsteghgreghvpNI---- 1235
Cdd:cd19535 210 EI----KEPRFTrrehrLSaEQW--QRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLL------------NLtlfn 271
|
330 340 350
....*....|....*....|....*....|....*..
gi 1238238751 1236 ------DISRTVGWFTSIypILL--DMGIPEPFEDQL 1264
Cdd:cd19535 272 rlplhpDVNDVVGDFTSL--LLLevDGSEGQSFLERA 306
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
360-851 |
4.01e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 73.73 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 360 EAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKrSIDAIV-GVLAVMKAGGVYIPIDAHYP 437
Cdd:PLN02479 27 ERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSiGPGSTVAVIAP-NIPAMYeAHFGVPMAGAVVNCVNIRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 438 KARIEYILRDSGADILLLQRELKHL-------ISNSPESEMSHIFL----DD------------------EGSFEESNCN 488
Cdd:PLN02479 106 APTIAFLLEHSKSEVVMVDQEFFTLaeealkiLAEKKKSSFKPPLLivigDPtcdpkslqyalgkgaieyEKFLETGDPE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 489 LNLSPAPEE--PVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFD--VFSGDLArtlTNGG 564
Cdd:PLN02479 186 FAWKPPADEwqSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNgwCFTWTLA---ALCG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 565 TLIVCpdeTRLEPAEIYKIIKSQRITVMESTPALI-----IPVMEYVyrnqFKLPDL-DILILGSdmvkAQDFKTLTDRF 638
Cdd:PLN02479 263 TNICL---RQVTAKAIYSAIANYGVTHFCAAPVVLntivnAPKSETI----LPLPRVvHVMTAGA----APPPSVLFAMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 639 GQSMRIINSYGVTEATIDSsfyeTSMGGECTGDNVPIG-----SPLPNVHMYVLSQTDQIQPIGVA---------GELCI 704
Cdd:PLN02479 332 EKGFRVTHTYGLSETYGPS----TVCAWKPEWDSLPPEeqarlNARQGVRYIGLEGLDVVDTKTMKpvpadgktmGEIVM 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 705 GGAGVAKGYHHKPdltqmKFTENPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE 784
Cdd:PLN02479 408 RGNMVMKGYLKNP-----KANEEAFANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLE 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238751 785 AAVAVQHDKNGQAGLAAYIVPSDVNTNALRAALT--------KELPAYMIPAYLI--PLvnmPLTLNGKLDRNALPA 851
Cdd:PLN02479 481 ASVVARPDERWGESPCAFVTLKPGVDKSDEAALAedimkfcrERLPAYWVPKSVVfgPL---PKTATGKIQKHVLRA 554
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
363-514 |
8.44e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 72.80 E-value: 8.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNET--EISYRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPK 438
Cdd:PRK13391 7 AQTTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSL-GLKRgdHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 439 ARIEYILRDSGADILLL---QREL-KHLISNSPESEMsHIFLDDEG------SFEESNCNLNLSPAPEEP--VYIIYTSG 506
Cdd:PRK13391 86 AEAAYIVDDSGARALITsaaKLDVaRALLKQCPGVRH-RLVLDGDGelegfvGYAEAVAGLPATPIADESlgTDMLYSSG 164
|
....*...
gi 1238238751 507 TTGAPKGV 514
Cdd:PRK13391 165 TTGRPKGI 172
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
348-845 |
1.15e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 73.08 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 348 FAQKDIP---FHRIFEAKAEENPEHIAVIDNETE-ISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVM 423
Cdd:PRK06814 624 FETSDYDrtlFEALIEAAKIHGFKKLAVEDPVNGpLTYRKLLTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQ 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 424 KAGgvYIPIDAHYpKARIEYIL---RDSGADILLLQR------ELKHLISNSpESEMSHIFLDD---------------E 479
Cdd:PRK06814 704 SAG--RVPAMINF-SAGIANILsacKAAQVKTVLTSRafiekaRLGPLIEAL-EFGIRIIYLEDvraqigladkikgllA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 480 GSFEE-SNCNlnlsPAPEEPVYIIYTSGTTGAPKGVIVTYQNF-THAAlawrqiyeldrkpvrllQIAS---FS-----F 549
Cdd:PRK06814 780 GRFPLvYFCN----RDPDDPAVILFTSGSEGTPKGVVLSHRNLlANRA-----------------QVAAridFSpedkvF 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 550 DV--------FSGDLARTLTNGGTLIVCPD--ETRLEPAEIYKIiksqRITVMESTPALIipvMEYV-YRNQFKLPDLDI 618
Cdd:PRK06814 839 NAlpvfhsfgLTGGLVLPLLSGVKVFLYPSplHYRIIPELIYDT----NATILFGTDTFL---NGYArYAHPYDFRSLRY 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 619 LILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFyetsmggectgdNVP-------IGSPLPNVHmyvlSQTD 691
Cdd:PRK06814 912 VFAGAEKVKEETRQTWMEKFG--IRILEGYGVTETAPVIAL------------NTPmhnkagtVGRLLPGIE----YRLE 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 692 QIQPIGVAGELCIGGAGVAKGYHHkpdltqmkfTENPFV---SGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIE 768
Cdd:PRK06814 974 PVPGIDEGGRLFVRGPNVMLGYLR---------AENPGVlepPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMIS 1044
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 769 ---TEEIESVLLQTGLvrEAAVAVQHDKNGQAgLAAYIVPSDVN-TNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKL 844
Cdd:PRK06814 1045 laaVEELAAELWPDAL--HAAVSIPDARKGER-IILLTTASDATrAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKI 1121
|
.
gi 1238238751 845 D 845
Cdd:PRK06814 1122 D 1122
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
375-843 |
1.52e-12 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 71.69 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 375 NETEISYRLLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVyipidahypKARIEYILRDSGadi 452
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDLGVQAgdFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSGDP--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 453 lllqreLKHLISNSpesEMSHIFLDdegsfeesncnlnlspaPEEPVYIIYTSGTTGAPKGVIVTY-QNFTHAAL--AWR 529
Cdd:cd05937 70 ------LIHCLKLS---GSRFVIVD-----------------PDDPAILIYTSGTTGLPKAAAISWrRTLVTSNLlsHDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 530 QIYELDR--KPVRLLQIASFSFDvfsgdLARTLTNGGTLIVCP--------DETRLEPAEIYKIIkSQRITVMESTPALI 599
Cdd:cd05937 124 NLKNGDRtyTCMPLYHGTAAFLG-----ACNCLMSGGTLALSRkfsasqfwKDVRDSGATIIQYV-GELCRYLLSTPPSP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 600 IPVMEYV---YRNQFKlPDLdililgsdmvkAQDFKtltDRFGQSMrIINSYGVTEATIDS-SFYETSMGGECTGDNVPI 675
Cdd:cd05937 198 YDRDHKVrvaWGNGLR-PDI-----------WERFR---ERFNVPE-IGEFYAATEGVFALtNHNVGDFGAGAIGHHGLI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 GS-PLPNVHMYVLSQTDQIQPI-----GVAGELCIGGAG------------VAKGYHHKPDLTQMKFTENPFVSGERLYR 737
Cdd:cd05937 262 RRwKFENQVVLVKMDPETDDPIrdpktGFCVRAPVGEPGemlgrvpfknreAFQGYLHNEDATESKLVRDVFRKGDIYFR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 738 TGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREA---AVAVQHdKNGQAGLAAYI------VPSDV 808
Cdd:cd05937 342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvyGVKVPG-HDGRAGCAAITleessaVPTEF 420
|
490 500 510
....*....|....*....|....*....|....*
gi 1238238751 809 NTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGK 843
Cdd:cd05937 421 TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHK 455
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
3-319 |
1.79e-12 |
|
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: 70.79 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 3 KPFDLSQaPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNNRNLPAlRIQYKDY-----AVWREGFKTg 77
Cdd:cd19545 93 APMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PPPFSRFvkylrQLDDEAAAE- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 78 dayktqeaYWLKQLEGELPVL--DLPADHARPPVRSfagdkvsfTLDQEVASGLHKLARENGSTlymVLLAAYTAFLSRL 155
Cdd:cd19545 170 --------FWRSYLAGLDPAVfpPLPSSRYQPRPDA--------TLEHSISLPSSASSGVTLAT---VLRAAWALVLSRY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 156 SGQEDIIVGSPIAGR--PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETALEAFEHQDYPfeeLVDKLELTRDM 233
Cdd:cd19545 231 TGSDDVVFGVTLSGRnaPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTG---LQNIRRLGPDA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 234 SRNPVFDAMFILQNVEKQDIDLREIKVRPANFAHHISLFD--ITLIATEISGSICCEMEFSTEVFLKATIERWADHFiEF 311
Cdd:cd19545 308 RAACNFQTLLVVQPALPSSTSESLELGIEEESEDLEDFSSygLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQF-EH 386
|
....*...
gi 1238238751 312 LHEALSTP 319
Cdd:cd19545 387 VLQQLASA 394
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
358-849 |
2.20e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 71.62 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 358 IFEAKAEENPEHIAVIDNETEISYRLLNERANRLARTLQN----RKGPKptVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNglglKKGDR--VALMMPNLLQYPIALFGILRAGMIVVNVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHYPKARIEYILRDSGADILLL-------------QRELKHLISNSPESEMS-------------------HIFLDDEGS 481
Cdd:PRK08974 106 PLYTPRELEHQLNDSGAKAIVIvsnfahtlekvvfKTPVKHVILTRMGDQLStakgtlvnfvvkyikrlvpKYHLPDAIS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 482 FEESncnlnLS---------P--APEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYE-LDRKPVRLLQIASFSF 549
Cdd:PRK08974 186 FRSA-----LHkgrrmqyvkPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpLLHPGKELVVTALPLY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 550 DVFsgdlART------LTNGGT--LIVCPdetRLEPAEIyKIIKSQRITVMESTPALIipvMEYVYRNQFKLPDLDILIL 621
Cdd:PRK08974 261 HIF----ALTvncllfIELGGQnlLITNP---RDIPGFV-KELKKYPFTAITGVNTLF---NALLNNEEFQELDFSSLKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 622 --GSDM----VKAQDFKTLTDRfgqsmRIINSYGVTEAT--IDSSFYEtsmggeCTGDNVPIGSPLPNVHMYVLSQTDQI 693
Cdd:PRK08974 330 svGGGMavqqAVAERWVKLTGQ-----YLLEGYGLTECSplVSVNPYD------LDYYSGSIGLPVPSTEIKLVDDDGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 694 QPIGVAGELCIGGAGVAKGYHHKPDLTQmKFTENPFVSgerlyrTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIE 773
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATD-EVIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 774 SVLLQTGLVRE-AAVAVQHDKNGQAgLAAYIVPSD--VNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK08974 472 DVVMLHPKVLEvAAVGVPSEVSGEA-VKIFVVKKDpsLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
497-846 |
3.91e-12 |
|
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: 69.22 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 497 EPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLArTLTNGGTLIVCPdetRLE 576
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALA-TFHAGGANVVME---KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 577 PAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDIlILGSDMVK-AQDFKTLTDrfgqsMRIINSYGVTEAti 655
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH-VLGLDAPEtIQRFEETTG-----ATFWSLYGQTET-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 656 dSSFYETSMGGECTGDnvpIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKFTENpfvsgerL 735
Cdd:cd17637 149 -SGLVTLSPYRERPGS---AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------W 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 736 YRTGDracwlpngtirlLGRMDYQ--------------VKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAA 801
Cdd:cd17637 218 HHTGD------------LGRFDEDgylwyagrkpekelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKA 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 802 YIVpsdvnTNALRAALTKELPA--------YMIPAYLIPLVNMPLTLNGKLDR 846
Cdd:cd17637 286 VCV-----LKPGATLTADELIEfvgsriarYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
405-789 |
5.21e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 70.21 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 405 VAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYP----KARIEYIlrdsGADILLLQRELKH----LISNSPESEMSHIFL 476
Cdd:PLN02860 60 VAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfeeaKSAMLLV----RPVMLVTDETCSSwyeeLQNDRLPSLMWQVFL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 477 DD---EGSFEESN--------------CNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPV 539
Cdd:PLN02860 136 ESpssSVFIFLNSflttemlkqralgtTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 540 rLLQIASFsfdVFSGDLARTLTN---GGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYR--NQFKLP 614
Cdd:PLN02860 216 -YLHTAPL---CHIGGLSSALAMlmvGACHVLLP---KFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKsmTWKVFP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 615 DLDILILGSDMVKAQDFKTLTDRFGQSmRIINSYGVTEA------------TIDSSFYETSMGGECTGDNVP------IG 676
Cdd:PLN02860 289 SVRKILNGGGSLSSRLLPDAKKLFPNA-KLFSAYGMTEAcssltfmtlhdpTLESPKQTLQTVNQTKSSSVHqpqgvcVG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 677 SPLPNVHMYVlsQTDQIQPIgvaGELCIGGAGVAKGYhhkpdltqmkFTENPFVSGERL----YRTGDRACWLPNGTIRL 752
Cdd:PLN02860 368 KPAPHVELKI--GLDESSRV---GRILTRGPHVMLGY----------WGQNSETASVLSndgwLDTGDIGWIDKAGNLWL 432
|
410 420 430
....*....|....*....|....*....|....*...
gi 1238238751 753 LGRMDYQVKINGYRIETEEIESVLLQ-TGLVREAAVAV 789
Cdd:PLN02860 433 IGRSNDRIKTGGENVYPEEVEAVLSQhPGVASVVVVGV 470
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
379-846 |
5.35e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 69.90 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPidahypkarieyilrdsgADILLLQR 457
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGvGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 458 ELKHLIsnspesemshifldDEGsfEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAwrQIYELDRK 537
Cdd:cd05974 63 DLRDRV--------------DRG--GAVYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLS--TMYWIGLK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 538 PVRL-LQIASFSFDVFSGDLARTLTNGGTLIVCPDETRLEPAEIYKIIKSQRITVMESTPAliipvmeyVYR-------N 609
Cdd:cd05974 125 PGDVhWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPT--------VWRmliqqdlA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 610 QFKLPDLDILILGS-------DMVKAQDFKTLTDRFGQsmriinsygvTEATIdssfyetsMGGECTGDNVPIGS---PL 679
Cdd:cd05974 197 SFDVKLREVVGAGEplnpeviEQVRRAWGLTIRDGYGQ----------TETTA--------LVGNSPGQPVKAGSmgrPL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 680 PNVHMYVLsqtDQIQPIGVAGELCIG-----GAGVAKGYHHKPDLTQMkftenpfVSGERLYRTGDRACWLPNGTIRLLG 754
Cdd:cd05974 259 PGYRVALL---DPDGAPATEGEVALDlgdtrPVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 755 RMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAAYIV------PSDVNTNALRAALTKELPAYMIPA 828
Cdd:cd05974 329 RADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyePSPETALEIFRFSRERLAPYKRIR 408
|
490
....*....|....*...
gi 1238238751 829 YLiPLVNMPLTLNGKLDR 846
Cdd:cd05974 409 RL-EFAELPKTISGKIRR 425
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
420-849 |
5.59e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 70.20 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 420 LAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLL-QRELKHLIS-------------------NSPESEM-SHIFLDD 478
Cdd:PRK05620 82 FAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAdPRLAEQLGEilkecpcvravvfigpsdaDSAAAHMpEGIKVYS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 479 EGSFEESNCNLNLSPAPEE--PVYIIYTSGTTGAPKGVIvtyqnFTHAALaWRQiyeldrkPVRLLQIASFS-------- 548
Cdd:PRK05620 162 YEALLDGRSTVYDWPELDEttAAAICYSTGTTGAPKGVV-----YSHRSL-YLQ-------SLSLRTTDSLAvthgesfl 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 549 -----FDVFSGDLARTLTNGGTLIVCPDETrLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGS 623
Cdd:PRK05620 229 ccvpiYHVLSWGVPLAAFMSGTPLVFPGPD-LSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 624 DMVKAQDFKTLTDRFGqsMRIINSYGVTEATIDSSFYETSMG--GEcTGDNVPIGSPLPNVHM--------YVLSQTDQI 693
Cdd:PRK05620 308 SAVPPILIKAWEERYG--VDVVHVWGMTETSPVGTVARPPSGvsGE-ARWAYRVSQGRFPASLeyrivndgQVMESTDRN 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 694 QpigvaGELCIGGAGVAKGYHHKP----DLTQMKFTENPFVSGERLY------RTGDRACWLPNGTIRLLGRMDYQVKIN 763
Cdd:PRK05620 385 E-----GEIQVRGNWVTASYYHSPteegGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 764 GYRIETEEIESVLLQTGLVREAAV-AVQHDKNGQAGLAAYIVPSDVNTNA-----LRAALTKELPAYMIPAYLIPLVNMP 837
Cdd:PRK05620 460 GEWIYSAQLENYIMAAPEVVECAViGYPDDKWGERPLAVTVLAPGIEPTRetaerLRDQLRDRLPNWMLPEYWTFVDEID 539
|
490
....*....|..
gi 1238238751 838 LTLNGKLDRNAL 849
Cdd:PRK05620 540 KTSVGKFDKKDL 551
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
496-849 |
8.51e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 69.93 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 496 EEPVYIIYTSGTTGAPKGVIVTYQNF-THAALAWRqiYELDRKPVRLLQ-------IASFSFDVFSgdlarTLTNGGTLI 567
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYmVYTATTFK--YAFDYKPTDVYWctadcgwITGHSYVTYG-----PMLNGATVL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 568 VC------PDetrlePAEIYKIIKSQRITVMESTPALIIPVM----EYVYRNQFKlpdlDILILGS--DMVKAQDFKTLT 635
Cdd:PLN02654 348 VFegapnyPD-----SGRCWDIVDKYKVTIFYTAPTLVRSLMrdgdEYVTRHSRK----SLRVLGSvgEPINPSAWRWFF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 636 DRFGQSmriinsygvtEATIDSSFYETSMGGECTgdnvpigSPLPNVHMYVLSQTD----QIQPIGV-----------AG 700
Cdd:PLN02654 419 NVVGDS----------RCPISDTWWQTETGGFMI-------TPLPGAWPQKPGSATfpffGVQPVIVdekgkeiegecSG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 701 ELCIGGA--GVAK---GYHHKPDLTQMKFTENPFVSGERLYRTGDRACWLPngtirllGRMDYQVKINGYRIETEEIESV 775
Cdd:PLN02654 482 YLCVKKSwpGAFRtlyGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLT-------GRVDDVINVSGHRIGTAEVESA 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 776 LLQTGLVREAA-VAVQHDKNGQaGLAAYI-----VP-SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNA 848
Cdd:PLN02654 555 LVSHPQCAEAAvVGIEHEVKGQ-GIYAFVtlvegVPySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRI 633
|
.
gi 1238238751 849 L 849
Cdd:PLN02654 634 L 634
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
360-849 |
8.59e-12 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 69.42 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 360 EAKAEENPEHIAVIDNETEI--SYRLLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAH 435
Cdd:cd05928 21 AGKRPPNPALWWVNGKGDEVkwSFRELGSLSRKAANVLSGACGLQRgdRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 436 YPKARIEYILRDSGADILL----LQRELKHLISNSPESE----MSHIFLDDEGSF--------EESNCnlnLSPAPEEPV 499
Cdd:cd05928 101 LTAKDILYRLQASKAKCIVtsdeLAPEVDSVASECPSLKtkllVSEKSRDGWLNFkellneasTEHHC---VETGSQEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 500 YIIYTSGTTGAPKGVIVTYQNFTHAALAWRQiYELDRKPVRLLQIASFSFDVFS--GDLARTLTNGGTLIV--CPdetRL 575
Cdd:cd05928 178 AIYFTSGTTGSPKMAEHSHSSLGLGLKVNGR-YWLDLTASDIMWNTSDTGWIKSawSSLFEPWIQGACVFVhhLP---RF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 576 EPAEIYKIIKSQRITVMESTPAliipvmeyVYR-------NQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSY 648
Cdd:cd05928 254 DPLVILKTLSSYPITTFCGAPT--------VYRmlvqqdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG--LDIYEGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 649 GVTEATIDSSFYET------SMGgectgdnvpigSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVakgyhhKPDLTQM 722
Cdd:cd05928 324 GQTETGLICANFKGmkikpgSMG-----------KASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPI------RPFGLFS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 723 KFTENP--FVSGER--LYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAG 798
Cdd:cd05928 387 GYVDNPekTAATIRgdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 799 LAAYIVPSDVNTNALRAALTKEL--------PAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05928 467 VKAFVVLAPQFLSHDPEQLTKELqqhvksvtAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
379-830 |
9.14e-12 |
|
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: 68.92 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGAdilllqr 457
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGlKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSA------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 458 elKHLISnspesemshiflddegsfeesncnlnlspapeEPVYIIYTSGTTGAPKGVIVTYqnfthaalawrqiyeldRK 537
Cdd:cd05940 77 --KHLVV--------------------------------DAALYIYTSGTTGLPKAAIISH-----------------RR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 538 PVRLLQIASFSFDVFSGD-----------------LARTLTNGGTLIVCP--------DETRLEPAEIYKIIKSQRITVM 592
Cdd:cd05940 106 AWRGGAFFAGSGGALPSDvlytclplyhstalivgWSACLASGATLVIRKkfsasnfwDDIRKYQATIFQYIGELCRYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 593 EStpaliiPVMEYVYRNQFKLpdldilILGSDMvKAQDFKTLTDRFGQSmRIINSYGVTEATIdsSFYETsmggectgDN 672
Cdd:cd05940 186 NQ------PPKPTERKHKVRM------IFGNGL-RPDIWEEFKERFGVP-RIAEFYAATEGNS--GFINF--------FG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 673 VP-----IGSPLPNVHMYVLSQTD--QIQPI------------GVAGELC--IGGAGVAKGYHhKPDLTQMKFTENPFVS 731
Cdd:cd05940 242 KPgaigrNPSLLRKVAPLALVKYDleSGEPIrdaegrcikvprGEPGLLIsrINPLEPFDGYT-DPAATEKKILRDVFKK 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 732 GERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV-AVQ---HDknGQAGLAAYIVPSD 807
Cdd:cd05940 321 GDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVyGVQvpgTD--GRAGMAAIVLQPN 398
|
490 500
....*....|....*....|....*
gi 1238238751 808 VNTN--ALRAALTKELPAYMIPAYL 830
Cdd:cd05940 399 EEFDlsALAAHLEKNLPGYARPLFL 423
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
950-1276 |
1.78e-11 |
|
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: 68.16 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 950 LTPIQRR--FFGQVHAFHYHYNqsvmLFSEKGFNAN----ALHLALRKITEHHDAIRMIFQRDqNGHVIQfnrginhkdh 1023
Cdd:cd19533 4 LTSAQRGvwFAEQLDPEGSIYN----LAEYLEITGPvdlaVLERALRQVIAEAETLRLRFTEE-EGEPYQ---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1024 elfglYISDWTKASLE----RAHLDEKLAAE---ETVIQSKMNVEKGPLLQAGLFKTAEGDHLLIA-LHHLVIDGVSWRI 1095
Cdd:cd19533 69 -----WIDPYTPVPIRhidlSGDPDPEGAAQqwmQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1096 LLEDLAAAYQQALEKKEIQLPPKTdSYLSYADGLTQIAESKQLLSEKTYWQTILDAhtafLPkdiENVPDKLQMNSDAAA 1175
Cdd:cd19533 144 FGQRVAEIYTALLKGRPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFED----LP---EPVSLARRAPGRSLA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1176 F-----VLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIdisrTVGWFTSIYPI 1250
Cdd:cd19533 216 FlrrtaELPPELTRTLL-EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQ----TPGMVANTLPL 290
|
330 340
....*....|....*....|....*.
gi 1238238751 1251 LLDMGIPEPFEDQLAYRIKTTKDMLR 1276
Cdd:cd19533 291 RLTVDPQQTFAELVAQVSRELRSLLR 316
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
375-851 |
2.52e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 67.37 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 375 NETEISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILL 454
Cdd:PRK08308 5 NDEEYSKSDFDLRLQRYEEMEQFQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 455 LQrELKHLISNSPESemshiflddegsfeesncnlnlspAPEEPVYIIYTSGTTGAPKGVivtyqnfthaALAWRQI--- 531
Cdd:PRK08308 85 YG-ESDFTKLEAVNY------------------------LAEEPSLLQYSSGTTGEPKLI----------RRSWTEIdre 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 532 ---Y------ELDRKPVRLLQIaSFSFDVFSGDLArTLTNGGTLIVCpdeTRLEPAEIYKIIKSQRITVMESTPALI--- 599
Cdd:PRK08308 130 ieaYnealncEQDETPIVACPV-THSYGLICGVLA-ALTRGSKPVII---TNKNPKFALNILRNTPQHILYAVPLMLhil 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 600 ---IPVMEYVYRnqfklpdldILILGSDMvKAQDFKTLTDRfgqSMRIINSYGVTEATIDSSFYETSMGGEctgdnvpIG 676
Cdd:PRK08308 205 grlLPGTFQFHA---------VMTSGTPL-PEAWFYKLRER---TTYMMQQYGCSEAGCVSICPDMKSHLD-------LG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 677 SPLPnvHMYVLSQTDQIQPigvaGELCIggagvakgyhhkpdltqmkftenpfVSGERLYRTGDRACWLPNGTIRLLGRM 756
Cdd:PRK08308 265 NPLP--HVSVSAGSDENAP----EEIVV-------------------------KMGDKEIFTKDLGYKSERGTLHFMGRM 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 757 DYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDK-NGQAGLAAYIVPSDVNTNALRAALTKELPAYMIPAYLIPLVN 835
Cdd:PRK08308 314 DDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTE 393
|
490
....*....|....*.
gi 1238238751 836 MPLTLNGKLDRNALPA 851
Cdd:PRK08308 394 IPKNANGKVSRKLLEL 409
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
370-843 |
2.88e-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: 68.07 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 370 IAVIDNE-TEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVY------------------ 429
Cdd:cd05943 89 YAAEDGErTEVTWAELRRRVARLAAALRALGvKPGDRVAGYLPNIPEAVVAMLATASIGAIWsscspdfgvpgvldrfgq 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 430 ------IPIDAH-YPKARIeyilrDSGADILLLQRELK--------HLISNSPESEMSHI----FLDDEGSFEESnCNLN 490
Cdd:cd05943 169 iepkvlFAVDAYtYNGKRH-----DVREKVAELVKGLPsllavvvvPYTVAAGQPDLSKIakalTLEDFLATGAA-GELE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 491 LSPAP-EEPVYIIYTSGTTGAPKGvIVtyqnFTHAALAWRQIYELdrkpvrLLQiasfsFDVFSGD-------------- 555
Cdd:cd05943 243 FEPLPfDHPLYILYSSGTTGLPKC-IV----HGAGGTLLQHLKEH------ILH-----CDLRPGDrlfyyttcgwmmwn 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 556 -LARTLTNGGTlIVCPDETRLEPAE--IYKIIKSQRITVMESTPALIIPVME--YVYRNQFKLPDLD-ILILGSDmVKAQ 629
Cdd:cd05943 307 wLVSGLAVGAT-IVLYDGSPFYPDTnaLWDLADEEGITVFGTSAKYLDALEKagLKPAETHDLSSLRtILSTGSP-LKPE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 630 DFKTLTDRFGQSMRIINSYGVTEatIDSSFyetsMGGectGDNVPIG-SPL--PNVHMYVLSQTDQIQP-IGVAGELCIG 705
Cdd:cd05943 385 SFDYVYDHIKPDVLLASISGGTD--IISCF----VGG---NPLLPVYrGEIqcRGLGMAVEAFDEEGKPvWGEKGELVCT 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 706 GA--GVAKGYHHKPDLTQMK---FTENPFVsgerlYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTG 780
Cdd:cd05943 456 KPfpSMPVGFWNDPDGSRYRaayFAKYPGV-----WAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIP 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 781 LVREAAVAVQHDKNGQAGLAAYIV--PSDVNTNALRAALTKELPAYM----IPAYLIPLVNMPLTLNGK 843
Cdd:cd05943 531 EVEDSLVVGQEWKDGDERVILFVKlrEGVELDDELRKRIRSTIRSALsprhVPAKIIAVPDIPRTLSGK 599
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
491-849 |
3.28e-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: 67.40 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 491 LSPAPEEPVYIIYTSGTTGAPKGVI-----VTYQNFTHAALA------WRQIYELdrkPVRLLQIASFSFdvfsgdLART 559
Cdd:cd05929 120 PIEDEAAGWKMLYSGGTTGRPKGIKrglpgGPPDNDTLMAAAlgfgpgADSVYLS---PAPLYHAAPFRW------SMTA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 560 LTNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPAL---IIPVMEYVyRNQFKLPDLDILI-LGSDM---VKAQdfk 632
Cdd:cd05929 191 LFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVPTMfvrLLKLPEAV-RNAYDLSSLKRVIhAAAPCppwVKEQ--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 633 tLTDRFGQsmRIINSYGVTEAT----IDSSFYETSMGGectgdnvpIGSPLPNVhMYVLSQTDQIQPIGVAGELCIGGAG 708
Cdd:cd05929 264 -WIDWGGP--IIWEYYGGTEGQgltiINGEEWLTHPGS--------VGRAVLGK-VHILDEDGNEVPPGEIGEVYFANGP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 709 vAKGYHHKPDLTQMKFTENPFVS-GERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAV 787
Cdd:cd05929 332 -GFEYTNDPEKTAAARNEGGWSTlGDVGYLDED-------GYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAV 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 788 -AVQHDKNGQAGLAAY-----IVPSDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:cd05929 404 vGVPDEELGQRVHAVVqpapgADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
363-804 |
4.21e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 67.31 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNET--EISYRLLNERANRLARTLQN---RKGpKPTVAVLAKRSIDAIVgVLAVMKAGGVYipidahyp 437
Cdd:PLN02330 38 AELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSlglRKG-QVVVVVLPNVAEYGIV-ALGIMAAGGVF-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 438 karieyilrdSGADILLLQRELKH---------LISNSPESE------MSHIFLDDEGSFEESNCNLNLSPAPE------ 496
Cdd:PLN02330 108 ----------SGANPTALESEIKKqaeaagaklIVTNDTNYGkvkglgLPVIVLGEEKIEGAVNWKELLEAADRagdtsd 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 497 -EPVY------IIYTSGTTGAPKGVIVTYQNFThaALAWRQIYELdrKPVRLLQIASFSFDVF------SGDLARTLTNG 563
Cdd:PLN02330 178 nEEILqtdlcaLPFSSGTTGISKGVMLTHRNLV--ANLCSSLFSV--GPEMIGQVVTLGLIPFfhiygiTGICCATLRNK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 564 GTLIVCpdeTRLEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDI-LILGSDMVKAQDFKTLTDRFGQSM 642
Cdd:PLN02330 254 GKVVVM---SRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqAIMTAAAPLAPELLTAFEAKFPGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 643 RIINSYGVTEATIDSSFYETSMGGECTGDNVPIGSPLPNVHM-YVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQ 721
Cdd:PLN02330 331 QVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSVGFILPNLEVkFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 722 MKFTENPFVsgerlyRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDKNGQAGLAA 801
Cdd:PLN02330 411 RTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAA 484
|
...
gi 1238238751 802 YIV 804
Cdd:PLN02330 485 CVV 487
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
480-789 |
5.87e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 67.31 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 480 GSFEESNCNLNLSPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQ-IYELDRKP------VRLLQIAS-FSFDV 551
Cdd:PTZ00216 248 GHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDrLNDLIGPPeedetyCSYLPLAHiMEFGV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 552 FSGDLAR----------TLTNGgTLIVCPDETRLEPaeiYKIIKSQRI--TVMESTPALIIPV----------------- 602
Cdd:PTZ00216 328 TNIFLARgaligfgsprTLTDT-FARPHGDLTEFRP---VFLIGVPRIfdTIKKAVEAKLPPVgslkrrvfdhayqsrlr 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 603 -----MEYVYRNQ--FKLPDLdilILGSDM-----------VKAQDFKTLTdrFGqsmRIINSYGVTEATIDSSFYETsm 664
Cdd:PTZ00216 404 alkegKDTPYWNEkvFSAPRA---VLGGRVramlsgggplsAATQEFVNVV--FG---MVIQGWGLTETVCCGGIQRT-- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 665 gGECTGDNVpiGSPLPNVHMYVL-----SQTDQIQPigvAGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTG 739
Cdd:PTZ00216 474 -GDLEPNAV--GQLLKGVEMKLLdteeyKHTDTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGW------FHTG 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1238238751 740 DRACWLPNGTIRLLGRMDYQVK-INGYRIETEEIESVLLQTGLVREAAVAV 789
Cdd:PTZ00216 542 DVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNELVVPNGVCV 592
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
495-804 |
7.51e-11 |
|
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: 66.36 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 PEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPvRLLQIASFSFD--VFSGDLARTLTNGGTLIVCPDE 572
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKD-RILSWMPLTHDmgLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 573 TRLEPAEIYKIIKSQRITVMeSTP----ALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQ-SMR---I 644
Cdd:cd05908 184 FIRRPILWLKKASEHKATIV-SSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKyGLKrnaI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 645 INSYGVTEAT-------IDSSFYETSMGGECTGDNVPI----------------GSPLPNVHMYVLSQTDQIQPIGVAGE 701
Cdd:cd05908 263 LPVYGLAEASvgaslpkAQSPFKTITLGRRHVTHGEPEpevdkkdsecltfvevGKPIDETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 702 LCIGGAGVAKGYHHKPDLTQMKFTENPFVsgerlyRTGDRAcWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ--- 778
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEEleg 415
|
330 340
....*....|....*....|....*.
gi 1238238751 779 TGLVREAAVAVQHDKNGQAGLAAYIV 804
Cdd:cd05908 416 VELGRVVACGVNNSNTRNEEIFCFIE 441
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
984-1219 |
9.02e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.29 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 984 ALHLALRKITEHHDAIRMIFQRDQNGHVIQFnrginhkdHELFGLYISDWTKASLERAHLDEKLAAEETVIQSK-MNVEK 1062
Cdd:PRK12316 88 ALERAFASLVQRHETLRTVFPRGADDSLAQV--------PLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQpFDLCE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1063 GPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLLSE 1141
Cdd:PRK12316 160 GPLLRVRLLRLGEEEHvLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1142 KTYWQTIL-DAHTAF-LPKDIENvPDKLQMNSDAAAFVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWTGHDQI 1219
Cdd:PRK12316 240 LEYWRAQLgEEHPVLeLPTDHPR-PAVPSYRGSRYEFSIDPALAEALR-GTARRQGLTLFMLLLGAFNVLLHRYSGQTDI 317
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
363-724 |
1.06e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 66.12 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAV--IDNETE-------ISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPID 433
Cdd:PRK05850 11 ASLQPDDAAFtfIDYEQDpagvaetLTWSQLYRRTLNVAEELRRHGSTGDRAVILAPQGLEYIVAFLGALQAGLIAVPLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 434 AHYPKA---RIEYILRDSGADILL-----LQRELKHLISNSPESEMSHIFLD--DEGSfeESNCNLNLSPAPEePVYIIY 503
Cdd:PRK05850 91 VPQGGAhdeRVSAVLRDTSPSVVLttsavVDDVTEYVAPQPGQSAPPVIEVDllDLDS--PRGSDARPRDLPS-TAYLQY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 504 TSGTTGAPKGVIVTYQNFThaalawrqiyeldrkpVRLLQIASFSFdvfsGDLARTLTNGGTLI--------------VC 569
Cdd:PRK05850 168 TSGSTRTPAGVMVSHRNVI----------------ANFEQLMSDYF----GDTGGVPPPDTTVVswlpfyhdmglvlgVC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 570 pdetrlepaeiykiiksqrITVMESTPA-LIIPV---------MEYVYRNQ----------FKLP-----DLDI------ 618
Cdd:PRK05850 228 -------------------APILGGCPAvLTSPVaflqrparwMQLLASNPhafsaapnfaFELAvrktsDDDMagldlg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 619 ----LILGSDMVKAQDFKTLTDRFGQ------SMRiiNSYGVTEATIdssFYETSMGGE-------------------CT 669
Cdd:PRK05850 289 gvlgIISGSERVHPATLKRFADRFAPfnlretAIR--PSYGLAEATV---YVATREPGQppesvrfdyeklsaghakrCE 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 670 GDN----VPIGSPLPNVHMYVLSQTDQIQPIGVAGELCIGGAGVAKGYHHKPDLTQMKF 724
Cdd:PRK05850 364 TGGgtplVSYGSPRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTF 422
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
380-831 |
1.39e-10 |
|
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: 65.94 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 380 SYRLLNERANRLARTLQNRKG-------------PKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILR 446
Cdd:cd17632 58 TLRLLPRFETITYAELWERVGavaaahdpeqpvrPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 447 DSG-------ADILLLQRELKhLISNSPES-----------------EMSHIFLDDEGSFEE-----SNCNLNLSPAP-- 495
Cdd:cd17632 138 ETEprllavsAEHLDLAVEAV-LEGGTPPRlvvfdhrpevdahraalESARERLAAVGIPVTtltliAVRGRDLPPAPlf 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 496 ------EEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGGT--LI 567
Cdd:cd17632 217 rpepddDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTayFA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 568 VCPDETRL-------EPAEI-------------YKIIKSQRITVMESTPALIIPVMEYVyRNQFKLPDLDILILGSDMVK 627
Cdd:cd17632 297 AASDMSTLfddlalvRPTELflvprvcdmlfqrYQAELDRRSVAGADAETLAERVKAEL-RERVLGGRLLAAVCGSAPLS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 628 AQdFKTLTDRFGQsMRIINSYGVTEAtidssfyetsmgGECTGDNVPIGSPlpnVHMYVLS--------QTDQIQPigvA 699
Cdd:cd17632 376 AE-MKAFMESLLD-LDLHDGYGSTEA------------GAVILDGVIVRPP---VLDYKLVdvpelgyfRTDRPHP---R 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 700 GELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlYRTGDRACWLPNGTIRLLGRMDYQVKIN-GYRIETEEIESVLLQ 778
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKLSqGEFVTVARLEAVFAA 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238751 779 TGLVREAAVavqHDKNGQAGLAAYIVPSD-----VNTNALRAALTK---------ELPAYMIPAYLI 831
Cdd:cd17632 510 SPLVRQIFV---YGNSERAYLLAVVVPTQdalagEDTARLRAALAEslqriareaGLQSYEIPRDFL 573
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
981-1172 |
2.38e-10 |
|
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: 64.59 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 981 NANALHLALRKITEHHDAIRMIFQrDQNGHVIQFnrgINHKDHELFGLYISDwtkasLERAHLDEKLAAEetvIQSKMNV 1060
Cdd:cd19538 37 DVQALQQALYDVVERHESLRTVFP-EEDGVPYQL---ILEEDEATPKLEIKE-----VDEEELESEINEA---VRYPFDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1061 EKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYAdgLTQiaesKQLL 1139
Cdd:cd19538 105 SEEPPFRATLFELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLPVQYADYA--LWQ----QELL 178
|
170 180 190
....*....|....*....|....*....|...
gi 1238238751 1140 SEKTYWQTILDAHTAFLPKDIENVPDKLQMNSD 1172
Cdd:cd19538 179 GDESDPDSLIARQLAYWKKQLAGLPDEIELPTD 211
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
496-846 |
2.78e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 64.78 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 496 EEPVYIIYTSGTTGAPKGVIVT---YqnFTHAALAWRqiYELDRKPVrllqiasfsfDVF------------S----GDL 556
Cdd:PRK00174 245 EDPLFILYTSGSTGKPKGVLHTtggY--LVYAAMTMK--YVFDYKDG----------DVYwctadvgwvtghSyivyGPL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 557 ArtltNGGTLIV------CPDETRlepaeIYKIIKSQRITVMESTPALIIPVMEYvyrnqfklpdldililGSDMVKAQD 630
Cdd:PRK00174 311 A----NGATTLMfegvpnYPDPGR-----FWEVIDKHKVTIFYTAPTAIRALMKE----------------GDEHPKKYD 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 631 FKTLtdrfgqsmRIINSYGVT---EATIdsSFYETSMGGEC----------TG-----------DNVPiGS---PLPNVH 683
Cdd:PRK00174 366 LSSL--------RLLGSVGEPinpEAWE--WYYKVVGGERCpivdtwwqteTGgimitplpgatPLKP-GSatrPLPGIQ 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 684 MYVLSQTDQIQPIGVAGELCIggagvakgyhHKPDLTQM--------KFTENPFVSGERLYRTGDRACWLPNGTIRLLGR 755
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGGNLVI----------KDPWPGMMrtiygdheRFVKTYFSTFKGMYFTGDGARRDEDGYYWITGR 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 756 MDYQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQaGLAAYIV------PSDVNTNALRAALTKELPAYMIPA 828
Cdd:PRK00174 505 VDDVLNVSGHRLGTAEIESALVAHPKVAEAAvVGRPDDIKGQ-GIYAFVTlkggeePSDELRKELRNWVRKEIGPIAKPD 583
|
410
....*....|....*...
gi 1238238751 829 YLIPLVNMPLTLNGKLDR 846
Cdd:PRK00174 584 VIQFAPGLPKTRSGKIMR 601
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
495-778 |
3.37e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 64.45 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 PEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTNGgtLIVCPDETR 574
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG--VPVVFAYNP 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 575 LEPAEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKaQDFKTLTDRFGQSMRIINSYGVTEA- 653
Cdd:PRK06334 260 LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFK-DSLYQEALKTFPHIQLRQGYGTTECs 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 654 ---TIDSsfyETSMGGECTgdnvpIGSPLPNVHMYVLSQTDQIQ-PIGVAGELCIGGAGVAKGYHHKpDLTQmKFTEnpf 729
Cdd:PRK06334 339 pviTINT---VNSPKHESC-----VGMPIRGMDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLGE-DFGQ-GFVE--- 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1238238751 730 VSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQ 778
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
363-740 |
3.38e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 64.51 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNET-----EISYRLLNERANRLARTLQNRK-GPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHY 436
Cdd:PRK08180 49 AQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGlSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 437 -----PKARIEYILR---------DSGAD-------ILLLQRELkhLISNSPESEMSHIFLDDegsFEESNCNLNLSPA- 494
Cdd:PRK08180 129 slvsqDFGKLRHVLElltpglvfaDDGAAfaralaaVVPADVEV--VAVRGAVPGRAATPFAA---LLATPPTAAVDAAh 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 ----PEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIY-ELDRKPVRLLQIASFSfDVFSG--DLARTLTNGGTLI 567
Cdd:PRK08180 204 aavgPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFpFLAEEPPVLVDWLPWN-HTFGGnhNLGIVLYNGGTLY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 568 VcpDETRLEPAEIYKIIKSQR-I--TVMESTPA---LIIPVMEY--VYRNQFkLPDLDILIL-GSDMvkAQDfktLTDRF 638
Cdd:PRK08180 283 I--DDGKPTPGGFDETLRNLReIspTVYFNVPKgweMLVPALERdaALRRRF-FSRLKLLFYaGAAL--SQD---VWDRL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 639 --------GQSMRIINSYGVTEATIDSSFyetsmggeCTGDNV---PIGSPLPNVHMyvlsqtdQIQPIGVAGELCIGGA 707
Cdd:PRK08180 355 drvaeatcGERIRMMTGLGMTETAPSATF--------TTGPLSragNIGLPAPGCEV-------KLVPVGGKLEVRVKGP 419
|
410 420 430
....*....|....*....|....*....|...
gi 1238238751 708 GVAKGYHHKPDLTQMKFTENPFvsgerlYRTGD 740
Cdd:PRK08180 420 NVTPGYWRAPELTAEAFDEEGY------YRSGD 446
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
862-932 |
6.67e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 56.79 E-value: 6.67e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 862 APVNDLQKTMAYIWEDVLSM--SRVGIHDSFF-ELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQELCGHI 932
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYL 75
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
771-843 |
1.12e-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: 56.01 E-value: 1.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238751 771 EIESVLLQTGLVREAAV-AVQHDKNGQAgLAAYIVP---SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGK 843
Cdd:pfam13193 1 EVESALVSHPAVAEAAVvGVPDELKGEA-PVAFVVLkpgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1061-1262 |
1.15e-09 |
|
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: 62.33 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1061 EKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPKTDSYLSYADGLTQIAESKQLL 1139
Cdd:cd20484 106 ENGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYDFVAWEQDMLAGAEGE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1140 SEKTYWQT-------ILDahtafLPKDIENvPDKLQMNSDAAAFVLSGDWTEKL-LFETQQAYGTDAneLLLTALGMALS 1211
Cdd:cd20484 186 EHRAYWKQqlsgtlpILE-----LPADRPR-SSAPSFEGQTYTRRLPSELSNQIkSFARSQSINLST--VFLGIFKLLLH 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1238238751 1212 EWTGHDQIVISTEGHGReghvPNIDISRTVGWFTSIYPILLDMGIPEPFED 1262
Cdd:cd20484 258 RYTGQEDIIVGMPTMGR----PEERFDSLIGYFINMLPIRSRILGEETFSD 304
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
874-927 |
1.72e-09 |
|
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: 54.88 E-value: 1.72e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238751 874 IWEDVLSMS--RVGIHDSFFELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQE 927
Cdd:pfam00550 6 LLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
493-805 |
2.75e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 61.65 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAA------------------LAWRQIYEldrkpvRLLQIASFSFDV--- 551
Cdd:PLN02736 218 PKPEDVATICYTSGTTGTPKGVVLTHGNLIANVagsslstkfypsdvhisyLPLAHIYE------RVNQIVMLHYGVavg 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 552 -FSGDLARTLTNGGTL---IVC--PdetRLEpAEIYKIIKSqriTVMESTPaliipVMEYVYRNQFKLPDlDILILGSDM 625
Cdd:PLN02736 292 fYQGDNLKLMDDLAALrptIFCsvP---RLY-NRIYDGITN---AVKESGG-----LKERLFNAAYNAKK-QALENGKNP 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 626 VKAQD---FKTLTDRFGQSMRIINS------------------------YGVTEAT-IDSSFYEtsmggectGDNVP--I 675
Cdd:PLN02736 359 SPMWDrlvFNKIKAKLGGRVRFMSSgasplspdvmeflricfggrvlegYGMTETScVISGMDE--------GDNLSghV 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 676 GSPLPNVHMYV-----LSQTDQIQPIGvAGELCIGGAGVAKGYHHKPDLTQMKFTENPFVsgerlyRTGDRACWLPNGTI 750
Cdd:PLN02736 431 GSPNPACEVKLvdvpeMNYTSEDQPYP-RGEICVRGPIIFKGYYKDEVQTREVIDEDGWL------HTGDIGLWLPGGRL 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238751 751 RLLGRMDYQVKI-NGYRIETEEIESVLLQTGLVREAAVavqHDKNGQAGLAAYIVP 805
Cdd:PLN02736 504 KIIDRKKNIFKLaQGEYIAPEKIENVYAKCKFVAQCFV---YGDSLNSSLVAVVVV 556
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
967-1250 |
3.26e-09 |
|
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: 60.79 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 967 HYNQSVMLFSeKGFNANALHLALRKITEHHDAIRMIFQRDQNGHVIQFNRGINHKDHELFglyisDWTKASLER-AHLDE 1045
Cdd:cd19547 24 YFNQNVLELV-GGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWALL-----DWSGEDPDRrAELLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1046 KLAAEETViqSKMNVEKGPLLQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQALEKKEIQLPPkTDSYLS 1124
Cdd:cd19547 98 RLLADDRA--AGLSLADCPLYRLTLVRLGGGRHyLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSP-CRPYRD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1125 YADGLTqiAESKQLLSEKTYWQTILDAHTaflPKDIENVPDKLQMNSDAAAFVLSGDWTEkLLFETQQAYGTDANELLLT 1204
Cdd:cd19547 175 YVRWIR--ARTAQSEESERFWREYLRDLT---PSPFSTAPADREGEFDTVVHEFPEQLTR-LVNEAARGYGVTTNAISQA 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1238238751 1205 ALGMALSEWTGHDQIVistegHGR--EGHVPNIDISR-TVGWFTSIYPI 1250
Cdd:cd19547 249 AWSMLLALQTGARDVV-----HGLtiAGRPPELEGSEhMVGIFINTIPL 292
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
363-596 |
5.32e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 60.73 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 363 AEENPEHIAVIDNETEISYRLLNERANRLARTLQNRK-GPKPTVAVLAKrSIDAIVGV-LAVMKAGGVYIPIDAHYPKAR 440
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGiGRGDTVAVLLP-NIPAMVEAhFGVPMAGAVLNTLNTRLDAAS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 441 IEYILRDSGADILLLQRELKHLISNS----------------PESEMSHIF--LDDEGSFEESNCNLNLS-PAPE-EPVY 500
Cdd:PRK08162 107 IAFMLRHGEAKVLIVDTEFAEVAREAlallpgpkplvidvddPEYPGGRFIgaLDYEAFLASGDPDFAWTlPADEwDAIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 IIYTSGTTGAPKGVIV----TYQNFTHAALAWrqiyELDRKPVRLLQIASF-----SFdvfsgdlARTLT-NGGTlIVCp 570
Cdd:PRK08162 187 LNYTSGTTGNPKGVVYhhrgAYLNALSNILAW----GMPKHPVYLWTLPMFhcngwCF-------PWTVAaRAGT-NVC- 253
|
250 260
....*....|....*....|....*.
gi 1238238751 571 dETRLEPAEIYKIIKSQRITVMESTP 596
Cdd:PRK08162 254 -LRKVDPKLIFDLIREHGVTHYCGAP 278
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
504-849 |
7.12e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 60.35 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 504 TSGTTGAPKGVIVTYQNftHAALAWRQIYELDRKPVRLLQIASFSFDVFS--GDLARTLTNGGTLIVCP-----DETRLe 576
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGN--EVANAWLGALLLGLGPGDTVFCGLPLFHVNAllVTGLAPLARGAHVVLATpqgyrGPGVI- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 577 pAEIYKIIKSQRITVMESTPALI-----IPVmeyvyrNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQsmRIINSYGVT 651
Cdd:PRK07529 298 -ANFWKIVERYRINFLSGVPTVYaallqVPV------DGHDISSLRYALCGAAPLPVEVFRRFEAATGV--RIVEGYGLT 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 652 EATIDSSFyetsmggectgdNVP--------IGSPLPNVHMYVLSQTDQ---IQPIGVA--GELCIGGAGVAKGYhhkpd 718
Cdd:PRK07529 369 EATCVSSV------------NPPdgerrigsVGLRLPYQRVRVVILDDAgryLRDCAVDevGVLCIAGPNVFSGY----- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 719 LTQMKftENPFVSGERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVAVQHDknGQAG 798
Cdd:PRK07529 432 LEAAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPD--AHAG 507
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238751 799 L--AAYI--VP-SDVNTNALRAALTKELP---AymIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK07529 508 ElpVAYVqlKPgASATEAELLAFARDHIAeraA--VPKHVRILDALPKTAVGKIFKPAL 564
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
379-830 |
1.69e-08 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 58.84 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 379 ISYRLLNERANRLARTLQNRKGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAHYPKARIEYILRDSGADILLLQ 456
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHAGLRPgdTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 457 RELKHLISN---SPESEMSHIFLDDEGSFEESNCNL--NLSPAPEEPVYI--------------IYTSGTTGAPKGVIVT 517
Cdd:cd05938 86 PELQEAVEEvlpALRADGVSVWYLSHTSNTEGVISLldKVDAASDEPVPAslrahvtikspalyIYTSGTTGLPKAARIS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 518 Y------QNFTHA--ALAWRQIYEldrkPVRLLQIASFSFDvFSGDLARtltnGGTLIVCPdetRLEPAEIYKIIKSQRI 589
Cdd:cd05938 166 HlrvlqcSGFLSLcgVTADDVIYI----TLPLYHSSGFLLG-IGGCIEL----GATCVLKP---KFSASQFWDDCRKHNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 590 TVMEstpaLIIPVMEYVYrNQFKLPDLDI----LILGSDmVKAQDFKTLTDRFGQsMRIINSYGVTEATIDSSFYetsmg 665
Cdd:cd05938 234 TVIQ----YIGELLRYLC-NQPQSPNDRDhkvrLAIGNG-LRADVWREFLRRFGP-IRIREFYGSTEGNIGFFNY----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 666 gecTGDNVPIG---SPLPNVHMYVLSQTD--QIQPIGVAGELCI----GGAG--VAK--------GYHHKPDLTQMKFTE 726
Cdd:cd05938 302 ---TGKIGAVGrvsYLYKLLFPFELIKFDveKEEPVRDAQGFCIpvakGEPGllVAKitqqspflGYAGDKEQTEKKLLR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 727 NPFVSGERLYRTGDracwlpngtirlLGRMDYQ------------VKINGYRIETEEIESVLLQTGLVREA---AVAVQ- 790
Cdd:cd05938 379 DVFKKGDVYFNTGD------------LLVQDQQnflyfhdrvgdtFRWKGENVATTEVADVLGLLDFLQEVnvyGVTVPg 446
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1238238751 791 HDknGQAGLAAYIV--PSDVNTNALRAALTKELPAYMIPAYL 830
Cdd:cd05938 447 HE--GRIGMAAVKLkpGHEFDGKKLYQHVREYLPAYARPRFL 486
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
378-848 |
2.07e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.60 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 378 EISYRLLNERANRLARTLQNRKGPKPTVAVLAKRSIDAIVGVLAVMKAGGVYIPIDAhyPK-----ARIEYILRDSGADI 452
Cdd:PRK12476 68 ELTWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFA--PElpghaERLDTALRDAEPTV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 453 LL----LQRELKHLISNSPESEMSHIFLDDE--GSFEESncnlnLSPAP---EEPVYIIYTSGTTGAPKGVIVTYQ---- 519
Cdd:PRK12476 146 VLtttaAAEAVEGFLRNLPRLRRPRVIAIDAipDSAGES-----FVPVEldtDDVSHLQYTSGSTRPPVGVEITHRavgt 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 520 NFTHAALAwrqIYELDRkpvrllQIASFSFDVFSGDLartltnGGTLIVCP-----DETRLEPAEI----YKIIKSQRIT 590
Cdd:PRK12476 221 NLVQMILS---IDLLDR------NTHGVSWLPLYHDM------GLSMIGFPavyggHSTLMSPTAFvrrpQRWIKALSEG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 591 VMESTPALIIPVMEYVYRNQFKLP----DLD----ILILGSDMVKAQDFKTLTDRFGQ----SMRIINSYGVTEATIDSS 658
Cdd:PRK12476 286 SRTGRVVTAAPNFAYEWAAQRGLPaegdDIDlsnvVLIIGSEPVSIDAVTTFNKAFAPyglpRTAFKPSYGIAEATLFVA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 659 ------------FYETSMGgecTGDNVPIGSPLPNVHMYV------LSQ--------TDQIQPIGVAGELCIGGAGVAKG 712
Cdd:PRK12476 366 tiapdaepsvvyLDREQLG---AGRAVRVAADAPNAVAHVscgqvaRSQwavivdpdTGAELPDGEVGEIWLHGDNIGRG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 713 YHHKPDLTQMKF---TENPFVSGE---------RLYRTGDRACWLpNGTIRLLGRMDYQVKINGYRIETEEIE-SVLLQT 779
Cdd:PRK12476 443 YWGRPEETERTFgakLQSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEaTVAEAS 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 780 GLVRE---AAVAVQHDKNGQAGLAAYIVPSDVNTN------ALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNA 848
Cdd:PRK12476 522 PMVRRgyvTAFTVPAEDNERLVIVAERAAGTSRADpapaidAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRA 599
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
5-314 |
3.95e-08 |
|
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: 57.26 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 5 FDLSQAPLFRAQIVKISDERHLLLVDMHHIISDGVSVNILIREFGELYNN---RNLPAL--RIQYKDYAVWREGFKTGDA 79
Cdd:cd19534 103 LDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQalaGEPIPLpsKTSFQTWAELLAEYAQSPA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 80 YKTQEAYWLKQLEGELPvlDLPADHarpPVRSFAGDKVSFTLDQE-VASGLHKLARENGSTLYMVLLAAYTAFLSRLSGQ 158
Cdd:cd19534 183 LLEELAYWRELPAADYW--GLPKDP---EQTYGDARTVSFTLDEEeTEALLQEANAAYRTEINDLLLAALALAFQDWTGR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 159 EDIIVGSPIAGR----PHKDLEPILGMFVNTLALRTRPEGGKPFVQYLQEVRETA---------------LEAFEHQDYP 219
Cdd:cd19534 258 APPAIFLEGHGReeidPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLrripnkgigygilryLTPEGTKRLA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 220 F----EELVDKLELTRDMSRNPVFDAMFILQNVEKQDIDLReikvRPAnfahhisLFDITLIATEisGSICCEMEFSTEV 295
Cdd:cd19534 338 FhpqpEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTP----RFA-------LLDINAVVEG--GQLVITVSYSRNM 404
|
330
....*....|....*....
gi 1238238751 296 FLKATIERWADHFIEFLHE 314
Cdd:cd19534 405 YHEETIQQLADSYKEALEA 423
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
951-1236 |
7.18e-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: 56.54 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 951 TPIQRRFFG----QVHAFHYHYNQSVmlfsEKGFNANALHLALRKITEHHDAIRM-IFQRDQNG--HVIqfnrginHKDH 1023
Cdd:cd19545 5 TPLQEGLMAltarQPGAYVGQRVFEL----PPDIDLARLQAAWEQVVQANPILRTrIVQSDSGGllQVV-------VKES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1024 ELfglyisDWTKASLERAHLDEKLAAEETViqskmnveKGPLLQAGLFK-TAEGDHLLIALHHLVIDGVSWRILLEDLAA 1102
Cdd:cd19545 74 PI------SWTESTSLDEYLEEDRAAPMGL--------GGPLVRLALVEdPDTERYFVWTIHHALYDGWSLPLILRQVLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1103 AYQQaleKKEIQLPPKTD--SYLSYADgltqIAESKQllsektYWQTILD-----AHTAFLPKDIENVPDKLQMNSDAAA 1175
Cdd:cd19545 140 AYQG---EPVPQPPPFSRfvKYLRQLD----DEAAAE------FWRSYLAgldpaVFPPLPSSRYQPRPDATLEHSISLP 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238238751 1176 FVLSGDWTekllfetqqaygtdANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNID 1236
Cdd:cd19545 207 SSASSGVT--------------LATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIE 253
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
500-849 |
1.15e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 56.25 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 500 YIIYTSGTTGAPKGVIVTYQNFT-HA-ALAWRQIYELDRKPVRLLQIASFSFDVFSGDLARTLTngGTLIVCPDEtRLEP 577
Cdd:PRK07008 180 SLCYTSGTTGNPKGALYSHRSTVlHAyGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLT--GAKLVLPGP-DLDG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 578 AEIYKIIKSQRITVMESTPALIIPVMEYVYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGqsMRIINSYGVTEAtids 657
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYG--VEVIHAWGMTEM---- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 658 sfyeTSMGGECT----GDNVPI----------GSPLPNVHMYVLSQTDQIQPI-GVA-GELCIGGAGVAKGYhhkpdltq 721
Cdd:PRK07008 331 ----SPLGTLCKlkwkHSQLPLdeqrkllekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRY-------- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 722 MKFTENPFVSGerLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAA-VAVQHDKNGQAGLA 800
Cdd:PRK07008 399 FRGDASPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAAcIACAHPKWDERPLL 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1238238751 801 AyIVP---SDVNTNALRAALTKELPAYMIPAYLIPLVNMPLTLNGKLDRNAL 849
Cdd:PRK07008 477 V-VVKrpgAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
498-784 |
7.76e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 53.59 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 498 PVYIIYTSGTTGAPKGVIVTY-QNFTHAALAWRQIYELDrKPVRLLQIASFSFDVFSGDLARTLTNGGTLIVCP-DETRL 575
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKD-IPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEgGIIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 576 EPAE--IYKIIKSQRITVMESTPALIIPVMEY-----VYRNQFKLPDLDILILGSDMVKaqdfKTLTDRFGQSMRI--IN 646
Cdd:PTZ00237 335 KHIEddLWNTIEKHKVTHTLTLPKTIRYLIKTdpeatIIRSKYDLSNLKEIWCGGEVIE----ESIPEYIENKLKIksSR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 647 SYGVTEATIDSSFyetsmggECTGDNVPI---GSPLPNVHMYVLSQTDQIQPIGVAGELCIG---GAGVAKGYHHKPDLT 720
Cdd:PTZ00237 411 GYGQTEIGITYLY-------CYGHINIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKF 483
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238238751 721 QMKFTENPfvsgeRLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVRE 784
Cdd:PTZ00237 484 KQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
934-1253 |
9.13e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 934 PLA--SQA--DQGP-AEGEAE----LTPIQrrffgQVHAFHYHYNQSV------MLFSEKGFNANALHLALRKITEHHDA 998
Cdd:PRK12316 4080 PLAglDQArlDALPlPLGEIEdiypLSPMQ-----QGMLFHSLYEQEAgdyinqMRVDVQGLDVERFRAAWQAALDRHDV 4154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 999 IRMIF-QRDQNGHVIQfnrgINHKDHELfGLYISDWTKASLERAHLDEKLAAEEtviQSKMNVEKGPLLQAGLFKTAEGD 1077
Cdd:PRK12316 4155 LRSGFvWQGELGRPLQ----VVHKQVSL-PFAELDWRGRADLQAALDALAAAER---ERGFDLQRAPLLRLVLVRTAEGR 4226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1078 HLLIAL-HHLVIDGVSWRILLEDLAAAYQQalekkeiQLPPKTDsyLSYADGLTQIAESKQLLSEKtYWQTILDAHTAFL 1156
Cdd:PRK12316 4227 HHLIYTnHHILMDGWSNSQLLGEVLERYSG-------RPPAQPG--GRYRDYIAWLQRQDAAASEA-FWREQLAALDEPT 4296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1157 PKDIENVPDKLQMNSDAAAFV--LSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPN 1234
Cdd:PRK12316 4297 RLAQAIARADLRSANGYGEHVreLDATATARLR-EFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPG 4375
|
330
....*....|....*....
gi 1238238751 1235 IDisRTVGWFTSIYPILLD 1253
Cdd:PRK12316 4376 IE--GQIGLFINTLPVIAT 4392
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1066-1104 |
9.74e-07 |
|
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: 52.81 E-value: 9.74e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1238238751 1066 LQAGLFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAY 1104
Cdd:cd19540 110 LRARLFRLGPDEHvLVLVVHHIAADGWSMAPLARDLATAY 149
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
456-782 |
5.98e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.89 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 456 QRELKHLISNSPESEMSH--IFLDDEG----SFEESNCNLNLS------------------PAPEEPVYIIYTSGTTGAP 511
Cdd:PLN02387 186 SKQLKKLIDISSQLETVKrvIYMDDEGvdsdSSLSGSSNWTVSsfseveklgkenpvdpdlPSPNDIAVIMYTSGSTGLP 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 512 KGVIVTYQNFTHAALAWRQIY-ELDRKPVRL--------LQIASFSFDVFSGDL-----ARTLTNGGTLI---VCPDETR 574
Cdd:PLN02387 266 KGVMMTHGNIVATVAGVMTVVpKLGKNDVYLaylplahiLELAAESVMAAVGAAigygsPLTLTDTSNKIkkgTKGDASA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 575 LEPaeiykiiksqriTVMESTPALIIPVMEYVYRN-------QFKLPDLDI-----LILGS------------DMVKaqd 630
Cdd:PLN02387 346 LKP------------TLMTAVPAILDRVRDGVRKKvdakgglAKKLFDIAYkrrlaAIEGSwfgawglekllwDALV--- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 631 FKTLTD------RF---------GQSMRIIN---------SYGVTEATIDSSFYE---TSMGgectgdnvPIGSPLPnvH 683
Cdd:PLN02387 411 FKKIRAvlggriRFmlsggaplsGDTQRFINiclgapigqGYGLTETCAGATFSEwddTSVG--------RVGPPLP--C 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 684 MYV---------LSQTDQIQPigvAGELCIGGAGVAKGYHHKPDLTQ--MKFTENpfvsGERLYRTGDRACWLPNGTIRL 752
Cdd:PLN02387 481 CYVklvsweeggYLISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDevYKVDER----GMRWFYTGDIGQFHPDGCLEI 553
|
410 420 430
....*....|....*....|....*....|.
gi 1238238751 753 LGRMDYQVKI-NGYRIETEEIESVLLQTGLV 782
Cdd:PLN02387 554 IDRKKDIVKLqHGEYVSLGKVEAALSVSPYV 584
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
381-846 |
6.92e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 50.39 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 381 YRLLNERANRLARTLQNRkGPKP--TVAVLAKRSIDAIVGVLAVMKAGGVYIPIDahYPKA---RIEYI------LRDSG 449
Cdd:PRK09192 52 YQTLRARAEAGARRLLAL-GLKPgdRVALIAETDGDFVEAFFACQYAGLVPVPLP--LPMGfggRESYIaqlrgmLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 450 ADILLLQRELKHLISNSPESE-----MSHIFLDDEgsfEESNCNLNlSPAPEEPVYIIYTSGTTGAPKGVIVTY------ 518
Cdd:PRK09192 129 PAAIITPDELLPWVNEATHGNpllhvLSHAWFKAL---PEADVALP-RPTPDDIAYLQYSSGSTRFPRGVIITHralman 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 519 -QNFTHAALawrQIYELDR------------------KPVrllqIASFSFDVF-SGDLARtltnggtlivcpdetrlEPA 578
Cdd:PRK09192 205 lRAISHDGL---KVRPGDRcvswlpfyhdmglvgfllTPV----ATQLSVDYLpTRDFAR-----------------RPL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 579 EIYKIIKSQRITVMESTPaliipvmeYVYR------NQFKLPDLD-----ILILGSDMVKAQDFKTLTDRFGQS----MR 643
Cdd:PRK09192 261 QWLDLISRNRGTISYSPP--------FGYElcarrvNSKDLAELDlscwrVAGIGADMIRPDVLHQFAEAFAPAgfddKA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 644 IINSYGVTEATIDSSFYETSMG-----------------------GECTGDNVPIGSPLPNVHMYVLSQTDQIQPIGVAG 700
Cdd:PRK09192 333 FMPSYGLAEATLAVSFSPLGSGivveevdrdrleyqgkavapgaeTRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 701 ELCIGGAGVAKGYHHKPDLTQMkftenpfVSGERLYRTGDRAcWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTG 780
Cdd:PRK09192 413 HICVRGPSLMSGYFRDEESQDV-------LAADGWLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEP 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 781 LVR--EAAVAVQHDKNGQAglAAYIVPSDVNTNALRAALTKELPAYMIPAY-------LIPLVNMPLTLNGKLDR 846
Cdd:PRK09192 485 ELRsgDAAAFSIAQENGEK--IVLLVQCRISDEERRGQLIHALAALVRSEFgveaaveLVPPHSLPRTSSGKLSR 557
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
493-851 |
7.20e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 50.41 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 493 PAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVRLLQIASF-SFDVFSGdLARTLTNGGTLIVCPd 571
Cdd:PRK13388 147 VDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFhSNAVMAG-WAPAVASGAAVALPA- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 572 etRLEPAEIYKIIKSQRITVME----------STPaliipvmeyvyrnqfKLPDlDI---LILG-----SDmvkaQDFKT 633
Cdd:PRK13388 225 --KFSASGFLDDVRRYGATYFNyvgkplayilATP---------------ERPD-DAdnpLRVAfgneaSP----RDIAE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 634 LTDRFGqsMRIINSYGVTE----ATIDSSFYETSmggectgdnvpIGSPLPNVHMYvlsQTDQIQPIGVA---------- 699
Cdd:PRK13388 283 FSRRFG--CQVEDGYGSSEgaviVVREPGTPPGS-----------IGRGAPGVAIY---NPETLTECAVArfdahgalln 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 700 -----GELC-IGGAGVAKGYHHKPDLTQMKFTENPFVSGERLYRTGDracwlpnGTIRLLGRMDYQVKINGYRIETEEIE 773
Cdd:PRK13388 347 adeaiGELVnTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDAD-------GWIYFAGRTADWMRVDGENLSAAPIE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 774 SVLLQTGLVREAAV-AVQHDKNGQAGLAAYIV--PSDVNTNALRAALT--KELPAYMIPAYLIPLVNMPLTLNGKLDRNA 848
Cdd:PRK13388 420 RILLRHPAINRVAVyAVPDERVGDQVMAALVLrdGATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRE 499
|
...
gi 1238238751 849 LPA 851
Cdd:PRK13388 500 LIA 502
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
911-1259 |
7.52e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.11 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 911 GWSMTiRDLFRYSTIQEL--------------C-----GHITP----LA----SQADQGP-AEGEAE----LTPIQrrff 958
Cdd:PRK12316 1489 HWSFS-REMFAEATVQRLaddyarelqaliehCcdernRGVTPsdfpLAglsqAQLDALPlPAGEIAdiypLSPMQ---- 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 959 gQVHAFHYHYNQSV------MLFSEKGFNANALHLALRKITEHHDAIRMIF----QRDQNGHVIqfnrginHKDHELfGL 1028
Cdd:PRK12316 1564 -QGMLFHSLYEQEAgdyinqLRVDVQGLDPDRFRAAWQATVDRHEILRSGFlwqdGLEQPLQVI-------HKQVEL-PF 1634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1029 YISDWTKASLERAHLDEKLAAEEtviQSKMNVEKGPLLQAGLFKTAEGDHLLI-ALHHLVIDGVSWRILLEDLAAAYQQa 1107
Cdd:PRK12316 1635 AELDWRGREDLGQALDALAQAER---QKGFDLTRAPLLRLVLVRTGEGRHHLIyTNHHILMDGWSNAQLLGEVLQRYAG- 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1108 lekkeiQLPPKTDsyLSYADGLTQIAESKQLLSEKTYWQTILDAHTAFLPKDIENVPDKLQMNSDaaAFVLSGDWTEKLL 1187
Cdd:PRK12316 1711 ------QPVAAPG--GRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGD--HQQLLDPAQTRAL 1780
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238238751 1188 FETQQAYGTDANELLLTALGMALSEWTGHDQIVISTEGHGREGHVPNIDisRTVGWFTSIYPILldmGIPEP 1259
Cdd:PRK12316 1781 AEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIE--QQIGLFINTLPVI---AAPRP 1847
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
882-932 |
1.17e-05 |
|
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: 44.93 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1238238751 882 SRVGIHDSFFELGGDSIKALQVAARLAAE-GWSMTIRDLFRYSTIQELCGHI 932
Cdd:smart00823 31 EAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHL 82
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
350-792 |
1.32e-05 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 49.59 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 350 QKDIPFHR-IFEaKAEENPEHIAVIDNET--EISYRLLNERANRLARTLQN---RKGPkpTVAVLAKRSIDAIVGVLAVM 423
Cdd:PLN02246 20 PNHLPLHDyCFE-RLSEFSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKlgiRQGD--VVMLLLPNCPEFVLAFLGAS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 424 KAGGVYIPIDAHYPKARIEYILRDSGADILLLQ-------RELKH-------LISNSPES--EMSHIFLDDEGSFEESNC 487
Cdd:PLN02246 97 RRGAVTTTANPFYTPAEIAKQAKASGAKLIITQscyvdklKGLAEddgvtvvTIDDPPEGclHFSELTQADENELPEVEI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 488 NlnlspaPEEPVYIIYTSGTTGAPKGVIVTYQNF-THAAlawRQI------YELDRKPVRLLQIASFSFDVFSGDLARTL 560
Cdd:PLN02246 177 S------PDDVVALPYSSGTTGLPKGVMLTHKGLvTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 561 TNGGTLIVCPdetRLEPAEIYKIIKSQRITVMESTPALII-----PVMEyvyrnQFKLPDLDILI-----LGSDMVKAQD 630
Cdd:PLN02246 248 RVGAAILIMP---KFEIGALLELIQRHKVTIAPFVPPIVLaiaksPVVE-----KYDLSSIRMVLsgaapLGKELEDAFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 631 FKTLTDRFGQsmriinSYGVTEA----TIDSSFYETSM---GGECtgdnvpiGSPLPNVHMYVL-SQTDQIQPIGVAGEL 702
Cdd:PLN02246 320 AKLPNAVLGQ------GYGMTEAgpvlAMCLAFAKEPFpvkSGSC-------GTVVRNAELKIVdPETGASLPRNQPGEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 703 CIGGAGVAKGYHHKPDLTQmkftenpfvsgerlyRTGDRACWLPNGTIRLL---------GRMDYQVKINGYRIETEEIE 773
Cdd:PLN02246 387 CIRGPQIMKGYLNDPEATA---------------NTIDKDGWLHTGDIGYIddddelfivDRLKELIKYKGFQVAPAELE 451
|
490
....*....|....*....
gi 1238238751 774 SVLLQTGLVREAAVAVQHD 792
Cdd:PLN02246 452 ALLISHPSIADAAVVPMKD 470
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
501-805 |
1.34e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 49.84 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 501 IIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKpVRLLQIASFSF----DVFSGDLARTLTNGGTLI--------- 567
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDR-VATEEDSYFSYlplaHVYDQVIETYCISKGASIgfwqgdiry 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 568 VCPDETRLEPA------EIYKIIKSQRITVMESTPALIIPVMEYVYrnQFKL-------------PDLDILIlgsdmvka 628
Cdd:PLN02861 304 LMEDVQALKPTifcgvpRVYDRIYTGIMQKISSGGMLRKKLFDFAY--NYKLgnlrkglkqeeasPRLDRLV-------- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 629 qdFKTLTDRFGQSMRIINS------------------------YGVTEA------TIDSSFyetSMGGEctgdnvpIGSP 678
Cdd:PLN02861 374 --FDKIKEGLGGRVRLLLSgaaplprhveeflrvtscsvlsqgYGLTEScggcftSIANVF---SMVGT-------VGVP 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 679 LPNVHmyvlSQTDQIQPIGV-------AGELCIGGAGVAKGYHHKPDLtqmkfTENPFVSGerLYRTGDRACWLPNGTIR 751
Cdd:PLN02861 442 MTTIE----ARLESVPEMGYdalsdvpRGEICLRGNTLFSGYHKRQDL-----TEEVLIDG--WFHTGDIGEWQPNGAMK 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1238238751 752 LLGRMDYQVKIN-GYRIETEEIESVLLQTGLVreAAVAVqHDKNGQAGLAAYIVP 805
Cdd:PLN02861 511 IIDRKKNIFKLSqGEYVAVENLENTYSRCPLI--ASIWV-YGNSFESFLVAVVVP 562
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
495-845 |
1.69e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 49.32 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 495 PEEPVYIIYTSGTTGAPKGVIvtyqnFTHAALAW--RQIYeldrkpvrllQIASFS-FDVFSGDL----ARTLTNG-GTL 566
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVV-----HSHKSLLAnvEQIK----------TIADFTpNDRFMSALplfhSFGLTVGlFTP 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 567 IVCPDETRLEPAEI-YKIIKS----QRITVMESTPALIipvMEYV-YRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGq 640
Cdd:PRK08043 429 LLTGAEVFLYPSPLhYRIVPElvydRNCTVLFGTSTFL---GNYArFANPYDFARLRYVVAGAEKLQESTKQLWQDKFG- 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 641 sMRIINSYGVTEATIDSSFyetsmggectgdNVP-------IGSPLPNVHMYVLSqtdqIQPIGVAGELCIGGAGVAKGY 713
Cdd:PRK08043 505 -LRILEGYGVTECAPVVSI------------NVPmaakpgtVGRILPGMDARLLS----VPGIEQGGRLQLKGPNIMNGY 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 714 H--HKPDLTQMKFTENpfVSGER---LYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIESVLLQTGLVREAAVA 788
Cdd:PRK08043 568 LrvEKPGVLEVPTAEN--ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATA 645
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238238751 789 VQHDKNGQAGLAAYIVPSDVNTNAL-RAALTKELPAYMIPAYLIPLVNMPLTLNGKLD 845
Cdd:PRK08043 646 IKSDASKGEALVLFTTDSELTREKLqQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
644-782 |
2.28e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 48.86 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 644 IINSYGVTEA---TIDSSFYETSMGGEctgdnvpIGSPLPNVHMYVLSQTD-QIQPIGVA--GELCIGGAGVAKGYHHKP 717
Cdd:PLN02614 414 VLQGYGLTEScagTFVSLPDELDMLGT-------VGPPVPNVDIRLESVPEmEYDALASTprGEICIRGKTLFSGYYKRE 486
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238751 718 DLTQMKFTENpfvsgerLYRTGDRACWLPNGTIRLLGRMDYQVKI-NGYRIETEEIESVLLQTGLV 782
Cdd:PLN02614 487 DLTKEVLIDG-------WLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAV 545
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
695-811 |
2.49e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 48.66 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 695 PIGV--AGELCIGGAGVAKGYHHKPDLTQMKFTENPFvsgerlyRTGDRACWLPNGTIRLLGRMDYQVKIN-GYRIETEE 771
Cdd:PLN02430 459 PLGEppRGEICVRGKCLFSGYYKNPELTEEVMKDGWF-------HTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEY 531
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1238238751 772 IESVLLQTGLVREAAVavqHDKNGQAGLAAYIVPSDVNTN 811
Cdd:PLN02430 532 LENVYGQNPIVEDIWV---YGDSFKSMLVAVVVPNEENTN 568
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1070-1279 |
3.14e-05 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 48.24 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1070 LFKTAEGDH-LLIALHHLVIDGVSWRILLEDLAAAYQQaleKKEIQLPPKTDSYLSYADG-------LTQIAESKQLLSE 1141
Cdd:cd19546 117 LFALSDTEHvLLLVVHRIAADDESLDVLVRDLAAAYGA---RREGRAPERAPLPLQFADYalwerelLAGEDDRDSLIGD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 1142 K-TYWQTILDAH--TAFLPKDIENvPDKLQMNSDAAAFVLSGDWTEKLLfETQQAYGTDANELLLTALGMALSEWTGHDQ 1218
Cdd:cd19546 194 QiAYWRDALAGApdELELPTDRPR-PVLPSRRAGAVPLRLDAEVHARLM-EAAESAGATMFTVVQAALAMLLTRLGAGTD 271
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238238751 1219 IVISTEGHGREGHvpnIDISRTVGWFTSIYPILLDMGIPEPFEDQLAYRIKTTKDMLRR--VP 1279
Cdd:cd19546 272 VTVGTVLPRDDEE---GDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHqdVP 331
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
497-851 |
3.89e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.02 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 497 EPVYIIYTSGTTGAPKGVivtyQNFT--HA-ALAWRQIYELDRKPVRLLQIAS-------FSFDVFSgdlarTLTNGGTL 566
Cdd:PRK10524 234 EPSYILYTSGTTGKPKGV----QRDTggYAvALATSMDTIFGGKAGETFFCASdigwvvgHSYIVYA-----PLLAGMAT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 567 IV---CPdeTRLEPAEIYKIIKSQRITVMESTPALIIPVMEY--VYRNQFKLPDLDILILGSDMVKAQDFKTLTDRFGQS 641
Cdd:PRK10524 305 IMyegLP--TRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQdpALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVP 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 642 mrIINSYGVTEatidssfyetsmggecTG----------DNVPI--GSPlpNVHMY-----VLSQTDqiqpigvaGELCi 704
Cdd:PRK10524 383 --VIDNYWQTE----------------TGwpilaiargvEDRPTrlGSP--GVPMYgynvkLLNEVT--------GEPC- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 705 gGAG----VAKGYHHKPDLTQMKFTENP-FVS------GERLYRTGDRACWLPNGTIRLLGRMDYQVKINGYRIETEEIE 773
Cdd:PRK10524 434 -GPNekgvLVIEGPLPPGCMQTVWGDDDrFVKtywslfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 774 SVLLQTGLVREAAV-AVQHDKNGQAGLAAYIV--PSDVNTNALRAALTKE--------LPAYMIPAYlIPLVNM-PLTLN 841
Cdd:PRK10524 513 ESISSHPAVAEVAVvGVKDALKGQVAVAFVVPkdSDSLADREARLALEKEimalvdsqLGAVARPAR-VWFVSAlPKTRS 591
|
410
....*....|
gi 1238238751 842 GKLDRNALPA 851
Cdd:PRK10524 592 GKLLRRAIQA 601
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
405-554 |
2.00e-04 |
|
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: 45.81 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 405 VAVLAKRSIDAIVGVLAVMKAGGVYIPI-DAHYPKArIEYILRDSGADILL------------LQRELKHL-----ISNS 466
Cdd:cd05933 36 VGILGFNSPEWFIAAVGAIFAGGIAVGIyTTNSPEA-CQYVAETSEANILVvenqkqlqkilqIQDKLPHLkaiiqYKEP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238751 467 PESEMSHIFLDDE---GSFEESNCNLNL---SPAPEEPVYIIYTSGTTGAPKGVIVTYQNFTHAALAWRQIYELDRKPVR 540
Cdd:cd05933 115 LKEKEPNLYSWDEfmeLGRSIPDEQLDAiisSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVG 194
|
170 180
....*....|....*....|...
gi 1238238751 541 ---------LLQIASFSFDVFSG 554
Cdd:cd05933 195 qesvvsylpLSHIAAQILDIWLP 217
|
|
| |
