|
Name |
Accession |
Description |
Interval |
E-value |
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1098-2372 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 1046.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1098 STILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQA 1176
Cdd:PRK10252 5 SQHLPLVAAQPGIWMAEKLSPLPSaWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1177 WPVQFCSVTPDLLEQT---IQEALQQPIHLDQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDF--IKAYQQ 1251
Cdd:PRK10252 85 PEIIDLRTQPDPHAAAqalMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIaaIYCAWL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQQLPVLEHSYETVIKALSGRDHETSKviWQRD-------LADLQPLILFNQAQQAVQETSYR-----LSAELGAKLQH 1319
Cdd:PRK10252 165 RGEPTPASPFTPFADVVEEYQRYRASEA--WQRDaafwaeqRRQLPPPASLSPAPLPGRSASADilrlkLEFTDGAFRQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1320 KLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGR--SAPIngleQQIGLFLNTIPVRVKLNMQQTLWE------- 1390
Cdd:PRK10252 243 AAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLRVHIAAQETLPElatrlaa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1391 QLPQL---QQLHVEHLEHDgLGLSAIQQliaqgNLFDSLLVVE------NYPDNQYLQQKLGDAAISKLTnrgyshypLA 1461
Cdd:PRK10252 319 QLKKMrrhQRYDAEQIVRD-SGRAAGDE-----PLFGPVLNIKvfdyqlDFPGVQAQTHTLATGPVNDLE--------LA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1462 LLVIPDHQIELLLE---QRGVIDQPEHFLERMIQLIEIALNEPETSLSHYRLQLAEEHDLIQKTNQTQYYVRQSTLQQLL 1538
Cdd:PRK10252 385 LFPDEHGGLSIEILanpQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1539 REQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK10252 465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQKDLAAIVH-PSIATFAFNELF---DETKVDLSSykttvitPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:PRK10252 545 DRLKMMLEDARPSLLITTADQLPRFADvPDLTSLCYNAPLapqGAAPLQLSQ-------PHHTAYIIFTSGSTGRPKGVM 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:PRK10252 618 VGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVP 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEilSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATlglhPEE---- 1850
Cdd:PRK10252 698 SMLAAFVASLTP--EGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAF----GEElaav 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 --SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADG 1928
Cdd:PRK10252 772 rgSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDG 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1929 SIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNKANV----QLVAYL--QTTAPVDIDQLKKQLAK 2001
Cdd:PRK10252 852 AVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEqAVTHACVINQAAATGgdarQLVGYLvsQSGLPLDTSALQAQLRE 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2002 HLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTpSNTEKQYATSAFEHELTRIFQQILNTDQNiGVNEDFFAIGGHS 2081
Cdd:PRK10252 932 RLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELK-AQVPGRAPKTGTETIIAAAFSSLLGCDVV-DADADFFALGGHS 1009
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2082 ILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQErlAEVEQTGMQPILPIRSGSGHPLFCFYPGSGSAWQYTVL 2161
Cdd:PRK10252 1010 LLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEE--DESRRLGFGTILPLREGDGPTLFCFHPASGFAWQFSVL 1087
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2162 NRYLHSDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLL 2241
Cdd:PRK10252 1088 SRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLL 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2242 DTYPAEIHQWLDLSVEEMN----AEAEQEQLQFfndiLADADSALSEEtrrLQEDIFANYRDAVRLLKPYKMPHFDGELH 2317
Cdd:PRK10252 1168 DTWPPETQNWREKEANGLDpevlAEIDREREAF----LAAQQGSLSTE---LFTTIEGNYADAVRLLTTAHSVPFDGKAT 1240
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 2318 LVVAEKDLLPYIQPEQQWSPLVKKLNIVRLSEAdHTDILSPQQLETLGPILNRMI 2372
Cdd:PRK10252 1241 LFVAERTLQEGMSPEQAWSPWIAELDVYRQDCA-HVDIISPEAFEKIGPILRATL 1294
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
152-2138 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1010.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVS--PFIGVNEVISER---QAYENSHQFkidqAFWKAYCEDLPSPISLS 226
Cdd:PRK12467 182 HHIISDGWSMRVLVEELVQLYSAYSQGREPSLPalPIQYADYAIWQRswlEAGERERQL----AYWQEQLGGEHTVLELP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 227 THH-LAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNdMMMSLSLH-YIYKMTDKAELVNGIPFMRRLGSKAIRSTL 304
Cdd:PRK12467 258 TDRpRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLF-MVLLASFQtLLHRYSGQSDIRIGVPNANRNRVETERLIG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 305 PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidihER--MYGPILNYKAFDQDLVIDGEKVK 382
Cdd:PRK12467 337 FFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQP----ERslSHSPLFQVMFNHQNTATGGRDRE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 383 THHISTGPIDDFE-------FSFIVQDHELIIELRAdSQRYTQDeLFNHG--QRLTL----LLEQALIRPeqpcsnfnit 449
Cdd:PRK12467 413 GAQLPGLTVEELSwarhtaqFDLALDTYESAQGLWA-AFTYATD-LFEATtiERLAThwrnLLEAIVAEP---------- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 450 tPQELTALTQSGIGPRVSHPEQYN---------NVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQ 520
Cdd:PRK12467 481 -RRRLGELPLLDAEERARELVRWNapateyapdCVHQLIEAQARQHPERPALVFGE----QVLSYAELNRQANRLAHVLI 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 521 ENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQL--PQNIQQLHLD 598
Cdd:PRK12467 556 AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLpvPAGLRSLCLD 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 599 QEGVQTQIRKQDASDIPaenrkFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYWPVLEAVNerfpdrplR 678
Cdd:PRK12467 636 EPADLLCGYSGHNPEVA-----LDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV---IAERLQLAADD--------S 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 679 AAHTHSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLIlI 757
Cdd:PRK12467 700 MLMVSTFAFDLGVTELFGALAsGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALV-C 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 758 GGEAAPLAL---WQQLNAQPALFahNLYGPTEYTVDTFRAELKQTARPV----IGNPIGNTQAYVLDRHLQRCPTGVIGE 830
Cdd:PRK12467 779 GGEALQVDLlarVRALGPGARLI--NHYGPTETTVGVSTYELSDEERDFgnvpIGQPLANLGLYILDHYLNPVPVGVVGE 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 831 LYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILT 909
Cdd:PRK12467 857 LYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQP 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 910 NVESAVVIAEPINNSHRLLGYCvVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:PRK12467 937 GVREAVVLAQPGDAGLQLVAYL-VPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKP 1015
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 990 ---QIRAHSRMAETPEQQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAp 1065
Cdd:PRK12467 1016 dasAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFA- 1094
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1066 qlTRLDEQQAAVSKPLFSADLEQKvqekygknstiLPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALI 1144
Cdd:PRK12467 1095 --QAVAAQQQGAQPALPDVDRDQP-----------LPLSYAQERQWFLWQLEPGSAaYHIPQALRLKGPLDIEALERSFD 1161
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1145 TVLKRHPQLGGHFDSElAEEPVFIysLHPtqAWPVQFCSVTPDL-------LEQTIQEALQQPIHLDQ-PygLIRATLIQ 1216
Cdd:PRK12467 1162 ALVARHESLRTTFVQE-DGRTRQV--IHP--VGSLTLEEPLLLAadkdeaqLKVYVEAEARQPFDLEQgP--LLRVGLLR 1234
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1217 HAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAY----QQTNQQLPVLEHSYETVI----KALSGRDHETSKVIWQRDLAD 1288
Cdd:PRK12467 1235 LAADEHVLVLTLHHIVSDGWSMQVLVDELVALYaaysQGQSLQLPALPIQYADYAvwqrQWMDAGERARQLAYWKAQLGG 1314
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1289 LQPLIL--FNQAQQAVQetSYR-------LSAELGAKLQHKLRQQGITLnvFMQMI--WAMTLNIYAHREDIVFGTPVSG 1357
Cdd:PRK12467 1315 EQPVLElpTDRPRPAVQ--SHRgarlafeLPPALAEGLRALARREGVTL--FMLLLasFQTLLHRYSGQDDIRVGVPIAN 1390
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1358 RS-APINGLeqqIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLglsAIQQLI---------AQGNLFDSLL 1427
Cdd:PRK12467 1391 RNrAETEGL---IGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDL---PFEQLVealqperslSHSPLFQVMF 1464
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1428 vvenypdNQYLQQKLGDAAISKLTNRGYS------HYPLALLVIPDHQiELLLEQRGVIDQPEH-FLERM----IQLIEI 1496
Cdd:PRK12467 1465 -------NHQRDDHQAQAQLPGLSVESLSwesqtaQFDLTLDTYESSE-GLQASLTYATDLFEAsTIERLaghwLNLLQG 1536
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1497 ALNEPETSLSHYRL-QLAEEHDLIQKTNQT-QYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQL 1574
Cdd:PRK12467 1537 LVADPERRLGELDLlDEAERRQILEGWNAThTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRL 1616
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1575 QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIvhPSIATFAFN 1654
Cdd:PRK12467 1617 IALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL--PLPDGLRSL 1694
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1655 ELfDETKVDLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVS 1730
Cdd:PRK12467 1695 VL-DQEDDWLEGYSDSnpavNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS 1773
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 VWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEIlssaqRQSLPICRVFCSGEALPT 1810
Cdd:PRK12467 1774 VWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQV-----EHPLSLRRVVCGGEALEV 1848
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1811 ALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQL 1889
Cdd:PRK12467 1849 EALRPWLERLpDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGL 1928
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1890 AMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVH 1967
Cdd:PRK12467 1929 ARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVrEAVVI 2008
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1968 AISSEQNKanvQLVAYLQTTAP--VDID--------QLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHlt 2037
Cdd:PRK12467 2009 AQDGANGK---QLVAYVVPTDPglVDDDeaqvalraILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD-- 2083
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2038 PSNTEKQYA--TSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAA 2115
Cdd:PRK12467 2084 ASELQQAYVapQSELEQRLAAIWQDVLGLEQ-VGLHDNFFELGGDSIISIQVVSRARQAGIRFTP-KDLFQHQTVQSLAA 2161
|
2090 2100
....*....|....*....|....*.
gi 490930577 2116 LLLTQERLAEVEQ---TGMQPILPIR 2138
Cdd:PRK12467 2162 VAQEGDGTVSIDQgpvTGDLPLLPIQ 2187
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
53-2138 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 912.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 53 VDIPTFKKAIQIGLNEADTVIASY--SSDPSQPFIELNNQVQFQIEEFDFchLTPKKAQQRLWDWMPSDRQCAKSLKAGE 130
Cdd:PRK12316 1590 LDPDRFRAAWQATVDRHEILRSGFlwQDGLEQPLQVIHKQVELPFAELDW--RGREDLGQALDALAQAERQKGFDLTRAP 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 131 tqLFRQVLFTT----HDKVYwyqRYHHIMLDGFSMINLTKRIVELYQ-QLQEGKDLSVSPFIGvnevISERQAYENShqf 205
Cdd:PRK12316 1668 --LLRLVLVRTgegrHHLIY---TNHHILMDGWSNAQLLGEVLQRYAgQPVAAPGGRYRDYIA----WLQRQDAAAS--- 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 206 kidQAFWKAYCEDLPSPISLSTHHLAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAEL 285
Cdd:PRK12316 1736 ---EAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETV 1812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 286 VNGipfmrrlGSKAIRST-LPTV--------NVLPVkfkVAEKDSWVSLA---QHVQEQLREIRPHQKYDAEQILRdlns 353
Cdd:PRK12316 1813 AFG-------ATVAGRPAeLPGIeqqiglfiNTLPV---IAAPRPDQSVAdwlQEVQALNLALREHEHTPLYDIQR---- 1878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 354 idihermYGPILNYKAFDQDLVIDGEKVkTHHISTGPIDDFEFSFIVqDHE---------------LIIELRADSQRYTQ 418
Cdd:PRK12316 1879 -------WAGQGGEALFDSLLVFENYPV-AEALKQGAPAGLVFGRVS-NHEqtnypltlavtlgetLSLQYSYDRGHFDA 1949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 419 DELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQYNnVLDIFYEQVKKYPERTAIVSGErp 498
Cdd:PRK12316 1950 AAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPG-VHQRIAEQAARAPEAIAVVFGD-- 2026
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 499 nlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFV 578
Cdd:PRK12316 2027 --QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 579 LTTQALAQQLP--QNIQQLHLDQEGvqtqirkqDASDIPAENRKFDF--QDVAYVIFTSGSTGRPKGVMNTHGSLLNLIl 654
Cdd:PRK12316 2105 LTQRHLLERLPlpAGVARLPLDRDA--------EWADYPDTAPAVQLagENLAYVIYTSGSTGLPKGVAVSHGALVAHC- 2175
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 655 shkptiywpvlEAVNERFPDRPL-RAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRrDAFGLVQEIQQRQIDTLDLP 732
Cdd:PRK12316 2176 -----------QAAGERYELSPAdCELQFMSFSFDGAHEQWFHpLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFP 2243
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 733 PSFCAQmmtnglFVENQHH----PSL--ILIGGEAAPLALW-QQLNAQPALFAHNLYGPTEYTVDTF-----RAELKQTA 800
Cdd:PRK12316 2244 PVYLQQ------LAEHAERdgrpPAVrvYCFGGEAVPAASLrLAWEALRPVYLFNGYGPTEAVVTPLlwkcrPQDPCGAA 2317
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 801 RPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH-GQRMYRTGDLVRWNSAGKL 879
Cdd:PRK12316 2318 YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVV 2397
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 880 EFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIeldektSEQLSQQYLSQLRQNLP 959
Cdd:PRK12316 2398 EYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDA------AEDLLAELRAWLAARLP 2471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 960 EYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAI 1036
Cdd:PRK12316 2472 AYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQeglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLAT 2551
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1037 MLCTQLRQ-RGYSLRPSDVFQFKTVAAMApqlTRLDEQQAAVSKPLFSADLEQKvqekygknstiLPLLPLQKGMLFLSQ 1115
Cdd:PRK12316 2552 QVVSRVRQdLGLEVPLRILFERPTLAAFA---ASLESGQTSRAPVLQKVTRVQP-----------LPLSHAQQRQWFLWQ 2617
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1116 VENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWPVQFCSVTPDLLEQTIQ 1194
Cdd:PRK12316 2618 LEPESaAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVA 2697
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1195 EALQQPIHLdQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ--QLPVLEHSYETVIKALSG 1272
Cdd:PRK12316 2698 EEIQRPFDL-ARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRgeQPTLPPLPLQYADYAAWQ 2776
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1273 RDHETSK------VIWQRDLADLQPLILF-------NQAQQAVQETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMT 1339
Cdd:PRK12316 2777 RAWMDSGegarqlDYWRERLGGEQPVLELpldrprpALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVL 2856
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1340 LNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGL----SAIQQ 1415
Cdd:PRK12316 2857 LHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFeqlvEALQP 2934
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1416 LIAQGN--LFDSLLVVENYPDNQYLQQKLGDAAISKLTNRGYSHYPLALLVIPDHQIELLLEQRGVIDQP--EHFLERMI 1491
Cdd:PRK12316 2935 ERSLSHspLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARtvERLARHWQ 3014
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1492 QLIEIALNEPETSLSHYRLQLAEEHDLI-QKTNQTQ-YYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCA 1569
Cdd:PRK12316 3015 NLLRGMVENPQRSVDELAMLDAEERGQLlEAWNATAaEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANR 3094
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQkdlaaivHPSIA 1649
Cdd:PRK12316 3095 LAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-------HLRLP 3167
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1650 TFAFNE--LFDETKVDLSSYKTTV-ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCT 1726
Cdd:PRK12316 3168 LAQGVQvlDLDRGDENYAEANPAIrTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS 3247
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaateILSSAQRQSLPICRVFCSGE 1806
Cdd:PRK12316 3248 FDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF------LEEEDAHRCTSLKRIVCGGE 3321
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 ALPTALAKSFTEHFSceLHNLYGPTEAAVDVSYMDATlglHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG 1886
Cdd:PRK12316 3322 ALPADLQQQVFAGLP--LYNLYGPTEATITVTHWQCV---EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGG 3396
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVV 1965
Cdd:PRK12316 3397 EGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVrEAV 3476
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1966 VHAISSEqnkanvQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEK 2043
Cdd:PRK12316 3477 VLAVDGR------QLVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDY 3550
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2044 QYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAALLLTQERL 2123
Cdd:PRK12316 3551 VAPVNELERRLAAIWADVLKLEQ-VGLTDNFFELGGDSIISLQVVSRARQAGIRFTP-KDLFQHQTIQGLARVARVGGGV 3628
|
2170
....*....|....*...
gi 490930577 2124 AeVEQ---TGMQPILPIR 2138
Cdd:PRK12316 3629 A-VDQgpvSGETLLLPIQ 3645
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1097-2338 |
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: 785.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1097 NSTILPLLPLQKGMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQA 1176
Cdd:COG1020 15 AAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1177 WPVQFCSVTPDL----LEQTIQEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ- 1251
Cdd:COG1020 95 PVVVLLVDLEALaeaaAEAAAAAEALAPFDLLRG-PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 -TNQQLPVLE------HSYETVIKALSGRDHETSKVIWQRDLADLQPLILFNQAQQAVQETSYR-------LSAELGAKL 1317
Cdd:COG1020 174 yAGAPLPLPPlpiqyaDYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgarvsfrLPAELTAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1318 QHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQ 1397
Cdd:COG1020 254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1398 LHVEHLEHDGLGLSAIQQLI------AQGNLFDSLLVVENYPDNQylqQKLGDAAISKLT-NRGYSHYPLALLVIP-DHQ 1469
Cdd:COG1020 332 TLLAAYAHQDLPFERLVEELqperdlSRNPLFQVMFVLQNAPADE---LELPGLTLEPLElDSGTAKFDLTLTVVEtGDG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1470 IELLLE-QRGVIDQP--EHFLERMIQLIEIALNEPETSLSHYRLQLAEEHD-LIQKTNQTQ-YYVRQSTLQQLLREQARI 1544
Cdd:COG1020 409 LRLTLEyNTDLFDAAtiERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQqLLAEWNATAaPYPADATLHELFEAQAAR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:COG1020 489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKDLAAIVHPSIATFAFNELfdetkvDLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:COG1020 569 LEDAGARLVLTQSALAARLPELGVPVLALDAL------ALAAEPATnppvPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVF 1780
Cdd:COG1020 643 VNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRAL 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 ENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSYMDATLGLHPEEScVAIGYPV 1859
Cdd:COG1020 723 LDAAPEALPSLR-------LVLVGGEALPPELVRRWRARLPgARLVNLYGPTETTVDSTYYEVTPPDADGGS-VPIGRPI 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1860 WNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFT-AGQRMYRTGDIARWHADGSIQYIGRADD 1938
Cdd:COG1020 795 ANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLEFLGRADD 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1939 QLKIRGQRIELGEIEQQLRLISGL-DVVVHAIssEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLV 2015
Cdd:COG1020 875 QVKIRGFRIELGEIEAALLQHPGVrEAVVVAR--EDAPGDKRLVAYVvpEAGAAAAAALLRLALALLLPPYMVPAAVVLL 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2016 EQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTDqnIGVNEDFFAIGGHSILVMKLAIEIRKVF 2095
Cdd:COG1020 953 LPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVV--VGDDDFFFFGGGLGLLLLLALARAARLL 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2096 KRTIPIGQLMSHVTIQRLAALLLTQERLAEVEQTGMQPILPIRsgsghPLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQ 2175
Cdd:COG1020 1031 LLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLP-----PLLLSLLALLLALLLLLALLALLALLLLLLLL 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2176 SPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDylgLLDTYPAEIHQWLDLS 2255
Cdd:COG1020 1106 LLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAE---LLAAAALLLLLALLLL 1182
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2256 VEEMNAEAEQEQLQFFNDILADADSALSEETRRLQEDIFANYRDAVRLLKPYKMPHFDGELHLVVAEKDLLPYIQPEQQW 2335
Cdd:COG1020 1183 ALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLAL 1262
|
...
gi 490930577 2336 SPL 2338
Cdd:COG1020 1263 ALA 1265
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
152-2138 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 773.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPF-IGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHH- 229
Cdd:PRK05691 808 HHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLpLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHp 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 230 LAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPfmrrlgsKAIRSTLPT--- 306
Cdd:PRK05691 888 RSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVP-------NANRPRLETqgl 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 307 ----VNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidihERMYGP---ILNYKAFDQDLV---- 375
Cdd:PRK05691 961 vgffINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQ----AREQGLfqvMFNHQQRDLSALrrlp 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 376 -IDGEKVKTHhistgpidDFEFSFIVQ-----DHELIIELRADsqrYTqDELFNH------GQRLTLLLEQALIRPEQPC 443
Cdd:PRK05691 1037 gLLAEELPWH--------SREAKFDLQlhseeDRNGRLTLSFD---YA-AELFDAatierlAEHFLALLEQVCEDPQRAL 1104
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 444 SNFNITTPQELTALTQSGIGP----RVSHPEQYNnvldifyEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFL 519
Cdd:PRK05691 1105 GDVQLLDAAERAQLAQWGQAPcapaQAWLPELLN-------EQARQTPERIALVWDG----GSLDYAELHAQANRLAHYL 1173
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 520 QENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQ-------NI 592
Cdd:PRK05691 1174 RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQaegvsaiAL 1253
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 593 QQLHLDQEGVQtqirkqdasdipAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIywpvleAVNERf 672
Cdd:PRK05691 1254 DSLHLDSWPSQ------------APGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATY------ALDDS- 1314
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 673 pDRPLRAAhthSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCaQMMTNGLFVENQHH 751
Cdd:PRK05691 1315 -DVLMQKA---PISFDVSVWECFWpLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLL-QLFIDEPLAAACTS 1389
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 752 PSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDT--FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVI 828
Cdd:PRK05691 1390 LRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAINVthWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVA 1469
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 829 GELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PRK05691 1470 GELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA 1549
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 908 LTNVESAVVIAEPINNSHRLLGYCVVkdieldEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PRK05691 1550 QPGVAQAAVLVREGAAGAQLVGYYTG------EAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALP 1623
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 988 KPQIRAHSRMA-ETPEQQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAP 1065
Cdd:PRK05691 1624 EPVWQQREHVEpRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFAE 1703
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1066 QLTRLDEQQAAVSK-PLFSADLEQKVqekygknstilPLLPLQKGMLFLSQVENQS-NYNAFTRLSLNGDIDPVRLQQAL 1143
Cdd:PRK05691 1704 QVARIQAAGERNSQgAIARVDRSQPV-----------PLSYSQQRMWFLWQMEPDSpAYNVGGMARLSGVLDVDRFEAAL 1772
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1144 ITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPVQ---FCSVTPDLLEQTIQEALQQPIHldQPYGL-----IRATLI 1215
Cdd:PRK05691 1773 QALILRHETLRTTFPSV---DGVPVQQVAEDSGLRMDwqdFSALPADARQQRLQQLADSEAH--QPFDLergplLRACLV 1847
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1216 QHAPEQSELLIMVHHLLTDGWSTPLFLQD-------FIKAYQQTNQQLPVLEHSYETVIKA-LSGRDHETSKVIWQRDLA 1287
Cdd:PRK05691 1848 KAAEREHYFVLTLHHIVTEGWAMDIFARElgalyeaFLDDRESPLEPLPVQYLDYSVWQRQwLESGERQRQLDYWKAQLG 1927
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1288 DLQPLILF--NQAQQAVQETS---YR--LSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSA 1360
Cdd:PRK05691 1928 NEHPLLELpaDRPRPPVQSHRgelYRfdLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIR 2007
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1361 PINglEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLG----LSAIQ--QLIAQGNLFDSLLVVENYPD 1434
Cdd:PRK05691 2008 PES--EGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPfdhlVEALQppRSAAYNPLFQVMCNVQRWEF 2085
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1435 NQylQQKLGDAAISKLTNRGYS-HYPLALLVIP-DHQIELLLE-QRGVIDQP------EHFLermiQLIEIALNEPETSL 1505
Cdd:PRK05691 2086 QQ--SRQLAGMTVEYLVNDARAtKFDLNLEVTDlDGRLGCCLTySRDLFDEPriarmaEHWQ----NLLEALLGDPQQRL 2159
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1506 SHY-RLQLAEEHDLIQKTNQTQY-YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGD 1583
Cdd:PRK05691 2160 AELpLLAAAEQQQLLDSLAGEAGeARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQV 2239
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1584 IVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAI--VHPSIATFAfnelFDETK 1661
Cdd:PRK05691 2240 RVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALgeLPAGVARWC----LEDDA 2315
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1662 VDLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWS 1737
Cdd:PRK05691 2316 AALAAYSDAplpfLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVP 2395
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1738 YLVGARLVIAPiDAHRDPLALLSLIQKYQVTTLHFVPSmlavFENAATEILSSaQRQSLPICRVFCSGEALPTALAKSFT 1817
Cdd:PRK05691 2396 LLCGARVVLRA-QGQWGAEEICQLIREQQVSILGFTPS----YGSQLAQWLAG-QGEQLPVRMCITGGEALTGEHLQRIR 2469
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1818 EHFSCEL-HNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHR 1896
Cdd:PRK05691 2470 QAFAPQLfFNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDR 2549
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1897 ADLTASRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQN 1974
Cdd:PRK05691 2550 PGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVrEAVVLALDTPSG 2629
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1975 KanvQLVAYLQT-TAPVDIDQ-------LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYA 2046
Cdd:PRK05691 2630 K---QLAGYLVSaVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAP 2706
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2047 TSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLAAlLLTQERLAEV 2126
Cdd:PRK05691 2707 RSELEQQLAQIWREVLNVER-VGLGDNFFELGGDSILSIQVVSRARQLGIHFSP-RDLFQHQTVQTLAA-VATHSEAAQA 2783
|
2090
....*....|....*
gi 490930577 2127 EQ---TGMQPILPIR 2138
Cdd:PRK05691 2784 EQgplQGASGLTPIQ 2798
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
17-1073 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 727.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 17 ARFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIE 96
Cdd:PRK10252 6 QHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 97 EF-DFCHLTPKKAQQRlwDWMPSDRQCAKSLKAGETqLFRQVLFTTHDK-VYWYQRYHHIMLDGFSMINLTKRIVELYQQ 174
Cdd:PRK10252 86 EIiDLRTQPDPHAAAQ--ALMQADLQQDLRVDSGKP-LVFHQLIQLGDNrWYWYQRYHHLLVDGFSFPAITRRIAAIYCA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 175 LQEGKDLSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHLAAKTTAT-FVKHQLRFSTGILEQI 253
Cdd:PRK10252 163 WLRGEPTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASAdILRLKLEFTDGAFRQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 254 QALAAQTKLAlnDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQL 333
Cdd:PRK10252 243 AAQASGVQRP--DLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 334 REIRPHQKYDAEQILRDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKTHHISTGPIDDFEFS-FIVQDHELIIELRAD 412
Cdd:PRK10252 321 KKMRRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELAlFPDEHGGLSIEILAN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 413 SQRYTQDELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQsgiGPRVSHPEQYNNVLDIFYEQVKKYPERTAI 492
Cdd:PRK10252 401 PQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQ---VNATAVEIPETTLSALVAQQAAKTPDAPAL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 493 VSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCED 572
Cdd:PRK10252 478 ADAR----YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLED 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 573 ANPLFVLTTQALAQQLPqniqqlHLDQEGVQTQIRKQDASDIPAENRKFDfQDVAYVIFTSGSTGRPKGVMNTHGSLLNL 652
Cdd:PRK10252 554 ARPSLLITTADQLPRFA------DVPDLTSLCYNAPLAPQGAAPLQLSQP-HHTAYIIFTSGSTGRPKGVMVGQTAIVNR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 653 ILshkptiyWpvleaVNERFPDRPL-RAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEIQQRQIDTLD 730
Cdd:PRK10252 627 LL-------W-----MQNHYPLTADdVVLQKTPCSFDVSVWEFFWpFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTH 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 731 LPPSFCAQMMtNGLFVENQHHPSLIL----IGGEAAPLAL---WQQLNAQPAlfaHNLYGPTEYTVD-----TFRAELKQ 798
Cdd:PRK10252 695 FVPSMLAAFV-ASLTPEGARQSCASLrqvfCSGEALPADLcreWQQLTGAPL---HNLYGPTEAAVDvswypAFGEELAA 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 799 -TARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSA 876
Cdd:PRK10252 771 vRGSSVpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDD 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 877 GKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-------SHRLLGYCVVKDIE-LDektSEQLsq 948
Cdd:PRK10252 851 GAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQaaatggdARQLVGYLVSQSGLpLD---TSAL-- 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 949 qyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQI--RAHSRMAETPEQQLLCQITASVLKLDAIGIDDDFF 1026
Cdd:PRK10252 926 --QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELkaQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFF 1003
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*...
gi 490930577 1027 MTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMApqlTRLDEQ 1073
Cdd:PRK10252 1004 ALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLA---TLLDAE 1048
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1039-2245 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 722.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1039 CTQLRQRGYSlrPSDvfqFKTVAAMAPQLTRLdeqqaavskPLFSADLEQkvqekygknstILPLLPLQKGMLFLSQVEN 1118
Cdd:PRK12467 2610 CCSNDQRGVT--PSD---FPLAGLSQEQLDRL---------PVAVGDIED-----------IYPLSPMQQGMLFHTLYEG 2664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1119 QS-NYNAFTRLSLNGdIDPVRLQQALITVLKRHPQLGGHF--DSELaEEPVFIysLHPTQAWPVQFC-----SVTPDLLE 1190
Cdd:PRK12467 2665 GAgDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlwDGEL-EEPLQV--VYKQARLPFSRLdwrdrADLEQALD 2740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1191 QTIQEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqTNQQLPVLEHSYETVIKAL 1270
Cdd:PRK12467 2741 ALAAADRQQGFDLLSA-PLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY--FGQPPPAREGRYRDYIAWL 2817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1271 SGRDHETSKVIWQRDLADLQPLILFNQAQQ-------AVQETSYR-LSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNI 1342
Cdd:PRK12467 2818 QAQDAEASEAFWKEQLAALEEPTRLARALYpapaeavAGHGAHYLhLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQR 2897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1343 YAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQQLIAQGN- 1421
Cdd:PRK12467 2898 FTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGe 2977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1422 -LFDSLLVVENYPDNQYLQQKL-GDAAISKLTNRGYSHYPLALLVIPDHQIEL-LLEQRGVIDQP--EHFLERMIQLIEI 1496
Cdd:PRK12467 2978 aLFDSILVFENYPISEALKQGApSGLRFGAVSSREQTNYPLTLAVGLGDTLELeFSYDRQHFDAAaiERLAESFDRLLQA 3057
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1497 ALNEPETSLSHYRLQLAEEHDLI--QKTNQTQYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQL 1574
Cdd:PRK12467 3058 MLNNPAARLGELPTLAAHERRQVlhAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL 3137
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1575 QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPsiatfAFN 1654
Cdd:PRK12467 3138 IAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAP-----AGD 3212
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1655 ELFDETKVDLSSYK----TTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVS 1730
Cdd:PRK12467 3213 TALTLDRLDLNGYSennpSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGA 3292
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 VWEFFWSYLVGARLVIAPIDaHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaateiLSSAQRQSL-PICRVFCSGEALP 1809
Cdd:PRK12467 3293 QERFLWTLICGGCLVVRDND-LWDPEELWQAIHAHRISIACFPPAYLQQF-------AEDAGGADCaSLDIYVFGGEAVP 3364
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 -TALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQ 1888
Cdd:PRK12467 3365 pAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVG 3444
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1889 LAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVV 1966
Cdd:PRK12467 3445 LARGYHQRPSLTAERFVADPFsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVrEAVV 3524
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1967 HAISSEQNKanvQLVAYLQTTAPVD--IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNtEKQ 2044
Cdd:PRK12467 3525 LARDGAGGK---QLVAYVVPADPQGdwRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR-EYV 3600
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2045 YATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLltqerla 2124
Cdd:PRK12467 3601 APRSEVEQQLAAIWADVLGVEQ-VGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS------- 3672
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2125 EVEQTGMQPILPI--RSGSGHPLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQSPR--PDGllANSTDMDELVEKQLEIM 2200
Cdd:PRK12467 3673 PLGDVPVNLLLDLnrLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLTCRHllDDG--WQDTSLQAMAVQYADYI 3750
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*
gi 490930577 2201 RKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLLDTYP 2245
Cdd:PRK12467 3751 LWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTL 3795
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
133-1340 |
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: 621.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 133 LFRQVLFTTHDKVYW-YQRYHHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSP-FIGVNEVISERQAYENSHQFKIDQA 210
Cdd:COG1020 130 LLRLLLLLLLLLLLLlLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPlPIQYADYALWQREWLQGEELARQLA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 211 FWKAYCEDLPSPISLSTHHL-AAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGI 289
Cdd:COG1020 210 YWRQQLAGLPPLLELPTDRPrPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGT 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 290 PFMRRLGSkAIRSTL-PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSIDIHERM--YGPILN 366
Cdd:COG1020 290 PVAGRPRP-ELEGLVgFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNplFQVMFV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 367 YKAFDQD-LVIDGEKVKTHHISTG-PIDDFEFSFIVQDHELIIELRADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCS 444
Cdd:COG1020 369 LQNAPADeLELPGLTLEPLELDSGtAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLG 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 445 NFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGA 524
Cdd:COG1020 449 DLPLLTAAERQQLLAEWNATAAPYPAD-ATLHELFEAQAARTPDAVAVVFGD----QSLTYAELNARANRLAHHLRALGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 525 RKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQ-NIQQLHLDQEgvq 603
Cdd:COG1020 524 GPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALDAL--- 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 604 tQIRKQDASDIPAENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiywpvleavNERFPDRP-LRAAHT 682
Cdd:COG1020 601 -ALAAEPATNPPVPVTP---DDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM------------QRRYGLGPgDRVLQF 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 683 HSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvENQHHPSLILIGGEA 761
Cdd:COG1020 665 ASLSFDASVWEIFGALLsGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAP--EALPSLRLVLVGGEA 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 762 APLALWQQLNAQ-PALFAHNLYGPTEYTVDT----FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF 836
Cdd:COG1020 743 LPPELVRRWRARlPGARLVNLYGPTETTVDStyyeVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGA 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 837 GIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAV 915
Cdd:COG1020 823 GLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAV 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 916 VIAEPINNSHRLLGYCVVkdielDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHS 995
Cdd:COG1020 903 VVAREDAPGDKRLVAYVV-----PEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 996 RMAETPEQQLLCQITASVLKL---DAIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPQLTRLDE 1072
Cdd:COG1020 978 AAAAPPAEEEEEEAALALLLLlvvVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAA 1057
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1073 QQAAVSKPLFSADLEQKVQEKYGKNSTILPLLPLQKGMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQ 1152
Cdd:COG1020 1058 AAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPR 1137
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1153 LGGHFDSELAEEPVFIYSLHPTQAWPVQfcsvtpdLLEQTIQEALQQPIHLDQPYGLIRATLIQHAPEQSELLIMVHHLL 1232
Cdd:COG1020 1138 LRLLVALAAALALAALLALLLAAAAAAA-------ELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLL 1210
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1233 TDGWSTPLFLQDFIKAYQQTNQQLPVLEHSYETVI----------KALSGRDHETSKVIWQRDLADLQPLILFNQAQQAV 1302
Cdd:COG1020 1211 LLLLLLLLLLLLLLAAAAAALLALALLLALLALAAllalaalaalAAALLALALALLALALLLLALALLLPALARARAAR 1290
|
1210 1220 1230
....*....|....*....|....*....|....*...
gi 490930577 1303 QETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMTL 1340
Cdd:COG1020 1291 TARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1537-2031 |
0e+00 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 620.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLssyKTTVITPQHPAYLIYTSGTTGQPKGVMVS 1696
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATP---PLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1697 HQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSM 1776
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1777 LAVFENAATeilsSAQRQSLPicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATlGLHPEEScVAIG 1856
Cdd:cd17646 240 LRVFLAEPA----AGSCASLR--RVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVR-GPAETPS-VPIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1857 YPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRA 1936
Cdd:cd17646 312 RPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1937 DDQLKIRGQRIELGEIEQQLR---LISGLDVVVHaissEQNKANVQLVAYLQ---TTAPVDIDQLKKQLAKHLPAYMVPT 2010
Cdd:cd17646 392 DDQVKIRGFRVEPGEIEAALAahpAVTHAVVVAR----AAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPA 467
|
490 500
....*....|....*....|.
gi 490930577 2011 HYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd17646 468 AFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1546-2031 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 594.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttvitPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd05930 81 EDSGAKLVLTD-------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAAT 1785
Cdd:cd05930 124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EILSSAQRqslpicRVFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSYMDATLGlHPEESCVAIGYPVWNTQL 1864
Cdd:cd05930 204 LAALPSLR------LVLVGGEALPPDLVRRWRELLPgARLVNLYGPTEATVDATYYRVPPD-DEEDGRVPIGRPIPNTRV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:cd05930 277 YVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQLRLISGL-DVVVHAIssEQNKANVQLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLS 2021
Cdd:cd05930 357 YRIELGEIEAALLAHPGVrEAAVVAR--EDGDGEKRLVAYvvPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
490
....*....|
gi 490930577 2022 HNGKLDRKAL 2031
Cdd:cd05930 435 PNGKVDRKAL 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1039-2120 |
8.75e-178 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 611.19 E-value: 8.75e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1039 CTQLRQRGysLRPSDVfqfktvaamapQLTRLDEQQAAvSKPLFSADLEQkvqekygknstILPLLPLQKGMLFLSQVEN 1118
Cdd:PRK12316 4066 CCDAERHG--VTPSDF-----------PLAGLDQARLD-ALPLPLGEIED-----------IYPLSPMQQGMLFHSLYEQ 4120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1119 QS-NYNAFTRLSLNGdIDPVRLQQALITVLKRHPQLGGHFDSELA-EEPVFIYSLHPTQAWPVQFCSVTPDL---LEQTI 1193
Cdd:PRK12316 4121 EAgDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGElGRPLQVVHKQVSLPFAELDWRGRADLqaaLDALA 4199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1194 QEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqTNQQLPVLEHSYETVIKALSGR 1273
Cdd:PRK12316 4200 AAERERGFDLQRA-PLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY--SGRPPAQPGGRYRDYIAWLQRQ 4276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1274 DHETSKVIWQRDLADLQ-PLILFNQAQQA-------VQETSYRLSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAH 1345
Cdd:PRK12316 4277 DAAASEAFWREQLAALDePTRLAQAIARAdlrsangYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTG 4356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1346 REDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQQLIAQGN--LF 1423
Cdd:PRK12316 4357 QDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGeaLF 4436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1424 DSLLVVENYPDNQYLQQKL-GDAAISKLTNRGYSHYPLALLVIPDHQIELLLE-QRGVIDQP--EHFLERMIQLIEIALN 1499
Cdd:PRK12316 4437 DSLLVFENYPVSEALQQGApGGLRFGEVTNHEQTNYPLTLAVGLGETLSLQFSyDRGHFDAAtiERLARHLTNLLEAMAE 4516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1500 EPETSLSHYR-LQLAEEHDLIQKTNQTQY-YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRA 1577
Cdd:PRK12316 4517 DPQRRLGELQlLEKAEQQRIVALWNRTDAgYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIAR 4596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1578 GVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPS-IATFAFNEl 1656
Cdd:PRK12316 4597 GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDgLASLALDR- 4675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1657 fDETKVDLSSYKTTV-ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFF 1735
Cdd:PRK12316 4676 -DEDWEGFPAHDPAVrLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLY 4754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1736 WSYLVGARLVIAPIDAHrDPLALLSLIQKYQVTTLHFVPSMLAVFENAAteilsSAQRQSLPICRVFCSGEAL-PTALAK 1814
Cdd:PRK12316 4755 HPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAEHA-----ERDGEPPSLRVYCFGGEAVaQASYDL 4828
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1815 SFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYL 1894
Cdd:PRK12316 4829 AWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYL 4908
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1895 HRADLTASRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRlisGLDVVVHAISSEQ 1973
Cdd:PRK12316 4909 ERPALTAERFVPDPFGApGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLR---EHPAVREAVVIAQ 4985
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1974 NKA-NVQLVAYL--QTTAPVDI--------DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPhlTPSNTE 2042
Cdd:PRK12316 4986 EGAvGKQLVGYVvpQDPALADAdeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP--DASLLQ 5063
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2043 KQYAT--SAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQ 2120
Cdd:PRK12316 5064 QAYVAprSELEQQVAAIWAEVLQLER-VGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAA 5142
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1039-2135 |
1.37e-176 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 607.34 E-value: 1.37e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1039 CTQLRQRGYSlrPSDVfqfktvaamapQLTRLDEQQAAvSKPLFSADLEQkvqekygknstILPLLPLQKGMLFLSQVEN 1118
Cdd:PRK12316 1520 CCDERNRGVT--PSDF-----------PLAGLSQAQLD-ALPLPAGEIAD-----------IYPLSPMQQGMLFHSLYEQ 1574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1119 QS-NYNAFTRLSLNGdIDPVRLQQALITVLKRHPQL--GGHFDSELaEEPVFIysLHPTQAWPvqfCSVTPDLLEQTIQE 1195
Cdd:PRK12316 1575 EAgDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILrsGFLWQDGL-EQPLQV--IHKQVELP---FAELDWRGREDLGQ 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1196 ALQQPIHLDQPYG-------LIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqTNQQLPVLEHSYETVIK 1268
Cdd:PRK12316 1648 ALDALAQAERQKGfdltrapLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY--AGQPVAAPGGRYRDYIA 1725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1269 ALSGRDHETSKVIWQRDLADLQ-PLILFNQAQQAVQETSY-----RLSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNI 1342
Cdd:PRK12316 1726 WLQRQDAAASEAFWKEQLAALEePTRLAQAARTEDGQVGYgdhqqLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQR 1805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1343 YAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQQLIAQGN- 1421
Cdd:PRK12316 1806 YTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGe 1885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1422 -LFDSLLVVENYPDNQYLQQKL-GDAAISKLTNRGYSHYPLALLVIPDHQIELLLE-QRGVID--QPEHFLERMIQLIEI 1496
Cdd:PRK12316 1886 aLFDSLLVFENYPVAEALKQGApAGLVFGRVSNHEQTNYPLTLAVTLGETLSLQYSyDRGHFDaaAIERLDRHLLHLLEQ 1965
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1497 ALNEPETSLSHYRLQLAEEHDLIQK--TNQTQYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQL 1574
Cdd:PRK12316 1966 MAEDAQAALGELALLDAGERQRILAdwDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRL 2045
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1575 QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHP-SIATFAF 1653
Cdd:PRK12316 2046 RARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPaGVARLPL 2125
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1654 nelfdETKVDLSSYKTTV----ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDV 1729
Cdd:PRK12316 2126 -----DRDAEWADYPDTApavqLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDG 2200
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1730 SVWEFFWSYLVGARLVIAPiDAHRDPLALLSLIQKYQVTTLHFVPSMLAVF-ENAATEilssaqRQSLPICRVFCSGEAL 1808
Cdd:PRK12316 2201 AHEQWFHPLLNGARVLIRD-DELWDPEQLYDEMERHGVTILDFPPVYLQQLaEHAERD------GRPPAVRVYCFGGEAV 2273
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1809 PTALAKSFTEHFSCE-LHNLYGPTEAAVDVSYMDAtlglHPEESC----VAIGYPVWNTQLYILDQYLRPVPVGVDGELY 1883
Cdd:PRK12316 2274 PAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKC----RPQDPCgaayVPIGRALGNRRAYILDADLNLLAPGMAGELY 2349
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1884 LAGHQLAMGYLHRADLTASRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL 1962
Cdd:PRK12316 2350 LGGEGLARGYLNRPGLTAERFVPDPFSAsGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAV 2429
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1963 -DVVVHAISSEQNKanvQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPS 2039
Cdd:PRK12316 2430 rEAVVVAQDGASGK---QLVAYVvpDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2040 NTEKQYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLT 2119
Cdd:PRK12316 2507 RQAYVAPQEGLEQRLAAIWQAVLKVEQ-VGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLES 2585
|
1130
....*....|....*....
gi 490930577 2120 QER---LAEVEQTGMQPIL 2135
Cdd:PRK12316 2586 GQTsraPVLQKVTRVQPLP 2604
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
487-2145 |
2.42e-175 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 603.31 E-value: 2.42e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAI--VSGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAgAIPRSIDSVVVMLSVLNSGASFLPLdldYP-- 562
Cdd:PRK05691 23 PDRLALrfLADDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVL-LFPSGPDYVAAFFGCLYAGVIAVPA---YPpe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 563 ------IDRMQMMCEDANPLFVLTTQALAQQLpQNIQQLHLDQEGVQTQIRKQDASdiPAEN-RKFDFQ--DVAYVIFTS 633
Cdd:PRK05691 99 sarrhhQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLCVDTLDPA--LAEAwQEPALQpdDIAFLQYTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 634 GSTGRPKGVMNTHGSLL-----------------NLILSHKP---------TIYWPVLEAV------NERFPDRPLRaah 681
Cdd:PRK05691 176 GSTALPKGVQVSHGNLVaneqlirhgfgidlnpdDVIVSWLPlyhdmgligGLLQPIFSGVpcvlmsPAYFLERPLR--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 682 thsfsfdssWLQVFWMLWG-------------------QELHIFDENMRRDAFGLVQEIQQrqiDTLDLppsFCAQMMTN 742
Cdd:PRK05691 253 ---------WLEAISEYGGtisggpdfayrlcservseSALERLDLSRWRVAYSGSEPIRQ---DSLER---FAEKFAAC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 743 GlFVENQHHPS-------LILIGGE--AAPLALwqQLNAQPalFAHNLYGPTEYTVdtfraeLKQTARPVIGNPIgntqA 813
Cdd:PRK05691 318 G-FDPDSFFASyglaeatLFVSGGRrgQGIPAL--ELDAEA--LARNRAEPGTGSV------LMSCGRSQPGHAV----L 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 814 YVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVanpfEH-GQRMYRTGDLvRWNSAGKLEFMGRCDDQIKIR 892
Cdd:PRK05691 383 IVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFV----EHdGRTWLRTGDL-GFLRDGELFVTGRLKDMLIVR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 893 GYRVEIGEVENAlsiltnVESAVviaePINNSHRLLGYCVVKD--------IELDEKTSEQLSQQYL-SQLRQNLPE--Y 961
Cdd:PRK05691 458 GHNLYPQDIEKT------VEREV----EVVRKGRVAAFAVNHQgeegigiaAEISRSVQKILPPQALiKSIRQAVAEacQ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 962 MVPSALTVMS--EFPRNVSGKVDKKA---------------LPKPQiRAHSRMAETPEQQLLCQITA---SVLKLDAIGI 1021
Cdd:PRK05691 528 EAPSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQ-AVEAAQTAASGDELQARIAAiwcEQLKVEQVAA 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1022 DDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAPQLTRLDEQQAAVSKPLFSADLEQKvqekygknsti 1100
Cdd:PRK05691 607 DDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAIARLPRGQA----------- 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPV 1179
Cdd:PRK05691 676 LPQSLAQNRLWLLWQLDPQSAaYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYER---DGVALQRIDAQGEFAL 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTpDLLE-------QTIQEA-LQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ 1250
Cdd:PRK05691 753 QRIDLS-DLPEaerearaAQIREEeARQPFDLEKgP--LLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYA 829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 QTNQ----QLPVLEHSY----ETVIKALSGRDHETSKVIWQRDLADLQPLILFN-------QAQQAVQETSYRLSAELGA 1315
Cdd:PRK05691 830 AACQgqtaELAPLPLGYadygAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELAtdhprsaRQAHSAARYSLRVDASLSE 909
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1316 KLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRsaPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQL 1395
Cdd:PRK05691 910 ALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR--PRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQV 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1396 QQLHVEHLEHDGLGLSAIQQLIAQGNLFDSLLVVENYP--DNQYLQQKLGDAAISKLTNRGYSHYPLALLVIPDHQIEL- 1472
Cdd:PRK05691 988 RQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFNHQqrDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRNGRLt 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1473 --------LLEQRGVIDQPEHFLermiQLIEIALNEPETSLSHYRLQLAEEHDLIQKTNQTQYYVRQSTLQQLLREQARI 1544
Cdd:PRK05691 1068 lsfdyaaeLFDAATIERLAEHFL----ALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQ 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:PRK05691 1144 TPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYM 1223
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKDLAAIVHPS-IATFAFNELfdetkvDLSSYKTTV----ITPQHPAYLIYTSGTTGQPKGVMVSHQA 1699
Cdd:PRK05691 1224 LADSGVELLLTQSHLLERLPQAEgVSAIALDSL------HLDSWPSQApglhLHGDNLAYVIYTSGSTGQPKGVGNTHAA 1297
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1700 IVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAV 1779
Cdd:PRK05691 1298 LAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQL 1377
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1780 F--ENAATEILSsaqrqslpICRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGlhpEESCVAIG 1856
Cdd:PRK05691 1378 FidEPLAAACTS--------LRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHWQCQAE---DGERSPIG 1446
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1857 YPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGR 1935
Cdd:PRK05691 1447 RPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGR 1526
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1936 ADDQLKIRGQRIELGEIEQQLRLISGLD---VVVHaisseQNKANVQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPT 2010
Cdd:PRK05691 1527 LDQQVKLRGFRVEPEEIQARLLAQPGVAqaaVLVR-----EGAAGAQLVGYYTGEAGQEAeaERLKAALAAELPEYMVPA 1601
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2011 HYMLVEQFPLSHNGKLDRKALPQP------HLTPSntekqyatSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILV 2084
Cdd:PRK05691 1602 QLIRLDQMPLGPSGKLDRRALPEPvwqqreHVEPR--------TELQQQIAAIWREVLGLPR-VGLRDDFFALGGHSLLA 1672
|
1770 1780 1790 1800 1810 1820
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 2085 MKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQErlAEVEQTGMQPILPIRSGSGHPL 2145
Cdd:PRK05691 1673 TQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQ--AAGERNSQGAIARVDRSQPVPL 1731
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1101-2134 |
7.25e-171 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 589.44 E-value: 7.25e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPV 1179
Cdd:PRK12467 50 IPLSYAQERQWFLWQLDPDSaAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQD---EEGFRQVIDASLSLTI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPD-------LLEQTIQEALQQPIHLdQPYGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQT 1252
Cdd:PRK12467 127 PLDDLANEqgraresQIEAYINEEVARPFDL-ANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1253 NQ----QLPVLEHSYETVikALSGR------DHETSKVIWQRDLADLQPLILF-----NQAQQAVQETSYRLS--AELGA 1315
Cdd:PRK12467 206 SQgrepSLPALPIQYADY--AIWQRswleagERERQLAYWQEQLGGEHTVLELptdrpRPAVPSYRGARLRVDlpQALSA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1316 KLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSApiNGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQL 1395
Cdd:PRK12467 284 GLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELLQQV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1396 QQLHVEHLEHDGLGLSA-IQQLIAQGNLFDSLL--VVENY-PDNQYLQQKLGdAAISKLT------NRGYSHYPLALLVI 1465
Cdd:PRK12467 362 KRTALGAQAHQDLPFEQlVEALQPERSLSHSPLfqVMFNHqNTATGGRDREG-AQLPGLTveelswARHTAQFDLALDTY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1466 PDHQ---IEL-----LLEQRGVIDQPEHFLErmiqLIEIALNEPETSLSHYRLQLAEEH-DLIQKTNQTQYYVRQSTLQQ 1536
Cdd:PRK12467 441 ESAQglwAAFtyatdLFEATTIERLATHWRN----LLEAIVAEPRRRLGELPLLDAEERaRELVRWNAPATEYAPDCVHQ 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PRK12467 517 LIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHP-SIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMV 1695
Cdd:PRK12467 597 PQDRLAYMLDDSGVRLLLTQSHLLAQLPVPaGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAI 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:PRK12467 677 SHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPS 756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLAVFenaateILSSAQRQSLPICRVFCSGEALPTAL-AKSFTEHFSCELHNLYGPTEAAVDVSYMDATlGLHPEESCVA 1854
Cdd:PRK12467 757 HLQAL------LQASRVALPRPQRALVCGGEALQVDLlARVRALGPGARLINHYGPTETTVGVSTYELS-DEERDFGNVP 829
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYI 1933
Cdd:PRK12467 830 IGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYL 909
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1934 GRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEqnkANVQLVAYLQTTAPVD-------IDQLKKQLAKHLPA 2005
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEARLLAQPGVrEAVVLAQPGD---AGLQLVAYLVPAAVADgaehqatRDELKAQLRQVLPD 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVM 2085
Cdd:PRK12467 987 YMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVER-VGLTDNFFELGGHSLLAT 1065
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 490930577 2086 KLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQerlAEVEQTGMQPI 2134
Cdd:PRK12467 1066 QVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ---QQGAQPALPDV 1111
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1101-2139 |
7.48e-170 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 586.54 E-value: 7.48e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWPV 1179
Cdd:PRK12316 50 DRLSYAQQRMWFLWQLEPQSGaYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPDLLEQTIQEALQ----QPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ--QT 1252
Cdd:PRK12316 130 DCSGLPEAEQEARLRDEAQreslQPFDLCEgP--LLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSayAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1253 NQ--QLPVLEHSYETVikALSGR------DHETSKVIWQRDLADLQPLILF-----NQAQQAVQETSYRLSAE--LGAKL 1317
Cdd:PRK12316 208 GAepGLPALPIQYADY--ALWQRswleagEQERQLEYWRAQLGEEHPVLELptdhpRPAVPSYRGSRYEFSIDpaLAEAL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1318 QHKLRQQGITLnvFMQMI--WAMTLNIYAHREDIVFGTPVSGRS-APINGLeqqIGLFLNTIPVRVKLNMQQTLWEQLPQ 1394
Cdd:PRK12316 286 RGTARRQGLTL--FMLLLgaFNVLLHRYSGQTDIRVGVPIANRNrAEVEGL---IGFFVNTQVLRSVFDGRTRVATLLAG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1395 LQQlHVehlehdgLGLSAIQQLIAQgNLFDSLLVVENYPDNQYLQQKLGD----AAISKLTnrGYSHYPLALLVIPDH-- 1468
Cdd:PRK12316 361 VKD-TV-------LGAQAHQDLPFE-RLVEALKVERSLSHSPLFQVMYNHqplvADIEALD--TVAGLEFGQLEWKSRtt 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1469 QIELLL---EQRGVIDQPEHF---------LERM----IQLIEIALNEPETSLSHYRLQLAEEH-DLIQKTNQT-QYYVR 1530
Cdd:PRK12316 430 QFDLTLdtyEKGGRLHAALTYatdlfeartVERMarhwQNLLRGMVENPQARVDELPMLDAEERgQLVEGWNATaAEYPL 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1531 QSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYL 1610
Cdd:PRK12316 510 QRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1611 PIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIvhpSIATFAFNELFDETKVDLSSYKT----TVITPQHPAYLIYTSGT 1686
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL---PLAAGVQVLDLDRPAAWLEGYSEenpgTELNPENLAYVIYTSGS 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1687 TGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQ 1766
Cdd:PRK12316 667 TGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREG 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1767 VTTLHFVPSMLAVFENAAteilssAQRQSLPICRVFCSGEALPTALAKS-FTEHFSCELHNLYGPTEAAVDVSYMDATlg 1845
Cdd:PRK12316 747 VDTLHFVPSMLQAFLQDE------DVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-- 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1846 lhpEE--SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIAR 1923
Cdd:PRK12316 819 ---EEggDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLAR 895
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1924 WHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEqnkanvQLVAY--LQTTAPVDIDQLKKQLA 2000
Cdd:PRK12316 896 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVrEAAVLAVDGK------QLVGYvvLESEGGDWREALKAHLA 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2001 KHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTdQNIGVNEDFFAIGGH 2080
Cdd:PRK12316 970 ASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGV-ERVGLDDNFFELGGD 1048
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 2081 SILVMKLAIEIRKVFKRTIPiGQLMSHVTIQRLaALLLTQERLAEVEQ---TGMQPILPIRS 2139
Cdd:PRK12316 1049 SIVSIQVVSRARQAGIQLSP-RDLFQHQTIRSL-ALVAKAGQATAADQgpaSGEVALAPVQR 1108
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
487-986 |
2.13e-158 |
|
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: 497.05 E-value: 2.13e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd05930 1 PDAVAVVDGD----QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTTQalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd05930 77 AYILEDSGAKLVLTDP-----------------------------------------DDLAYVIYTSGSTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLILSHkptiywpvleavNERFPDRP-LRAAHTHSFSFDSSWLQVFWML-WGQELHIFDENMRRDAFGLVQEIQQR 724
Cdd:cd05930 116 RGLVNLLLWM------------QEAYPLTPgDRVLQFTSFSFDVSVWEIFGALlAGATLVVLPEEVRKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 725 QIDTLDLPPSFCAQMMTNGlfvENQHHPSL--ILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVD-TF---RAELK 797
Cdd:cd05930 184 GITVLHLTPSLLRLLLQEL---ELAALPSLrlVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDaTYyrvPPDDE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 798 QTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAG 877
Cdd:cd05930 261 EDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 878 KLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKDieldekTSEQLSQQYLSQLRQ 956
Cdd:cd05930 341 NLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEkRLVAYVVPDE------GGELDEEELRAHLAE 414
|
490 500 510
....*....|....*....|....*....|
gi 490930577 957 NLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05930 415 RLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1546-2031 |
6.99e-156 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 491.42 E-value: 6.99e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEQKDLAAIVHPSIATFAFNElfdETKVDLSSYKTTViTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALA---AAAAAPAAPRTPV-SPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPsmlavfenAAT 1785
Cdd:cd12116 157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATP--------ATW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EILSSAQRQSLPICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAVDVSYMDATLGLHPeescVAIGYPVWNTQLY 1865
Cdd:cd12116 229 RMLLDAGWQGRAGLTALCGGEALPPDLAARLLSR-VGSLWNLYGPTETTIWSTAARVTAAAGP----IPIGRPLANTQVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1866 ILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:cd12116 304 VLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQLRLISGLD---VVVHaisseQNKANVQLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFP 2019
Cdd:cd12116 384 HRIELGEIEAALAAHPGVAqaaVVVR-----EDGGDRRLVAYvvLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALP 458
|
490
....*....|..
gi 490930577 2020 LSHNGKLDRKAL 2031
Cdd:cd12116 459 LTANGKLDRKAL 470
|
|
| NRPS_MxcG |
NF038078 |
myxochelin non-ribosomal peptide synthetase MxcG; |
15-1079 |
4.50e-155 |
|
myxochelin non-ribosomal peptide synthetase MxcG;
Pssm-ID: 468336 [Multi-domain] Cd Length: 1444 Bit Score: 521.59 E-value: 4.50e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 15 QPARFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQ 94
Cdd:NF038078 1 QEARWPLSAAQHGIWLGQQLDLASPVYNAGECIEIRGPVDPAVFEAALRQAVGEAEALHMRFVPGEEGPRQLLDPSADWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 95 IEEFDFCHLT-PKKAQQrlwDWMPSDrqCAKSLKAGETQLFRQVLFTTH-DKVYWYQRYHHIMLDGFSMINLTKRIVELY 172
Cdd:NF038078 81 LHRVDVSGTPdPWAAAQ---AWMRED--LARTVDLSRGPLFAEALFKAApDRFFWYQRAHHIALDGFGFSLLARRVAELY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 173 QQLQEGKDlSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSThhlAAKTTATFVKHQLRFSTGILEQ 252
Cdd:NF038078 156 TARVTGRP-ATGGFGSLRAVLDEDAAYRAGPQCELDRAFWMERFADRPTPVSLAE---PAPMSRSFVRQTRHLSPSEMER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 253 IQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQ 332
Cdd:NF038078 232 LQAVARQAGLSWPDLVLAATAAWLHRRTGAPEVVLGLPVMGRLGSAALRVPCMAMNIVPLRVPVRPGAGLLALARGVAAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 333 LREIRPHQKYDAEQILRDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKTHHISTGPIDDFEFSFIVQD--HELIIELR 410
Cdd:NF038078 312 LRAIRPHLRYRYEQLRRDLKLVGGQRRLFGPVVNIMPFDYALRFAGMPAIAHNISAGPVEDLSIGVYARSdgRGPRVDFD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 411 ADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCSNFNITTP-------QELTALTQSGIGPRVSHPeqynnVLDIFYEQV 483
Cdd:NF038078 392 ANPACYSADELDAHQREFLQLLEALLAAPEQAVARALIPGAaapapaaSRPGSLLDGGPLPAPARP-----VLELIAERA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 484 KKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:NF038078 467 REQPDAIAVEHGPR----RMTYRELLLAARALAARLVAAGARPDTLVAVMLPRSIDAIVASLGVLFSGAGYLPLDPFGPS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 564 DRMQMMCEDANPLFVLTTQALA---QQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRkfdfqdVAYVIFTSGSTGRPK 640
Cdd:NF038078 543 SRTAAILADAAPALIVTSSEHAptaKAGPQAPGALVVRRLEEAVPSPAPEAPPRPADER------LAYVIYTSGSTGQPN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 641 GVMNTHGSLLNLILShkPTIYWPVleavneRFPDRPLRAAHTHsfsFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQ 719
Cdd:NF038078 617 GVQISRGALAHFVAG--ATQRYGV------RRDDRVLQFAPLH---FDASVEEIFLTLCaGARLVLRTDEMLQSVPRLLD 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 720 EIQQRQIDTLDLPPSF---CAQMMTNGLFVenqhHPS---LILIGGEAA-P--LALWQQlNAQPALFAHNLYGPTEYTVD 790
Cdd:NF038078 686 ACAEHGITVLDLPTAFwheLAYSVSTGAAR----LPSslrTVIIGGEAAlPerVARWRA-AVGPRVRLLNTYGPTEATVV 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 791 TFRAELKQTARPV-------IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVA-NPFEHGQ 862
Cdd:NF038078 761 ATVATLSGGGAAGdegdevpIGRPLPGVRAALLDAQGRLVAPGAEGELYLLGGGLARGYLGRPELDAARFTTlEALPGRP 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 863 RMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLLGYCVVKDIeldEK 941
Cdd:NF038078 841 RAYRTGDLVRLREDGQLVFVGRVDDEFKISGHRIDPAEVETVLLGHPGVrEAAVVGQVLPGGTRRLCAHVVADAP---AP 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 942 TSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQI---RAHSRMAETPEQQLLCQITASVLKLDA 1018
Cdd:NF038078 918 SAAELRR----HLLSALPAPMVPGAFVFAERLPRTSTGKIDRAALRRAGPaeeSATSAAAATALERVVLRVWEQVLGVSG 993
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1019 IGIDDDFFMTGGDSISAIMLCTQLR-QRGYSLRPSDVFQFKTVAAMAPQLtrldEQQAAVSK 1079
Cdd:NF038078 994 LSAQDDFFELGGQSLQSIQVANRLGvALGREVPVATVFRHPTAAGLAQAL----EHGASVAA 1051
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1538-2032 |
1.86e-146 |
|
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: 465.28 E-value: 1.86e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHP 1617
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 TERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLSsyKTTVITPQHPAYLIYTSGTTGQPKGVMVSH 1697
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAE--PDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 QAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLhFVPsml 1777
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRV-FLP--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1778 AVFENAATEILSSAQRQSLPICRVFCSGEALPT--ALAKSFTEHFSCELHNLYGPTEAAVDVSY-MDATLGLHPEEscVA 1854
Cdd:cd17651 235 TVALRALAEHGRPLGVRLAALRYLLTGGEQLVLteDLREFCAGLPGLRLHNHYGPTETHVVTALsLPGDPAAWPAP--PP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKAnvQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd17651 393 RADDQVKIRGFRIELGEIEAALARHPGVrEAVVLAREDRPGEK--RLVAYVvgDPEAPVDAAELRAALATHLPEYMVPSA 470
|
490 500
....*....|....*....|.
gi 490930577 2012 YMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17651 471 FVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1536-2034 |
2.17e-146 |
|
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: 465.26 E-value: 2.17e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ 1615
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1616 HPTERIKFMLQDAKSKLVIGEQKdlaaiVHPSIATFAFNELFDETkvDLSSYKTT----VITPQHPAYLIYTSGTTGQPK 1691
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSH-----LQPPIAFIGLIDLLDED--TIYHEESEnlepVSKSDDLAYVIYTSGSTGKPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLH 1771
Cdd:cd17655 154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1772 FVPSMLAVFENAAteilssaQRQSLPICRVFCSGEALPTALAKSFTEHF--SCELHNLYGPTEAAVDVSYMDATLGLHPE 1849
Cdd:cd17655 234 LTPAHLKLLDAAD-------DSEGLSLKHLIVGGEALSTELAKKIIELFgtNPTITNAYGPTETTVDASIYQYEPETDQQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 EScVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGS 1929
Cdd:cd17655 307 VS-VPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNkaNVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMV 2008
Cdd:cd17655 386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKeAVVIARKDEQG--QNYLCAYIVSEKELPVAQLREFLARELPDYMI 463
|
490 500
....*....|....*....|....*.
gi 490930577 2009 PTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:cd17655 464 PSYFIKLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1536-2031 |
4.97e-143 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 455.51 E-value: 4.97e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ 1615
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1616 HPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLSsyktTVITPQHPAYLIYTSGTTGQPKGVMV 1695
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPA----VPVSPDDLAYVMYTSGSTGRPKGVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNriLWMQSEY-PLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:cd12117 157 THRGVVR--LVKNTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEILSSAqRQslpicrVFCSGEALPTALAKSFTEHfsC---ELHNLYGPTEAAVDVSY--MDAtlgLHPE 1849
Cdd:cd12117 235 ALFNQLADEDPECFAGL-RE------LLTGGEVVSPPHVRRVLAA--CpglRLVNGYGPTENTTFTTShvVTE---LDEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 ESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGS 1929
Cdd:cd12117 303 AGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAIssEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMV 2008
Cdd:cd12117 383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVrEAVVVVR--EDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMV 460
|
490 500
....*....|....*....|...
gi 490930577 2009 PTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd12117 461 PAAFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1569-1966 |
1.63e-138 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 439.39 E-value: 1.63e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1569 ALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQK--DLAAIVH 1645
Cdd:TIGR01733 11 RLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSAlaSRLAGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1646 PSIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPC 1725
Cdd:TIGR01733 91 LPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1726 TFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLS-LIQKYQVTTLHFVPSMLAVfenaateiLSSAQRQSLPICR-VFC 1803
Cdd:TIGR01733 171 SFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLAL--------LAAALPPALASLRlVIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGEL 1882
Cdd:TIGR01733 243 GGEALTPALVDRWRARGpGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1883 YLAGHQLAMGYLHRADLTASRFVANPF--TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLIS 1960
Cdd:TIGR01733 323 YIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHP 402
|
....*.
gi 490930577 1961 GLDVVV 1966
Cdd:TIGR01733 403 GVREAV 408
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1546-2031 |
1.82e-136 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 435.20 E-value: 1.82e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttvitPQHPAYLIYTSGTTGQPKGVMVSHqAIVNRIL 1705
Cdd:cd17643 81 ADSGPSLLLTD-------------------------------------PDDLAYVIYTSGSTGRPKGVVVSH-ANVLALF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 W-MQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaa 1784
Cdd:cd17643 123 AaTQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQL---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1785 TEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHF---SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWN 1861
Cdd:cd17643 199 VEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFgldRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFT-AGQRMYRTGDIARWHADGSIQYIGRADDQL 1940
Cdd:cd17643 279 LRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1941 KIRGQRIELGEIEQQLRLISGL-DVVVhaISSEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQ 2017
Cdd:cd17643 359 KIRGFRIELGEIEAALATHPSVrDAAV--IVREDEPGDTRLVAYVvaDDGAAADIAELRALLKELLPDYMVPARYVPLDA 436
|
490
....*....|....
gi 490930577 2018 FPLSHNGKLDRKAL 2031
Cdd:cd17643 437 LPLTVNGKLDRAAL 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
124-1317 |
1.87e-135 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 477.53 E-value: 1.87e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 124 KSLKAGETqlfRQVLFTThdkvywyqrYHHIMLDGFSMINLTKRIVELYQQLQEGK--DLSVSPFIGVNEVISER---QA 198
Cdd:PRK12316 166 RLLRLGEE---EHVLLLT---------LHHIVSDGWSMNVLIEEFSRFYSAYATGAepGLPALPIQYADYALWQRswlEA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 199 YENSHQFkidqAFWKAYCEDLPSPISLSTHH-LAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIY 277
Cdd:PRK12316 234 GEQERQL----EYWRAQLGEEHPVLELPTDHpRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLH 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 278 KMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidih 357
Cdd:PRK12316 310 RYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKV---- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 358 ER--MYGPILNYKAFDQDLVIDGEKVKT-HHISTGPID----DFEFSFIVQDHELIIELRAdSQRYTQDeLFN------- 423
Cdd:PRK12316 386 ERslSHSPLFQVMYNHQPLVADIEALDTvAGLEFGQLEwksrTTQFDLTLDTYEKGGRLHA-ALTYATD-LFEartverm 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 424 --HGQRLtllLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQ 501
Cdd:PRK12316 464 arHWQNL---LRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQ-RGVHRLFEEQVERTPEAPALAFGE----E 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 502 HLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTT 581
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 582 QALAQQLP--QNIQQLHLDQEGVQTQIRKQDASDIPAenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPT 659
Cdd:PRK12316 616 SHLGRKLPlaAGVQVLDLDRPAAWLEGYSEENPGTEL-----NPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 660 IYWPVLEAVNERFPdrplraahthsFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSfcaq 738
Cdd:PRK12316 691 YGLGVGDTVLQKTP-----------FSFDVSVWEFFWPLMsGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS---- 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 739 mMTNGLF----VENQHHPSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVD----TFRAELKQTarPVIGNPIG 809
Cdd:PRK12316 756 -MLQAFLqdedVASCTSLRRIVCSGEALPADAQEQVFAKlPQAGLYNLYGPTEAAIDvthwTCVEEGGDS--VPIGRPIA 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 810 NTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQI 889
Cdd:PRK12316 833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 890 KIRGYRVEIGEVENALSILTNVESAVVIAEpinNSHRLLGYCVVKDIELDekTSEQLSQqylsQLRQNLPEYMVPSALTV 969
Cdd:PRK12316 913 KLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQLVGYVVLESEGGD--WREALKA----HLAASLPEYMVPAQWLA 983
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 970 MSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQRG 1046
Cdd:PRK12316 984 LERLPLTPNGKLDRKALPAPEASVAQQGYVAPRnalERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAG 1063
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1047 YSLRPSDVFQFKTVAAMAPQLTRldEQQAAVSKplfsadleqkvqekyGKNSTILPLLPLQKgMLFLSQVENQSNYNAFT 1126
Cdd:PRK12316 1064 IQLSPRDLFQHQTIRSLALVAKA--GQATAADQ---------------GPASGEVALAPVQR-WFFEQAIPQRQHWNQSL 1125
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1127 RLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAE------EPVFIYSLhptqaWPVQFCSVTPdlLEQTIQEAlQQP 1200
Cdd:PRK12316 1126 LLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGwqqayaAPQAGEVL-----WQRQAASEEE--LLALCEEA-QRS 1197
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1201 IHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQLPVLEHSYETVIKALSGrdHETSK 1279
Cdd:PRK12316 1198 LDLEQgP--LLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHE--HAGAR 1273
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*..
gi 490930577 1280 V----IWQRDLADLQPLILFNQAQQAVQ-----ETSYRLSAELGAKL 1317
Cdd:PRK12316 1274 AeeldYWQAQLEDAPHELPCENPDGALEnrherKLELRLDAERTRQL 1320
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
152-1324 |
2.96e-134 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 473.49 E-value: 2.96e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVS--PFIGVNEVISERQAYENSHQFKiDQAFWKAYC----------EDL 219
Cdd:PRK12467 1247 HHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPalPIQYADYAVWQRQWMDAGERAR-QLAYWKAQLggeqpvlelpTDR 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 220 PSPISLSthHLAAKttatfvkHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKA 299
Cdd:PRK12467 1326 PRPAVQS--HRGAR-------LAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAET 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 300 IRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSidihERMYG--PILNYkAFDQDLVID 377
Cdd:PRK12467 1397 EGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQP----ERSLShsPLFQV-MFNHQRDDH 1471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 378 GEKVKTHHIStgpIDDFEFSFIVQDHELIIELRADSQ------RYTQDeLFNHG--QRLTL----LLEQALIRPEQPCSN 445
Cdd:PRK12467 1472 QAQAQLPGLS---VESLSWESQTAQFDLTLDTYESSEglqaslTYATD-LFEAStiERLAGhwlnLLQGLVADPERRLGE 1547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 446 FNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGAR 525
Cdd:PRK12467 1548 LDLLDEAERRQILEGWNATHTGYPLA-RLVHQLIEDQAAATPEAVALVFGE----QELTYGELNRRANRLAHRLIALGVG 1622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 526 KQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLP--QNIQQLHLDQEgvQ 603
Cdd:PRK12467 1623 PEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPlpDGLRSLVLDQE--D 1700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 604 TQIRKQDASDiPAENrkFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLilshkptiywpvLEAVNERFPdrpLRAA--- 680
Cdd:PRK12467 1701 DWLEGYSDSN-PAVN--LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNR------------LCATQEAYQ---LSAAdvv 1762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 681 -HTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIG 758
Cdd:PRK12467 1763 lQFTSFAFDVSVWELFWpLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCG 1842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 759 GEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDTF-----RAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELY 832
Cdd:PRK12467 1843 GEALEVEALRPWLERlPDTGLFNLYGPTETAVDVThwtcrRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELY 1922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 833 ISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV 911
Cdd:PRK12467 1923 LGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 912 ESAVVIAEPINNSHRLLGYCVVKDIEL-DEKTSEQLSQQYLSQ-LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:PRK12467 2003 REAVVIAQDGANGKQLVAYVVPTDPGLvDDDEAQVALRAILKNhLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 990 QIRAHSRMAETPE---QQLLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMApq 1066
Cdd:PRK12467 2083 DASELQQAYVAPQselEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA-- 2160
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1067 lTRLDEQQAAVSkplfsadLEQkvqekyGKNSTILPLLPLQKgMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITV 1146
Cdd:PRK12467 2161 -AVAQEGDGTVS-------IDQ------GPVTGDLPLLPIQQ-MFFADDIPERHHWNQSVLLEPREALDAELLEAALQAL 2225
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1147 LKRHPQL------------GGHFDSELAEEPVFiyslhptqaWPVQFCSVtpDLLEQTIQEALQQpihLDQPYG-LIRAT 1213
Cdd:PRK12467 2226 LVHHDALrlgfvqedggwsAMHRAPEQERRPLL---------WQVVVADK--EELEALCEQAQRS---LDLEEGpLLRAV 2291
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1214 LIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQLPVLEHSYETVIKALSGR--DHETSKVI------WQRD 1285
Cdd:PRK12467 2292 LATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERlqTYAASAALadelgyWQAQ 2371
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|.
gi 490930577 1286 LADLQPLILFNQAQQAVQeTSYRLSA--ELGAKLQHKLRQQ 1324
Cdd:PRK12467 2372 LQGASTELPCDHPQGGLQ-RRHAASVttHLDSEWTRRLLQE 2411
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1546-2032 |
1.46e-133 |
|
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: 426.28 E-value: 1.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVigeqkdlaaivhpsiatfafnelfdetkvdlssykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd17652 81 ADARPALL-------------------------------------LTTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAAt 1785
Cdd:cd17652 124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 eilssaqrqsLPICRVFCS-GEALPTALAKSFTEHfsCELHNLYGPTEAAVDVSYMDATlglhPEESCVAIGYPVWNTQL 1864
Cdd:cd17652 203 ----------LPDLRTLVVaGEACPAELVDRWAPG--RRMINAYGPTETTVCATMAGPL----PGGGVPPIGRPVPGTRV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd17652 267 YVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1944 GQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLS 2021
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEAV-VVVRDDRPGDKRLVAYVvpAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLT 425
|
490
....*....|.
gi 490930577 2022 HNGKLDRKALP 2032
Cdd:cd17652 426 PNGKLDRRALP 436
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
477-986 |
5.68e-132 |
|
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: 423.54 E-value: 5.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDR----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 557 LDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqqlhldQEGVQTQIRKQDASDIPAENRKFDFQDVAYVIFTSGST 636
Cdd:cd12117 77 LDPELPAERLAFMLADAGAKVLLTDRSLAGRAGG--------LEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 637 GRPKGVMNTHGSLLNLILSHkptiyWPVLEAVNERFpdrplraAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAF 715
Cdd:cd12117 149 GRPKGVAVTHRGVVRLVKNT-----NYVTLGPDDRV-------LQTSPLAFDASTFEIWGaLLNGARLVLAPKGTLLDPD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 716 GLVQEIQQRQIDTLdlppsfcaqMMTNGLFveNQ---HHPSL------ILIGGEAAPLALWQQ-LNAQPALFAHNLYGPT 785
Cdd:cd12117 217 ALGALIAEEGVTVL---------WLTAALF--NQladEDPECfaglreLLTGGEVVSPPHVRRvLAACPGLRLVNGYGPT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 786 EYTVDT--FR-AELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHG 861
Cdd:cd12117 286 ENTTFTtsHVvTELDEVAGSIpIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 862 QRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYcVVKDIELDe 940
Cdd:cd12117 366 ERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGgDKRLVAY-VVAEGALD- 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 490930577 941 ktSEQLSqqylSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12117 444 --AAELR----AFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
477-986 |
4.30e-131 |
|
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: 4.30e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGR----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 557 LDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqqLHLDQEGVQTQIRKQDASDIPAENRKfdfQDVAYVIFTSGST 636
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTTADLAARLPA----GGDVALLGDEALAAPPATPPLVPPRP---DNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 637 GRPKGVMNTHGSLLNLILshkptiyWpvleaVNERFP----DRPLRAAhthSFSFDSSWLQVFW-MLWGQELHIFDENMR 711
Cdd:cd17646 151 GRPKGVMVTHAGIVNRLL-------W-----MQDEYPlgpgDRVLQKT---PLSFDVSVWELFWpLVAGARLVVARPGGH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 712 RDAFGLVQEIQQRQIDTLDLPPSfcaqMMtnGLFVEN---QHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTE 786
Cdd:cd17646 216 RDPAYLAALIREHGVTTCHFVPS----ML--RVFLAEpaaGSCASLrrVFCSGEALPPELAARFLALPGAELHNLYGPTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 787 YTVDT--FRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQR 863
Cdd:cd17646 290 AAIDVthWPVRGPAETPSVpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 864 MYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKDIELDEKT 942
Cdd:cd17646 370 MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAaRLVGYVVPAAGAAGPDT 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490930577 943 SEqlsqqYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17646 450 AA-----LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1100-2117 |
4.97e-130 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 460.02 E-value: 4.97e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIysLHPTQAWP 1178
Cdd:PRK05691 3257 VYPLTPMQEGLLLHTLLEPGTGlYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQV--IHKPGRTP 3334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 VQFC---SVTPDLLEQTIQEALQQPIH-----LDQPYGLIRatLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ 1250
Cdd:PRK05691 3335 IDYLdwrGLPEDGQEQRLQALHKQEREagfdlLNQPPFHLR--LIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYT 3412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 Q----TNQQLPVLEHsYETVIKALSGRDHETSKVIWQRDLADLQ---------PLI---LFNQAQQAVQETSYRLSAELG 1314
Cdd:PRK05691 3413 AlgegREAQLPVPPR-YRDYIGWLQRQDLAQARQWWQDNLRGFErptpipsdrPFLrehAGDSGGMVVGDCYTRLDAADG 3491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1315 AKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKL---NMQQTLWEQ 1391
Cdd:PRK05691 3492 ARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLpaaGQRCSVRQW 3571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1392 LPQLQQLHVEHLEHDGLGLSAIQQL--IAQGN-LFDSLLVVENYP-DNQYLQQKLGDAAISKlTNRGYSHYPLALLVIP- 1466
Cdd:PRK05691 3572 LQGLLDSNMELREYEYLPLVAIQECseLPKGQpLFDSLFVFENAPvEVSVLDRAQSLNASSD-SGRTHTNFPLTAVCYPg 3650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1467 -DHQIELLLEQRgVIDQPEhfLERMI---QLIEIALNEP-ETSLSHYRLQLAEEHD-LIQKTNQTQ--YYVRQSTLQqLL 1538
Cdd:PRK05691 3651 dDLGLHLSYDQR-YFDAPT--VERLLgefKRLLLALVQGfHGDLSELPLLGEQERDfLLDGCNRSErdYPLEQSYVR-LF 3726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1539 REQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK05691 3727 EAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPA 3806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVI--GEQKDLAAIVHPSIATFAFNEL--FDETKVDLSSYKTTVI--TPQHPAYLIYTSGTTGQPKG 1692
Cdd:PRK05691 3807 QRLQRIIELSRTPVLVcsAACREQARALLDELGCANRPRLlvWEEVQAGEVASHNPGIysGPDNLAYVIYTSGSTGLPKG 3886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1693 VMVSHQAIVNRILwmqSEYP---LSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTT 1769
Cdd:PRK05691 3887 VMVEQRGMLNNQL---SKVPylaLSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITV 3963
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHFVPSMLavfenaaTEILSSaQRQSLPICR-VFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSY----MDAT 1843
Cdd:PRK05691 3964 LESVPSLI-------QGMLAE-DRQALDGLRwMLPTGEAMPPELARQWLQRYpQIGLVNAYGPAECSDDVAFfrvdLAST 4035
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1844 LGlhpeeSCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTA-GQRMYRTGDIA 1922
Cdd:PRK05691 4036 RG-----SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGApGERLYRTGDLA 4110
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1923 RWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKanvQLVAYLQTTAPVD-----IDQLK 1996
Cdd:PRK05691 4111 RRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVrEAAVAVQEGVNGK---HLVGYLVPHQTVLaqgalLERIK 4187
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1997 KQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYA-TSAFEHELTRIFQQILNTDQnIGVNEDFF 2075
Cdd:PRK05691 4188 QRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLApRNELEQTLATIWADVLKVER-VGVHDNFF 4266
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 490930577 2076 AIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALL 2117
Cdd:PRK05691 4267 ELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1546-2032 |
3.51e-129 |
|
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: 414.46 E-value: 3.51e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd17649 81 EDSGAGLLLTH------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaAT 1785
Cdd:cd17649 125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQL---AE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EILSSAQRQSLPIcRVFCS-GEAL-PTALAKSFTEHfsCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQ 1863
Cdd:cd17649 202 EADRTGDGRPPSL-RLYIFgGEALsPELLRRWLKAP--VRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF-TAGQRMYRTGDIARWHADGSIQYIGRADDQLKI 1942
Cdd:cd17649 279 AYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1943 RGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKanvQLVAYL----QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQ 2017
Cdd:cd17649 359 RGFRIELGEIEAALLEHPGvREAAVVALDGAGGK---QLVAYVvlraAAAQPELRAQLRTALRASLPDYMVPAHLVFLAR 435
|
490
....*....|....*
gi 490930577 2018 FPLSHNGKLDRKALP 2032
Cdd:cd17649 436 LPLTPNGKLDRKALP 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
479-987 |
1.97e-128 |
|
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: 413.66 E-value: 1.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 479 FYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:cd17651 1 FERQAARTPDAPALVAEGR----RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 559 LDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqqlhlDQEGVQTQIRKQDASDIPAENR-KFDFQDVAYVIFTSGSTG 637
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPALAGELAV-------ELVAVTLLDQPGAAAGADAEPDpALDADDLAYVIYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 638 RPKGVMNTHGSLLNLILSHkptiywpvleavNERFP-DRPLRAAHTHSFSFDSSWLQVFWML-WGQELHIFDENMRRDAF 715
Cdd:cd17651 150 RPKGVVMPHRSLANLVAWQ------------ARASSlGPGARTLQFAGLGFDVSVQEIFSTLcAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 716 GLVQEIQQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSL--ILIGGEAAPL--ALWQQLNAQPALFAHNLYGPTEYTVDT 791
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVA-LRALAEHGRPLGVRLAALryLLTGGEQLVLteDLREFCAGLPGLRLHNHYGPTETHVVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 792 FRaELKQ-----TARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYR 866
Cdd:cd17651 297 AL-SLPGdpaawPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 867 TGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP-INNSHRLLGYcVVKDIELDEKTSEq 945
Cdd:cd17651 376 TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVAY-VVGDPEAPVDAAE- 453
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 490930577 946 LSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17651 454 LRA----ALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
487-986 |
5.00e-128 |
|
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: 411.68 E-value: 5.00e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd12116 1 PDATAVRDDDRS----LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAenrkfdfqDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd12116 77 RYILEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPD--------DLAYVIYTSGSTGRPKGVVVSH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLilshkptiywpvLEAVNERF---PDRPLRAAHThsFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQEIQ 722
Cdd:cd12116 149 RNLVNF------------LHSMRERLglgPGDRLLAVTT--YAFDISLLELLLPLLaGARVVIAPRETQRDPEALARLIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 723 QRQIDTLDLPPSfCAQMMtngLFVENQHHPSL-ILIGGEAAPLALWQQLNAQPALfAHNLYGPTEYTVDTFRAELKQTAR 801
Cdd:cd12116 215 AHSITVMQATPA-TWRML---LDAGWQGRAGLtALCGGEALPPDLAARLLSRVGS-LWNLYGPTETTIWSTAARVTAAAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 802 PV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH-GQRMYRTGDLVRWNSAGKL 879
Cdd:cd12116 290 PIpIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpGSRLYRTGDLVRRRADGRL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 880 EFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIE-LDEktsEQLSQqylsQLRQNL 958
Cdd:cd12116 370 EYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAaPDA---AALRA----HLRATL 442
|
490 500
....*....|....*....|....*...
gi 490930577 959 PEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12116 443 PAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1534-2031 |
4.88e-127 |
|
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: 407.86 E-value: 4.88e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIgeqkdlaaivhpsiatfafnelfdetkvdlssykttvITPQHPAYLIYTSGTTGQPKGV 1693
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVL-------------------------------------TDPDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIApidahRDPLALLSLIQKYQVTTLHFV 1773
Cdd:cd12115 124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PSmlavfenAATEILS-SAQRQSLpicRVFC-SGEALPTALAKSFTEHFSCE-LHNLYGPTEaavDVSYMDAT-LGLHPE 1849
Cdd:cd12115 199 PS-------AAAELLRhDALPASV---RVVNlAGEPLPRDLVQRLYARLQVErVVNLYGPSE---DTTYSTVApVPPGAS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 EScVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGS 1929
Cdd:cd12115 266 GE-VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD---VVVHaissEQNKANVQLVAYLQTTAP--VDIDQLKKQLAKHLP 2004
Cdd:cd12115 345 LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVReavVVAI----GDAAGERRLVAYIVAEPGaaGLVEDLRRHLGTRLP 420
|
490 500
....*....|....*....|....*..
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd12115 421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
152-1324 |
1.85e-126 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 448.64 E-value: 1.85e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 152 HHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPF-IGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHL 230
Cdd:PRK12316 2731 HHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLpLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRP 2810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 231 -AAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNV 309
Cdd:PRK12316 2811 rPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNT 2890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 310 LPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQIL------RDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKT 383
Cdd:PRK12316 2891 QVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVealqpeRSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAW 2970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 384 HHISTGPidDFEFSFIVQDHELIIELRADSQRYTQDELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIG 463
Cdd:PRK12316 2971 DGAATQF--DLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNA 3048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 464 PRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVV 543
Cdd:PRK12316 3049 TAAEYPLE-RGVHRLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVG 3123
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 544 MLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPaenrkfdf 623
Cdd:PRK12316 3124 LLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMP-------- 3195
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 624 QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEAVNERFPDRPLRAAhthSFSFDSSWLQVFWMLW-GQE 702
Cdd:PRK12316 3196 ENLAYVIYTSGSTGKPKGVGIRHSALSNHLCW--------MQQAYGLGVGDRVLQFT---TFSFDVFVEELFWPLMsGAR 3264
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 703 LHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNglfVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFahN 780
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEE---EDAHRCTSLkrIVCGGEALPADLQQQVFAGLPLY--N 3339
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 781 LYGPTEYTVDT--FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF 858
Cdd:PRK12316 3340 LYGPTEATITVthWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF 3419
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 859 EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEpinNSHRLLGYCVVKDIEL 938
Cdd:PRK12316 3420 VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV---DGRQLVAYVVPEDEAG 3496
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 939 DektseqLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP---QIRAHSRMAETPEQQLLCQITASVLK 1015
Cdd:PRK12316 3497 D------LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPdaaLLQQDYVAPVNELERRLAAIWADVLK 3570
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1016 LDAIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPqLTRLDEQQAAVSKPLfsadleqkvqekyg 1095
Cdd:PRK12316 3571 LEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLAR-VARVGGGVAVDQGPV-------------- 3635
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1096 knSTILPLLPLQKGmLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQ 1175
Cdd:PRK12316 3636 --SGETLLLPIQQQ-FFEEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGG 3712
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1176 AWPVQFCSVTPDLLEQTIQEAlQQPIHL-DQPygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ 1254
Cdd:PRK12316 3713 ALLWRAELDDAEELERLGEEA-QRSLDLaDGP--LLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQ 3789
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1255 ----QLPVLEHSYETVIKALSGRDHETSK----VIWQRDLADLQPLILFNQAQQAVQETSYR-LSAELGAKLQHKLRQQ 1324
Cdd:PRK12316 3790 geapRLPAKTSSFKAWAERLQEHARGEALkaelAYWQEQLQGVSSELPCDHPQGALQNRHAAsVQTRLDRELTRRLLQQ 3868
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
479-989 |
2.37e-126 |
|
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: 407.87 E-value: 2.37e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 479 FYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:cd17655 3 FEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 559 LDYPIDRMQMMCEDANPLFVLTTQALAQQLpQNIQQLHLDQEGvqtQIRKQDASDIPAENRkfdFQDVAYVIFTSGSTGR 638
Cdd:cd17655 79 PDYPEERIQYILEDSGADILLTQSHLQPPI-AFIGLIDLLDED---TIYHEESENLEPVSK---SDDLAYVIYTSGSTGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 639 PKGVMNTHGSLLNLILSHKPTIYwpvleavnerfPDRPLRAAHTHSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGL 717
Cdd:cd17655 152 PKGVMIEHRGVVNLVEWANKVIY-----------QGEHLRVALFASISFDASVTEIFAsLLSGNTLYIVRKETVLDGQAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 718 VQEIQQRQIDTLDLPPSFCAQMMTNGLFVE-NQHHpslILIGGEAAPLALWQQL----NAQPALFahNLYGPTEYTVDT- 791
Cdd:cd17655 221 TQYIRQNRITIIDLTPAHLKLLDAADDSEGlSLKH---LIVGGEALSTELAKKIielfGTNPTIT--NAYGPTETTVDAs 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 792 ---FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTG 868
Cdd:cd17655 296 iyqYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP-INNSHRLLGYcVVKDIELdekTSEQLS 947
Cdd:cd17655 376 DLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKdEQGQNYLCAY-IVSEKEL---PVAQLR 451
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 490930577 948 QqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:cd17655 452 E----FLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
53-1072 |
1.26e-122 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 436.31 E-value: 1.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 53 VDIPTFKKAIQIGLNEADTVIASY--SSDPSQPFIELNNQVQFQIEEFDFCHLTPKKAQqrLWDWMPSDRQCAKSLKagE 130
Cdd:PRK12316 4136 LDVERFRAAWQAALDRHDVLRSGFvwQGELGRPLQVVHKQVSLPFAELDWRGRADLQAA--LDALAAAERERGFDLQ--R 4211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 131 TQLFRQVLFTT----HDKVYwyqRYHHIMLDGFSMINLTKRIVELYQQLQEGK-DLSVSPFIGvnevISERQAYENShqf 205
Cdd:PRK12316 4212 APLLRLVLVRTaegrHHLIY---TNHHILMDGWSNSQLLGEVLERYSGRPPAQpGGRYRDYIA----WLQRQDAAAS--- 4281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 206 kidQAFWKAYCEDLPSPISLSTHHLAAK--TTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKA 283
Cdd:PRK12316 4282 ---EAFWREQLAALDEPTRLAQAIARADlrSANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQD 4358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 284 ELVNGIPFMRRLGS-KAIRSTLPT-VNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRD--------LNS 353
Cdd:PRK12316 4359 TVAFGATVAGRPAElPGIEGQIGLfINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWagqggealFDS 4438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 354 IDIHERMygPILNY--KAFDQDLVIDgeKVKTHHISTGPIDdfeFSFIVQDhELIIELRADSQRYTQDELFNHGQRLTLL 431
Cdd:PRK12316 4439 LLVFENY--PVSEAlqQGAPGGLRFG--EVTNHEQTNYPLT---LAVGLGE-TLSLQFSYDRGHFDAATIERLARHLTNL 4510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 432 LEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVK 511
Cdd:PRK12316 4511 LEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPAT-RCVHQLVAERARMTPDAVAVVFDE----EKLTYAELNRR 4585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 512 VNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLP-- 589
Cdd:PRK12316 4586 ANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPip 4665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 590 QNIQQLHLDQEGvqtqirkqDASDIPAEN--RKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEA 667
Cdd:PRK12316 4666 DGLASLALDRDE--------DWEGFPAHDpaVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHA--------TGER 4729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 668 VNERFPDRPLraaHTHSFSFDSSWLQVFWMLW-GQELHIFDENMRrDAFGLVQEIQQRQIDTLDLPPSFCaQMMTNGlFV 746
Cdd:PRK12316 4730 YELTPDDRVL---QFMSFSFDGSHEGLYHPLInGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYL-QQLAEH-AE 4803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 747 ENQHHPSL--ILIGGEAAPLALWQQ-LNAQPALFAHNLYGPTEYTVDTfraeLKQTARPV---------IGNPIGNTQAY 814
Cdd:PRK12316 4804 RDGEPPSLrvYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTV----LLWKARDGdacgaaympIGTPLGNRSGY 4879
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 815 VLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRG 893
Cdd:PRK12316 4880 VLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRG 4959
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 894 YRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQ--LSQQYLSQLRQNLPEYMVPSALTVMS 971
Cdd:PRK12316 4960 FRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRERLPEYMVPAHLVFLA 5039
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 972 EFPRNVSGKVDKKALPKPQIRAHSRMAETPEQQLLCQITA---SVLKLDAIGIDDDFFMTGGDSISAIMLCTQLR-QRGY 1047
Cdd:PRK12316 5040 RMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAiwaEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQlELGL 5119
|
1050 1060
....*....|....*....|....*
gi 490930577 1048 SLRPSDVFQFKTVAAMAPQLTRLDE 1072
Cdd:PRK12316 5120 ELPLRELFQTPTLAAFVELAAAAGS 5144
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
487-987 |
2.03e-120 |
|
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: 388.53 E-value: 2.03e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17652 1 PDAPAVVFGDE----TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTTQAlaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17652 77 AYMLADARPALLLTTPD-----------------------------------------NLAYVIYTSGSTGRPKGVVVTH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLIlshkptiywpvlEAVNERFPDRP-LRAAHTHSFSFDSSwlqvFWMLW-----GQELHIFDENMRRDAFGLVQE 720
Cdd:cd17652 116 RGLANLA------------AAQIAAFDVGPgSRVLQFASPSFDAS----VWELLmallaGATLVLAPAEELLPGEPLADL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 721 IQQRQIDTLDLPPSFCAQMMTNGLfvenqhhPSL--ILIGGEAAPLALWQQLNAQPALFahNLYGPTEYTVDTFRAELKQ 798
Cdd:cd17652 180 LREHRITHVTLPPAALAALPPDDL-------PDLrtLVVAGEACPAELVDRWAPGRRMI--NAYGPTETTVCATMAGPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 799 TARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRWNSA 876
Cdd:cd17652 251 GGGVPpIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRAD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 877 GKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKDIELDekTSEQLSQqylsQLR 955
Cdd:cd17652 331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDkRLVAYVVPAPGAAP--TAAELRA----HLA 404
|
490 500 510
....*....|....*....|....*....|..
gi 490930577 956 QNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17652 405 ERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1534-2031 |
6.96e-120 |
|
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: 388.82 E-value: 6.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEvrLQVCA--LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLP 1611
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAE--LDRLSsrLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1612 IDLQHPTERIKFMLQDAKSKLVigeqkdlaaivhpsiatfafnelfdetkvdLSSykttviTPQHPAYLIYTSGTTGQPK 1691
Cdd:cd05918 79 LDPSHPLQRLQEILQDTGAKVV------------------------------LTS------SPSDAAYVIFTSGSTGKPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLAllSLIQKYQVTTLH 1771
Cdd:cd05918 123 GVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLA--GFINRLRVTWAF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1772 FVPSMLAVFenaateilssaQRQSLPICRVFCS-GEALPTALAKSFTEHfsCELHNLYGPTEAAVDVSYMDATLGLHPEE 1850
Cdd:cd05918 201 LTPSVARLL-----------DPEDVPSLRTLVLgGEALTQSDVDTWADR--VRLINAYGPAECTIAATVSPVVPSTDPRN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 scvaIGYPVwNTQLYILDQ--YLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANP-------FTAGQRMYRTGDI 1921
Cdd:cd05918 268 ----IGRPL-GATCWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLI--SGLDVVVHAISSEQNKANVQLVAYLQT------------- 1986
Cdd:cd05918 343 VRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlpGAKEVVVEVVKPKDGSSSPQLVAFVVLdgsssgsgdgdsl 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1987 ------TAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05918 423 flepsdEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1546-2031 |
2.65e-119 |
|
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: 385.67 E-value: 2.65e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVigeqkdlaaivhpsiatfafnelfdetkvdlssykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd17650 81 EDSGAKLL-------------------------------------LTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSA-TDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSML-AVFENA 1783
Cdd:cd17650 124 AWRREYELDSfPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIrPVMAYV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1784 ATEILSSAQRQSLPICRVFCSGEALPTALAKsFTEHFscELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNTQ 1863
Cdd:cd17650 204 YRNGLDLSAMRLLIVGSDGCKAQDFKTLAAR-FGQGM--RIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd17650 281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1944 GQRIELGEIEQQLRLISGLDVVVHAIsSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHN 2023
Cdd:cd17650 361 GFRIELGEIESQLARHPAIDEAVVAV-REDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPN 439
|
....*...
gi 490930577 2024 GKLDRKAL 2031
Cdd:cd17650 440 GKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
54-1064 |
1.29e-116 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 416.48 E-value: 1.29e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 54 DIPTFKKAIQIGLNEADTVIASYSSDP--SQPFIELNNQVQFQIEEFDFchLTPKKAQQRLWDWMPSDRQcaKSLKAGET 131
Cdd:PRK12467 2681 DVERFRTAWQAVIDRHEILRSGFLWDGelEEPLQVVYKQARLPFSRLDW--RDRADLEQALDALAAADRQ--QGFDLLSA 2756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 132 QLFRQVLFTT-HDKVYWYQRYHHIMLDGFSMINLTKRIVELYQqlqeGKDLSvSPFIGVNEVISERQAYENSHQfkidQA 210
Cdd:PRK12467 2757 PLLRLTLVRTgEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF----GQPPP-AREGRYRDYIAWLQAQDAEAS----EA 2827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 211 FWKAYCEDLPSPISL--STHHLAAKTTATFVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNG 288
Cdd:PRK12467 2828 FWKEQLAALEEPTRLarALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFG 2907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 289 ipfmrrlgskAIRSTLPT------------VNVLPVkfkVAEKDSWVSLA---QHVQEQLREIRPHQKYDAEQILR---- 349
Cdd:PRK12467 2908 ----------ATVAGRPAqlrgaeqqlglfINTLPV---IASPRAEQTVSdwlQQVQAQNLALREFEHTPLADIQRwagq 2974
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 350 ----DLNSIDIHErmygpilNY-------KAFDQDLVIdgEKVKTHHISTGPIDdfefSFIVQDHELIIELRADSQRYTQ 418
Cdd:PRK12467 2975 ggeaLFDSILVFE-------NYpisealkQGAPSGLRF--GAVSSREQTNYPLT----LAVGLGDTLELEFSYDRQHFDA 3041
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 419 DELFNHGQRLTLLLEQALIRPEQPCSNFNITTPQELTALTQSGIGPRVSHPEQyNNVLDIFYEQVKKYPERTAIVSGErp 498
Cdd:PRK12467 3042 AAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSE-RLVHQLIEAQVARTPEAPALVFGD-- 3118
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 499 nlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFV 578
Cdd:PRK12467 3119 --QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLL 3196
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 579 LTTQALAQQLPQ--NIQQLHLDQEGVQTQIRKQDASDIPAENrkfdfqdVAYVIFTSGSTGRPKGVMNTHGSLLNLIlsh 656
Cdd:PRK12467 3197 LTQAHLLEQLPApaGDTALTLDRLDLNGYSENNPSTRVMGEN-------LAYVIYTSGSTGKPKGVGVRHGALANHL--- 3266
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 657 kptiYWpVLEAVNERFPDRPLRAAhthSFSFDSSWLQVFWMLW-GQELHIFDeNMRRDAFGLVQEIQQRQIDTLDLPPSF 735
Cdd:PRK12467 3267 ----CW-IAEAYELDANDRVLLFM---SFSFDGAQERFLWTLIcGGCLVVRD-NDLWDPEELWQAIHAHRISIACFPPAY 3337
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 736 CAQMMTNGlfvENQHHPSL--ILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDTFRAELKQTARPV-----IGNP 807
Cdd:PRK12467 3338 LQQFAEDA---GGADCASLdiYVFGGEAVPPAAFEQVKRKlKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEapyapIGRP 3414
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 808 IGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFE-HGQRMYRTGDLVRWNSAGKLEFMGRCD 886
Cdd:PRK12467 3415 VAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRID 3494
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 887 DQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYcVVKDIEldektSEQLSQQYLSQLRQNLPEYMVPSA 966
Cdd:PRK12467 3495 HQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAY-VVPADP-----QGDWRETLRDHLAASLPDYMVPAQ 3568
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 967 LTVMSEFPRNVSGKVDKKALPKPQI---RAHSRMAETPEQQlLCQITASVLKLDAIGIDDDFFMTGGDSISAIMLCTQLR 1043
Cdd:PRK12467 3569 LLVLAAMPLGPNGKVDRKALPDPDAkgsREYVAPRSEVEQQ-LAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIR 3647
|
1050 1060
....*....|....*....|..
gi 490930577 1044 Q-RGYSLRPSDVFQFKTVAAMA 1064
Cdd:PRK12467 3648 QsLGLKLSLRDLMSAPTIAELA 3669
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
504-916 |
8.48e-115 |
|
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: 371.21 E-value: 8.48e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 504 SFAELAVKVNQLTRFLQEN-GARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQQLPQnIQQLHLDQEGVQTQIRkQDASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiyw 662
Cdd:TIGR01733 81 ALASRLAG-LVLPVILLDPLELAAL-DDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 663 pvleavNERFPDRPL-RAAHTHSFSFDSSWLQVFWMLW-GQELHIFDENMRRDAFGLVQE-IQQRQIDTLDLPPSFcAQM 739
Cdd:TIGR01733 153 ------ARRYGLDPDdRVLQFASLSFDASVEEIFGALLaGATLVVPPEDEERDDAALLAAlIAEHPVTVLNLTPSL-LAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 740 MTNGLfVENQHHPSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTVDTF-----RAELKQTARPVIGNPIGNTQA 813
Cdd:TIGR01733 226 LAAAL-PPALASLRLVILGGEALTPALVDRWRARgPGARLINLYGPTETTVWSTatlvdPDDAPRESPVPIGRPLANTRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 814 YVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF--EHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKI 891
Cdd:TIGR01733 305 YVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI 384
|
410 420
....*....|....*....|....*
gi 490930577 892 RGYRVEIGEVENALSILTNVESAVV 916
Cdd:TIGR01733 385 RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1536-2031 |
4.07e-114 |
|
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: 370.10 E-value: 4.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ 1615
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1616 HPTERIKFMLQDAKSKLVIgeqkdlaaivhpsiatfafnelfdetkvdlssyktTVITPQHPAYLIYTSGTTGQPKGVMV 1695
Cdd:cd17653 81 LPSARIQAILRTSGATLLL-----------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIApidAHRDPLAllSLIQKyqVTTLHFVPS 1775
Cdd:cd17653 126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLA---DPSDPFA--HVART--VDALMSTPS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLAVFEnaateilssaqRQSLP-ICRVFCSGEALPTALAKSFTEhfSCELHNLYGPTEAAVDVSYmdatLGLHPEEScVA 1854
Cdd:cd17653 199 ILSTLS-----------PQDFPnLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTM----TELLPGQP-VT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17653 261 IGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNkanvqLVAYLqTTAPVDIDQLKKQLAKHLPAYMVPTHYML 2014
Cdd:cd17653 341 REDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGR-----LVAFV-TPETVDVDGLRSELAKHLPSYAVPDRIIA 414
|
490
....*....|....*..
gi 490930577 2015 VEQFPLSHNGKLDRKAL 2031
Cdd:cd17653 415 LDSFPLTANGKVDRKAL 431
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
41-1288 |
4.39e-114 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 408.40 E-value: 4.39e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 41 YTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIEEFDFCHLTPKKAQQRLWDWmpSDR 120
Cdd:PRK05691 1751 YNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQL--ADS 1828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 121 QCAKSLKAGETQLFRQVLFTTHD-KVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQEGKD--LSVSPFIGVNEVISERQ 197
Cdd:PRK05691 1829 EAHQPFDLERGPLLRACLVKAAErEHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDREspLEPLPVQYLDYSVWQRQ 1908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 198 AYENSH-QFKIDqaFWKAycedlpspiSLSTHH----LAAKTTATFVK-HQ---LRF--STGILEQIQALAAQTKLALNd 266
Cdd:PRK05691 1909 WLESGErQRQLD--YWKA---------QLGNEHplleLPADRPRPPVQsHRgelYRFdlSPELAARVRAFNAQRGLTLF- 1976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 267 MMMSLSLH-YIYKMTDKAELVNGIPFMRRL--GSKAIRSTLPTVNVLPVKFkvaekDSWVSLAQhVQEQLR----EIRPH 339
Cdd:PRK05691 1977 MTMTATLAaLLYRYSGQRDLRIGAPVANRIrpESEGLIGAFLNTQVLRCQL-----DGQMSVSE-LLEQVRqtviEGQSH 2050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 340 QKYDAEQILRDLNSIdiHERMYGPILNYK------AFDQDLVIDGEKVKthhistgpiddfefsFIVQD-----HELIIE 408
Cdd:PRK05691 2051 QDLPFDHLVEALQPP--RSAAYNPLFQVMcnvqrwEFQQSRQLAGMTVE---------------YLVNDaratkFDLNLE 2113
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 409 LRADSQR------YTQDeLFN---------HGQRLtllLEQALIRPEQPCSNFNITTPQELTALTQSgIGPRVSHPEQYN 473
Cdd:PRK05691 2114 VTDLDGRlgccltYSRD-LFDepriarmaeHWQNL---LEALLGDPQQRLAELPLLAAAEQQQLLDS-LAGEAGEARLDQ 2188
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 474 NVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGAS 553
Cdd:PRK05691 2189 TLHGLFAAQAARTPQAPALTFAG----QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 554 FLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQ---QLPQNIQQLHLDQEGVQtqIRKQDASDIPAENRKfdfQDVAYVI 630
Cdd:PRK05691 2265 YVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEalgELPAGVARWCLEDDAAA--LAAYSDAPLPFLSLP---QHQAYLI 2339
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 631 FTSGSTGRPKGVMNTHGSllnlILSHkptiywpvLEAVNERFPDRPLRAA-HTHSFSFDSSWLQVFWMLWGQELHIFDEN 709
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGE----IAMH--------CQAVIERFGMRADDCElHFYSINFDAASERLLVPLLCGARVVLRAQ 2407
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 710 MRRDAFGLVQEIQQRQIDTLDLPPSFCAQMmTNGLFVENQHHP-SLILIGGEAAPLALWQQLNA--QPALFaHNLYGPTE 786
Cdd:PRK05691 2408 GQWGAEEICQLIREQQVSILGFTPSYGSQL-AQWLAGQGEQLPvRMCITGGEALTGEHLQRIRQafAPQLF-FNAYGPTE 2485
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 787 YTVDTFRA----ELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH- 860
Cdd:PRK05691 2486 TVVMPLAClapeQLEEGAASVpIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAd 2565
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 861 GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDE 940
Cdd:PRK05691 2566 GGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDD 2645
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 941 KTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPEQQL---LCQITASVLKLD 1017
Cdd:PRK05691 2646 EAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELeqqLAQIWREVLNVE 2725
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1018 AIGIDDDFFMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPQLTRldeqqaavskplfsadlEQKVQEKYGKN 1097
Cdd:PRK05691 2726 RVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATH-----------------SEAAQAEQGPL 2788
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1098 STILPLLPLQKgMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEepvfiyslhptqaW 1177
Cdd:PRK05691 2789 QGASGLTPIQH-WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGR-------------W 2854
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1178 PVQFCSVTPDLLEQTIQEA-----------LQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDF 1245
Cdd:PRK05691 2855 QAEYRAVTAQELLWQVTVAdfaecaalfadAQRSLDLQQgP--LLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDL 2932
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1246 IKAYQQ----TNQQLPVLEHS---YETVIKALSGRDH-ETSKVIWQRDLAD 1288
Cdd:PRK05691 2933 QALYRQlsagAEPALPAKTSAfrdWAARLQAYAGSESlREELGWWQAQLGG 2983
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1546-2031 |
2.05e-113 |
|
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: 370.06 E-value: 2.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIGEQKDLAAIVHPSIATFAFNElFDETKVDLSSyktTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLD-ALAAPAPPPP---VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPsmlAVFENAAT 1785
Cdd:cd12114 157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVP---ALLEMLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1786 EiLSSAQRQSLPICRVFCSGE----ALPTALAKSFTEhfsCELHNLYGPTEAAVDVSYMDATlGLHPEESCVAIGYPVWN 1861
Cdd:cd12114 234 V-LEAAQALLPSLRLVLLSGDwiplDLPARLRALAPD---ARLISLGGATEASIWSIYHPID-EVPPDWRSIPYGRPLAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPftAGQRMYRTGDIARWHADGSIQYIGRADDQLK 1941
Cdd:cd12114 309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1942 IRGQRIELGEIEQQLRLISGLD-VVVHAIsseQNKANVQLVAYLQTTA---PVDIDQLKKQLAKHLPAYMVPTHYMLVEQ 2017
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVArAVVVVL---GDPGGKRLAAFVVPDNdgtPIAPDALRAFLAQTLPAYMIPSRVIALEA 463
|
490
....*....|....
gi 490930577 2018 FPLSHNGKLDRKAL 2031
Cdd:cd12114 464 LPLTANGKVDRAAL 477
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1533-2032 |
5.97e-113 |
|
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: 368.30 E-value: 5.97e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKG 1692
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQPENLA-------------------------------------YVIYTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1693 VMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHF 1772
Cdd:cd17644 124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1773 VPSMLAVFENAAT-EILSSAQRQSLpicrVFCSGEALPTALAKSFTEHFS--CELHNLYGPTEAAVDVSYMDATLGLHPE 1849
Cdd:cd17644 204 PPAYWHLLVLELLlSTIDLPSSLRL----VIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 ESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPF--TAGQRMYRTGDIARWHAD 1927
Cdd:cd17644 280 ITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsSESERLYKTGDLARYLPD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1928 GSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYL--QTTAPVDIDQLKKQLAKHLPA 2005
Cdd:cd17644 360 GNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAV-VIVREDQPGNKRLVAYIvpHYEESPSTVELRQFLKAKLPD 438
|
490 500
....*....|....*....|....*..
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17644 439 YMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
487-986 |
4.87e-112 |
|
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: 365.09 E-value: 4.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17643 1 PEAVAVVDED----RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17643 77 AFILADSGPSLLLT-----------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLilshkptiywpvLEAVnerfpDRPLRAAHT------HSFSFDSSwlqvFWMLWGQELH-----IFDENMRRDAF 715
Cdd:cd17643 116 ANVLAL------------FAAT-----QRWFGFNEDdvwtlfHSYAFDFS----VWEIWGALLHggrlvVVPYEVARSPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 716 GLVQEIQQRQIDTLDLPPSFCAQMMTnGLFVENQHHPSL--ILIGGEAAPLAL---WQQ--LNAQPALFahNLYGPTEYT 788
Cdd:cd17643 175 DFARLLRDEGVTVLNQTPSAFYQLVE-AADRDGRDPLALryVIFGGEALEAAMlrpWAGrfGLDRPQLV--NMYGITETT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 789 VD-TFR----AELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQ 862
Cdd:cd17643 252 VHvTFRpldaADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGS 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 863 RMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVKDieldek 941
Cdd:cd17643 332 RMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADD------ 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 490930577 942 TSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1538-1943 |
1.47e-111 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 362.40 E-value: 1.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALS-DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAIVHP--------------SIATFAFNELFDETKVDLSSYKTTVITPQ--HPAYL 1680
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEalgklevvklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPPPDpdDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1681 IYTSGTTGQPKGVMVSHQAIVNRILWMQSEYP----LSATDTILQKTPCTFDVSV-WEFFWSYLVGARLVIAPIDAHRDP 1755
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLIQKYQVTTLHFVPSMLAVFENAATeiLSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAV 1835
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGA--PKRALLSSLRL--VLSGGAPLPPELARRFRELFGGALVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1836 DVSYMDatLGLHPEESCVAIGYPVWNTQLYILDQY-LRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVAnpftagQR 1914
Cdd:pfam00501 317 VVTTPL--PLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DG 388
|
410 420
....*....|....*....|....*....
gi 490930577 1915 MYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:pfam00501 389 WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1542-2031 |
1.70e-110 |
|
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: 360.41 E-value: 1.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:cd05945 81 REILDAAKPALLIADGDDNA-------------------------------------YIIFTSGSTGRPKGVQISHDNLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1702 NRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS---MLA 1778
Cdd:cd05945 124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSfaaMCL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1779 VFENAATEILSSAqRQSLpicrvFCsGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGY 1857
Cdd:cd05945 204 LSPTFTPESLPSL-RHFL-----FC-GEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1858 PVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPftaGQRMYRTGDIARWHADGSIQYIGRAD 1937
Cdd:cd05945 277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1938 DQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPVDI---DQLKKQLAKHLPAYMVPTHYML 2014
Cdd:cd05945 354 FQVKLNGYRIELEEIEAALRQVPGVKEAV-VVPKYKGEKVTELIAFVVPKPGAEAgltKAIKAELAERLPPYMIPRRFVY 432
|
490
....*....|....*..
gi 490930577 2015 VEQFPLSHNGKLDRKAL 2031
Cdd:cd05945 433 LDELPLNANGKIDRKAL 449
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1535-2032 |
4.55e-109 |
|
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: 356.09 E-value: 4.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1535 QQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDL 1614
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1615 QHPTERIKFMLQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVM 1694
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPDDLA-------------------------------------YVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTtLHFVP 1774
Cdd:cd17645 124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAvfenaatEILSSAQRQSLPIcrVFCSGEALPTALAKSFTehfsceLHNLYGPTEAAVdvsyMDATLGLHPEESCVA 1854
Cdd:cd17645 203 TGAA-------EQFMQLDNQSLRV--LLTGGDKLKKIERKGYK------LVNNYGPTENTV----VATSFEIDKPYANIP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1855 IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17645 264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYML 2014
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAA-VLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVH 422
|
490
....*....|....*...
gi 490930577 2015 VEQFPLSHNGKLDRKALP 2032
Cdd:cd17645 423 LKALPLTANGKVDRKALP 440
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
478-987 |
4.42e-108 |
|
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: 354.05 E-value: 4.42e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 478 IFYEQVKKYPERTAIVSgERpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL 557
Cdd:cd17644 5 LFEEQVERTPDAVAVVF-ED---QQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 558 DLDYPIDRMQMMCEDANpLFVLTTQalaqqlPQNIqqlhldqegvqtqirkqdasdipaenrkfdfqdvAYVIFTSGSTG 637
Cdd:cd17644 81 DPNYPQERLTYILEDAQ-ISVLLTQ------PENL----------------------------------AYVIYTSGSTG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 638 RPKGVMNTHGSLLNLIlshkptiyWPVLEAVNERFPDRPLRAAhthSFSFDSSWLQVFwMLW--GQELHIFDENMRRDAF 715
Cdd:cd17644 120 KPKGVMIEHQSLVNLS--------HGLIKEYGITSSDRVLQFA---SIAFDVAAEEIY-VTLlsGATLVLRPEEMRSSLE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 716 GLVQEIQQRQIDTLDLPPSFCAQMMTNGL--FVENQHHPSLILIGGEAAPLALWQQL--NAQPALFAHNLYGPTEYTVDT 791
Cdd:cd17644 188 DFVQYIQQWQLTVLSLPPAYWHLLVLELLlsTIDLPSSLRLVIVGGEAVQPELVRQWqkNVGNFIQLINVYGPTEATIAA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 792 FRAELK-----QTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEH--GQRM 864
Cdd:cd17644 268 TVCRLTqlterNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 865 YRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYcVVKDIELDEKTS 943
Cdd:cd17644 348 YKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVrEDQPGNKRLVAY-IVPHYEESPSTV 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490930577 944 EQlsQQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17644 427 EL--RQFLK---AKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1534-2037 |
6.07e-108 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 353.35 E-value: 6.07e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIGeqkdlaaivhpsiatfafnelfdetkvdlssykttvitpqhpAYLIYTSGTTGQPKGV 1693
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYL-VGARLVIAPidaHRDPLALLSLIQKYQVTTLHF 1772
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLlAGATLVLLP---RFDPERVLELIERERVTVLFG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1773 VPSM---LAVFENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPE 1849
Cdd:COG0318 196 VPTMlarLLRHPEFARYDLSSLR-------LVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 ESCvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpftagQRMYRTGDIARWHADGS 1929
Cdd:COG0318 269 GSV---GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVV----HAISSEQNKANVQLVAylqtTAPVDIDQLKKQLAKHLP 2004
Cdd:COG0318 339 LYIVGRKKDMIISGGENVYPAEVEEVLAAHPGvAEAAVvgvpDEKWGERVVAFVVLRP----GAELDAEELRAFLRERLA 414
|
490 500 510
....*....|....*....|....*....|...
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLT 2037
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
477-986 |
1.98e-107 |
|
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: 351.62 E-value: 1.98e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDE----SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 557 LDLDYPIDRMQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGST 636
Cdd:cd12115 79 LDPAYPPERLRFILEDAQARLVLT-----------------------------------------DPDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 637 GRPKGVMNTHGSLLNLIlshkptiYWpvleaVNERFPDRPLRA--AHThSFSFDSSWLQVFWML-WGQELHIFDenmrrD 713
Cdd:cd12115 118 GRPKGVAIEHRNAAAFL-------QW-----AAAAFSAEELAGvlAST-SICFDLSVFELFGPLaTGGKVVLAD-----N 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 714 AFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQhhpSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEYTV-DT 791
Cdd:cd12115 180 VLALPDLPAAAEVTLINTVPSAAAELLRHDALPASV---RVVNLAGEPLPRDLVQRLYARlQVERVVNLYGPSEDTTyST 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 792 FRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDL 870
Cdd:cd12115 257 VAPVPPGASGEVsIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 871 VRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVKDieldekTSEQLSQQ 949
Cdd:cd12115 337 VRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAiGDAAGERRLVAYIVAEP------GAAGLVED 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 490930577 950 YLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12115 411 LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
487-987 |
2.55e-107 |
|
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: 351.29 E-value: 2.55e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17649 1 PDAVALVFGD----QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTtqalaqQLPQNIqqlhldqegvqtqirkqdasdipaenrkfdfqdvAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17649 77 RYMLEDSGAGLLLT------HHPRQL----------------------------------AYVIYTSGSTGTPKGVAVSH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLIlshkptiywpvlEAVNERFP----DRPLRAAhthSFSFDSSWLQVFW-MLWGQELHIFDENMRRDAFGLVQEI 721
Cdd:cd17649 117 GPLAAHC------------QATAERYGltpgDRELQFA---SFNFDGAHEQLLPpLICGACVVLRPDELWASADELAEMV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 722 QQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAhNLYGPTEYTV-----DTFRA 794
Cdd:cd17649 182 RELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLrlYIFGGEALSPELLRRWLKAPVRLF-NAYGPTEATVtplvwKCEAG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 795 ELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-EHGQRMYRTGDLVRW 873
Cdd:cd17649 261 AARAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARW 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 874 NSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQLSQqylsQ 953
Cdd:cd17649 341 RDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRT----A 416
|
490 500 510
....*....|....*....|....*....|....
gi 490930577 954 LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17649 417 LRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1545-2032 |
6.73e-105 |
|
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: 345.61 E-value: 6.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKdlaaivHPSIATFAFN----ELFDETKVDLSSYkTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:cd17656 81 MLDSGVRVVLTQRH------LKSKLSFNKStillEDPSISQEDTSNI-DYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLhFVPSMLAVF 1780
Cdd:cd17656 154 VNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 enaateILSSAQ-RQSLPIC--RVFCSGEALptALAKSFTEHF---SCELHNLYGPTEAAVDVSYMdatlgLHPEESCV- 1853
Cdd:cd17656 233 ------IFSEREfINRFPTCvkHIITAGEQL--VITNEFKEMLhehNVHLHNHYGPSETHVVTTYT-----INPEAEIPe 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 --AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQ 1931
Cdd:cd17656 300 lpPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1932 YIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANvQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd17656 380 FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEK-YLCAYFVMEQELNISQLREYLAKQLPEYMIPSF 458
|
490 500
....*....|....*....|.
gi 490930577 2012 YMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17656 459 FVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1546-2032 |
7.06e-102 |
|
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: 335.91 E-value: 7.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFM 1624
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLsVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVMVSHQAIVNRI 1704
Cdd:cd17648 81 LEDTGARVVITNSTDLA-------------------------------------YAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1705 LWMQSEYPLSATDT--ILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFEn 1782
Cdd:cd17648 124 TSLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYD- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1783 aateiLSSaqRQSLPicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVdvsYMDATLGLHPEESCVAIGYPVWNT 1862
Cdd:cd17648 203 -----LAR--LPHLK--RVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTV---TNHKRFFPGDQRFDKSLGRPVRNT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1863 QLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQ--------RMYRTGDIARWHADGSIQYIG 1934
Cdd:cd17648 271 KCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1935 RADDQLKIRGQRIELGEIEQQLRLISGLD--VVVHAISSEQNKANVQ--LVA-YLQTTAPVDIDQLKKQLAKHLPAYMVP 2009
Cdd:cd17648 351 RNDFQVKIRGQRIEPGEVEAALASYPGVRecAVVAKEDASQAQSRIQkyLVGyYLPEPGHVPESDLLSFLRAKLPRYMVP 430
|
490 500
....*....|....*....|...
gi 490930577 2010 THYMLVEQFPLSHNGKLDRKALP 2032
Cdd:cd17648 431 ARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
487-986 |
7.61e-102 |
|
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: 336.55 E-value: 7.61e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd12114 1 PDATAVICGD----GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEgvqtqirKQDASDIPAEnRKFDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAVFDVLILDLD-------ALAAPAPPPP-VDVAPDDLAYVIFTSGSTGTPKGVMISH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLIlshkptiywpvlEAVNERF----PDRPLRAAhthSFSFDSSWLQVFWML-WGQELHIFDENMRRDAFGLVQEI 721
Cdd:cd12114 149 RAALNTI------------LDINRRFavgpDDRVLALS---SLSFDLSVYDIFGALsAGATLVLPDEARRRDPAHWAELI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 722 QQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSL--ILIGGEAAPLAL---WQQLNAQPALFAhnLYGPTE-------YTV 789
Cdd:cd12114 214 ERHGVTLWNSVPAL-LEMLLDVLEAAQALLPSLrlVLLSGDWIPLDLparLRALAPDARLIS--LGGATEasiwsiyHPI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 790 DTFRAELKqtarpVI--GNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPfeHGQRMYRT 867
Cdd:cd12114 291 DEVPPDWR-----SIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 868 GDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYcVVKDIELDEKTSEQLS 947
Cdd:cd12114 364 GDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAF-VVPDNDGTPIAPDALR 442
|
490 500 510
....*....|....*....|....*....|....*....
gi 490930577 948 QqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12114 443 A----FLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
487-987 |
1.95e-94 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 315.18 E-value: 1.95e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17656 2 PDAVAVVFEN----QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEgvqtQIRKQDASDIPAENRKfdfQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17656 78 IYIMLDSGVRVVLTQRHLKSKLSFNKSTILLEDP----SISQEDTSNIDYINNS---DDLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLILSHKptiywpvlEAVNERFPDRPLRAAhthSFSFDSSWLQVF-WMLWGQELHIFDENMRRDAFGLVQEIQQRQ 725
Cdd:cd17656 151 KNMVNLLHFER--------EKTNINFSDKVLQFA---TCSFDVCYQEIFsTLLSGGTLYIIREETKRDVEQLFDLVKRHN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 726 IDTLDLPPSFCAQmmtngLFVENQHHPSL------ILIGGEAAPLA-LWQQLNAQPALFAHNLYGPTE---YTVDTFRAE 795
Cdd:cd17656 220 IEVVFLPVAFLKF-----IFSEREFINRFptcvkhIITAGEQLVITnEFKEMLHEHNVHLHNHYGPSEthvVTTYTINPE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 796 LKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNS 875
Cdd:cd17656 295 AEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 876 AGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVkdieLDEKTSEQLSqqylSQL 954
Cdd:cd17656 375 DGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDkADDKGEKYLCAYFVM----EQELNISQLR----EYL 446
|
490 500 510
....*....|....*....|....*....|...
gi 490930577 955 RQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17656 447 AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
478-987 |
3.02e-94 |
|
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: 313.34 E-value: 3.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 478 IFYEQVKKYPERTAIVSgerpNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL 557
Cdd:cd17645 3 LFEEQVERTPDHVAVVD----RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 558 DLDYPIDRMQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTG 637
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLT-----------------------------------------NPDDLAYVIYTSGSTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 638 RPKGVMNTHGSLLNLILSHKPtiYWPVLEAvnerfpDRPLRAAhthSFSFDSSWLQVF-WMLWGQELHIFDENMRRDAFG 716
Cdd:cd17645 118 LPKGVMIEHHNLVNLCEWHRP--YFGVTPA------DKSLVYA---SFSFDASAWEIFpHLTAGAALHVVPSERRLDLDA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 717 LVQEIQQRQIDTLDLPPSFCAQMMTnglfVENqHHPSLILIGGEAAplalwQQLNAQPALFAHNlYGPTEYTVDTFRAEL 796
Cdd:cd17645 187 LNDYFNQEGITISFLPTGAAEQFMQ----LDN-QSLRVLLTGGDKL-----KKIERKGYKLVNN-YGPTENTVVATSFEI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 797 -KQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNS 875
Cdd:cd17645 256 dKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLP 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 876 AGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIA-EPINNSHRLLGYCVVKdielDEKTSEQLSqqylSQL 954
Cdd:cd17645 336 DGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAkEDADGRKYLVAYVTAP----EEIPHEELR----EWL 407
|
490 500 510
....*....|....*....|....*....|...
gi 490930577 955 RQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17645 408 KNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
475-986 |
8.45e-94 |
|
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: 313.71 E-value: 8.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 475 VLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASF 554
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWD----GSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 555 LPLDLDYPIDRMQMMCEDANPLFVLTTQAlaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfQDVAYVIFTSG 634
Cdd:cd05918 77 VPLDPSHPLQRLQEILQDTGAKVVLTSSP----------------------------------------SDAAYVIFTSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 635 STGRPKGVMNTHGSLLNLILSHKPtiywpvLEAVNERfpDRPLRAAhthSFSFDSSWLQVFWMLwgqelhIF-------- 706
Cdd:cd05918 117 STGKPKGVVIEHRALSTSALAHGR------ALGLTSE--SRVLQFA---SYTFDVSILEIFTTL------AAggclcips 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 707 DENMRRDafgLVQEIQQRQIDTLDLPPSFcAQMMTNGLFvenqhhPSL--ILIGGEAAPLALWQQLNAQPALFahNLYGP 784
Cdd:cd05918 180 EEDRLND---LAGFINRLRVTWAFLTPSV-ARLLDPEDV------PSLrtLVLGGEALTQSDVDTWADRVRLI--NAYGP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 785 TEYTVDTFRAELKQTARP-VIGNPIGNTqAYVLD--RHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANP---- 857
Cdd:cd05918 248 AECTIAATVSPVVPSTDPrNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlk 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 858 ---FEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALS----ILTNVESAVVIAEPINNSHRLLGY 930
Cdd:cd05918 327 qegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRqslpGAKEVVVEVVKPKDGSSSPQLVAF 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 931 CVVKDIELDEKTSEQLSQQYLSQ-----------LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05918 407 VVLDGSSSGSGDGDSLFLEPSDEfralvaelrskLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
487-986 |
2.69e-92 |
|
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: 307.86 E-value: 2.69e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd17650 1 PDAIAVSDATR----QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd17650 77 QYMLEDSGAKLLLT-----------------------------------------QPEDLAYVIYTSGTTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLILShkptiyWPVLEAVnERFPDRPLRAAhthSFSFDsswlqVFW------MLWGQELHIFDENMRRDAFGLVQE 720
Cdd:cd17650 116 RNVAHAAHA------WRREYEL-DSFPVRLLQMA---SFSFD-----VFAgdfarsLLNGGTLVICPDEVKLDPAALYDL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 721 IQQRQIDTLDLPPSFCAQMMTngLFVENQHHPS---LILIGGEAAPLALWQQLNAQpaLFAH----NLYGPTEYTVDTF- 792
Cdd:cd17650 181 ILKSRITLMESTPALIRPVMA--YVYRNGLDLSamrLLIVGSDGCKAQDFKTLAAR--FGQGmriiNSYGVTEATIDSTy 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 793 ----RAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTG 868
Cdd:cd17650 257 yeegRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVkdielDEKTSEQLS 947
Cdd:cd17650 337 DLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEaRLCAYVVA-----AATLNTAEL 411
|
490 500 510
....*....|....*....|....*....|....*....
gi 490930577 948 QQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17650 412 RAFLA---KELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
487-987 |
5.96e-89 |
|
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: 298.54 E-value: 5.96e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGA-RKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:cd17648 1 PDRVAVVYGD----KRLTYRELNERANRLAHYLLSVAEiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 566 MQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNT 645
Cdd:cd17648 77 IQFILEDTGARVVIT-----------------------------------------NSTDLAYAIYTSGTTGKPKGVLVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 646 HGSLLNLILShkptiywpvleaVNERFPDRPLRAAHTHSFS---FDSSWLQ-VFWMLWGQELHIFDENMRRDAFGLVQEI 721
Cdd:cd17648 116 HGSVVNLRTS------------LSERYFGRDNGDEAVLFFSnyvFDFFVEQmTLALLNGQKLVVPPDEMRFDPDRFYAYI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 722 QQRQIDTLDLPPSFCAQmmtnglfVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQT 799
Cdd:cd17648 184 NREKVTYLSGTPSVLQQ-------YDLARLPHLkrVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGD 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 800 AR--PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQ--------RMYRTGD 869
Cdd:cd17648 257 QRfdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 870 LVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH------RLLGYCVVKDIELDEkts 943
Cdd:cd17648 337 LVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAqsriqkYLVGYYLPEPGHVPE--- 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490930577 944 eqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd17648 414 ----SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1100-1501 |
4.86e-88 |
|
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: 294.88 E-value: 4.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIysLHPTQAWP 1178
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGaYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQV--VLKDRKLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 VQF---CSVTPDLLEQTIQEAL----QQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ- 1250
Cdd:cd19543 79 WREldlSHLSEAEQEAELEALAeedrERGFDLARA-PLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 QTNQQLPVLE--HSYETVIKALSGRDHETSKVIWQRDLADL--QPLILFNQA-----QQAVQETSYRLSAELGAKLQHKL 1321
Cdd:cd19543 158 LGEGQPPSLPpvRPYRDYIAWLQRQDKEAAEAYWREYLAGFeePTPLPKELPadadgSYEPGEVSFELSAELTARLQELA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1322 RQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVE 1401
Cdd:cd19543 238 RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1402 HLEHDGLGLSAIQQLIAQG-NLFDSLLVVENYPDNQYLQQKLGDAA--ISKLTNRGYSHYPLALLVIPDHQIELLLE-QR 1477
Cdd:cd19543 318 LREHEYVPLYEIQAWSEGKqALFDHLLVFENYPVDESLEEEQDEDGlrITDVSAEEQTNYPLTVVAIPGEELTIKLSyDA 397
|
410 420
....*....|....*....|....*.
gi 490930577 1478 GVIDQP--EHFLERMIQLIEIALNEP 1501
Cdd:cd19543 398 EVFDEAtiERLLGHLRRVLEQVAANP 423
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
483-986 |
1.50e-87 |
|
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: 294.15 E-value: 1.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 483 VKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYP 562
Cdd:cd05945 1 AAANPDRPAVVEGGRT----LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 563 IDRMQMMCEDANPLFVLTTQAlaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqDVAYVIFTSGSTGRPKGV 642
Cdd:cd05945 77 AERIREILDAAKPALLIADGD-----------------------------------------DNAYIIFTSGSTGRPKGV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 643 MNTHGSLLNLIlshkptiywpvlEAVNERFPDRP-LRAAHTHSFSFDSSWLQVF--WMLwGQELHIFDENMRRDAFGLVQ 719
Cdd:cd05945 116 QISHDNLVSFT------------NWMLSDFPLGPgDVFLNQAPFSFDLSVMDLYpaLAS-GATLVPVPRDATADPKQLFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 720 EIQQRQIDTLDLPPSFCAQMMTNGLFVEnQHHPSL--ILIGGEAAPLALWQQL-NAQPALFAHNLYGPTEYTVDT----F 792
Cdd:cd05945 183 FLAEHGITVWVSTPSFAAMCLLSPTFTP-ESLPSLrhFLFCGEVLPHKTARALqQRFPDARIYNTYGPTEATVAVtyieV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 793 RAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPfehGQRMYRTGDLV 871
Cdd:cd05945 262 TPEVLDGYDRLpIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 872 RWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYcvvkdIELDEKTSEQLSQQY 950
Cdd:cd05945 339 RLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVtELIAF-----VVPKPGAEAGLTKAI 413
|
490 500 510
....*....|....*....|....*....|....*.
gi 490930577 951 LSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05945 414 KAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
477-986 |
1.51e-87 |
|
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: 293.83 E-value: 1.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLG----GSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 557 LDLDYPIDRMQMMCEDANPLFVLTTqalaqqlpqniqqlhldqegvqtqirkqDASDipaenrkfdfqDVAYVIFTSGST 636
Cdd:cd17653 77 LDAKLPSARIQAILRTSGATLLLTT----------------------------DSPD-----------DLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 637 GRPKGVMNTHGSLLNLilshkptiywpvLEAVNERFPDRP-LRAAHTHSFSFDSSWLQVFWML-WGQELHIFDENmrrDA 714
Cdd:cd17653 118 GIPKGVMVPHRGVLNY------------VSQPPARLDVGPgSRVAQVLSIAFDACIGEIFSTLcNGGTLVLADPS---DP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 715 FGLVQeiqqRQIDTLDLPPSFCAQmmtnglfVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFahNLYGPTEYTVDTF 792
Cdd:cd17653 183 FAHVA----RTVDALMSTPSILST-------LSPQDFPNLktIFLGGEAVPPSLLDRWSPGRRLY--NAYGPTECTISST 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 793 RAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVR 872
Cdd:cd17653 250 MTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 873 WNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN-ALSILTNVESAVVIAepINNshRLLGYCVVKDIELDEKTSEqlsqqyl 951
Cdd:cd17653 330 WTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIV--VNG--RLVAFVTPETVDVDGLRSE------- 398
|
490 500 510
....*....|....*....|....*....|....*
gi 490930577 952 sqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17653 399 --LAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
479-892 |
5.65e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 288.44 E-value: 5.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 479 FYEQVKKYPERTAIVSGERpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:pfam00501 1 LERQAARTPDKTALEVGEG---RRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 559 LDYPIDRMQMMCEDANPLFVLTTQAL--------AQQLPQNIQQLHLDQEGVQT----QIRKQDASDIPAENRKFDFQDV 626
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLDRDPVLKeeplPEEAKPADVPPPPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 627 AYVIFTSGSTGRPKGVMNTHGSLLNLILSHKptIYWPVLEAVNERfpdrpLRAAHTHSFSFDSSWLQVFW--MLWGQELH 704
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIK--RVRPRGFGLGPD-----DRVLSTLPLFHDFGLSLGLLgpLLAGATVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 705 IFDENMRRDAFGLVQEIQQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLY 782
Cdd:pfam00501 231 LPPGFPALDPAALLELIERYKVTVLYGVPTL-LNMLLEAGAPKRALLSSLrlVLSGGAPLPPELARRFRELFGGALVNGY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 783 GPTEYTVDT---FRAELKQTARPVIGNPIGNTQAYVLD-RHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVAnpf 858
Cdd:pfam00501 310 GLTETTGVVttpLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE--- 386
|
410 420 430
....*....|....*....|....*....|....
gi 490930577 859 ehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIR 892
Cdd:pfam00501 387 ---DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
478-1075 |
2.78e-79 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 294.00 E-value: 2.78e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 478 IFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL 557
Cdd:PRK05691 3725 LFEAQVAAHPQRIAASCLD----QQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 558 DLDYPIDRMQMMCE-DANPLFVLTTQALAQ------QLPQNIQQLHLDQEGVQtqirkqdASDIPAEN--RKFDFQDVAY 628
Cdd:PRK05691 3801 DPGLPAQRLQRIIElSRTPVLVCSAACREQaralldELGCANRPRLLVWEEVQ-------AGEVASHNpgIYSGPDNLAY 3873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 629 VIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVnerfpdrplraAHTHSFSFD-SSWLQVFWMLWGQELHIFD 707
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVI-----------AQTASQSFDiSVWQFLAAPLFGARVEIVP 3942
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 708 ENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNglfvENQHHPSL--ILIGGEAAPLALWQQ-LNAQPALFAHNLYGP 784
Cdd:PRK05691 3943 NAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAE----DRQALDGLrwMLPTGEAMPPELARQwLQRYPQIGLVNAYGP 4018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 785 TEYTVDT--FRAELKQTARPV--IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF-E 859
Cdd:PRK05691 4019 AECSDDVafFRVDLASTRGSYlpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgA 4098
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 860 HGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHrLLGYCVVKDIEL 938
Cdd:PRK05691 4099 PGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVrEAAVAVQEGVNGKH-LVGYLVPHQTVL 4177
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 939 DEktsEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQI-RAHSRMAETPE---QQLLCQITASVL 1014
Cdd:PRK05691 4178 AQ---GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIgQLQSQAYLAPRnelEQTLATIWADVL 4254
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1015 KLDAIGIDDDFFMTGGDSISAIMLCTQLR---QRGYSLRPsdVFQFKTVAAMAPQL-----TRLDEQQA 1075
Cdd:PRK05691 4255 KVERVGVHDNFFELGGHSLLATQIASRVQkalQRNVPLRA--MFECSTVEELAEYIeglagSAIDEQKV 4321
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1529-2377 |
3.47e-78 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 279.28 E-value: 3.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 YLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTG 1688
Cdd:COG3319 81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1689 QPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVT 1768
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1769 TLHFVPSMLAVFENAATEILSSAQRQSLPICRVFCSGEALPTALAksftehfscELHNLYGPTEAAVDVSYMDATLGLHP 1848
Cdd:COG3319 241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAA---------AAALAAGGTATTAAVTTTAAAAAPGV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFT--AGQRMYRTGDIARWHA 1926
Cdd:COG3319 312 AGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGagARGRLRRGGDRGRRLG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1927 DGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAY 2006
Cdd:COG3319 392 GGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2007 MVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAFEHELTRIFQQILNTDqnIGVNEDFFAIGGHSILVMK 2086
Cdd:COG3319 472 LPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGL--VGDDDDFFGGGGGSLLALL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2087 LAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQERLAEVEQtgmqPILPIRSGSGHPLFCFYPGSGSAWQYTVLNRYLH 2166
Cdd:COG3319 550 LLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSP----LVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALG 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2167 SDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVAAKLTEQGEKVDYLGLLDTYP- 2245
Cdd:COG3319 626 PDRPVYGLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAp 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2246 ------------------AEIHQWLDLSVEEMNAEAEQEQLQFFNDILADADSALSEETRRLqEDIFANYRDAVRLLKPY 2307
Cdd:COG3319 706 galarldeaellaallrdLARGVDLPLDAEELRALDPEERLARLLERLREAGLPAGLDAERL-RRLLRVFRANLRALRRY 784
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 2308 KMPHFDGELHLVVAEKDLLP-YIQPEQQWSPLVK-KLNIVRLsEADHTDILSPQQLETLGPILNRMICQARG 2377
Cdd:COG3319 785 RPRPYDGPVLLFRAEEDPPGrADDPALGWRPLVAgGLEVHDV-PGDHFSMLREPHVAELAAALRAALAAAEA 855
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
18-439 |
8.98e-77 |
|
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: 261.92 E-value: 8.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 18 RFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIEE 97
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 98 FDF-CHLTPKKAQQrlwDWMPSDRQCAKSLKAGEtqLFRQVLFTT-HDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQL 175
Cdd:cd19533 81 IDLsGDPDPEGAAQ---QWMQEDLRKPLPLDNDP--LFRHALFTLgDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 176 QEGKDLSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHhlAAKTTATFVKHQLRFSTGILEQIQA 255
Cdd:cd19533 156 LKGRPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARR--APGRSLAFLRRTAELPPELTRTLLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 256 LAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLRE 335
Cdd:cd19533 234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 336 IRPHQKYDAEQILRDLNSIDIHERMYGPILNYKAFDQDLVIDGEKVKTHHISTGPIDDFE-FSFIVQDH-ELIIELRADS 413
Cdd:cd19533 314 LLRHQRYRYEDLRRDLGLTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSiFVYDRDDEsGLRIDFDANP 393
|
410 420
....*....|....*....|....*.
gi 490930577 414 QRYTQDELFNHGQRLTLLLEQALIRP 439
Cdd:cd19533 394 ALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
475-986 |
3.32e-76 |
|
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: 261.67 E-value: 3.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 475 VLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASF 554
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR----RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 555 LPLDLDYPIDRMQMMCEDANPLFVLTtqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqdvAYVIFTSG 634
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVT----------------------------------------------ALILYTSG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 635 STGRPKGVMNTHGSLLNlilshkptiywpVLEAVNERFPDRP-LRAAHTHSFSFDSSWLQVFWM--LWGQELHIFDenmR 711
Cdd:COG0318 111 TTGRPKGVMLTHRNLLA------------NAAAIAAALGLTPgDVVLVALPLFHVFGLTVGLLAplLAGATLVLLP---R 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 712 RDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFvENQHHPSL--ILIGGEAAPLALWQQLNAQ--PALFahNLYGPTE- 786
Cdd:COG0318 176 FDPERVLELIERERVTVLFGVPTMLARLLRHPEF-ARYDLSSLrlVVSGGAPLPPELLERFEERfgVRIV--EGYGLTEt 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 787 YTVDTFRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFvanpfEHGqrMY 865
Cdd:COG0318 253 SPVVTVNPEDPGERRPGsVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-----RDG--WL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 866 RTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSH-RLLGYCVVKD-IELDEkts 943
Cdd:COG0318 326 RTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGeRVVAFVVLRPgAELDA--- 402
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 490930577 944 EQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:COG0318 403 EEL----RAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1542-2031 |
4.93e-68 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 239.41 E-value: 4.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGeqkdlaaiVHPSIATFAFNELFDETKVDLSSYKTTVITPQHP------AYLIYTSGTTGQPKGVMV 1695
Cdd:PRK04813 92 EMIIEVAKPSLIIA--------TEELPLEILGIPVITLDELKDIFATGNPYDFDHAvkgddnYYIIFTSGTTGKPKGVQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1696 SHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:PRK04813 164 SHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 M--LAVFENAATEilssaqrQSLPICRVF--CsGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEE 1850
Cdd:PRK04813 244 FadMCLLDPSFNE-------EHLPNLTHFlfC-GEELPHKTAKKLLERFpSATIYNTYGPTEATVAVTSIEITDEMLDQY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvanpFT-AGQRMYRTGDIARWhADGS 1929
Cdd:PRK04813 316 KRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTfDGQPAYHTGDAGYL-EDGL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPvDID-------QLKKQLAKH 2002
Cdd:PRK04813 391 LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAV-VVPYNKDHKVQYLIAYVVPKEE-DFErefeltkAIKKELKER 468
|
490 500
....*....|....*....|....*....
gi 490930577 2003 LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK04813 469 LMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1676-2027 |
2.47e-64 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 222.93 E-value: 2.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPidaHRDP 1755
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLIQKYQVTTLHFVPSM---LAVFENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTE 1832
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLlarLLKAPESAGYDLSSLR-------ALVSGGAPLPPELLERFEEAPGIKLVNGYGLTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 AAVDVSYMDATLGlhpEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftag 1912
Cdd:cd04433 151 TGGTVATGPPDDD---ARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1913 qrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVD 1991
Cdd:cd04433 223 --WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGvAEAAVVGVPDPEWGERVVAVVVLRPGADLD 300
|
330 340 350
....*....|....*....|....*....|....*.
gi 490930577 1992 IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:cd04433 301 AEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1534-2031 |
1.11e-59 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 213.96 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIgeqkdlaaivhpsiATFAFNELFdetKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGV 1693
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALI--------------VAVSFTDLL---AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHQAIVNRIL----WMqsEYPLSATDTILQKTPctfdvsvweFFWSY----------LVGARLVIAPidahR-DPLAL 1758
Cdd:cd05936 144 MLTHRNLVANALqikaWL--EDLLEGDDVVLAALP---------LFHVFgltvalllplALGATIVLIP----RfRPIGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1759 LSLIQKYQVTTLHFVPSMLAVFENAatEILSSAQRQSLPICrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAvdvs 1838
Cdd:cd05936 209 LKEIRKHRVTIFPGVPTMYIALLNA--PEFKKRDFSSLRLC--ISGGAPLPVEVAERFEELTGVPIVEGYGLTETS---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 ymDATLGLHPEESCVA--IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmy 1916
Cdd:cd05936 281 --PVVAVNPLDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVV----HAISSEQNKANVQlvayLQTTAPVD 1991
Cdd:cd05936 352 RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLyEHPAVAEAAVvgvpDPYSGEAVKAFVV----LKEGASLT 427
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 490930577 1992 IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05936 428 EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
473-986 |
4.66e-58 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 210.52 E-value: 4.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 473 NNVLDIFYEQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQT--VIAGAipRSIDSVVVMLSVLNS 550
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLG----EKLTYGQLKEDSDALAAFIDSLKLPDKSpiIVFGH--MSPEMLATFLGAVKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 551 GASFLPLDLDYPIDRMQMMCEDANPLFVLttqalaqqlpqNIQQLHLDQEGVQTqIRKQDASDIPAENRKFDFQ------ 624
Cdd:PRK04813 76 GHAYIPVDVSSPAERIEMIIEVAKPSLII-----------ATEELPLEILGIPV-ITLDELKDIFATGNPYDFDhavkgd 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLL---NLILSHKPTiywpvleavnerfPDRP--LRAAhthSFSFDsswLQVfwMLW 699
Cdd:PRK04813 144 DNYYIIFTSGTTGKPKGVQISHDNLVsftNWMLEDFAL-------------PEGPqfLNQA---PYSFD---LSV--MDL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 700 ------GQELHIFDENMRRDAFGLVQEIQQRQIDTLDLPPSFcAQM-MTNGLFVEnQHHPSL--ILIGGEAAPLALWQQL 770
Cdd:PRK04813 203 yptlasGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSF-ADMcLLDPSFNE-EHLPNLthFLFCGEELPHKTAKKL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 771 -NAQPALFAHNLYGPTEYTVDTFRAE-----LKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLG 844
Cdd:PRK04813 281 lERFPSATIYNTYGPTEATVAVTSIEitdemLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 845 RADLSAARFVanpFEHGQRMYRTGDLVRWNSaGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIaePINNS 924
Cdd:PRK04813 361 NPEKTAEAFF---TFDGQPAYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PYNKD 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 925 HR---LLGYCVVKDIELDEktSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK04813 435 HKvqyLIAYVVPKEEDFER--EFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1570-2130 |
1.46e-55 |
|
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: 214.54 E-value: 1.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKdlAAIVHPSIA 1649
Cdd:TIGR03443 283 LAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEK--AGTLDQLVR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1650 TFAFNELFDETKV-------------------------DLSSYKTT----VITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:TIGR03443 361 DYIDKELELRTEIpalalqddgslvggsleggetdvlaPYQALKDTptgvVVGPDSNPTLSFTSGSEGIPKGVLGRHFSL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATD--TILQ---KTPCTFDVsvwefFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:TIGR03443 441 AYYFPWMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPA 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLAVFENAATeilssAQRQSLPicRVFCSGEALPT-------ALAKSftehfsCELHNLYGPTEAAVDVSYM-------D 1841
Cdd:TIGR03443 516 MGQLLSAQAT-----TPIPSLH--HAFFVGDILTKrdclrlqTLAEN------VCIVNMYGTTETQRAVSYFeipsrssD 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1842 ATLgLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVD--GELYLAGHQLAMGYLHRADLTASRFVAN------------ 1907
Cdd:TIGR03443 583 STF-LKNLKDVMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNwfvdpshwidld 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1908 --------PFTAG--QRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR-------------------- 1957
Cdd:TIGR03443 662 kennkperEFWLGprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSqhplvrenvtlvrrdkdeep 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1958 -LISGLDVVVHAISSEQNKANV-------QLVAYLQTTAPVdIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRK 2029
Cdd:TIGR03443 742 tLVSYIVPQDKSDELEEFKSEVddeessdPVVKGLIKYRKL-IKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2030 ALPQP-----HLTPSNTEKQYATSAF---EHELTRIFQQIL-NTDQNIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIP 2100
Cdd:TIGR03443 821 ALPFPdtaqlAAVAKNRSASAADEEFtetEREIRDLWLELLpNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELP 900
|
650 660 670
....*....|....*....|....*....|
gi 490930577 2101 IGQLMSHVTIQRLAALLltqERLAEVEQTG 2130
Cdd:TIGR03443 901 LGLIFKSPTIKGFAKEV---DRLKKGEELA 927
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1537-2031 |
1.08e-54 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 202.26 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTAL-----SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLP 1611
Cdd:COG0365 14 CLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1612 I--DLqhPTERIKFMLQDAKSKLVI--------GEQKDLAAIVH------PSIAT----------------FAFNELFDE 1659
Cdd:COG0365 94 VfpGF--GAEALADRIEDAEAKVLItadgglrgGKVIDLKEKVDealeelPSLEHvivvgrtgadvpmegdLDWDELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1660 TKVDLSSYKTTvitPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILW-MQSEYPLSATDTILqktpCTFDVSvWEFFWSY 1738
Cdd:COG0365 172 ASAEFEPEPTD---ADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGDVFW----CTADIG-WATGHSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 LV------GARLVI---APIdaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpicRVFCS-GEAL 1808
Cdd:COG0365 244 IVygpllnGATVVLyegRPD--FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSL---RLLGSaGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1809 PTALAKSFTEHFSCELHNLYGPTEAavdVSYMDATLGLHPeescV---AIGYPVWNTQLYILDQYLRPVPVGVDGELYLA 1885
Cdd:COG0365 319 NPEVWEWWYEAVGVPIVDGWGQTET---GGIFISNLPGLP----VkpgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1886 GHQLAM--GYLHRADLTASRFvanpFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-L 1962
Cdd:COG0365 392 GPWPGMfrGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAvA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577 1963 DVVVhaISSEQNKANVQLVAYLQTTAPVD-----IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:COG0365 468 EAAV--VGVPDEIRGQVVKAFVVLKPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1533-2031 |
7.27e-54 |
|
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: 198.47 E-value: 7.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAKSKLVI-------------GEQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVIT-PQHP- 1677
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVtsserldllhpalPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDAdPPHPv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 -----AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAH 1752
Cdd:TIGR03098 161 idsdmAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 RDplaLLSLIQKYQVTTLHFVPSMLA-VFENAATEILSSAQRqslpicRVFCSGEALPTALAKSFTEHFS-CELHNLYGP 1830
Cdd:TIGR03098 241 RD---VLKALEKHGITGLAAVPPLWAqLAQLDWPESAAPSLR------YLTNSGGAMPRATLSRLRSFLPnARLFLMYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1831 TEaAVDVSYMD-ATLGLHPEescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANP- 1908
Cdd:TIGR03098 312 TE-AFRSTYLPpEEVDRRPD----SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPp 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1909 FTAGQRMYRT----GDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQ---QLRLISglDVVVHAISSEQNKANVQLV 1981
Cdd:TIGR03098 387 FPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEvayATGLVA--EAVAFGVPDPTLGQAIVLV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 490930577 1982 AYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:TIGR03098 465 VTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1097-1519 |
7.98e-54 |
|
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: 196.40 E-value: 7.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1097 NSTILPLLPLQKGMLFLSQVE-NQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPV-FIYSLHPT 1174
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEpHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVqVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1175 QAWPVQFCSVTPDLLEQTIQEA----LQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ 1250
Cdd:pfam00668 81 ELEIIDISDLSESEEEEAIEAFiqrdLQSPFDLEKG-PLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 QT--NQQLPVLE-HSYETVIKALSGR----DHETSKVIWQRDLA-DLQPLILFNQAQQAVQ------ETSYRLSAELGAK 1316
Cdd:pfam00668 160 QLlkGEPLPLPPkTPYKDYAEWLQQYlqseDYQKDAAYWLEQLEgELPVLQLPKDYARPADrsfkgdRLSFTLDEDTEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1317 LQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQ 1396
Cdd:pfam00668 240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1397 QLHVEHLEHDGLGL------SAIQQLIAQGNLFDSLLVVENYPDnQYLQQKLGDAAISKLTNRGYSH----YPLALLVIP 1466
Cdd:pfam00668 318 EDLLSAEPHQGYPFgdlvndLRLPRDLSRHPLFDPMFSFQNYLG-QDSQEEEFQLSELDLSVSSVIEeeakYDLSLTASE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1467 DH-QIELLLE-QRGVIDQP--EHFLERMIQLIEIALNEPETSLSHYRLQLAEEHDLI 1519
Cdd:pfam00668 397 RGgGLTIKIDyNTSLFDEEtiERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1526-2035 |
1.60e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 197.72 E-value: 1.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1526 QYYvrQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK06187 2 QDY--PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQK--DLAAIVHPSIAT---------------FAFNELFDETKVDLSS-Y 1667
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILPQLPTvrtvivegdgpaaplAPEVGEYEELLAAASDtF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1668 KTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCtFDVSVWEffWSYL---VGARL 1744
Cdd:PRK06187 160 DFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWG--LPYLalmAGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 VIapidAHR-DPLALLSLIQKYQVTTLHFVPSMLavfenaaTEILSS--AQRQSLPICRVFCSG-EALPTALAKSFTEHF 1820
Cdd:PRK06187 237 VI----PRRfDPENLLDLIETERVTFFFAVPTIW-------QMLLKAprAYFVDFSSLRLVIYGgAALPPALLREFKEKF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1821 SCELHNLYGPTEAAVDVSYmdatlgLHPEESCVAI-------GYPVWNTQLYILDQYLRPVPV--GVDGELYLAGHQLAM 1891
Cdd:PRK06187 306 GIDLVQGYGMTETSPVVSV------LPPEDQLPGQwtkrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISG----LDVVVH 1967
Cdd:PRK06187 380 GYWNRPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELED---ALYGhpavAEVAVI 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1968 AISSEQNKANVqlVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK06187 450 GVPDEKWGERP--VAVvvLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1538-2028 |
3.66e-53 |
|
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: 193.98 E-value: 3.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHP 1617
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 TERIKFMLQDAKSKLVIGEqkdlaaivhpsiatfafnelfdetkvdlssykttvitpqhPAYLIYTSGTTGQPKGVMVSH 1697
Cdd:cd17631 81 PPEVAYILADSGAKVLFDD----------------------------------------LALLMYTSGTTGRPKGAMLTH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 QAIVNRILWMQSEYPLSATDTILQKTPcTFDVSVWEFFW--SYLVGARLVIAPidaHRDPLALLSLIQKYQVTTLHFVPS 1775
Cdd:cd17631 121 RNLLWNAVNALAALDLGPDDVLLVVAP-LFHIGGLGVFTlpTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLAVF---ENAATEILSSAQRqslpicrVFCSGEALPTALAKSFTEhFSCELHNLYGPTEAAVDVSYMDATlglHPEESC 1852
Cdd:cd17631 197 MIQALlqhPRFATTDLSSLRA-------VIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPE---DHRRKL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1853 VAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQY 1932
Cdd:cd17631 266 GSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1933 IGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd17631 339 VDRKKDMIISGGENVYPAEVEDVLyEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKS 418
|
490
....*....|....*..
gi 490930577 2012 YMLVEQFPLSHNGKLDR 2028
Cdd:cd17631 419 VEFVDALPRNATGKILK 435
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1558-2031 |
1.50e-52 |
|
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: 192.69 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI--G 1635
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLqnK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQKDLAAIVHPSIATFAfnelfdetkvdlssykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSA 1715
Cdd:cd17654 97 ELDNAPLSFTPEHRHFN------------------IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1716 TDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALL-SLIQKYQVTTLHFVPSMLAVF--ENAATEILSSAq 1792
Cdd:cd17654 159 EDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLAdILFKRHRITVLQATPTLFRRFgsQSIKSTVLSAT- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1793 rQSLPICRVfcSGEALPTALAKSFTEHFSCELH--NLYGPTEaavdVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQy 1870
Cdd:cd17654 238 -SSLRVLAL--GGEPFPSLVILSSWRGKGNRTRifNIYGITE----VSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQ- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1871 lrpVPVGVDGELYLAGhqLAMGYLHRADLTasrfvanpfTAGQRMYRTGDIARwHADGSIQYIGRADDQLKIRGQRIELG 1950
Cdd:cd17654 310 ---NGSEGTGQVFLGG--LNRVCILDDEVT---------VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1951 EIEQQLRLISGLDVVVHAISSEQnkanvQLVAYLqTTAPVDiDQLKKQLAKH-LPAYMVPTHYMLVEQFPLSHNGKLDRK 2029
Cdd:cd17654 375 LIQQVIESCLGVESCAVTLSDQQ-----RLIAFI-VGESSS-SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKS 447
|
..
gi 490930577 2030 AL 2031
Cdd:cd17654 448 EL 449
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1100-1500 |
6.92e-52 |
|
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: 189.44 E-value: 6.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLfLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVfiyslhpTQ---- 1175
Cdd:cd19542 1 IYPCTPMQEGML-LSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTF-------LQvvlk 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1176 --AWPVQFCSVTPDLLEQTIQEALQQPIHLDQPygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYqqtN 1253
Cdd:cd19542 73 slDPPIEEVETDEDSLDALTRDLLDDPTLFGQP--PHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY---N 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1254 QQLPVLEHSYETVIKALSGRDHETSKVIWQRDLADLQPLILFNQAQQAVQETSYRLSAELGAKLQHKLRQQGITLNVFMQ 1333
Cdd:cd19542 148 GQLLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1334 MIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAI 1413
Cdd:cd19542 228 AAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1414 QQLIAQ---GNLFDSLLVVENYPDNQyLQQKLGDAAISKLTNRGYSHYPLALLVIPDH-QIELLLEQRG-VIDQPehFLE 1488
Cdd:cd19542 308 QRALGLwpsGTLFNTLVSYQNFEASP-ESELSGSSVFELSAAEDPTEYPVAVEVEPSGdSLKVSLAYSTsVLSEE--QAE 384
|
410
....*....|..
gi 490930577 1489 RMIQLIEIALNE 1500
Cdd:cd19542 385 ELLEQFDDILEA 396
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1553-2026 |
7.95e-51 |
|
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: 188.58 E-value: 7.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1553 DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKL 1632
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 VIGEQKDLAAI-----------------VHPSIATFAFNELFDETKVDLSSYKTTVIT-PQHPAYLIYTSGTTGQPKGVM 1694
Cdd:cd05911 86 IFTDPDGLEKVkeaakelgpkdkiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRIL--WMQSEYPLSATDTILQKTPctfdvsvweFFWSY---------LVGARLVIAPIDahrDPLALLSLIQ 1763
Cdd:cd05911 166 LSHRNLIANLSqvQTFLYGNDGSNDVILGFLP---------LYHIYglfttlaslLNGATVIIMPKF---DSELFLDLIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSYMda 1842
Cdd:cd05911 234 KYKITFLYLVPPIAAAL--AKSPLLDKYDLSSLR--VILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVN-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 TLGLHPEESCvaiGYPVWNTQLYILDQYLRP-VPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDI 1921
Cdd:cd05911 308 PDGDDKPGSV---GRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVV----HAISSEQNKANVQLVAYLQTTApvdiDQLK 1996
Cdd:cd05911 379 GYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVaDAAVigipDEVSGELPRAYVVRKPGEKLTE----KEVK 454
|
490 500 510
....*....|....*....|....*....|....*.
gi 490930577 1997 KQLAKHlpaymVPTHYML------VEQFPLSHNGKL 2026
Cdd:cd05911 455 DYVAKK-----VASYKQLrggvvfVDEIPKSASGKI 485
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1546-2031 |
8.83e-50 |
|
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: 185.98 E-value: 8.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKF 1623
Cdd:cd05926 1 PDAPALvvPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1624 MLQDAKSKLVI----GEQKDLAAIVHPSIAT-------------FAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGT 1686
Cdd:cd05926 81 YLADLGSKLVLtpkgELGPASRAASKLGLAIlelaldvgvliraPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1687 TGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDVS--VWEFFWSYLVGARLVIAP-IDAHRdplaLLSLIQ 1763
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMP-LFHVHglVASLLSTLAAGGSVVLPPrFSAST----FWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLAVFENAATEILSSAqRQSLPICRvfCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDAT 1843
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNRPEPNPESP-PPKLRFIR--SCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1844 LGLHPEEScvaIGYPVwNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIAR 1923
Cdd:cd05926 313 PGPRKPGS---VGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1924 WHADGSIQYIGRADDqLKIR-GQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAK 2001
Cdd:cd05926 383 LDADGYLFLTGRIKE-LINRgGEKISPLEVDGVLLSHPAvLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRK 461
|
490 500 510
....*....|....*....|....*....|
gi 490930577 2002 HLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05926 462 HLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
211-1105 |
1.62e-49 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 194.90 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 211 FWKAYCEDLPspISLSTHHLAAKTTATFVKHQLRFstgileQIQALAAQTKLALNDMMMSLSLH--YIYKMTDKAELV-- 286
Cdd:TIGR03443 1 RWSERLDNPT--LSVLPHDYLRPANNRLVEATYSL------QLPSAEVTAGGGSTPFIILLAAFaaLVYRLTGDEDIVlg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 287 -----NGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVS---LAQHVQEQLREIRPhqkydaeqilrdlnsidihe 358
Cdd:TIGR03443 73 tssnkSGRPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPfdeLSEHIQAAKKLERT-------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 359 rmygPILNYKAFdqdlvIDGEKVKTHHISTGPIDDFEFSFIVQDHELIIELRADSQRYTQDELFNHGQRLTLLLEQALIR 438
Cdd:TIGR03443 133 ----PPLFRLAF-----QDAPDNQQTTYSTGSTTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 439 PEQPCSNFNITTPQELTALtqsgigprvshPEQYNN---------VLDIFYEQVKKYPERTAIV---SGERPNLQHLSF- 505
Cdd:TIGR03443 204 PDEPIGKVSLITPSQKSLL-----------PDPTKDldwsgfrgaIHDIFADNAEKHPDRTCVVetpSFLDPSSKTRSFt 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 506 -AELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANP--LFVLTTQ 582
Cdd:TIGR03443 273 yKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPraLIVIEKA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQQLPQN-----------IQQLHLDQEG-VQTQIRKQDASDIPAENRKFDFQDVAYVI---------FTSGSTGRPKG 641
Cdd:TIGR03443 353 GTLDQLVRDyidkelelrteIPALALQDDGsLVGGSLEGGETDVLAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 642 VMNTHGSLlnlilshkpTIYWPvleavnerfpdrplraahthsfsfdsswlqvfWMlwGQELHIfDENmrrDAFGLVQEI 721
Cdd:TIGR03443 433 VLGRHFSL---------AYYFP--------------------------------WM--AKRFGL-SEN---DKFTMLSGI 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 722 Q----QRQIDTldlPPSFCAQMmtnglfvenqHHPSLILIGGEAApLALW----------------QQLNAQ-----PAL 776
Cdd:TIGR03443 466 AhdpiQRDMFT---PLFLGAQL----------LVPTADDIGTPGR-LAEWmakygatvthltpamgQLLSAQattpiPSL 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 777 -------------------------FAHNLYGPTE-------YTV------DTFRAELKQtarpVI--GNPIGNTQAYVL 816
Cdd:TIGR03443 532 hhaffvgdiltkrdclrlqtlaenvCIVNMYGTTEtqravsyFEIpsrssdSTFLKNLKD----VMpaGKGMKNVQLLVV 607
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 817 DRH--LQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPF------------------EHGQ----RMYRTGDLVR 872
Cdd:TIGR03443 608 NRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperEFWLgprdRLYRTGDLGR 687
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 873 WNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALS----ILTNV--------ESAVVIAE--PINNSHRLLGYCVVKDiel 938
Cdd:TIGR03443 688 YLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSqhplVRENVtlvrrdkdEEPTLVSYivPQDKSDELEEFKSEVD--- 764
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 939 DEKTSEQ----------LSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP---QIRA----HSRMAE-- 999
Cdd:TIGR03443 765 DEESSDPvvkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaQLAAvaknRSASAAde 844
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1000 --TPEQQLLCQITASVL--KLDAIGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMAPQLTRL-DEQ 1073
Cdd:TIGR03443 845 efTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTIKGFAKEVDRLkKGE 924
|
1050 1060 1070
....*....|....*....|....*....|...
gi 490930577 1074 QAAVSKPLFSADLEQKVQEKYGKNS-TILPLLP 1105
Cdd:TIGR03443 925 ELADEGDSEIEEEETVLELDYAKDAkTLVDSLP 957
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1567-2031 |
2.03e-48 |
|
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: 180.71 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1567 VCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA----YLPIDLQHPTERIKFMLQDAKSKLVIGEQK---- 1638
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGaadr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1639 -DLAAIVHPSIATFAFNELFDETKVDLSSYkttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05922 83 lRDALPASPDPGTVLDADGIRAARASAPAH---EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TILQKTPCTFDVSVWEFFWSYLVGARLVIAPidAHRDPLALLSLIQKYQVTTLHFVPSMLavfenaatEILSSAQRQ--S 1795
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTN--DGVLDDAFWEDLREHGATGLAGVPSTY--------AMLTRLGFDpaK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 LPICRVFC-SGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEEScvaIGYPVWNTQLYILDQYLRP 1873
Cdd:cd05922 230 LPSLRYLTqAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPERILEKPGS---IGLAIPGGEFEILDDDGTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1874 VPVGVDGELYLAGHQLAMGYLHRadltaSRFVANPFTAGQRMYrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:cd05922 307 TPPGEPGEIVHRGPNVMKGYWND-----PPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIE 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1954 QQLRLIsGLDVVVHAISSEqNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05922 381 AAARSI-GLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
625-982 |
3.00e-48 |
|
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: 176.71 E-value: 3.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEAVNERFPDRPLraaHTHSFSFDSSWLQVFWML-WGQEL 703
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA--------LAASGGLTEGDVFL---STLPLFHIGGLFGLLGALlAGGTV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 704 HIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFvENQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNL 781
Cdd:cd04433 70 VLLP---KFDPEAALELIEREKVTILLGVPTLLARLLKAPES-AGYDLSSLraLVSGGAPLPPELLERFEEAPGIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 782 YGPTE--YTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANpfe 859
Cdd:cd04433 146 YGLTEtgGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 860 hgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGY----CVVKD 935
Cdd:cd04433 223 ----WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVP----DPEWGErvvaVVVLR 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490930577 936 iELDEKTSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:cd04433 295 -PGADLDAEELRA----HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1548-2034 |
9.14e-47 |
|
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: 177.71 E-value: 9.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1548 QTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQD 1627
Cdd:cd17647 11 PSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1628 AKSKLVIGEQKdLAAIVHP-SIATFAFnelfdetkvdlssykttvitpqhpayliyTSGTTGQPKGVMVSHQAIVNRILW 1706
Cdd:cd17647 91 AKPRGLIVIRA-AGVVVGPdSNPTLSF-----------------------------TSGSEGIPKGVLGRHFSLAYYFPW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1707 MQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATE 1786
Cdd:cd17647 141 MAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1787 ilssaqrQSLPICRVFCSGEALPT---ALAKSFTEhfSCELHNLYGPTEAAVDVSYMDATLG------LHPEESCVAIGY 1857
Cdd:cd17647 221 -------PFPKLHHAFFVGDILTKrdcLRLQTLAE--NVRIVNMYGTTETQRAVSYFEVPSRssdptfLKNLKDVMPAGR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1858 PVWNTQLYILDQYLRPVPVGVD--GELYLAGHQLAMGYLHRADLTASRFVAN--------------------PFTAG--Q 1913
Cdd:cd17647 292 GMLNVQLLVVNRNDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGprD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1914 RMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrlISGLDVVVHAISSEQNKANVQ--LVAYL------- 1984
Cdd:cd17647 372 RLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH---ISQHPLVRENITLVRRDKDEEptLVSYIvprfdkp 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1985 ------QTTAPVD----------------IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:cd17647 449 ddesfaQEDVPKEvstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1100-1476 |
1.14e-44 |
|
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: 167.86 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSqVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSELAEEPVFIYSLHPTQAWpv 1179
Cdd:cd19545 1 IYPCTPLQEGLMALT-ARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISW-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 qfcsVTPDLLEQTIQEALQQPIHLDQPygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQLPVl 1259
Cdd:cd19545 78 ----TESTSLDEYLEEDRAAPMGLGGP--LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1260 ehSYETVIKALSGRDHETSKVIWQRDLADLQPLIlFNQAQqavqetSYRLSAELGAKLQHKLR-----QQGITLNVFMQM 1334
Cdd:cd19545 151 --PFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAV-FPPLP------SSRYQPRPDATLEHSISlpssaSSGVTLATVLRA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1335 IWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEHLEHDGLGLSAIQ 1414
Cdd:cd19545 222 AWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1415 QLI---AQGNLFDSLLVVEnyPDNQYLQQKLGDAAISKLTNR--GYSHYPLALL-----------------VIPDHQIEL 1472
Cdd:cd19545 302 RLGpdaRAACNFQTLLVVQ--PALPSSTSESLELGIEEESEDleDFSSYGLTLEcqlsgsglrvrarydssVISEEQVER 379
|
....
gi 490930577 1473 LLEQ 1476
Cdd:cd19545 380 LLDQ 383
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1558-2031 |
4.32e-43 |
|
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: 164.43 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 KDlaaivhpsiatfafnelfdetkvdlssykttvitpqhPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05972 81 ED-------------------------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TILqktpCTFDVSVWEFFWSYLVGARLVIAPIDAHR----DPLALLSLIQKYQVTTLHFVPsmlAVFENAATEILSSAQR 1793
Cdd:cd05972 124 IHW----NIADPGWAKGAWSSFFGPWLLGATVFVYEgprfDAERILELLERYGVTSFCGPP---TAYRMLIKQDLSSYKF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSyMDATLGLHPEescvAIGYPVWNTQLYILDQYLRP 1873
Cdd:cd05972 197 SHLRL--VVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVG-NFPDMPVKPG----SMGRPTPGYDVAIIDDDGRE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1874 VPVGVDGEL--YLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGE 1951
Cdd:cd05972 270 LPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1952 IEQQLR-----LISGLDVVVHAISSEQNKANVQLVAYLQTTaPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:cd05972 343 VESALLehpavAEAAVVGSPDPVRGEVVKAFVVLTSGYEPS-EELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
....*
gi 490930577 2027 DRKAL 2031
Cdd:cd05972 422 RRVEL 426
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1557-2032 |
4.95e-43 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 164.00 E-value: 4.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIge 1636
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 qkdlaaivhpsiatfafnelfdetkVDlssykttvitpqhPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05934 81 -------------------------VD-------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGED 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTPcTF--DVSVWEFFWSYLVGARLVIAPidahR-DPLALLSLIQKYQVTTLHFVPSMLAVFenAATEIlsSAQR 1793
Cdd:cd05934 123 DVYLTVLP-LFhiNAQAVSVLAALSVGATLVLLP----RfSASRFWSDVRRYGATVTNYLGAMLSYL--LAQPP--SPDD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSLPIcRVFCSGEALPtALAKSFTEHFSCELHNLYGPTEAAVdvsymdATLGLHPEESCV-AIGYPVWNTQLYILDQYLR 1872
Cdd:cd05934 194 RAHRL-RAAYGAPNPP-ELHEEFEERFGVRLLEGYGMTETIV------GVIGPRDEPRRPgSIGRPAPGYEVRIVDDDGQ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1873 PVPVGVDGELYL---AGHQLAMGYLHRADLTASRFvANpftagqRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIEL 1949
Cdd:cd05934 266 ELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RN------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1950 GEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd05934 339 AEVERAILRHPAvREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAK 418
|
....
gi 490930577 2029 KALP 2032
Cdd:cd05934 419 AQLR 422
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1558-2026 |
7.41e-43 |
|
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: 164.09 E-value: 7.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSK-LVIGE 1636
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKvFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 ---QKDLAAIvhpsiatfafnelfdetkvdlssykttvitPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPL 1713
Cdd:cd05903 82 rfrQFDPAAM------------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1714 SATDTILQKTPCT-FDVSVWEFFWSYLVGARLVIAPIdahRDPLALLSLIQKYQVTTL----HFVPSMLAVFENAATEil 1788
Cdd:cd05903 132 GPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEP-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1789 ssaqrqsLPICRVF-CSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLglhPEESCVAIGYPVWNTQLYIL 1867
Cdd:cd05903 207 -------LSRLRTFvCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAP---EDRRLYTDGRPLPGVEIKVV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 DQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDqLKIR-GQR 1946
Cdd:cd05903 277 DDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRSKD-IIIRgGEN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1947 IELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQL-----KKQLAKHlpayMVPTHYMLVEQFPL 2020
Cdd:cd05903 349 IPVLEVEDLLLGHPGvIEAAVVALPDERLGERACAVVVTKSGALLTFDELvayldRQGVAKQ----YWPERLVHVDDLPR 424
|
....*.
gi 490930577 2021 SHNGKL 2026
Cdd:cd05903 425 TPSGKV 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1548-2031 |
1.00e-42 |
|
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: 163.40 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1548 QTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID-LQHPTErIKFMLQ 1626
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINpLLHPDD-YAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1627 DAKSKLVIGEQKDLAaivhpsiatfafnelfdetkvdlssykttvitpqhpaYLIYTSGTTGQPKGVMVSHQAIVNRILW 1706
Cdd:cd05919 80 DCEARLVVTSADDIA-------------------------------------YLLYSSGTTGPPKGVMHAHRDPLLFADA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1707 MQSEY-PLSATDTILQKTPCTFDV----SVWeFFWSylVGARLVIAPidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFE 1781
Cdd:cd05919 123 MAREAlGLTPGDRVFSSAKMFFGYglgnSLW-FPLA--VGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1782 NAATeiLSSAQRQSLPICrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEaaVDVSYMDATLGLHPEESCvaiGYPVWN 1861
Cdd:cd05919 198 DSCA--GSPDALRSLRLC--VSAGEALPRGLGERWMEHFGGPILDGIGATE--VGHIFLSNRPGAWRLGST---GRPVPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLK 1941
Cdd:cd05919 269 YEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLK 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1942 IRGQRIELGEIEQqlrLISGLDVVVHA--ISSEQNKANVQLVAYLQTTAPVDIDQ-----LKKQLAKHLPAYMVPTHYML 2014
Cdd:cd05919 342 VGGQWVSPVEVES---LIIQHPAVAEAavVAVPESTGLSRLTAFVVLKSPAAPQEslardIHRHLLERLSAHKVPRRIAF 418
|
490
....*....|....*..
gi 490930577 2015 VEQFPLSHNGKLDRKAL 2031
Cdd:cd05919 419 VDELPRTATGKLQRFKL 435
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1533-2031 |
1.47e-42 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 164.60 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSD--ENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYL 1610
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1611 PIDLQHPTERIKFMLQDAKSKLVIgeqKDLAAIVHPSIATFAFNELFDETKVDLS-------SYKTTVITPQHPAYLIYT 1683
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAV---IAVDAQVMDAIFQSGVRVLALSDLVGLGepesagpLIEDPPREPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1684 SGTTGQPKGVMVSHQAIVNRILWM--QSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIDAhrDPLALLSL 1761
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADALKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1762 IQKYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMD 1841
Cdd:cd05923 237 IEQERVTSLFATPTHLDAL--AAAAEFAGLKLSSLR--HVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1842 ATLGlhpeescvAIGYPVWNTQLYILDQYLRPV---PVGVDGELY--LAGHQLAMGYLHRADLTASRFVanpftagQRMY 1916
Cdd:cd05923 313 ARTG--------TEMRPGFFSEVRIVRIGGSPDealANGEEGELIvaAAADAAFTGYLNQPEATAKKLQ-------DGWY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-VVVHAISSEQNKANVQLVAYLQtTAPVDIDQL 1995
Cdd:cd05923 378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTeVVVIGVADERWGQSVTACVVPR-EGTLSADEL 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 490930577 1996 KK-QLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05923 457 DQfCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1537-2031 |
1.84e-42 |
|
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: 164.46 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQ-----------KDLAAIVH--------PSIATFAFNELFDETKVDLSSYKTtviTPQHP 1677
Cdd:cd05959 89 TPDDYAYYLEDSRARVVVVSGelapvlaaaltKSEHTLVVlivsggagPEAGALLLAELVAAEAEQLKPAAT---HADDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVnrilWMQSEYplsaTDTILQKTPCTFDVSVWEFFWSY----------LVGARLVIA 1747
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIY----WTAELY----ARNVLGIREDDVCFSAAKLFFAYglgnsltfplSVGATTVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 PidAHRDPLALLSLIQKYQVTTLHFVP----SMLAVfENAATEILSsaqrqSLPICrvFCSGEALPTALAKSFTEHFSCE 1823
Cdd:cd05959 238 P--ERPTPAAVFKRIRRYRPTVFFGVPtlyaAMLAA-PNLPSRDLS-----SLRLC--VSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1824 LHNLYGPTEAavdvsymdatlgLH------PEESCV-AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHR 1896
Cdd:cd05959 308 ILDGIGSTEM------------LHiflsnrPGRVRYgTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1897 ADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlRLISGLDVVVHA-ISSEQNK 1975
Cdd:cd05959 376 RDKTRDTFQGE-------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVES--ALVQHPAVLEAAvVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1976 ANVQLVAYL-----QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05959 447 GLTKPKAFVvlrpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1559-2031 |
1.32e-40 |
|
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: 157.21 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1559 SFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIgeqk 1638
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1639 dlaaivhpsiatfafnelfdetkVDLSSykttvitpqHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDT 1718
Cdd:cd05971 84 -----------------------TDGSD---------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1719 ILQKTPCT-------FDVsvweFFWSYLVGArlviaPIDAHR----DPLALLSLIQKYQVTTLHFVPSMLAVFEnAATEI 1787
Cdd:cd05971 132 DLYWTPADwawigglLDV----LLPSLYFGV-----PVLAHRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMR-QQGEQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1788 LSSAQRQSLPIcrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEescvAIGYPVWNTQLYIL 1867
Cdd:cd05971 202 LKHAQVKLRAI---ATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPG----SMGKPIPGHRVAIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 DQYLRPVPVGVDGELYLAGHQLAM--GYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQ 1945
Cdd:cd05971 275 DDNGTPLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSGY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1946 RIELGEIEQQL-RLISGLDVVV----HAISSEQNKANVQLVAylqttAPVDIDQLKKQLAKH----LPAYMVPTHYMLVE 2016
Cdd:cd05971 348 RIGPAEIEECLlKHPAVLMAAVvgipDPIRGEIVKAFVVLNP-----GETPSDALAREIQELvktrLAAHEYPREIEFVN 422
|
490
....*....|....*
gi 490930577 2017 QFPLSHNGKLDRKAL 2031
Cdd:cd05971 423 ELPRTATGKIRRREL 437
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1547-2031 |
3.74e-40 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 155.91 E-value: 3.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1547 EQTALSDENHQLSFSEVRLQVCALAQQLQRAG-VQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFML 1625
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1626 QDAKSKLVIgeqkDLAAIvhpsiatfafnelfdetkvdlssykttvitpqhpaylIYTSGTTGQPKGVMVSHQAIVNRIL 1705
Cdd:cd05941 81 TDSEPSLVL----DPALI-------------------------------------LYTSGTTGRPKGVVLTHANLAANVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1706 WMQSEYPLSATDTILQKTP------------CTFdvsvweffwsyLVGARLVIAPIDahrDPLALLSLIQKYQVTTLHFV 1773
Cdd:cd05941 120 ALVDAWRWTEDDVLLHVLPlhhvhglvnallCPL-----------FAGASVEFLPKF---DPKEVAISRLMPSITVFMGV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PSM----LAVFENAATEIlSSAQRQSLPICRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTEAAvdvsyMDATLGLHP 1848
Cdd:cd05941 186 PTIytrlLQYYEAHFTDP-QFARAAAAERLRLMVSGSAaLPVPTLEEWEAITGHTLLERYGMTEIG-----MALSNPLDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCVAIGYPVWNTQLYILDQ-YLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHAD 1927
Cdd:cd05941 260 ERRPGTVGMPLPGVQARIVDEeTGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1928 GSIQYIGR-ADDQLKIRGQRIELGEIEQQLRLISGLD--VVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLP 2004
Cdd:cd05941 334 GYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSecAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLA 413
|
490 500
....*....|....*....|....*..
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1528-2031 |
4.23e-40 |
|
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: 156.72 E-value: 4.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1528 YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:cd05920 11 YWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 ayLPIdLQHPTER---IKFMLQDAKSKlvigeqkdlAAIVHPSIATFAFNELFDETKVDlssykttviTPQhPAYLIYTS 1684
Cdd:cd05920 91 --VPV-LALPSHRrseLSAFCAHAEAV---------AYIVPDRHAGFDHRALARELAES---------IPE-VALFLLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1685 GTTGQPKGVMVSHQaivnrilwmQSEYPLSATDTILQKTPCT-----------FDVSVWEFFWSYLVGARLVIAPiDAhr 1753
Cdd:cd05920 149 GTTGTPKLIPRTHN---------DYAYNVRASAEVCGLDQDTvylavlpaahnFPLACPGVLGTLLAGGRVVLAP-DP-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEilSSAQRQSLPICRVfcSGEALPTALAKSFTEHFSCELHNLYGPTEA 1833
Cdd:cd05920 217 SPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQV--GGARLSPALARRVPPVLGCTLQQVFGMAEG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1834 AVDVSYMDatlglHPEESCVAI-GYPVW-NTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFta 1911
Cdd:cd05920 293 LLNYTRLD-----DPDEVIIHTqGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1912 gqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTaPV 1990
Cdd:cd05920 366 ----YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVhDAAVVAMPDELLGERSCAFVVLRDP-PP 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 490930577 1991 DIDQLKKQL-AKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05920 441 SAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1100-1501 |
4.30e-40 |
|
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: 155.30 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSqvENQS-------NYNAFTRLSLNGDidpvRLQQALITVLKRHPQLGGHFDseLAEEPVFIYSLH 1172
Cdd:cd19536 1 MYPLSSLQEGMLFHS--LLNPggsvylhNYTYTVGRRLNLD----LLLEALQVLIDRHDILRTSFI--EDGLGQPVQVVH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1173 PTQAWPVQFCSVTP-DLLEQTIQEALQQPIHLDQPYG---LIRATLIQHAP-EQSELLIMVHHLLTDGWSTPLFLQDFIK 1247
Cdd:cd19536 73 RQAQVPVTELDLTPlEEQLDPLRAYKEETKIRRFDLGrapLVRAALVRKDErERFLLVISDHHSILDGWSLYLLVKEILA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1248 AYQQTNQQLPVLE---HSYETVIK-ALSGRDHETSKVIWQRDL--ADLQPLILFNQAQQA--VQETSYRLSAELGAKLQH 1319
Cdd:cd19536 153 VYNQLLEYKPLSLppaQPYRDFVAhERASIQQAASERYWREYLagATLATLPALSEAVGGgpEQDSELLVSVPLPVRSRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1320 KLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNmQQTLWEQLPQLQQLH 1399
Cdd:cd19536 233 LAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1400 VEHLEHDGLGLSAIQQLIAQGNLFDSLLVVENYPDNQYLQQKLGDAAIS--KLTNRGYSHYPLALLVIPdHQIELLLE-- 1475
Cdd:cd19536 312 LESLSHEQVPLADIQRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRrgLLFSEFKSNYDVNLSVLP-KQDRLELKla 390
|
410 420
....*....|....*....|....*....
gi 490930577 1476 -QRGVID--QPEHFLERMIQLIEIALNEP 1501
Cdd:cd19536 391 yNSQVLDeeQAQRLAAYYKSAIAELATAP 419
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
41-458 |
1.11e-39 |
|
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: 154.80 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 41 YTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELN-NQVQFQIEEFDFCHLTPKKAQQRLWDWMPSD 119
Cdd:pfam00668 27 YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVIlEERPFELEIIDISDLSESEEEEAIEAFIQRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 120 RQcaKSLKAGETQLFRQVLFT-THDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPFIGVNEVISERQA 198
Cdd:pfam00668 107 LQ--SPFDLEKGPLFRAGLFRiAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGEPLPLPPKTPYKDYAEWLQQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 199 YENSHQFKIDQAFWKAYCEDLPSPISLSTHHlAAKTTATFVKHQLRFST--GILEQIQALAAQTKLALNDMMMSLSLHYI 276
Cdd:pfam00668 185 YLQSEDYQKDAAYWLEQLEGELPVLQLPKDY-ARPADRSFKGDRLSFTLdeDTEELLRKLAKAHGTTLNDVLLAAYGLLL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 277 YKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNS--I 354
Cdd:pfam00668 264 SRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRLprD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 355 DIHERMYGPILNYKAFDQDLVIDGE--------KVKTHHISTGPiddFEFSFIVQDHE--LIIELRADSQRYTQDELFNH 424
Cdd:pfam00668 344 LSRHPLFDPMFSFQNYLGQDSQEEEfqlseldlSVSSVIEEEAK---YDLSLTASERGggLTIKIDYNTSLFDEETIERF 420
|
410 420 430
....*....|....*....|....*....|....
gi 490930577 425 GQRLTLLLEQALIRPEQPCSNFNITTPQELTALT 458
Cdd:pfam00668 421 AEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
469-986 |
1.84e-39 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 156.81 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 469 PEQYN---NVLDifyEQVKKYPERTAIVS-GERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVM 544
Cdd:COG0365 5 GGRLNiayNCLD---RHAEGRGDKVALIWeGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 545 L---------SVLNSGasFLPLDLdypIDRMqmmcEDANPLFVLTT----------------QALAQQLPQNIQQLHLDQ 599
Cdd:COG0365 82 LacarigavhSPVFPG--FGAEAL---ADRI----EDAEAKVLITAdgglrggkvidlkekvDEALEELPSLEHVIVVGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 600 EGVQT---------QIRKQDASDIPAENRKFDfqDVAYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvleavne 670
Cdd:COG0365 153 TGADVpmegdldwdELLAAASAEFEPEPTDAD--DPLFILYTSGTTGKPKGVVHTHGGYL-------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 671 rfpdrpLRAAHTHSFSFDsswLQ---VFW-------------MLWGQELH-----IFDEN-MRRDAFGLVQEIQQRQIDT 728
Cdd:COG0365 211 ------VHAATTAKYVLD---LKpgdVFWctadigwatghsyIVYGPLLNgatvvLYEGRpDFPDPGRLWELIEKYGVTV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 729 LDLPPSFCAQMMTNGLFVENQHHPS---LILIGGEAAPLALWQQLNAQPALFAHNLYGPTEytvdtfraelkqTARPVIG 805
Cdd:COG0365 282 FFTAPTAIRALMKAGDEPLKKYDLSslrLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTE------------TGGIFIS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 806 NPIGNT-------------QAYVLDRHLQRCPTGVIGELYISGF--GIANGYLGRADlsaaRFVANPFEHGQRMYRTGDL 870
Cdd:COG0365 350 NLPGLPvkpgsmgkpvpgyDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPE----RYRETYFGRFPGWYRTGDG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 871 VRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV-IAEPINNsHRLLGYCVVKD-IELDEKTSEQLS 947
Cdd:COG0365 426 ARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVaEAAVVgVPDEIRG-QVVKAFVVLKPgVEPSDELAKELQ 504
|
570 580 590
....*....|....*....|....*....|....*....
gi 490930577 948 QqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:COG0365 505 A----HVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1533-2031 |
1.89e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 155.83 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAKSKLVIGEQ----------KDLAAIVHpsIATFAFNELFDETKVDLS----------SYKTTVI 1672
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGlflgvdysatTRLPALEH--VVICETEEDDPHTEKMKTftdflaagdpAERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPAYLIYTSGTTGQPKGVMVSH-QAIVNRILWmqSEY-PLSATDTILQKTPctfdvsvweFF--------W--SYLV 1740
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHrQLLSNAADW--AEYlGLTEGDRYLAANP---------FFhvfgykagVnaPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1741 GARLVIAPidaHRDPLALLSLIQKYQVTTLHFVPSM---LAVFENAATEILSSaqrqslpiCRVFCSGEA-LPTALAKSF 1816
Cdd:PRK07656 233 GATILPLP---VFDPDEVFRLIETERITVLPGPPTMynsLLQHPDRSAEDLSS--------LRLAVTGAAsMPVALLERF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFSCE-LHNLYGPTEAA-VdvsymdATL-GLHPEESCVA--IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAM 1891
Cdd:PRK07656 302 ESELGVDiVLTGYGLSEASgV------TTFnRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVV---- 1966
Cdd:PRK07656 376 GYYDDPEATAAAIDADGW------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVaEAAVigvp 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1967 HAISSEQNKANVqlvaYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07656 450 DERLGEVGKAYV----VLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1537-2031 |
1.16e-38 |
|
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: 153.56 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALS----DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:cd12119 1 LLEHAARLHGDREIVSrtheGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAKSKLVI--GEQKDLAAIVHPSIATF-AFNELFDETKVDLSSYKT-----TVITPQHPAY----- 1679
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFvdRDFLPLLEAIAPRLPTVeHVVVMTDDAAMPEPAGVGvlayeELLAAESPEYdwpdf 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 -------LIYTSGTTGQPKGVMVSHQAIV--NRILWMQSEYPLSATDTILqktPCT--FDVSVWEF-FWSYLVGARLVIa 1747
Cdd:cd12119 161 dentaaaICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVL---PVVpmFHVNAWGLpYAAAMVGAKLVL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 PiDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAateiLSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHnL 1827
Cdd:cd12119 237 P-GPYLDPASLAELIEREGVTFAAGVPTVWQGLLDH----LEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIH-A 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAA--VDVSYMDATLGLHPEESCVAI----GYPVWNTQLYILDQYLRPVPvgVD----GELYLAGHQLAMGYLHRA 1897
Cdd:cd12119 311 WGMTETSplGTVARPPSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDGRELP--WDgkavGELQVRGPWVTKSYYKND 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1898 DlTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKA 1976
Cdd:cd12119 389 E-ESEALTEDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAvAEAAVIGVPHPKWGE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1977 NVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd12119 462 RPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1557-2031 |
1.32e-38 |
|
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: 151.09 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI-- 1634
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1635 GEQKDLAAIVhpsiatfafnelfdetkvdlssykttvitpqhpayliYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLS 1714
Cdd:cd05935 81 SELDDLALIP-------------------------------------YTSGTTGLPKGCMHTHFSAAANALQSAVWTGLT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1715 ATDTILQKTPcTFDVSvwEFFWSYL----VGARLVIApidAHRDPLALLSLIQKYQVTTLHFVPSMLAVfenaateILSS 1790
Cdd:cd05935 124 PSDVILACLP-LFHVT--GFVGSLNtavyVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVD-------LLAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 A--QRQSLPICRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTEAavdVSYMDATLGLHPEESCvaIGYPVWNTQLYIL 1867
Cdd:cd05935 191 PefKTRDLSSLKVLTGGGApMPPAVAEKLLKLTGLRFVEGYGLTET---MSQTHTNPPLRPKLQC--LGIP*FGVDARVI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 D-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQR 1946
Cdd:cd05935 266 DiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1947 IELGEIEQQL---RLIsgLDVVVHAI----SSEQNKANVQL-VAYLQTTAPVDIDQLKKQlakHLPAYMVPTHYMLVEQF 2018
Cdd:cd05935 343 VWPAEVEAKLykhPAI--*EVCVISVpderVGEEVKAFIVLrPEYRGKVTEEDIIEWARE---QMAAYKYPREVEFVDEL 417
|
490
....*....|...
gi 490930577 2019 PLSHNGKLDRKAL 2031
Cdd:cd05935 418 PRSASGKILWRLL 430
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
503-986 |
3.06e-38 |
|
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: 150.70 E-value: 3.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQqlpqniQQLHLDQEGVQTQIRKQDASdipaenrkfdfqdvAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIyw 662
Cdd:cd17654 97 ELDN------APLSFTPEHRHFNIRTDECL--------------AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLF-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 663 pVLEAVNERFPDRPLraahthsfSFDSSWLQVFWMLWGQELHIFDENMRRDAFGLVQEI--QQRQIDTLDLPPSFCAQMM 740
Cdd:cd17654 155 -NITSEDILFLTSPL--------TFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITVLQATPTLFRRFG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 741 TNGLFVEN-QHHPSL--ILIGGEAAP----LALWQQLNAQPALFahNLYGPTEYTVDTFRAELKQTARPV-IGNPIGNTQ 812
Cdd:cd17654 226 SQSIKSTVlSATSSLrvLALGGEPFPslviLSSWRGKGNRTRIF--NIYGITEVSCWALAYKVPEEDSPVqLGSPLLGTV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 813 AYVLDrhlqRCPTGVIGELY---ISGFGIANGYLGRADlsaarfvanpfehGQrMYRTGDLVRwNSAGKLEFMGRCDDQI 889
Cdd:cd17654 304 IEVRD----QNGSEGTGQVFlggLNRVCILDDEVTVPK-------------GT-MRATGDFVT-VKDGELFFLGRKDSQI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 890 KIRGYRVEIGEVENALSILTNVESAVVIAEpinNSHRLLGYCV---VKDIELDEKTSEQLSqqylsqlRQNLPEYMVpsa 966
Cdd:cd17654 365 KRRGKRINLDLIQQVIESCLGVESCAVTLS---DQQRLIAFIVgesSSSRIHKELQLTLLS-------SHAIPDTFV--- 431
|
490 500
....*....|....*....|
gi 490930577 967 ltVMSEFPRNVSGKVDKKAL 986
Cdd:cd17654 432 --QIDKLPLTSHGKVDKSEL 449
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
485-983 |
7.85e-38 |
|
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: 148.91 E-value: 7.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 485 KYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDldypid 564
Cdd:cd17631 7 RHPDRTALVFGGRS----LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 565 rmqmmcedanplFVLTTQALAQQLpqniqqlhldqegvqtqirkQDASDipaenrKFDFQDVAYVIFTSGSTGRPKGVMN 644
Cdd:cd17631 77 ------------FRLTPPEVAYIL--------------------ADSGA------KVLFDDLALLMYTSGTTGRPKGAML 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 645 THGSLLNLILSHkpTIYWPVLEAvnerfpDRPLRAAH-THSFSFDSSWLQVFWMlwGQELHIfdenMRR-DAFGLVQEIQ 722
Cdd:cd17631 119 THRNLLWNAVNA--LAALDLGPD------DVLLVVAPlFHIGGLGVFTLPTLLR--GGTVVI----LRKfDPETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 723 QRQIDTLDLPPSFCAQMMTNGLFvENQHHPSL--ILIGGEAAPLALWQQLNAQPALFaHNLYGPTE--YTVDTFRAELKQ 798
Cdd:cd17631 185 RHRVTSFFLVPTMIQALLQHPRF-ATTDLSSLraVIYGGAPMPERLLRALQARGVKF-VQGYGMTEtsPGVTFLSPEDHR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 799 TARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAArfvanPFEHGqrMYRTGDLVRWNSAGK 878
Cdd:cd17631 263 RKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA-----AFRDG--WFHTGDLGRLDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 879 LEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKD-IELDEktseqlsQQYLS 952
Cdd:cd17631 336 LYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVP----DEKWGeavvaVVVPRPgAELDE-------DELIA 404
|
490 500 510
....*....|....*....|....*....|.
gi 490930577 953 QLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17631 405 HCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1529-2032 |
8.20e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 151.62 E-value: 8.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVaLPR-SVKLSIAILAVIEAGA 1607
Cdd:PRK07788 46 RRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARnHRGFVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 --AYLPIDLQHPT-------ERIKFMLQDAK-SKLVIGEQKDL----AAIVHPSIATFAFNElfDETKVDLSSYKTTVIT 1673
Cdd:PRK07788 125 riILLNTGFSGPQlaevaarEGVKALVYDDEfTDLLSALPPDLgrlrAWGGNPDDDEPSGST--DETLDDLIAGSSTAPL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 P---QHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPC--TFDVSVWEFfwSYLVGARLVIap 1748
Cdd:PRK07788 203 PkppKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTL--AMALGSTVVL-- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 idaHR--DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHN 1826
Cdd:PRK07788 279 ---RRrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKI--IFVSGSALSPELATRALEAFGPVLYN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1827 LYGPTEAAVdvsymdATLGlHPEESCVA---IGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYlhradlTASR 1903
Cdd:PRK07788 354 LYGSTEVAF------ATIA-TPEDLAEApgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1904 fvaNPFTAGQRMyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGL-DVV-VHAISSEQNKANVQLV 1981
Cdd:PRK07788 421 ---DKQIIDGLL-SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED---LLAGHpDVVeAAVIGVDDEEFGQRLR 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1982 AYLQTT--APVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALP 2032
Cdd:PRK07788 494 AFVVKApgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1538-2035 |
1.61e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 149.34 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHP 1617
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 TERIKFMLQDAKSKLVIGEQkDLAAIVHPSIaTFAFNELFDETKVDlssykttvITPQHPAYL------IYTSGTTGQPK 1691
Cdd:PRK03640 88 REELLWQLDDAEVKCLITDD-DFEAKLIPGI-SVKFAELMNGPKEE--------AEIQEEFDLdevatiMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSHQ----AIVNRILWMQseypLSATDTILQKTPcTFDVSVWE-FFWSYLVGARLVIAPidaHRDPLALLSLIQKYQ 1766
Cdd:PRK03640 158 GVIQTYGnhwwSAVGSALNLG----LTEDDCWLAAVP-IFHISGLSiLMRSVIYGMRVVLVE---KFDAEKINKLLQTGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1767 VTTLHFVPSMLavfenaaTEILSSAQRQSLPI---CRVFCSGEALPTALAKsftehfsCELHNL-----YGPTEAAVDVs 1838
Cdd:PRK03640 230 VTIISVVSTML-------QRLLERLGEGTYPSsfrCMLLGGGPAPKPLLEQ-------CKEKGIpvyqsYGMTETASQI- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 ymdATLGlhPEESCVAI---GYPVWNTQLYILDQyLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrm 1915
Cdd:PRK03640 295 ---VTLS--PEDALTKLgsaGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF------ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1916 yRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQlVAYLQTTAPVDIDQL 1995
Cdd:PRK03640 363 -KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVP-VAFVVKSGEVTEEEL 440
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 490930577 1996 KKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK03640 441 RHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
21-434 |
1.94e-37 |
|
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: 147.56 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 21 LASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASY---SSDPSQPFIELnnQVQFQIEE 97
Cdd:cd19066 4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFceeAGRYEQVVLDK--TVRFRIEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 98 FDFCHLTPKKAqqRLWDWMPSDRQCAKSLKAGEtqLFRQVLFTTHD-KVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQ 176
Cdd:cd19066 82 IDLRNLADPEA--RLLELIDQIQQTIYDLERGP--LVRVALFRLADeRDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 177 EGKDLSVSPFIGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHL-AAKTTATFVKHQLRFSTGILEQIQA 255
Cdd:cd19066 158 RQKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRpSQVASYEVLTLEFFLRSEETKRLRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 256 LAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLRE 335
Cdd:cd19066 238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 336 IRPHQKYDAEQILRDLNSIDIHER--MYGPILNYKAFDQ-DLVIDGEKVKT--HHISTGPIDDFEFSFIVQDH-ELIIEL 409
Cdd:cd19066 318 AIEHQRVPFIELVRHLGVVPEAPKhpLFEPVFTFKNNQQqLGKTGGFIFTTpvYTSSEGTVFDLDLEASEDPDgDLLLRL 397
|
410 420
....*....|....*....|....*
gi 490930577 410 RADSQRYTQDELFNHGQRLTLLLEQ 434
Cdd:cd19066 398 EYSRGVYDERTIDRFAERYMTALRQ 422
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1559-2031 |
2.40e-36 |
|
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: 144.51 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1559 SFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG--- 1635
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTdsl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 -EQKDLAAIVHPSIatfafnELFDETKVDLSSYkttvITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLS 1714
Cdd:TIGR01923 81 lEEKDFQADSLDRI------EAAGRYETSLSAS----FNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1715 ATDTILQKTPcTFDVSVWEFFW-SYLVGARLVIAPIDAhrdplALLSLIQKYQVTTLHFVPSMLavfenaaTEILSSAQR 1793
Cdd:TIGR01923 151 EDDNWLLSLP-LYHISGLSILFrWLIEGATLRIVDKFN-----QLLEMIANERVTHISLVPTQL-------NRLLDEGGH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSLpICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAVDVSYMDaTLGLHPEEScvaIGYPVWNTQLYILdqylRP 1873
Cdd:TIGR01923 218 NEN-LRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGMTETCSQVTTAT-PEMLHARPD---VGRPLAGREIKIK----VD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1874 VPVGVdGELYLAGHQLAMGYLHRADLtasrfvaNPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:TIGR01923 288 NKEGH-GEIMVKGANLMKGYLYQGEL-------TPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIE 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1954 QQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:TIGR01923 360 TVLYQHPGIQEAV-VVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1528-2031 |
2.77e-36 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 146.44 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1528 YVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:COG1021 21 YWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 ayLPIdLQHPTER---IKFMLQDAKSKLVIGEQK-------DLAAIV---HPSIAT----------FAFNELFDEtKVDL 1664
Cdd:COG1021 101 --IPV-FALPAHRraeISHFAEQSEAVAYIIPDRhrgfdyrALARELqaeVPSLRHvlvvgdagefTSLDALLAA-PADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1665 SSYkttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIV------NRILWMQSE------------YPLSAtdtilqktPCT 1726
Cdd:COG1021 177 SEP---RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLysvrasAEICGLDADtvylaalpaahnFPLSS--------PGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVsvwefFWsylVGARLVIAPiDAhrDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEilSSAQRQSLpicRVFCSGE 1806
Cdd:COG1021 246 LGV-----LY---AGGTVVLAP-DP--SPDTAFPLIERERVTVTALVPPLALLWLDAAER--SRYDLSSL---RVLQVGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 A-LPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDatlglHPEEScvaigypVWNTQ---------LYILDQYLRPVPV 1876
Cdd:COG1021 310 AkLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLD-----DPEEV-------ILTTQgrpispddeVRIVDEDGNPVPP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1877 GVDGELYLAGHQLAMGYlHRAD-LTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLkIR-GQRIELGEIEQ 1954
Cdd:COG1021 378 GEVGELLTRGPYTIRGY-YRAPeHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1955 QLrlisgldvVVH-AIsseqnkANVQLV------------AYLQTT-APVDIDQLKKQL-AKHLPAYMVPTHYMLVEQFP 2019
Cdd:COG1021 450 LL--------LAHpAV------HDAAVVampdeylgerscAFVVPRgEPLTLAELRRFLrERGLAAFKLPDRLEFVDALP 515
|
570
....*....|..
gi 490930577 2020 LSHNGKLDRKAL 2031
Cdd:COG1021 516 LTAVGKIDKKAL 527
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1558-2031 |
8.33e-36 |
|
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: 143.41 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVigeq 1637
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kdlaaIVHPsiatfafnELFDETkvdlssykttviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05969 77 -----ITTE--------ELYERT------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 tilqKTPCTFDV-----SVWEFFWSYLVGARLVIapIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQ 1792
Cdd:cd05969 132 ----IYWCTADPgwvtgTVYGIWAPWLNGVTNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1793 RQSLpicRVFCS-GEAL-PTALAKSfTEHFSCELHNLYGPTEAAVDV--SY--MDATLGlhpeescvAIGYPVWNTQLYI 1866
Cdd:cd05969 206 LSSL---RFIHSvGEPLnPEAIRWG-MEVFGVPIHDTWWQTETGSIMiaNYpcMPIKPG--------SMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1867 LDQYLRPVPVGVDGELYLAGHQLAM--GYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:cd05969 274 VDENGNELPPGTKGILALKPGWPSMfrGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQL---RLISGLDVV--VHAISSEQNKANVQLVAYLQTTapvdiDQLKKQLAKH----LPAYMVPTHYMLV 2015
Cdd:cd05969 347 HRVGPFEVESALmehPAVAEAGVIgkPDPLRGEIIKAFISLKEGFEPS-----DELKEEIINFvrqkLGAHVAPREIEFV 421
|
490
....*....|....*.
gi 490930577 2016 EQFPLSHNGKLDRKAL 2031
Cdd:cd05969 422 DNLPKTRSGKIMRRVL 437
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1101-1494 |
1.38e-35 |
|
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: 142.16 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQ-VENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFdSELAEEPVFIYSLHPTQAWPV 1179
Cdd:cd19066 2 IPLSPMQRGMWFLKKlATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQVVLDKTVRFRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPDLLEQTIQEALQQPIH--LDQPYG-LIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQQ- 1255
Cdd:cd19066 81 IIDLRNLADPEARLLELIDQIQQtiYDLERGpLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1256 --LPVLEHSYETVIKALSGR----DHETSKVIWQRDLADLQPLILFNQAQQAVQETSYR-------LSAELGAKLQHKLR 1322
Cdd:cd19066 161 ptLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEvltleffLRSEETKRLREVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1323 QQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVEH 1402
Cdd:cd19066 241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1403 LEH-DGLGLSAIQQLIAQGNLFDSLL--VVENYPDNQYLQQKLGDAAISKL--TNRGYSHYPLALLVIPDHQIELLLE-- 1475
Cdd:cd19066 319 IEHqRVPFIELVRHLGVVPEAPKHPLfePVFTFKNNQQQLGKTGGFIFTTPvyTSSEGTVFDLDLEASEDPDGDLLLRle 398
|
410 420
....*....|....*....|..
gi 490930577 1476 -QRGVIDQP--EHFLERMIQLI 1494
Cdd:cd19066 399 ySRGVYDERtiDRFAERYMTAL 420
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1530-2031 |
1.02e-34 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 142.11 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:PRK13295 22 HDRTINDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAY---LPIDLQHpteRIKFMLQDAKSKLVIGEQK----DLAAIV---HPSIATF------------AFNELFDETK 1661
Cdd:PRK13295 102 RIGAVLnplMPIFRER---ELSFMLKHAESKVLVVPKTfrgfDHAAMArrlRPELPALrhvvvvggdgadSFEALLITPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1662 VDLSSYKTTVITPQHP-----AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSvweFFW 1736
Cdd:PRK13295 179 WEQEPDAPAILARLRPgpddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTG---FMY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1737 SYLV----GARLVIAPIdahRDPLALLSLIQKYQVTtlhfvpsmlavFENAATEILS------SAQRQSLPICRVF-CSG 1805
Cdd:PRK13295 256 GLMMpvmlGATAVLQDI---WDPARAAELIRTEGVT-----------FTMASTPFLTdltravKESGRPVSSLRTFlCAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1806 EALPTALAKSFTEHFSCELHNLYGPTE-AAVDVSYMDATlglhPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYL 1884
Cdd:PRK13295 322 APIPGALVERARAALGAKIVSAWGMTEnGAVTLTKLDDP----DERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1885 AGHQLAMGYLHRADLTAsrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLkIRG-QRIELGEIEQQL-RLISGL 1962
Cdd:PRK13295 398 RGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGgENIPVVEIEALLyRHPAIA 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1963 DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQL-AKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK13295 469 QVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
486-989 |
1.36e-34 |
|
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: 141.12 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 486 YPERTAIV---SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYP 562
Cdd:cd17647 1 FPERTCVVetpSLNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 563 IDRMQMMCEDANPlfvlttQALaqqlpqniqqlhldqegvqTQIRKQDASDIPAENRKFDFqdvayvifTSGSTGRPKGV 642
Cdd:cd17647 81 PARQNIYLGVAKP------RGL-------------------IVIRAAGVVVGPDSNPTLSF--------TSGSEGIPKGV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 643 MNTHGSLlnlilshkpTIYWPVLeavnerfpdrplraahthSFSFDSSWLQVFWMLWGqelhIFDENMRRDAFG---LVQ 719
Cdd:cd17647 128 LGRHFSL---------AYYFPWM------------------AKRFNLSENDKFTMLSG----IAHDPIQRDMFTplfLGA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 720 EIQQRQIDTLDLPPSFCAQMMTNGLFVeNQHHPSL--ILIGGEAAPL------------------ALWQQLnaQPALFAH 779
Cdd:cd17647 177 QLLVPTQDDIGTPGRLAEWMAKYGATV-THLTPAMgqLLTAQATTPFpklhhaffvgdiltkrdcLRLQTL--AENVRIV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 780 NLYGPTEytvdTFRA----ELKQTA---------RPVI--GNPIGNTQAYVLDRH--LQRCPTGVIGELYISGFGIANGY 842
Cdd:cd17647 254 NMYGTTE----TQRAvsyfEVPSRSsdptflknlKDVMpaGRGMLNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGY 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 843 LGRADLSAARFVAN--------------------PFEHG--QRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGE 900
Cdd:cd17647 330 RGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 901 VENALSILTNV-ESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQ---------------------LSQQYLSQLRQNL 958
Cdd:cd17647 410 IDTHISQHPLVrENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQedvpkevstdpivkgligyrkLIKDIREFLKKRL 489
|
570 580 590
....*....|....*....|....*....|.
gi 490930577 959 PEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:cd17647 490 ASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1556-2011 |
2.40e-34 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 139.27 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG 1635
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EqkdlaaivhpsiatfafnelfdetkvdlssykttviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSA 1715
Cdd:cd05907 84 E------------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1716 TDTILQKTPCT--FDVSVWEFFWSYLvGARLVIAPIDAhrdplALLSLIQKYQVTTLHFVPSML-AVFENAATEILSSAQ 1792
Cdd:cd05907 128 GDRHLSFLPLAhvFERRAGLYVPLLA-GARIYFASSAE-----TLLDDLSEVRPTVFLAVPRVWeKVYAAIKVKAVPGLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1793 RQ-----SLPICRVFCSGEA-LPTALAKSFtEHFSCELHNLYGPTE--AAVDVSymdatlglHPEESCVA-IGYPVWNTQ 1863
Cdd:cd05907 202 RKlfdlaVGGRLRFAASGGApLPAELLHFF-RALGIPVYEGYGLTEtsAVVTLN--------PPGDNRIGtVGKPLPGVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYIldqylrpvpvGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd05907 273 VRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDLIITS 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1944 -GQRIELGEIEQQLR---LISglDVVVHAissEQNKANVQLVAylqttapVDIDQLKKQLAKHLPAYMVPTH 2011
Cdd:cd05907 337 gGKNISPEPIENALKaspLIS--QAVVIG---DGRPFLVALIV-------PDPEALEAWAEEHGIAYTDVAE 396
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1523-1967 |
5.98e-34 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 140.62 E-value: 5.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1523 NQTQYYVRQSTLQQLLREQARITPEQTALSD-ENHQ---LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIA 1598
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1599 ILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIAT-------FAFNELFDETKVDLSSYKTTV 1671
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDElpslrhiVVLDPRGLRDDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1672 ------------------ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILqktpctfdvS--- 1730
Cdd:COG1022 162 algrevadpaelearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL---------Sflp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 ---VWEFFWSYLV---GARLVIAPidahrDPLALLSLIQKYQVTTLHFVPsmlAVFENAATEILSSAQRQS--------- 1795
Cdd:COG1022 233 lahVFERTVSYYAlaaGATVAFAE-----SPDTLAEDLREVKPTFMLAVP---RVWEKVYAGIQAKAEEAGglkrklfrw 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 -------------------------LPI----------------CRVFCSG-EALPTALAKsFtehFSC---ELHNLYGP 1830
Cdd:COG1022 305 alavgrryararlagkspslllrlkHALadklvfsklrealggrLRFAVSGgAALGPELAR-F---FRAlgiPVLEGYGL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1831 TEAAVDVSymdatlgLHPEESCVA--IGYPVWNTQLYIldqylrpvpvGVDGELYLAGHQLAMGYLHRADLTASRFVANP 1908
Cdd:COG1022 381 TETSPVIT-------VNRPGDNRIgtVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADG 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1909 FtagqrmYRTGDIARWHADGSIQYIGRADDQLKIR-GQRIELGEIEQQLR---LISglDVVVH 1967
Cdd:COG1022 444 W------LHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKaspLIE--QAVVV 498
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1529-2026 |
9.20e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 138.91 E-value: 9.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:PRK08316 8 ARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 YLPIDLQHPTERIKFMLQDAKSKLVIGEQkDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQH------------ 1676
Cdd:PRK08316 88 HVPVNFMLTGEELAYILDHSGARAFLVDP-ALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADwaeagsvaepdv 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 ------PAYLIYTSGTTGQPKGVMVSHQAIVnrilwmqSEY-------PLSATDTILQKTP---CT-FDVsvweFFWSYL 1739
Cdd:PRK08316 167 eladddLAQILYTSGTESLPKGAMLTHRALI-------AEYvscivagDMSADDIPLHALPlyhCAqLDV----FLGPYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1740 -VGARLVI--APidahrDPLALLSLIQKYQVTTLhFVP-----SML--AVFEnaaTEILSSaqrqslpICRVFCSGEALP 1809
Cdd:PRK08316 236 yVGATNVIldAP-----DPELILRTIEAERITSF-FAPptvwiSLLrhPDFD---TRDLSS-------LRKGYYGASIMP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 TALAKSFTEHF-SCELHNLYGPTEAAvdvSYmdATLgLHPEE------SCvaiGYPVWNTQLYILDQYLRPVPVGVDGEL 1882
Cdd:PRK08316 300 VEVLKELRERLpGLRFYNCYGQTEIA---PL--ATV-LGPEEhlrrpgSA---GRPVLNVETRVVDDDGNDVAPGEVGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1883 YLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL 1962
Cdd:PRK08316 371 VHRSPQLMLGYWDDPEKTAEAFRGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1963 -DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:PRK08316 444 aEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
2144-2368 |
1.34e-33 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 130.20 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2144 PLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQSPRPDGLLANSTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYA 2223
Cdd:pfam00975 2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2224 VAAKLTEQGEKVDYLGLLDTY-PAEIHQWLdlsveeMNAEAEQEQLQFFNDILADADSALSEEtrRLQEDIFANYRDAVR 2302
Cdd:pfam00975 82 VARRLERQGEAVRSLFLSDASaPHTVRYEA------SRAPDDDEVVAEFTDEGGTPEELLEDE--ELLSMLLPALRADYR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2303 LLKPYKMPHFDG-ELHLVVAEKDLLPYIQPEQQW-SPLVKKLNIVRLSEADHTDILS--PQQLETLGPIL 2368
Cdd:pfam00975 154 ALESYSCPPLDAqSATLFYGSDDPLHDADDLAEWvRDHTPGEFDVHVFDGDHFYLIEhlEAVLEIIEAKL 223
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
475-986 |
1.58e-33 |
|
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: 136.92 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 475 VLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASF 554
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK----LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 555 LPLDLDYPIDRMQMMCEDANPLFVLTTQALaqqlpqniqqlhldqegvQTQIRKQDASDIPAENRKfdfQDVAYVIFTSG 634
Cdd:cd05936 77 VPLNPLYTPRELEHILNDSGAKALIVAVSF------------------TDLLAAGAPLGERVALTP---EDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 635 STGRPKGVMNTHGSLL-NL--ILSHKPTIYWP---VLEAVnerfpdrPLraahTHSFSFDSSwLQVFWMLwGQELHIFDe 708
Cdd:cd05936 136 TTGVPKGAMLTHRNLVaNAlqIKAWLEDLLEGddvVLAAL-------PL----FHVFGLTVA-LLLPLAL-GATIVLIP- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 709 nmRRDAFGLVQEIQQRQidtldlPPSFCAqmmTNGLFVENQHHP--------SLILIGGEAAPLALwQQLNAQPALFAHN 780
Cdd:cd05936 202 --RFRPIGVLKEIRKHR------VTIFPG---VPTMYIALLNAPefkkrdfsSLRLCISGGAPLPV-EVAERFEELTGVP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 781 L---YGPTE----YTVDTFRAELKQTArpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:cd05936 270 IvegYGLTEtspvVAVNPLDGPRKPGS---IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 854 VANPFehgqrmyRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG---- 929
Cdd:cd05936 347 VDGWL-------RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVP----DPYSGeavk 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 930 -YCVVKDielDEKTSEQlsqQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05936 416 aFVVLKE---GASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1103-1329 |
9.13e-33 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 128.62 E-value: 9.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1103 LLPLQKGMLFLSQveNQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPVFIysLHPTQAWPVQFC 1182
Cdd:COG4908 1 LSPAQKRFLFLEP--GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEE-DGEPVQR--IDPDADLPLEVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1183 SVT-------PDLLEQTIQEALQQPIHLDQPYgLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ---- 1251
Cdd:COG4908 76 DLSalpeperEAELEELVAEEASRPFDLARGP-LLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAAlleg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQQLPVLEHSYETVI----KALSGRDHETSKVIWQRDLADLQPLILF-------NQAQQAVQETSYRLSAELGAKLQHK 1320
Cdd:COG4908 155 EPPPLPELPIQYADYAawqrAWLQSEALEKQLEYWRQQLAGAPPVLELptdrprpAVQTFRGATLSFTLPAELTEALKAL 234
|
....*....
gi 490930577 1321 LRQQGITLN 1329
Cdd:COG4908 235 AKAHGATVN 243
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1100-1466 |
1.58e-32 |
|
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: 133.21 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLF--LSQVENQSNYNAfTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFD-SELAEEPVFIYS-LHPTQ 1175
Cdd:cd19547 1 VYPLAPMQEGMLFrgLFWPDSDAYFNQ-NVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDdLAPPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1176 A---WPVQFCSVTPDLLEQTIQEALQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ 1251
Cdd:cd19547 80 AlldWSGEDPDRRAELLERLLADDRAAGLSLADcP--LYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1252 TNQ-QLPVLE-----HSYETVIKALSGRDHETSKvIWQRDLADLQPLI----------LFNQAQQAVQETSYRLSAELGa 1315
Cdd:cd19547 158 LAHgREPQLSpcrpyRDYVRWIRARTAQSEESER-FWREYLRDLTPSPfstapadregEFDTVVHEFPEQLTRLVNEAA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1316 klqhklRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQL 1395
Cdd:cd19547 236 ------RGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETI 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1396 QQLHVEHLEHDGLGLSAIQ-----QLIAQGNLFDSLLVVENYPDNQYLQQKLGDAAISkLTNRGYSHYPLALLVIP 1466
Cdd:cd19547 310 HRDLATTAAHGHVPLAQIKswasgERLSGGRVFDNLVAFENYPEDNLPGDDLSIQIID-LHAQEKTEYPIGLIVLP 384
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1542-2031 |
1.85e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 134.24 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQK--DLAAIVHPSIATFAFNelfdETKVDLSSYKTTVITPQHPA------YLIYTSGTTGQPKGV 1693
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEfdAIVALETPKIVIDAAA----QADSRRLAQGGLEIPPQAAVaptdlvRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSHqaivNRILWMQSEYP----LSATDTILQKTPC----TFDVSVWEFFWsylVGARLVIapidaHR--DPLALLSLIQ 1763
Cdd:PRK06145 168 MHSY----GNLHWKSIDHVialgLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLavfenaaTEILSSAQRQSLPICR---VFCSGEALPTALAKSFTEHFS-CELHNLYGPTEAAVDVSY 1839
Cdd:PRK06145 236 RHRLTCAWMAPVML-------SRVLTVPDRDRFDLDSlawCIGGGEKTPESRIRDFTRVFTrARYIDAYGLTETCSGDTL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1840 MDATLGLhpeESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTG 1919
Cdd:PRK06145 309 MEAGREI---EKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1920 DIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQ 1998
Cdd:PRK06145 379 DVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVaEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRH 458
|
490 500 510
....*....|....*....|....*....|...
gi 490930577 1999 LAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06145 459 CRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
503-986 |
1.94e-32 |
|
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: 132.85 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedanplfvlTTQ 582
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPL----------------------TTL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQQLPQNIQqlHLDQEGVQTqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGSLLnlilSHKPTIYW 662
Cdd:cd05972 59 LGPKDIEYRLE--AAGAKAIVT-----------------DAEDPALIYFTSGTTGLPKGVLHTHSYPL----GHIPTAAY 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 663 PVleavnerfpdrPLRAAHTHSFSFDSSWLQVFWM----LWGQELHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSFCA 737
Cdd:cd05972 116 WL-----------GLRPDDIHWNIADPGWAKGAWSsffgPWLLGATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 738 QMMTNGLFVENQHHPSLILIGGEaaPL-----ALWQqlnAQPALFAHNLYGPTE--YTVDTFR-AELKQTArpvIGNPIG 809
Cdd:cd05972 185 MLIKQDLSSYKFSHLRLVVSAGE--PLnpeviEWWR---AATGLPIRDGYGQTEtgLTVGNFPdMPVKPGS---MGRPTP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 810 NTQAYVLDRHLQRCPTGVIGELYI--SGFGIANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDD 887
Cdd:cd05972 257 GYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 888 QIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKDielDEKTSEQLSQQYLSQLRQNLPEYM 962
Cdd:cd05972 330 IIKSSGYRIGPFEVESALLEHPAVAEAAVVGSP----DPVRGevvkaFVVLTS---GYEPSEELAEELQGHVKKVLAPYK 402
|
490 500
....*....|....*....|....
gi 490930577 963 VPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05972 403 YPREIEFVEELPKTISGKIRRVEL 426
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1558-2031 |
3.00e-32 |
|
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: 133.61 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRaGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05909 8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 K--DLAAIVHPSIATFAFNELF-DETKVDLSSYKTTVI--------------------TPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:cd05909 87 QfiEKLKLHHLFDVEYDARIVYlEDLRAKISKADKCKAflagkfppkwllrifgvapvQPDDPAVILFTSGSEGLPKGVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVNRILWMQSEYPLSATDTILQKTPC----TFDVSVWEFFwsyLVGARLVIAPidahrDPL---ALLSLIQKYQV 1767
Cdd:cd05909 167 LSHKNLLANVEQITAIFDPNPEDVVFGALPFfhsfGLTGCLWLPL---LSGIKVVFHP-----NPLdykKIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1768 TTLHFVPSMLAVFENAATEilssaqrQSLPICR-VFCSGEALPTALAKSFTEHFSCELHNLYGPTEA----AVDVSYMDA 1842
Cdd:cd05909 239 TILLGTPTFLRGYARAAHP-------EDFSSLRlVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECspviSVNTPQSPN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 tlglhpEESCVaiGYPVWNTQLYILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTAsrfvanpFTAGQRMYRTGDI 1921
Cdd:cd05909 312 ------KEGTV--GRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQLVAYLQTTAPvDIDQLKKQLAK 2001
Cdd:cd05909 377 GKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGEKIVLLTTTTDT-DPSSLNDILKN 455
|
490 500 510
....*....|....*....|....*....|.
gi 490930577 2002 H-LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05909 456 AgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1542-2034 |
3.67e-31 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 131.03 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK13382 53 AQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQ-------KDLAAIVHP--SIA-TFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPK 1691
Cdd:PRK13382 133 AEVVTREGVDTVIYDEefsatvdRALADCPQAtrIVAwTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1692 GVMVSH-------QAIVNRIlwmqseyPLSATDTILQKTPCtfdVSVWEFfwSYLVGARLVIAPIDAHR--DPLALLSLI 1762
Cdd:PRK13382 213 GARRSGpggigtlKAILDRT-------PWRAEEPTVIVAPM---FHAWGF--SQLVLAASLACTIVTRRrfDPEATLDLI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1763 QKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDA 1842
Cdd:PRK13382 281 DRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRF--AAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 TLGLHPEEScvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADltasrfvaNPFTAGqrMYRTGDIA 1922
Cdd:PRK13382 359 DLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST--------KDFHDG--FMASGDVG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1923 RWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlRLISGLDVVVHA--ISSEQNKANVQLVAYLQTT--APVDIDQLKKQ 1998
Cdd:PRK13382 425 YLDENGRLFVVGRDDEMIVSGGENVYPIEVE---KTLATHPDVAEAavIGVDDEQYGQRLAAFVVLKpgASATPETLKQH 501
|
490 500 510
....*....|....*....|....*....|....*.
gi 490930577 1999 LAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:PRK13382 502 VRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1677-2031 |
5.91e-31 |
|
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: 125.91 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDVSVWEFFW-SYLVGARLVIAPidahRDP 1755
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVrSLLAGAELVLLE----RNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLiQKYQVTTLHFVPSMLavfENAATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAV 1835
Cdd:cd17630 77 ALAEDL-APPGVTHVSLVPTQL---QRLLDSGQGPAALKSLR--AVLLGGAPIPPELLERAADR-GIPLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1836 DVSymDATLGLHPEESCvaiGYPVWNTQLYILDqylrpvpvgvDGELYLAGHQLAMGYLhradltasRFVANPFTAGQRM 1915
Cdd:cd17630 150 QVA--TKRPDGFGRGGV---GVLLPGRELRIVE----------DGEIWVGGASLAMGYL--------RGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1916 YRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEqnKANVQLVAYLQTTAPVDIDQ 1994
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAvRDAFVVGVPDE--ELGQRPVAVIVGRGPADPAE 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 490930577 1995 LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd17630 285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
491-981 |
2.77e-30 |
|
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: 127.71 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 491 AIVSGErpNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMC 570
Cdd:cd05911 1 AQIDAD--TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 571 EDANPLFVLTTQAL------AQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDF--------QDVAYVIFTSGST 636
Cdd:cd05911 79 KISKPKVIFTDPDGlekvkeAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLppplkdgkDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 637 GRPKGVMNTHgslLNLILSHKPTIYwpvLEAVNERFPDR-----PLraahTHSFSFdssWLQVFWMLWGQELHIfdenMR 711
Cdd:cd05911 159 GLPKGVCLSH---RNLIANLSQVQT---FLYGNDGSNDVilgflPL----YHIYGL---FTTLASLLNGATVII----MP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 712 R---DAFglVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQhHPSLILIGGEAAPLA--LWQQLNAQ-PALFAHNLYGPT 785
Cdd:cd05911 222 KfdsELF--LDLIEKYKITFLYLVPPIAAALAKSPLLDKYD-LSSLRVILSGGAPLSkeLQELLAKRfPNATIKQGYGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 786 EYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHL-QRCPTGVIGELYISGFGIANGYLGRADLSAARFvanpFEHGqrM 864
Cdd:cd05911 299 ETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF----DEDG--W 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 865 YRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKdiELDEKTSE 944
Cdd:cd05911 373 LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVR--KPGEKLTE 450
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 490930577 945 QLSQQYLSqlrQNLPEYmvpSALT----VMSEFPRNVSGKV 981
Cdd:cd05911 451 KEVKDYVA---KKVASY---KQLRggvvFVDEIPKSASGKI 485
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1531-2029 |
3.14e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 128.58 E-value: 3.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1531 QSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA-- 1608
Cdd:PRK05605 31 DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 -----YLPIDLQHPTER---------------------------------IKFM--LQDAKSKLVIGEQKDL-AAIVHPS 1647
Cdd:PRK05605 111 ehnplYTAHELEHPFEDhgarvaivwdkvaptverlrrttpletivsvnmIAAMplLQRLALRLPIPALRKArAALTGPA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1648 IATFAFNELFDET---KVDLSSYKTtvITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL----WMQSeyplsatdtiL 1720
Cdd:PRK05605 191 PGTVPWETLVDAAiggDGSDVSHPR--PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkaWVPG----------L 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1721 QKTPCTFdVSVWEFFWSY----------LVGARLVIAPidAHRDPLaLLSLIQKYQVTtlhFVPSMLAVFENaateILSS 1790
Cdd:PRK05605 259 GDGPERV-LAALPMFHAYgltlcltlavSIGGELVLLP--APDIDL-ILDAMKKHPPT---WLPGVPPLYEK----IAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 AQRQSLPICRV---FCSGEALPTALAKSFTEHFSCELHNLYGPTEAAvdvsymDATLG--LHPEESCVAIGYPVWNTQLY 1865
Cdd:PRK05605 328 AEERGVDLSGVrnaFSGAMALPVSTVELWEKLTGGLLVEGYGLTETS------PIIVGnpMSDDRRPGYVGVPFPDTEVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1866 ILDQ--YLRPVPVGVDGELYLAGHQLAMGYLHRADLTasrfvANPFTAGqrMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:PRK05605 402 IVDPedPDETMPDGEEGELLVRGPQVFKGYWNRPEET-----AKSFLDG--WFRTGDVVVMEEDGFIRIVDRIKELIITG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1944 GQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSH 2022
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVeDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQ 554
|
....*..
gi 490930577 2023 NGKLDRK 2029
Cdd:PRK05605 555 LGKVRRR 561
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1543-2026 |
3.28e-30 |
|
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: 128.85 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1543 RITPEQTAL---SDENHQ---LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd17634 64 RENGDRTAIiyeGDDTSQsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVI--------GEQKDLAAIV----HPSIATFAFNELFDETKVDL------------------SS 1666
Cdd:cd17634 144 APEAVAGRIIDSSSRLLItadggvraGRSVPLKKNVddalNPNVTSVEHVIVLKRTGSDIdwqegrdlwwrdliakasPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILW-MQSEYPLSATDTILqktpCTFDVSvWEFFWSYLV----- 1740
Cdd:cd17634 224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYW----CTADVG-WVTGHSYLLygpla 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1741 -GARLVI---APIdaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPIcrVFCSGEALPTALAKSF 1816
Cdd:cd17634 299 cGATTLLyegVPN--WPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRI--LGSVGEPINPEAYEWY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFS---CELHNLYGPTEAA-VDVSYMDATLGLHPEESCVaigyPVWNTQLYILDQYLRPVPVGVDGELYLAGH--QLA 1890
Cdd:cd17634 375 WKKIGkekCPVVDTWWQTETGgFMITPLPGAIELKAGSATR----PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQT 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1891 MGYLHRADltasRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL----RLISGLDV-V 1965
Cdd:cd17634 451 RTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLvahpKVAEAAVVgI 526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1966 VHAISSEQNKANVQLVAYLqTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:cd17634 527 PHAIKGQAPYAYVVLNHGV-EPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1104-1382 |
4.01e-30 |
|
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: 125.93 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1104 LPL---QKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPV-FIyslHPTQAWP 1178
Cdd:cd19531 2 LPLsfaQQRLWFLDQLEPGSAaYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEV-DGEPVqVI---LPPLPLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 VQFCSVTPDL-------LEQTIQEALQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAY- 1249
Cdd:cd19531 78 LPVVDLSGLPeaereaeAQRLAREEARRPFDLARgP--LLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYa 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1250 ---QQTNQQLPVLEHSYetvikalsgRDHetskVIWQRD-----------------LADLQPLI--LFNQAQQAVQetSY 1307
Cdd:cd19531 156 aflAGRPSPLPPLPIQY---------ADY----AVWQREwlqgevlerqlaywreqLAGAPPVLelPTDRPRPAVQ--SF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1308 R-------LSAELGAKLQhKL-RQQGITLnvFMQMI--WAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIP 1377
Cdd:cd19531 221 RgarvrftLPAELTAALR-ALaRREGATL--FMTLLaaFQVLLHRYSGQDDIVVGTPVAGRNRA--ELEGLIGFFVNTLV 295
|
....*
gi 490930577 1378 VRVKL 1382
Cdd:cd19531 296 LRTDL 300
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
512-986 |
4.14e-30 |
|
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: 126.40 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 512 VNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGAS----FLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQ 587
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 588 LPQNIQQLHLDQEGVQTQIRKQDASDIPA-ENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNlilshkptiywpVLE 666
Cdd:cd05922 83 LRDALPASPDPGTVLDADGIRAARASAPAhEVSH---EDLALLLYTSGSTGSPKLVRLSHQNLLA------------NAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 667 AVNERFPDRPL-RAAHTHSFSFDSSWLQVF-WMLWGQELHIFDENMRRDAFglVQEIQQRQIDTLDLPPSFCAQMMTNGL 744
Cdd:cd05922 148 SIAEYLGITADdRALTVLPLSYDYGLSVLNtHLLRGATLVLTNDGVLDDAF--WEDLREHGATGLAGVPSTYAMLTRLGF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 745 fvENQHHPSLILI--GGEAAPLALWQQLN-AQPALFAHNLYGPTEYT--VDTFRAELKQTARPVIGNPIGNTQAYVLDRH 819
Cdd:cd05922 226 --DPAKLPSLRYLtqAGGRLPQETIARLReLLPGAQVYVMYGQTEATrrMTYLPPERILEKPGSIGLAIPGGEFEILDDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 820 LQRCPTGVIGELYISGfgiANGYLGRADlsAARFVANPFEHGQRMYrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIG 899
Cdd:cd05922 304 GTPTPPGEPGEIVHRG---PNVMKGYWN--DPPYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 900 EVENALSILTNVESAVVIAEPINNSHRLLgYCVVKDIELDEKTSeqlsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSG 979
Cdd:cd05922 378 EIEAAARSIGLIIEAAAVGLPDPLGEKLA-LFVTAPDKIDPKDV-------LRSLAERLPPYKVPATVRVVDELPLTASG 449
|
....*..
gi 490930577 980 KVDKKAL 986
Cdd:cd05922 450 KVDYAAL 456
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1530-2031 |
5.33e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 130.81 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDE-NHQLSFSEVRLQVCALAQQLQRaGVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:PRK08633 613 ALPPLAEAWIDTAKRNWSRLAVADStGGELSYGKALTGALALARLLKR-ELKDEENVGILLPPSVAGALANLALLLAGKV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 ylPIDLQHPTER--IKFMLQDAKSKLVIG--------EQKDLAAIVHPSIATFAFNELFDE-TKVD-------------- 1663
Cdd:PRK08633 692 --PVNLNYTASEaaLKSAIEQAQIKTVITsrkfleklKNKGFDLELPENVKVIYLEDLKAKiSKVDkltallaarllpar 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1664 -LSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFFWSY---- 1738
Cdd:PRK08633 770 lLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLP---------FFHSFgltv 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 ------LVGARLViapidAHRDPL---ALLSLIQKYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPIcrVFCSGEALP 1809
Cdd:PRK08633 841 tlwlplLEGIKVV-----YHPDPTdalGIAKLVAKHRATILLGTPTFLRLY--LRNKKLHPLMFASLRL--VVAGAEKLK 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 TALAKSFTEHFSCELHNLYGPTE----AAVDV-SYMDATLGLHPEESCVAIGYPVWNTQLYILD-QYLRPVPVGVDGELY 1883
Cdd:PRK08633 912 PEVADAFEEKFGIRILEGYGATEtspvASVNLpDVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLIL 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1884 LAGHQLAMGYLHRADLTASRFVAnpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-- 1961
Cdd:PRK08633 992 IGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGge 1068
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1962 -LDVVVHAISSEqnKANVQLVAyLQTTAPVDIDQLKKQLAK-HLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK08633 1069 eVVFAVTAVPDE--KKGEKLVV-LHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1542-1999 |
7.60e-30 |
|
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: 127.35 E-value: 7.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGvQAGDIVAVALPRSVKLSIAILAVIEAGA----AYLP 1611
Cdd:cd05931 3 AAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAiavpLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1612 iDLQHPTERIKFMLQDAKSKLVIGEQKDLAAiVHPSIATFAFNELFDETKVDL------SSYKTTVITPQHPAYLIYTSG 1685
Cdd:cd05931 82 -TPGRHAERLAAILADAGPRVVLTTAAALAA-VRAFAASRPAAGTPRLLVVDLlpdtsaADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1686 TTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEF-FWSYLVGARLV-IAPIDAHRDPLALLSLIQ 1763
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVlMSPAAFLRRPLRWLRLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTlHFVPSMlAvFENAATEIlSSAQRQSLPICRV---FCSGEAL-PTALAKsFTEHFSCelHNL--------YGPT 1831
Cdd:cd05931 240 RYRATI-SAAPNF-A-YDLCVRRV-RDEDLEGLDLSSWrvaLNGAEPVrPATLRR-FAEAFAP--FGFrpeafrpsYGLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1832 EAAVDVS-----------YMDATLGLHPEESC----------VAIGYPVWNTQLYILD-QYLRPVPVGVDGELYLAGHQL 1889
Cdd:cd05931 313 EATLFVSggppgtgpvvlRVDRDALAGRAVAVaaddpaarelVSCGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1890 AMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHaDGSIqYI-GRADDQLKIRGQRIELGEIEQQLRLISGL----DV 1964
Cdd:cd05931 393 ASGYWGRPEATAETFGALAATDEGGWLRTGDLGFLH-DGEL-YItGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpgCV 470
|
490 500 510
....*....|....*....|....*....|....*
gi 490930577 1965 VVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQL 1999
Cdd:cd05931 471 AAFSVPDDGEERLVVVAEVERGADPADLAAIAAAI 505
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1541-2031 |
8.24e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 126.07 E-value: 8.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1541 QARITPEQTALSD--ENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK09088 4 HARLQPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQKdLAAIVHPSIATFAFNELFDETKVDLSSYkttvITPQHPAYLIYTSGTTGQPKGVMVSHQ 1698
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDA-VAAGRTDVEDLAAFIASADALEPADTPS----IPPERVSLILFTSGTSGQPKGVMLSER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1699 AIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFFwsYLVGARLVIAPIDAHR---------DPLALLSLIQKYQVTT 1769
Cdd:PRK09088 159 NLQQTAHNFGVLGRVDAHSSFLCDAP---------MF--HIIGLITSVRPVLAVGgsilvsngfEPKRTLGRLGDPALGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHF--VPSMLAVFENAATEILSSAQRqslpICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEA------AVDVSYMD 1841
Cdd:PRK09088 228 THYfcVPQMAQAFRAQPGFDAAALRH----LTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAgtvfgmSVDCDVIR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1842 ATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvanpftAGQRMYRTGDI 1921
Cdd:PRK09088 303 AKAG--------AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLA 2000
Cdd:PRK09088 369 ARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIrECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLS 448
|
490 500 510
....*....|....*....|....*....|.
gi 490930577 2001 KHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK09088 449 TRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1542-2033 |
1.08e-29 |
|
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: 126.46 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTAL-----SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd05970 27 AKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKD-----------------LAAIVHPSIAT--FAFNELFDETKVDLSSYKTTVITPQHP 1677
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAIAEDnipeeiekaapecpskpKLVWVGDPVPEgwIDFRKLIKNASPDFERPTANSYPCGED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIY-TSGTTGQPKgvMVSHQ------AIVNRILWMQSE---YPLSATDTILQKtpctfdvSVW-EFFWSYLVGARLVI 1746
Cdd:cd05970 187 ILLVYfSSGTTGMPK--MVEHDftyplgHIVTAKYWQNVReggLHLTVADTGWGK-------AVWgKIYGQWIAGAAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1747 APIDAHrDPLALLSLIQKYQVTTLHFVPSmlaVFENAATEILSSAQRQSLPICRVfcSGEALPTALAKSFTEHFSCELHN 1826
Cdd:cd05970 258 YDYDKF-DPKALLEKLSKYGVTTFCAPPT---IYRFLIREDLSRYDLSSLRYCTT--AGEALNPEVFNTFKEKTGIKLME 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1827 LYGPTEAAVDV---SYMDATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYL---AGHQLAM--GYLHRAD 1898
Cdd:cd05970 332 GFGQTETTLTIatfPWMEPKPG--------SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGLfgGYYKDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1899 LTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIelGEIEQQLRLISGLDVVVHAISSEQN---- 1974
Cdd:cd05970 404 KTAEVWHDG-------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRI--GPFEVESALIQHPAVLECAVTGVPDpirg 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1975 ---KANVQLVAYLQTTapvdiDQLKKQLAKHLPAYMVPTHY----MLVEQFPLSHNGKLDRKALPQ 2033
Cdd:cd05970 475 qvvKATIVLAKGYEPS-----EELKKELQDHVKKVTAPYKYprivEFVDELPKTISGKIRRVEIRE 535
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
488-986 |
6.72e-29 |
|
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: 122.40 E-value: 6.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 488 ERTAIVSGERpnlqHLSFAELAVKVNQL-TRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:cd05941 1 DRIAIVDDGD----SITYADLVARAARLaNRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANPLFVLttqalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfqDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:cd05941 77 EYVITDSEPSLVL---------------------------------------------DPALILYTSGTTGRPKGVVLTH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 647 GSLLNLILShkptiywpVLEAVNERFPDR-----PLRaaHTHSFsfdssWLQVFWMLW-GQELHI---FD---ENMRRD- 713
Cdd:cd05941 112 ANLAANVRA--------LVDAWRWTEDDVllhvlPLH--HVHGL-----VNALLCPLFaGASVEFlpkFDpkeVAISRLm 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 714 ----AFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvenqHHPSLILIGGEAAP---LALWQQLNAQPALfahNLYGPTE 786
Cdd:cd05941 177 psitVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA-----ERLRLMVSGSAALPvptLEEWEAITGHTLL---ERYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 787 yTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRC-PTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrm 864
Cdd:cd05941 249 -IGMALSNPLDGERRPgTVGMPLPGVQARIVDEETGEPlPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------ 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 865 YRTGDLVRWNSAGKLEFMGR-CDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELdEKTS 943
Cdd:cd05941 322 FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVP----DPDWGERVVAVVVL-RAGA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490930577 944 EQLS-QQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05941 397 AALSlEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
492-986 |
7.07e-29 |
|
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: 123.58 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 492 IVSGERPNLqhlSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCE 571
Cdd:cd05926 7 VVPGSTPAL---TYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 572 DANPLFVLT-------TQALAQQLPQNIQQLHLDqegVQTQIRKQDASDIPAENRKFDFQ---------DVAYVIFTSGS 635
Cdd:cd05926 84 DLGSKLVLTpkgelgpASRAASKLGLAILELALD---VGVLIRAPSAESLSNLLADKKNAksegvplpdDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 636 TGRPKGVMNTHGSLL----NLILSHKPTiywpvleavnerFPDR-----PLraAHTHSF------------------SFD 688
Cdd:cd05926 161 TGRPKGVPLTHRNLAasatNITNTYKLT------------PDDRtlvvmPL--FHVHGLvasllstlaaggsvvlppRFS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 689 SSwlqVFWmlwgqelhifdenmrrdafglvQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLALwQ 768
Cdd:cd05926 227 AS---TFW----------------------PDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPP-A 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 769 QLNAQPALFAHNL---YGPTEYTVDTFRAELKQTARPV--IGNPIGnTQAYVLDRHLQRCPTGVIGELYISGFGIANGYL 843
Cdd:cd05926 281 VLEALEATFGAPVleaYGMTEAAHQMTSNPLPPGPRKPgsVGKPVG-VEVRILDEDGEILPPGVVGEICLRGPNVTRGYL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 844 GRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinn 923
Cdd:cd05926 360 NNPEANAEAAFKDGW------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVP--- 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 924 sHRLLGYCVVKDIELDEK---TSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05926 431 -DEKYGEEVAAAVVLREGasvTEEEL----RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1526-2031 |
1.96e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 123.23 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1526 QYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK06178 27 EYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GAAYLPIDLQHPTERIKFMLQDAKSKLVIG------------EQKDLAAIVH-------PSIATFAFNELFDETKV---- 1662
Cdd:PRK06178 107 GAVHVPVSPLFREHELSYELNDAGAEVLLAldqlapvveqvrAETSLRHVIVtsladvlPAEPTLPLPDSLRAPRLaaag 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1663 --DL--SSYKTTVITPQHPAYLI------YTSGTTGQPKGVMVSHQaivNRILWMQSEYPLSATDTilqkTPCTFdVSVW 1732
Cdd:PRK06178 187 aiDLlpALRACTAPVPLPPPALDalaalnYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVGG----EDSVF-LSFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1733 EFFW----------SYLVGARLVIApidAHRDPLALLSLIQKYQVTtlhfvpSMLAVFENAAtEIL---SSAQR--QSLP 1797
Cdd:PRK06178 259 PEFWiagenfgllfPLFSGATLVLL---ARWDAVAFMAAVERYRVT------RTVMLVDNAV-ELMdhpRFAEYdlSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1798 ICRVFCSGEALPTALAKSFTEHFSCELHNL-YGPTEA----AVDVSYMDATLGLHPEEscVAIGYPVWNTQLYILD-QYL 1871
Cdd:PRK06178 329 QVRVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTEThtcdTFTAGFQDDDFDLLSQP--VFVGLPVPGTEFKICDfETG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1872 RPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGE 1951
Cdd:PRK06178 407 ELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1952 IEQQLRL---ISGLDVVVHAissEQNKANVQlVAYLQTT--APVDIDQLKKQLAKHLPAYMVPTHYmLVEQFPLSHNGKL 2026
Cdd:PRK06178 480 VEALLGQhpaVLGSAVVGRP---DPDKGQVP-VAFVQLKpgADLTAAALQAWCRENMAVYKVPEIR-IVDALPMTATGKV 554
|
....*
gi 490930577 2027 DRKAL 2031
Cdd:PRK06178 555 RKQDL 559
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1531-2026 |
2.15e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 122.76 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1531 QSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK08314 9 ETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQkDLAAIVHPSIATFAF---------NELFDETKVDLSSYKTT---------- 1670
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGS-ELAPKVAPAVGNLRLrhvivaqysDYLPAEPEIAVPAWLRAepplqalapg 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 ------------------VITPQHPAYLIYTSGTTGQPKGVMVSHQ----AIVNRILWMQSeyplSATDTILQKTPcTFD 1728
Cdd:PRK08314 168 gvvawkealaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRtvmaNAVGSVLWSNS----TPESVVLAVLP-LFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1729 VS--VWEFFWSYLVGARLVIAPI-DahRDplALLSLIQKYQVTTLHFVPSMLAVFenaateiLSSAQRQSLPICRVFC-- 1803
Cdd:PRK08314 243 VTgmVHSMNAPIYAGATVVLMPRwD--RE--AAARLIERYRVTHWTNIPTMVVDF-------LASPGLAERDLSSLRYig 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 -SGEALPTALAKSFTEHFSCELHNLYGPTE--AAVDVSYMDatlglHPEESCVAIgyPVWNTQLYILD-QYLRPVPVGVD 1879
Cdd:PRK08314 312 gGGAAMPEAVAERLKELTGLDYVEGYGLTEtmAQTHSNPPD-----RPKLQCLGI--PTFGVDARVIDpETLEELPPGEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1880 GELYLAGHQLAMGYLHRADLTASRFVAnpfTAGQRMYRTGDIARWHADGsiqYIGRAdDQLK----IRGQRIELGEIE-- 1953
Cdd:PRK08314 385 GEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEG---YFFIT-DRLKrminASGFKVWPAEVEnl 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1954 -------QQLRLISGLDvvvhAISSEQNKANVQLVA-YLQTTAPVDIDQLKKQlakHLPAYMVPTHYMLVEQFPLSHNGK 2025
Cdd:PRK08314 458 lykhpaiQEACVIATPD----PRRGETVKAVVVLRPeARGKTTEEEIIAWARE---HMAAYKYPRIVEFVDSLPKSGSGK 530
|
.
gi 490930577 2026 L 2026
Cdd:PRK08314 531 I 531
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1535-2031 |
3.16e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 122.02 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1535 QQLLREQARiTPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIdl 1614
Cdd:PRK06188 16 HLLVSALKR-YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1615 qHPT---ERIKFMLQDAKSK-LVIGEQK------DLAAIVhPSI-ATFAFNELfdETKVDLSSYKTTV--------ITPQ 1675
Cdd:PRK06188 93 -HPLgslDDHAYVLEDAGIStLIVDPAPfveralALLARV-PSLkHVLTLGPV--PDGVDLLAAAAKFgpaplvaaALPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTfDVSVWEFFWSYLVGARLVIAPidaHRDP 1755
Cdd:PRK06188 169 DIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVLA---KFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLIQKYQVTTLHFVPSMLAVF---ENAATEILSSAQrqslpicRVFCSGEAL-PTALAKSFtEHFSCELHNLYGPT 1831
Cdd:PRK06188 245 AEVLRAIEEQRITATFLVPTMIYALldhPDLRTRDLSSLE-------TVYYGASPMsPVRLAEAI-ERFGPIFAQYYGQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1832 EAAVDVSYM--DATLGLHPE--ESCvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvan 1907
Cdd:PRK06188 317 EAPMVITYLrkRDHDPDDPKrlTSC---GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1908 pftAGQRMyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlrlisglDVVV--HAISS--------EQNKAN 1977
Cdd:PRK06188 391 ---RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVE---------DVLAehPAVAQvavigvpdEKWGEA 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 490930577 1978 VQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06188 458 VTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1537-2025 |
7.67e-28 |
|
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: 120.10 E-value: 7.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:cd12118 9 FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKdlaaivhpsiatFAFNELFDETKVDLssyktTVITPQ---HPAYLIYTSGTTGQPKGV 1693
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDRE------------FEYEDLLAEGDPDF-----EWIPPAdewDPIALNYTSGTTGRPKGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1694 MVSH-----QAIVNRILWMQSEYPlsatdTILQKTPcTFDVSVWEFFWS-YLVGARLVIAPidaHRDPLALLSLIQKYQV 1767
Cdd:cd12118 152 VYHHrgaylNALANILEWEMKQHP-----VYLWTLP-MFHCNGWCFPWTvAAVGGTNVCLR---KVDAKAIYDLIEKHKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1768 TtlHF--VPSMLAVFENAAteilsSAQRQSLP-ICRVFCSGEALPTALAKSFTEHFSCELHnLYGPTEA---AVDVSYMD 1841
Cdd:cd12118 223 T--HFcgAPTVLNMLANAP-----PSDARPLPhRVHVMTAGAPPPAAVLAKMEELGFDVTH-VYGLTETygpATVCAWKP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1842 ATLGLHPEESCV-----AIGYPVwNTQLYILD-QYLRPVPV-GVD-GELYLAGHQLAMGYLHRADLTASRFvanpftAGQ 1913
Cdd:cd12118 295 EWDELPTEERARlkarqGVRYVG-LEEVDVLDpETMKPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAF------RGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1914 rMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQ----NKANVQLVAYLQTTA 1988
Cdd:cd12118 368 -WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAvLEAAVVARPDEKwgevPCAFVELKEGAKVTE 446
|
490 500 510
....*....|....*....|....*....|....*..
gi 490930577 1989 pvdiDQLKKQLAKHLPAYMVPTHYMLVEqFPLSHNGK 2025
Cdd:cd12118 447 ----EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1530-2033 |
1.27e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 120.23 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK06164 8 RADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQK----DLAAI---VHPSI-----ATFAFNELFDETKVDLSsYKTTVITPQH- 1676
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVWPGfkgiDFAAIlaaVPPDAlpplrAIAVVDDAADATPAPAP-GARVQLFALPd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 ----------------PAYLIYTSGTTGQPKGVM------VSHQAIVNRIlwmqseYPLSATDTILQKTP-CTFdvsvwe 1733
Cdd:PRK06164 167 pappaaageraadpdaGALLFTTSGTTSGPKLVLhrqatlLRHARAIARA------YGYDPGAVLLAALPfCGV------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1734 FFWSYLV-----GARLVIAPI-DAHRDplalLSLIQKYQVTtlHFVPSmlavfENAATEILSSA-QRQSLPICRVF---- 1802
Cdd:PRK06164 235 FGFSTLLgalagGAPLVCEPVfDAART----ARALRRHRVT--HTFGN-----DEMLRRILDTAgERADFPSARLFgfas 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1803 ---CSGEALPTALAKSFTehfsceLHNLYGPTEAAVDVSYMDATLglhPE-ESCVAIGYPVW-NTQLYILD-QYLRPVPV 1876
Cdd:PRK06164 304 fapALGELAALARARGVP------LTGLYGSSEVQALVALQPATD---PVsVRIEGGGRPASpEARVRARDpQDGALLPD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1877 GVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:PRK06164 375 GESGEIEIRAPSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1957 RLISGL-DVVVHAISSEQNKANVQLVAyLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFP--LSHNG-KLDRKALP 2032
Cdd:PRK06164 449 EALPGVaAAQVVGATRDGKTVPVAFVI-PTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPvtESANGaKIQKHRLR 527
|
.
gi 490930577 2033 Q 2033
Cdd:PRK06164 528 E 528
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1549-2035 |
2.69e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 119.03 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1549 TALSDENHqLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDA 1628
Cdd:PRK12406 4 TIISGDRR-RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1629 KSKLVIGeQKDLAAIVHPSI--------------------------ATFAFNELFDETKVDLSSYkTTVITPQhPAYLIY 1682
Cdd:PRK12406 83 GARVLIA-HADLLHGLASALpagvtvlsvptppeiaaayrispallTPPAGAIDWEGWLAQQEPY-DGPPVPQ-PQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1683 TSGTTGQPKGV---------MVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFfwsylvGARLVIAPidaHR 1753
Cdd:PRK12406 160 TSGTTGHPKGVrraaptpeqAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRL------GGVLVLQP---RF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpicRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTE 1832
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSL---RHVIHAAApCPADVKRAMIEWWGPVIYEYYGSTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 AAVdVSYMDATLGL-HPEescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLA----------GHQLAMGYLHRADLTA 1901
Cdd:PRK12406 308 SGA-VTFATSEDALsHPG----TVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRiagnpdftyhNKPEKRAEIDRGGFIT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1902 SrfvanpftagqrmyrtGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQL 1980
Cdd:PRK12406 383 S----------------GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVhDCAVFGIPDAEFGEALMA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1981 VAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK12406 447 VVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1534-2033 |
3.78e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 118.94 E-value: 3.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARitPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:PRK10946 27 LTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHP-TERIKFMLQDAKSKLVIGEQKDLAA---------IVHPSIATFAFneLFDETKVDLSSY-----KTTVITPQHP- 1677
Cdd:PRK10946 105 FSHQrSELNAYASQIEPALLIADRQHALFSdddflntlvAEHSSLRVVLL--LNDDGEHSLDDAinhpaEDFTATPSPAd 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 --AYLIYTSGTTGQPKGVMVSHQaivnrilwmQSEYPLSATDTILQKTPCT-----------FDVSVWEFFWSYLVGARL 1744
Cdd:PRK10946 183 evAFFQLSGGSTGTPKLIPRTHN---------DYYYSVRRSVEICGFTPQTrylcalpaahnYPMSSPGALGVFLAGGTV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 VIAPidahrDPLALL--SLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLPICRVfcSGEALPTALAKSFTEHFSC 1822
Cdd:PRK10946 254 VLAP-----DPSATLcfPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQV--GGARLSETLARRIPAELGC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1823 ELHNLYGPTEAAVDVSYMDATlglhPEESCVAIGYPVW-NTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTA 1901
Cdd:PRK10946 327 QLQQVFGMAEGLVNYTRLDDS----DERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1902 SRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLisgLDVVVHA--ISSEQNKANVQ 1979
Cdd:PRK10946 403 SAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLR---HPAVIHAalVSMEDELMGEK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1980 LVAYLQTTAPVDIDQLKKQLAKHLPA-YMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK10946 474 SCAFLVVKEPLKAVQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1546-1956 |
4.39e-27 |
|
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: 118.11 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSD--ENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID-LQHPTERIK 1622
Cdd:cd05904 19 PSRPALIDaaTGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1623 FMlQDAKSKLVIG--------EQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVM 1694
Cdd:cd05904 99 QV-KDSGAKLAFTtaelaeklASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQ------AIVNRILWMQSEYPlsatDTILQKTPctfdvsvweFFWSY----------LVGARLVIAPidaHRDPLAL 1758
Cdd:cd05904 178 LTHRnliamvAQFVAGEGSNSDSE----DVFLCVLP---------MFHIYglssfalgllRLGATVVVMP---RFDLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1759 LSLIQKYQVTTLHFVPSMLAVFENAAteILSSAQRQSLPicRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDV 1837
Cdd:cd05904 242 LAAIERYKVTHLPVVPPIVLALVKSP--IVDKYDLSSLR--QIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1838 SYMDAtlglhPEESCV---AIGYPVWNTQLYILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpftaGQ 1913
Cdd:cd05904 318 AMCFA-----PEKDRAkygSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KE 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 490930577 1914 RMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:cd05904 387 GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL 429
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1513-2031 |
7.86e-27 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 117.94 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1513 AEEHDLI-QKTNQTQYYVRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPR 1591
Cdd:PRK06155 1 GEPLGAGlAARAVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1592 SVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVHPSIATFAFNELF-----DETKVDLSs 1666
Cdd:PRK06155 81 RIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWlldapASVSVPAG- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTT------------VITPQHPAYLIYTSGTTGQPKGVMVSHQaivnRILW----MQSEYPLSATDTILQKTPCTFDVS 1730
Cdd:PRK06155 160 WSTAplppldapapaaAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 VWEFFWSYLVGARLVIAP-IDAHRDPLALlsliQKYQVTTLHFVPSMLAVFENAATEILSSAQRqslpiCRVFCSGeALP 1809
Cdd:PRK06155 236 LNAFFQALLAGATYVLEPrFSASGFWPAV----RRHGATVTYLLGAMVSILLSQPARESDRAHR-----VRVALGP-GVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1810 TALAKSFTEHFSCELHNLYGPTEAAVDVSymdatlGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG--- 1886
Cdd:PRK06155 306 AALHAAFRERFGVDLLDGYGSTETNFVIA------VTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdep 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASrfvanpftAGQRM-YRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDV 1964
Cdd:PRK06155 380 FAFATGYFGMPEKTVE--------AWRNLwFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAvAAA 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1965 VVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06155 452 AVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
503-983 |
1.56e-26 |
|
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: 115.56 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldYPIDRmqmmceDANPLFVLTTq 582
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFR------EHELAFILRR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQQLPqniqqlhldqegvqtqirkqdasdIPAENRKFDFQ----DVAYVIFTSGSTGRPKGVMNTHGSLLNLILshkp 658
Cdd:cd05903 72 AKAKVFV------------------------VPERFRQFDPAampdAVALLLFTSGTTGEPKGVMHSHNTLSASIR---- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 659 tiywPVLEAVNERFPDRPLRAAH-THSFSFDSSWLQVfwMLWGQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCA 737
Cdd:cd05903 124 ----QYAERLGLGPGDVFLVASPmAHQTGFVYGFTLP--LLLGAPVVLQD---IWDPDKALALMREHGVTFMMGATPFLT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 738 QMMTNGLFVeNQHHPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVI--GNPIGNTQA 813
Cdd:cd05903 195 DLLNAVEEA-GEPLSRLrtFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYtdGRPLPGVEI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 814 YVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAArfvanpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIR- 892
Cdd:cd05903 274 KVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGRSKDII-IRg 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 893 GYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVKD---IELDEKTseqlsqQYLSqlRQNLPEYMVPSALT 968
Cdd:cd05903 346 GENIPVLEVEDLLLGHPGVIEAAVVALPDERlGERACAVVVTKSgalLTFDELV------AYLD--RQGVAKQYWPERLV 417
|
490
....*....|....*
gi 490930577 969 VMSEFPRNVSGKVDK 983
Cdd:cd05903 418 HVDDLPRTPSGKVQK 432
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
471-986 |
1.70e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 116.44 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 471 QYNNVLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNS 550
Cdd:PRK06187 4 YPLTIGRILRHGARKHPDKEAVYFDGRR----TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 551 GASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHL--------DQEGVQTQIRKQDASD-IPAENRKF 621
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTvrtvivegDGPAAPLAPEVGEYEElLAAASDTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 622 DFQDV----AYVIF-TSGSTGRPKGVMNTHGSLLNLILShkpTIYWPVLEAvNERF-PDRPLraAHTHSfsfdSSWLQVF 695
Cdd:PRK06187 160 DFPDIdendAAAMLyTSGTTGHPKGVVLSHRNLFLHSLA---VCAWLKLSR-DDVYlVIVPM--FHVHA----WGLPYLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 696 WMLwGQELHIfdenMRR-DAFGLVQEIQQRQIDTldlppSFCA----QMMTNGLFVENQHHPSL--ILIGGEAAPLALwq 768
Cdd:PRK06187 230 LMA-GAKQVI----PRRfDPENLLDLIETERVTF-----FFAVptiwQMLLKAPRAYFVDFSSLrlVIYGGAALPPAL-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 769 qLNAQPALFAHNL---YGPTE----YTVDTFRAELK-QTARPV-IGNPIGNTQAYVLDRHLQRCP--TGVIGELYISGFG 837
Cdd:PRK06187 298 -LREFKEKFGIDLvqgYGMTEtspvVSVLPPEDQLPgQWTKRRsAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPW 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 838 IANGYLGRADLSAARFVanpfeHGqrMYRTGDLvrwnsaGKLEFMG------RCDDQIKIRG---YRVeigEVENALSIL 908
Cdd:PRK06187 377 LMQGYWNRPEATAETID-----GG--WLHTGDV------GYIDEDGylyitdRIKDVIISGGeniYPR---ELEDALYGH 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 909 TNVESAVVIAEPINNS-HRLLGYCVVKD-IELDEKtseqlsqQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06187 441 PAVAEVAVIGVPDEKWgERPVAVVVLKPgATLDAK-------ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
481-986 |
3.30e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 115.39 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 481 EQVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLD 560
Cdd:PRK07656 13 RAARRFGDKEAYVFGD----QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 561 YPIDRMQMMCE--DANPLFVLTT-QALAQQLPQNIQQLHL-----DQEGVQTQIRKQDASDI--PAENRKF----DFQDV 626
Cdd:PRK07656 89 YTADEAAYILArgDAKALFVLGLfLGVDYSATTRLPALEHvviceTEEDDPHTEKMKTFTDFlaAGDPAERapevDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 627 AYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiyWPVLEAVNERfpDRPLrAAHT--HSFSFDSSWLQ----------- 693
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMLTHRQLLSNAAD------WAEYLGLTEG--DRYL-AANPffHVFGYKAGVNAplmrgatilpl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 694 -VFwmlwgqelhifdenmrrDAFGLVQEIQQRQIDTLDLPPSfcaqmMTNGLF------VENQHHPSLILIGGEAAPLAL 766
Cdd:PRK07656 240 pVF-----------------DPDEVFRLIETERITVLPGPPT-----MYNSLLqhpdrsAEDLSSLRLAVTGAASMPVAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 767 WQ----QLNAQPALFAhnlYGPTEYT-VDTF-RAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIA 839
Cdd:PRK07656 298 LErfesELGVDIVLTG---YGLSEASgVTTFnRLDDDRKTVAgTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 840 NGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAE 919
Cdd:PRK07656 375 KGYYDDPEATAAAIDADGWLH------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 920 PinnsHRLLG-----YCVVKD-IELDEktseqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07656 449 P----DERLGevgkaYVVLKPgAELTE-------EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1542-2033 |
4.27e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.88 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLqRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQKDLAAIVHPSIATFafneLFDETKVDLSSYKTT---VITPQH-PAYLIYTSGTTGQPKGVMVSH 1697
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLPDEEGRVI----EIDEWKRMIEKYLPTyapIENVQNaPFYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 QAivnrilWMQS------EYPLSATDTILqkTPCTFDVSVWEF--FWSYLVGARLVIAPidaHRDPLALLSLIQKYQVTT 1769
Cdd:PRK07638 166 QS------WLHSfdcnvhDFHMKREDSVL--IAGTLVHSLFLYgaISTLYVGQTVHLMR---KFIPNQVLDKLETENISV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHFVPSMlavfenaaTEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVdVSYmdatlgLHP 1848
Cdd:PRK07638 235 MYTVPTM--------LESLYKENRVIENKMKIISSGAKWEAEAKEKIKNIFpYAKLYEFYGASELSF-VTA------LVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCV---AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTagqrmyrTGDIARWH 1925
Cdd:PRK07638 300 EESERrpnSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMT-------VRDVGYED 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1926 ADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVVhAISSEQNKANVQLVAYLQTTApvDIDQLKKQLAKHLPA 2005
Cdd:PRK07638 373 EEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV-VIGVPDSYWGEKPVAIIKGSA--TKQQLKSFCLQRLSS 449
|
490 500
....*....|....*....|....*...
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK07638 450 FKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1526-2033 |
4.70e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 115.62 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1526 QYYVRQSTLQQLLREQARITPEQTALSDeNHQLSFSEVRLQVCA--LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:PRK06087 17 QGYWGDASLADYWQQTARAMPDKIAVVD-NHGASYTYSALDHAAsrLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG----EQKDLAAIVHP---SIATFAFNELFDETKVDLSSYKTTVI---- 1672
Cdd:PRK06087 96 KVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfKQTRPVDLILPlqnQLPQLQQIVGVDKLAPATSSLSLSQIiady 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TP-QHP--------AYLIYTSGTTGQPKGVMVSHqaivNRILWMQSEYP----LSATDTILQKTPCTFDVSvweFFWS-- 1737
Cdd:PRK06087 176 EPlTTAitthgdelAAVLFTSGTEGLPKGVMLTH----NNILASERAYCarlnLTWQDVFMMPAPLGHATG---FLHGvt 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1738 --YLVGARLVIapiDAHRDPLALLSLIQKYQVTTLH----FVPSMLAVFENAATEilssaqrqsLPICRVF-CSGEALPT 1810
Cdd:PRK06087 249 apFLIGARSVL---LDIFTPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQPAD---------LSALRFFlCGGTTIPK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1811 ALAKSFTEHfSCELHNLYGPTEAAVDVsymdatlgLHPEESCVAI-----GYPVWNTQLYILDQYLRPVPVGVDGELYLA 1885
Cdd:PRK06087 317 KVARECQQR-GIKLLSVYGSTESSPHA--------VVNLDDPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1886 GHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDqLKIR-GQRIELGEIEQQLRLISGL-D 1963
Cdd:PRK06087 388 GPNVFMGYLDEPELTARALDEEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIhD 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577 1964 VVVHAISSEqnKANVQLVAYLQTTAPVDIDQLKKQLA----KHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK06087 461 ACVVAMPDE--RLGERSCAYVVLKAPHHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
504-986 |
9.49e-26 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 112.91 E-value: 9.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 504 SFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedaNPLFvlTTQA 583
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL----------------FALF--GPEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 584 LAQQLPQNiqqlhldqegvQTQIRKQDASDipaenrkfdfqDVAYVIFTSGSTGRPKGVMNTHgsllNLILSHKPTIYWP 663
Cdd:cd05971 70 LEYRLSNS-----------GASALVTDGSD-----------DPALIIYTSGTTGPPKGALHAH----RVLLGHLPGVQFP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 664 vleavNERFPdRPLRAAHTHSfsfDSSW----LQVF--WMLWGqeLHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSFC 736
Cdd:cd05971 124 -----FNLFP-RDGDLYWTPA---DWAWigglLDVLlpSLYFG--VPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTAL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 737 AQMMTNGlfvENQHHPSL----ILIGGEA--APLALW--QQLNAQpalfAHNLYGPTEYTVDTFRAELKQTARP-VIGNP 807
Cdd:cd05971 193 KMMRQQG---EQLKHAQVklraIATGGESlgEELLGWarEQFGVE----VNEFYGQTECNLVIGNCSALFPIKPgSMGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 808 IGNTQAYVLDRHLQRCPTGVIGELYISgFGIANGYLG--RADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRC 885
Cdd:cd05971 266 IPGHRVAIVDDNGTPLPPGEVGEIAVE-LPDPVAFLGywNNPSATEKKMAGDW------LLTGDLGRKDSDGYFWYVGRD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 886 DDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVkdIELDEKTSEQLSQQYLSQLRQNLPEYMVPS 965
Cdd:cd05971 339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV--LNPGETPSDALAREIQELVKTRLAAHEYPR 416
|
490 500
....*....|....*....|.
gi 490930577 966 ALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05971 417 EIEFVNELPRTATGKIRRREL 437
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1102-1435 |
1.46e-25 |
|
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: 112.09 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRHPQL--------GGHFDSELA---EEPVFIY 1169
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPaYNIPGAWRLTGPLDVEALREALRDVVARHEALrtllvrddGGVPRQEILppgPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1170 SLHPTQAWPVQfcsvtpdLLEQTIQEALQQPIHLDQPYgLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDfIKAY 1249
Cdd:cd19539 83 DLSDPDSDRER-------RLEELLRERESRGFDLDEEP-PIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARD-LAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1250 QQTNQQ-----LPVLEHSYETVikALSGRDHETSKVI------WQRDLADLQPLILFNQAQQAVQ------ETSYRLSAE 1312
Cdd:cd19539 154 YAARRKgpaapLPELRQQYKEY--AAWQREALAAPRAaelldfWRRRLRGAEPTALPTDRPRPAGfpypgaDLRFELDAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1313 LGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWEQL 1392
Cdd:cd19539 232 LVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLI 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490930577 1393 PQLQQLHVEHLEHDGLGLSAIQQLIAQGN------LFDSLLVVENYPDN 1435
Cdd:cd19539 310 ARVRKALVDAQRHQELPFQQLVAELPVDRdagrhpLVQIVFQVTNAPAG 358
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1517-2031 |
1.76e-25 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 114.51 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1517 DLIQKTNQTQYYV--RQSTLQQLLREQARITPEQTALSDENHQ-----LSFSEVRLQVCALAQQLQRAGVQAGDIVAVAL 1589
Cdd:cd05968 44 DLSGGKPWAAWFVggRMNIVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1590 PRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI--------GEQKDLAAIVHPSIATFAFNE------ 1655
Cdd:cd05968 124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItadgftrrGREVNLKEEADKACAQCPTVEkvvvvr 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 ----LFDETKVDLSSYKTTVITP---------QHPAYLIYTSGTTGQPKGVMVSHQAI-VNRILWMQSEYPLSATDTILQ 1721
Cdd:cd05968 204 hlgnDFTPAKGRDLSYDEEKETAgdgaertesEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTW 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1722 KTPCTFDVSVWEFFWSYLVGARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpi 1798
Cdd:cd05968 284 FTDLGWMMGPWLIFGGLILGATMVLydgAP--DHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSL-- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1799 cRVFCS-GEALPTALAKSFTEHF---SCELHNLYGPTEAAvdvsymDATLGLHPEESCVAIGY--PVWNTQLYILDQYLR 1872
Cdd:cd05968 360 -RVLGStGEPWNPEPWNWLFETVgkgRNPIINYSGGTEIS------GGILGNVLIKPIKPSSFngPVPGMKADVLDESGK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1873 PVPVGVdGELYLAGHQLAM--GYLHRADltasRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELG 1950
Cdd:cd05968 433 PARPEV-GELVLLAPWPGMtrGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPA 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1951 EIEQQL----RLISGLDV-VVHAISSEqnkANVQLVAYLQTTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHN 2023
Cdd:cd05968 508 EIESVLnahpAVLESAAIgVPHPVKGE---AIVCFVVLKPGVTPTEAlaEELMERVADELGKPLSPERILFVKDLPKTRN 584
|
....*...
gi 490930577 2024 GKLDRKAL 2031
Cdd:cd05968 585 AKVMRRVI 592
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
562-987 |
2.00e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 111.61 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 562 PIDRMQMMCeDANPLFVLTTQAL----AQQLPQNIqqlHLDQEGVQTQIRKQDAsdipaenrKFDFQDVAYVIFTSGSTG 637
Cdd:cd05934 27 PGDRVALML-DNCPEFLFAWFALaklgAVLVPINT---ALRGDELAYIIDHSGA--------QLVVVDPASILYTSGTTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 638 RPKGVMNTHGSLLNlilshkptiyWPVLEAvnERFPDRPLRAAHT-----HSFSFDSSWLQVFWMlwGQELHIFDENMRR 712
Cdd:cd05934 95 PPKGVVITHANLTF----------AGYYSA--RRFGLGEDDVYLTvlplfHINAQAVSVLAALSV--GATLVLLPRFSAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 713 DAFGLVQEIQQRQIDTLDLPPSF-CAQMMTnglfVENQHHPsLILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDT 791
Cdd:cd05934 161 RFWSDVRRYGATVTNYLGAMLSYlLAQPPS----PDDRAHR-LRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 792 FRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYI---SGFGIANGYLGRADLSAARFvanpfEHGqrMYRTG 868
Cdd:cd05934 236 IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-----RNG--WFHTG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELDEktSEQLSQ 948
Cdd:cd05934 309 DLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVP----DEVGEDEVKAVVVLRP--GETLDP 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 490930577 949 QYLSQ-LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:cd05934 383 EELFAfCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
482-986 |
3.51e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 111.98 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 482 QVKKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDY 561
Cdd:PRK03640 11 RAFLTPDRTAIEFEE----KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 562 PIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHldqegvqTQIRKQDASDIPAENrKFDFQDVAYVIFTSGSTGRPKG 641
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDDDFEAKLIPGISVKF-------AELMNGPKEEAEIQE-EFDLDEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 642 VMNT---H-----GSLLNLILSHKPTiyWpvLEAVnerfpdrPLraAHTHSFS--FDSswlqvfwMLWGQELHIFDenmR 711
Cdd:PRK03640 159 VIQTygnHwwsavGSALNLGLTEDDC--W--LAAV-------PI--FHISGLSilMRS-------VIYGMRVVLVE---K 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 712 RDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNglFVENQHHPSL--ILIGGEAAPLALWQQlnAQpalfAHNL-----YGP 784
Cdd:PRK03640 216 FDAEKINKLLQTGGVTIISVVSTMLQRLLER--LGEGTYPSSFrcMLLGGGPAPKPLLEQ--CK----EKGIpvyqsYGM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 785 TEYT--VDTFRAELKQTARPVIGNPIGNTQAYVLDrHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgq 862
Cdd:PRK03640 288 TETAsqIVTLSPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 863 rmyRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEkt 942
Cdd:PRK03640 363 ---KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTE-- 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490930577 943 sEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK03640 438 -EELRH----FCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1546-2032 |
7.17e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 111.63 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTE------ 1619
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDalaaal 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1620 ---RIKFMLQDAKSKLVIGEQKDLAAIVHPSIATfafnelfdetkVDLSSYKTTVITPQHPAYLiyTSGTTGQPKGVMVS 1696
Cdd:PRK13383 129 rahHISTVVADNEFAERIAGADDAVAVIDPATAG-----------AEESGGRPAVAAPGRIVLL--TSGTTGKPKGVPRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1697 HQAIVNRILWMQ--SEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIapiDAHRDPLALLSLIQKYQVTTLHFVP 1774
Cdd:PRK13383 196 PQLRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLT---HRHFDAEAALAQASLHRADAFTAVP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1775 SMLAVFENAATEILSsaqRQSLPICRV-FCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEescv 1853
Cdd:PRK13383 273 VVLARILELPPRVRA---RNPLPQLRVvMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPE---- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYlhrADLTASRFVANpftagqrMYRTGDIARWHADGSIQYI 1933
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDG-------MTSTGDMGYLDNAGRLFIV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1934 GRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHY 2012
Cdd:PRK13383 416 GREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDI 495
|
490 500
....*....|....*....|
gi 490930577 2013 MLVEQFPLSHNGKLDRKALP 2032
Cdd:PRK13383 496 NIVSSIPRNPTGKVLRKELP 515
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
601-986 |
8.99e-25 |
|
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: 109.86 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 601 GVQTQIRKQDASDIPAENRK----FDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiyWPVlEAVNERFPDRP 676
Cdd:cd05919 64 VINPLLHPDDYAYIARDCEArlvvTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADA------MAR-EALGLTPGDRV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 677 LRAAHTHsFSFDSSWLQVFWMLWGQELHIFDEnmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFveNQHHPSLIL 756
Cdd:cd05919 137 FSSAKMF-FGYGLGNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYGVPTFYANLLDSCAG--SPDALRSLR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 757 I---GGEAAPLALWQQLNAQPALFAHNLYGPTEyTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELY 832
Cdd:cd05919 212 LcvsAGEALPRGLGERWMEHFGGPILDGIGATE-VGHIFLSNRPGAWRLgSTGRPVPGYEIRLVDEEGHTIPPGEEGDLL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 833 ISGFGIANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVE 912
Cdd:cd05919 291 VRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVA 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 913 SAVVIAEPinNSHRLL---GYCVVKDiELDekTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05919 364 EAAVVAVP--ESTGLSrltAFVVLKS-PAA--PQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1558-2033 |
1.46e-24 |
|
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: 108.97 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLvigeq 1637
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kdlaaivhPSIATfafnelfdetkvdlssykttvitpqhpayLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD 1717
Cdd:cd05912 77 --------DDIAT-----------------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TILQKTPcTFDVSvwefFWSYLVgaRLVI--APIDAHR--DPLALLSLIQKYQVTTLHFVPSMLavfeNAATEILSSAQR 1793
Cdd:cd05912 120 NWLCALP-LFHIS----GLSILM--RSVIygMTVYLVDkfDAEQVLHLINSGKVTIISVVPTML----QRLLEILGEGYP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSLPiCRVFCSGEALPTALAKsftehfsCELHNL-----YGPTEAAVDVsymdatLGLHPEESCVAI---GYPVWNTQLY 1865
Cdd:cd05912 189 NNLR-CILLGGGPAPKPLLEQ-------CKEKGIpvyqsYGMTETCSQI------VTLSPEDALNKIgsaGKPLFPVELK 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1866 ILDQYLRPvpvGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQ 1945
Cdd:cd05912 255 IEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1946 RIELGEIEQQLRLISGL-DVVVHAISSEqnKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNG 2024
Cdd:cd05912 325 NIYPAEIEEVLLSHPAIkEAGVVGIPDD--KWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASG 402
|
....*....
gi 490930577 2025 KLDRKALPQ 2033
Cdd:cd05912 403 KLLRHELKQ 411
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1101-1380 |
1.48e-24 |
|
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: 109.28 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQS-NYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPV-FIysLHPTQAWP 1178
Cdd:cd19538 2 IPLSFAQRRLWFLHQLEGPSaTYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEE-DGVPYqLI--LEEDEATP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1179 V-QFCSVTPDLLEQTIQEALQQPIHLDQPYGlIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ--TNQQ 1255
Cdd:cd19538 79 KlEIKEVDEEELESEINEAVRYPFDLSEEPP-FRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRArcKGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1256 -----LPVLEHSYETVIKALSGRDHETSKVI------WQRDLA---DLQPLILFNQAQQAVQETSYRLSAELGAKLQHKL 1321
Cdd:cd19538 158 pelapLPVQYADYALWQQELLGDESDPDSLIarqlayWKKQLAglpDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1322 ----RQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSApiNGLEQQIGLFLNTIPVRV 1380
Cdd:cd19538 238 lqlaKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRND--DSLEDLVGFFVNTLVLRT 298
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
465-986 |
1.90e-24 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 110.28 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 465 RVSHPEQYNNVLDIFYEQVKKYPERTAIV----SGERpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDS 540
Cdd:cd05970 9 SINVPENFNFAYDVVDAMAKEYPDKLALVwcddAGEE---RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 541 VVVMLSVLNSGASFLPL-------DLDYPIDRMQM---MCEDANPLFVLTTQALAQ--QLPQNIQQLHLDQEGvQTQIRK 608
Cdd:cd05970 86 WYSLLALHKLGAIAIPAthqltakDIVYRIESADIkmiVAIAEDNIPEEIEKAAPEcpSKPKLVWVGDPVPEG-WIDFRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 609 --QDASDI---PAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKptiYWPvleavNERFPDRPLRAAhth 683
Cdd:cd05970 165 liKNASPDferPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAK---YWQ-----NVREGGLHLTVA--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 684 sfsfDSSWLQVFW-MLWGQEL---HIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIG 758
Cdd:cd05970 234 ----DTGWGKAVWgKIYGQWIagaAVFVYDYDKfDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 759 GEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYIS---- 834
Cdd:cd05970 310 GEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskg 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 835 -GFGIANGYLGRADLSAarfvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-E 912
Cdd:cd05970 390 kPVGLFGGYYKDAEKTA-----EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVlE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 913 SAVV-IAEPINnshrllGYCVVKDIEL--DEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05970 463 CAVTgVPDPIR------GQVVKATIVLakGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1532-2031 |
2.14e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 111.20 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTALS--------DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAYlPID-LQHPtERIKFMLQDAKSKLVI------------------GEQKDLAAIV-------------------- 1644
Cdd:PRK07529 105 AAGIAN-PINpLLEP-EQIAELLRAAGAKVLVtlgpfpgtdiwqkvaevlAALPELRTVVevdlarylpgpkrlavplir 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1645 -HPSIATFAFNELFDETKVDLSSYkTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKT 1723
Cdd:PRK07529 183 rKAHARILDFDAELARQPGDRLFS-GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1724 PcTFDVsvwefFWSYLV-------GARLVIAPIDAHRDPLA---LLSLIQKYQVTTLHFVPSMLAVFenaateilssAQR 1793
Cdd:PRK07529 262 P-LFHV-----NALLVTglaplarGAHVVLATPQGYRGPGVianFWKIVERYRINFLSGVPTVYAAL----------LQV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 -------QSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEA--AVDVSYMDATLGLHpeescvAIGYPVWNTQL 1864
Cdd:PRK07529 326 pvdghdiSSLRY--ALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEAtcVSSVNPPDGERRIG------SVGLRLPYQRV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YIL-----DQYLRPVPVGVDGELYLAGHQLAMGYLhRADLTASRFVanpftaGQRMYRTGDIARWHADGSIQYIGRADDq 1939
Cdd:PRK07529 398 RVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKD- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1940 LKIR-GQRIELGEIEQQLrliSGLDVVVH--AISSEQNKANVQLVAYLQTT--APVDIDQLKKQLAKHLP---AymVPTH 2011
Cdd:PRK07529 470 LIIRgGHNIDPAAIEEAL---LRHPAVALaaAVGRPDAHAGELPVAYVQLKpgASATEAELLAFARDHIAeraA--VPKH 544
|
570 580
....*....|....*....|
gi 490930577 2012 YMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07529 545 VRILDALPKTAVGKIFKPAL 564
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1680-2031 |
3.17e-24 |
|
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: 108.33 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQ---AIVNRilWMQSEYPLSATDTILQKTPCTFDVS---VWEFFWSylVGARLVIAPidaHR 1753
Cdd:cd05958 102 LAFTSGTTGAPKATMHFHRdplASADR--YAVNVLRLREDDRFVGSPPLAFTFGlggVLLFPFG--VGASGVLLE---EA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 DPLALLSLIQKYQVTTLHFVPSMLAvfenAATEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEA 1833
Cdd:cd05958 175 TPDLLLSAIARYKPTVLFTAPTAYR----AMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1834 avdvsymdatlgLH------PEESCV-AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGhqlAMGYLHRADLTASRFVA 1906
Cdd:cd05958 251 ------------FHifisarPGDARPgATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 NPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISSEQNKANVQLV-AYL- 1984
Cdd:cd05958 316 GGWNI------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDV--LLQHPAVAECAVVGHPDESRGVVVkAFVv 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1985 ----QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05958 388 lrpgVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1559-2031 |
5.70e-24 |
|
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: 108.71 E-value: 5.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1559 SFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kDLAAIVH------PSIAT------------FAFNELFDETKVDLSSYKTTvitPQHPAYLIYTSGTTGQPKgvMVSHQ- 1698
Cdd:cd05928 123 -ELAPEVDsvasecPSLKTkllvseksrdgwLNFKELLNEASTEHHCVETG---SQEPMAIYFTSGTTGSPK--MAEHSh 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1699 ------AIVNRILWMQseypLSATDTILqktpCTFDVSVWEFFWSYLVGARLVIAPIDAHR----DPLALLSLIQKYQVT 1768
Cdd:cd05928 197 sslglgLKVNGRYWLD----LTASDIMW----NTSDTGWIKSAWSSLFEPWIQGACVFVHHlprfDPLVILKTLSSYPIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1769 TLHFVPSmlaVFENAATEILSSAQRQSLPICrvFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVdvsyMDATL-GLH 1847
Cdd:cd05928 269 TFCGAPT---VYRMLVQQDLSSYKFPSLQHC--VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGL----ICANFkGMK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1848 PEESCVAIGYPVWNTQlyILDQYLRPVPVGVDGELYL-----AGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIA 1922
Cdd:cd05928 340 IKPGSMGKASPPYDVQ--IIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD-------FYLTGDRG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1923 RWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISS-------EQNKANVQLVAYLQTTAPvdiDQL 1995
Cdd:cd05928 411 IMDEDGYFWFMGRADDVINSSGYRIGPFEVESA--LIEHPAVVESAVVSspdpirgEVVKAFVVLAPQFLSHDP---EQL 485
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 490930577 1996 KKQLAKHLPAYMVPTHY----MLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05928 486 TKELQQHVKSVTAPYKYprkvEFVQELPKTVTGKIQRNEL 525
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1679-2027 |
6.91e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 105.93 E-value: 6.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1679 YLIYTSGTTGQPKGVMVSHQAIVnRILW----MQSEYPLSATDTILQKT-----------PCTFDVSVWEFFWSYLVGAR 1743
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIF-RMLMggadFGTGEFTPSEDAHKAAAaaagtvmfpapPLMHGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1744 LVIapIDAHRDPLALLSLIQKYQVTTLHFVPSMLAvfeNAATEILSSAQRQSLPICRVFCSGEALPTALAKS-FTEHF-S 1821
Cdd:cd05924 86 VVL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMA---RPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQgLLELVpN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 CELHNLYGPTEAAVDVSYMDATLGlHPEESCVAIgypvwNTQLYILDQYLRPVPVGVDGELYLA--GHqLAMGYLHRADL 1899
Cdd:cd05924 161 ITLVDAFGSSETGFTGSGHSAGSG-PETGPFTRA-----NPDTVVLDDDGRVVPPGSGGVGWIArrGH-IPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1900 TASRFvanPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANV 1978
Cdd:cd05924 234 TAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVyDVLVVGRPDERWGQEV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490930577 1979 QLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:cd05924 311 VAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
474-981 |
9.16e-24 |
|
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: 108.82 E-value: 9.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 474 NVLDifyEQVKKYPERTAIV--SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSG 551
Cdd:cd17634 57 NALD---RHLRENGDRTAIIyeGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 552 ASFLPLDLDYPIDRMQMMCEDANPLFVLTT-----------------QALAQQLPQNIQQLHLDQEGV------------ 602
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITAdggvragrsvplkknvdDALNPNVTSVEHVIVLKRTGSdidwqegrdlww 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 603 QTQIRKQDASDIPAenrKFDFQDVAYVIFTSGSTGRPKGVMNTHG--------SLLNLILSHKPTIYWpvleavneRFPD 674
Cdd:cd17634 214 RDLIAKASPEHQPE---AMNAEDPLFILYTSGTTGKPKGVLHTTGgylvyaatTMKYVFDYGPGDIYW--------CTAD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 675 RPLRAAHthsfsfdsSWLQVFWMLWGQELHIFD-ENMRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGL-FVENQHHP 752
Cdd:cd17634 283 VGWVTGH--------SYLLYGPLACGATTLLYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDdAIEGTDRS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 753 SLILIGGEAAPLA------LWQQLNAQ--PALfahNLYGPTEY-----TVDTFRAELKQ--TARPVIGnpignTQAYVLD 817
Cdd:cd17634 355 SLRILGSVGEPINpeayewYWKKIGKEkcPVV---DTWWQTETggfmiTPLPGAIELKAgsATRPVFG-----VQPAVVD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 818 RHLQRCPTGVIGELYISGF--GIANGYLGRADlsaaRFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYR 895
Cdd:cd17634 427 NEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHR 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 896 VEIGEVENALSILTNV-ESAVV-IAEPINNShRLLGYCVVKDIELDektSEQLSQQYLSQLRQNLPEYMVPSALTVMSEF 973
Cdd:cd17634 503 LGTAEIESVLVAHPKVaEAAVVgIPHAIKGQ-APYAYVVLNHGVEP---SPELYAELRNWVRKEIGPLATPDVVHWVDSL 578
|
....*...
gi 490930577 974 PRNVSGKV 981
Cdd:cd17634 579 PKTRSGKI 586
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1676-2028 |
2.08e-23 |
|
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: 103.64 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAivnrilWMQS------EYPLSATDTILQKTPCTFDVSVWEFFWSYLVGaRLVIapI 1749
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERS------WIESfvcnedLFNISGEDAILAPGPLSHSLFLYGAISALYLG-GTFI--G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1750 DAHRDPLALLSLIQKYQVTTLHFVPSMLavfenaatEILSSAQRQSLPICRVFCSGEALPTALAKSFTEHF-SCELHNLY 1828
Cdd:cd17633 72 QRKFNPKSWIRKINQYNATVIYLVPTML--------QALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEAAVdVSYmdatlgLHPEESCVA--IGYPVWNTQLYILDQylrpvPVGVDGELYLAGHQLAMGYLHRADLTASRFva 1906
Cdd:cd17633 144 GTSELSF-ITY------NFNQESRPPnsVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 npftagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD--VVVHAISSEQNKANVQLVAYL 1984
Cdd:cd17633 210 ---------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEeaIVVGIPDARFGEIAVALYSGD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 490930577 1985 QTTAPvdidQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd17633 281 KLTYK----QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1558-2031 |
2.16e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 106.06 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 KDLAaivhpSIATFAFNELFdetkvdlssykttvitpqhpayliyTSGTTGQPKGVMVSHQAIVNRILWMqsEYPLSATD 1717
Cdd:cd05973 81 ANRH-----KLDSDPFVMMF-------------------------TSGTTGLPKGVPVPLRALAAFGAYL--RDAVDLRP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 tilqktpctfDVSVWEFF---WSY-LVGArlVIAPIdAHRDPLALLS----------LIQKYQVTTLHFVPSMLAVFENA 1783
Cdd:cd05973 129 ----------EDSFWNAAdpgWAYgLYYA--ITGPL-ALGHPTILLEggfsvestwrVIERLGVTNLAGSPTAYRLLMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1784 ATEilsSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSymdatlGLHPEESCV---AIGYPVW 1860
Cdd:cd05973 196 GAE---VPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLA------NHHALEHPVhagSAGRAMP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1861 NTQLYILDQYLRPVPVGVDGELYLAGHQLAM----GYLHRADLTASrfvanpftagQRMYRTGDIARWHADGSIQYIGRA 1936
Cdd:cd05973 267 GWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPAID----------GGYYLTGDTVEFDPDGSFSFIGRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1937 DDQLKIRGQRIELGEIEQQlrLISGLDVVVHAI-------SSEQNKANVQLVA-YLQTTAPVDIDQL--KKQLAKHlpAY 2006
Cdd:cd05973 337 DDVITMSGYRIGPFDVESA--LIEHPAVAEAAVigvpdpeRTEVVKAFVVLRGgHEGTPALADELQLhvKKRLSAH--AY 412
|
490 500
....*....|....*....|....*
gi 490930577 2007 MVPTHYmlVEQFPLSHNGKLDRKAL 2031
Cdd:cd05973 413 PRTIHF--VDELPKTPSGKIQRFLL 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1532-2033 |
2.43e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 106.89 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK05852 16 PRIADLVEVAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVI------GEQKDLAAIVHPSIATFAFNELFDETKVDLSSYKTTVITPQHP------ 1677
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLidadgpHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATStpeglr 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 ---AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAP----ID 1750
Cdd:PRK05852 176 pddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPargrFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1751 AHR--DPLALLSLIQKYQVTTLHFVpsmlaVFENAATEiLSSAQRQSLPICRVfCSGeALPTALAKSFTEHFSCELHNLY 1828
Cdd:PRK05852 256 AHTfwDDIKAVGATWYTAVPTIHQI-----LLERAATE-PSGRKPAALRFIRS-CSA-PLTAETAQALQTEFAAPVVCAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEAAVDVSYMDATLGLHPEESCVAIGYPVWNT--QLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTAsrfvA 1906
Cdd:PRK05852 328 GMTEATHQVTTTQIEGIGQTENPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITA----A 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 NpFTAGqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQ 1985
Cdd:PRK05852 404 N-FTDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNvMEAAVFGVPDQLYGEAVAAVIVPR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 490930577 1986 TTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK05852 481 ESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1682-2028 |
2.62e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 103.90 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1682 YTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTP---CtFDVSVweffwSYLV----GARLViaPIDAHRD 1754
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPlfhC-FGSVL-----GVLAclthGATMV--FPSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1755 PLALLSLIQKYQVTTLHFVPSMlavFEnaatEILSSAQRQSLPICRV---FCSGEALPTALAKSFTE--HFScELHNLYG 1829
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTM---FI----AELEHPDFDKFDLSSLrtgIMAGAPCPPELMKRVIEvmNMK-DVTIAYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1830 PTEAAvDVSYMdATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVP-VGVDGELYLAGHQLAMGYLHRADLTASRFvanp 1908
Cdd:cd05917 153 MTETS-PVSTQ-TRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAI---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1909 ftAGQRMYRTGDIARWHADGSIQYIGRADDQLkIRG-QRIELGEIEQQL-RLISGLDVVVHAISSEqnKANVQLVAY--L 1984
Cdd:cd05917 227 --DGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLhTHPKVSDVQVVGVPDE--RYGEEVCAWirL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 490930577 1985 QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd05917 302 KEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1530-2050 |
2.80e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.79 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLReQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PRK07786 16 RQNWVNQLAR-HALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQ--KDLAAIVH---PSIAT------------FAFNELFDETKVDLSSYKttvI 1672
Cdd:PRK07786 95 VPVNFRLTPPEIAFLVSDCGAHVVVTEAalAPVATAVRdivPLLSTvvvaggssddsvLGYEDLLAEAGPAHAPVD---I 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTI-LQKTPCTFDVSVWEFFWSYLVGARLVIAPIDA 1751
Cdd:PRK07786 172 PNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1752 HrDPLALLSLIQKYQVTTLHFVPSMLAVFENAATeilssAQRQSLPIcRVFCSGEA-LPTALAKSFTEHF-SCELHNLYG 1829
Cdd:PRK07786 252 F-DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQ-----ARPRDLAL-RVLSWGAApASDTLLRQMAATFpEAQILAAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1830 PTEAAvDVSYM----DA--TLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASR 1903
Cdd:PRK07786 325 QTEMS-PVTCMllgeDAirKLG--------SVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1904 FVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVV-VHAISSEQNK---ANVQ 1979
Cdd:PRK07786 396 FAGGWF-------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENV--LASHPDIVeVAVIGRADEKwgeVPVA 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1980 LVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSAF 2050
Cdd:PRK07786 467 VAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNVERRSASAGF 537
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
625-986 |
3.27e-23 |
|
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: 103.18 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHgslLNLILShkptiywpvLEAVNERFPDRP-------LRAAHThsfsfdsSWLQVF-- 695
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTA---ANLLAS---------AAGLHSRLGFGGgdswllsLPLYHV-------GGLAILvr 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 696 WMLWGQELHIFDENmrrdaFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLALWQQLnAQPA 775
Cdd:cd17630 62 SLLAGAELVLLERN-----QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERA-ADRG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 776 LFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRhlqrcptgviGELYISGFGIANGYLgradlsAARFVA 855
Cdd:cd17630 136 IPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL------RGQLVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 856 NPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKD 935
Cdd:cd17630 200 EFNEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVP----DEELGQRPVAV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490930577 936 IELDEKTSEQLSQQYLSQLrqnLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17630 274 IVGRGPADPAELRAWLKDK---LARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
503-986 |
3.96e-23 |
|
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: 105.28 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAqqlpqniqqlhldqegvqtqirkqdasdipaenRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILS------- 655
Cdd:cd05969 81 ELY---------------------------------ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTgkyvldl 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 656 HKPTIYWpvleavnerfpdrplraaHTHsfsfDSSWLQ-VFWMLWGQELH----IFDENmRRDAFGLVQEIQQRQIDTLD 730
Cdd:cd05969 128 HPDDIYW------------------CTA----DPGWVTgTVYGIWAPWLNgvtnVVYEG-RFDAESWYGIIERVKVTVWY 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 731 LPPSFCAQMMTNGLFVENQH---HPSLILIGGEAA-PLALWQQLNAQPALFaHNLYGPTEYTVDTFRAELKQTARP-VIG 805
Cdd:cd05969 185 TAPTAIRMLMKEGDELARKYdlsSLRFIHSVGEPLnPEAIRWGMEVFGVPI-HDTWWQTETGSIMIANYPCMPIKPgSMG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 806 NPIGNTQAYVLDRHLQRCPTGVIGELYI-SGF-GIANGYLGradlSAARFvANPFEHGqrMYRTGDLVRWNSAGKLEFMG 883
Cdd:cd05969 264 KPLPGVKAAVVDENGNELPPGTKGILALkPGWpSMFRGIWN----DEERY-KNSFIDG--WYLTGDLAYRDEDGYFWFVG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 884 RCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELDE--KTSEQLSQQYLSQLRQNLPEY 961
Cdd:cd05969 337 RADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP----DPLRGEIIKAFISLKEgfEPSDELKEEIINFVRQKLGAH 412
|
490 500
....*....|....*....|....*
gi 490930577 962 MVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05969 413 VAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
470-986 |
4.07e-23 |
|
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: 105.91 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 470 EQYNNVLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLN 549
Cdd:cd05959 1 EKYNAATLVDLNLNEGRGDKTAFIDDAG----SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 550 SGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQniqQLHLDQEGVQTQIRKQDASDIPAENRKFDF------ 623
Cdd:cd05959 77 AGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAA---ALTKSEHTLVVLIVSGGAGPEAGALLLAELvaaeae 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 624 ---------QDVAYVIFTSGSTGRPKGVMNTHGSllnlilshkptIYW-------PVLeAVNERfpDRPLRAAHT-HSFS 686
Cdd:cd05959 154 qlkpaathaDDPAFWLYSSGSTGRPKGVVHLHAD-----------IYWtaelyarNVL-GIRED--DVCFSAAKLfFAYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 687 FDSSWLqvFWMLWGQELHIFDENMRRDAFglVQEIQQRQIDTLDLPPSFCAQMMTN-GLFVENQHHPSLILIGGEAAPLA 765
Cdd:cd05959 220 LGNSLT--FPLSVGATTVLMPERPTPAAV--FKRIRRYRPTVFFGVPTLYAAMLAApNLPSRDLSSLRLCVSAGEALPAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 766 LWQQLNAqpaLFAHNLY---GPTE----YTVDTFRA-ELKQTARPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGFG 837
Cdd:cd05959 296 VGERWKA---RFGLDILdgiGSTEmlhiFLSNRPGRvRYGTTGKPVPG-----YEVELRDEDGGDVADGEPGELYVRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 838 IANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV 916
Cdd:cd05959 368 SATMYWNNRDKTRDTFQGE-------WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVlEAAVV 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577 917 iaePINNSHRLL---GYCVVKD-IELDEKTSEQLsQQYlsqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05959 441 ---GVEDEDGLTkpkAFVVLRPgYEDSEALEEEL-KEF---VKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1557-1965 |
6.47e-23 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 104.75 E-value: 6.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGE 1636
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 --QKDLAAIvhpsiatfafnelfdetkvdlssykttvitpqhpaylIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLS 1714
Cdd:cd17640 85 ndSDDLATI-------------------------------------IYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1715 ATDTILQKTPctfdvsVWEFF---WSYLVGARLVIapiDAHRDPLALLSLIQKYQVTTLHFVPSML-AVFENAATEIL-S 1789
Cdd:cd17640 128 PGDRFLSILP------IWHSYersAEYFIFACGCS---QAYTSIRTLKDDLKRVKPHYIVSVPRLWeSLYSGIQKQVSkS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1790 SAQRQSLPICRVF--------CSGEALPTALAKsFTEHFSCELHNLYGPTEAAVDVSymdatLGLHPEESCVAIGYPVWN 1861
Cdd:cd17640 199 SPIKQFLFLFFLSggifkfgiSGGGALPPHVDT-FFEAIGIEVLNGYGLTETSPVVS-----ARRLKCNVRGSVGRPLPG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLR-PVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQL 1940
Cdd:cd17640 273 TEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTI 346
|
410 420
....*....|....*....|....*....
gi 490930577 1941 KIR-GQRIELGEIEQQL---RLISGLDVV 1965
Cdd:cd17640 347 VLSnGENVEPQPIEEALmrsPFIEQIMVV 375
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1677-2028 |
7.73e-23 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 102.34 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSE-YPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIApiDAHRDP 1755
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG--GENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LALLSLIQKYQVTTLHFVPSMLAVFENAATEILssaqrQSLPICRVFCSGEALPTALAKSFTEHF-SCELHNLYGPTE-- 1832
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSAN-----ATVPSLRLIGYGGSRAIAADVRFIEATgLTNTAQVYGLSEtg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 AAVDVSYMDATLGLHpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtag 1912
Cdd:cd17635 156 TALCLPTDDDSIEIN------AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1913 qrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLvaYLQTTAPVD 1991
Cdd:cd17635 227 ----NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVqECACYEISDEEFGELVGL--AVVASAELD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490930577 1992 ---IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd17635 301 enaIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1533-2027 |
9.31e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 104.97 E-value: 9.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI 1612
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1613 DLQHPTERIKFMLQDAksklvigeqkDLAAIVHPSiatfAFNELFDETKVDLSSYKTTV--------------------I 1672
Cdd:PRK07798 84 NYRYVEDELRYLLDDS----------DAVALVYER----EFAPRVAEVLPRLPKLRTLVvvedgsgndllpgavdyedaL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPA-----------YLIYTSGTTGQPKGVMVSHQAIV----NRILWMQSEYPLSATDTILQKTPCTFDV-------- 1729
Cdd:PRK07798 150 AAGSPErdfgerspddlYLLYTGGTTGMPKGVMWRQEDIFrvllGGRDFATGEPIEDEEELAKRAAAGPGMRrfpapplm 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1730 ---SVWEFFWSYLVGARLVIAPiDAHRDPLALLSLIQKYQVTTLHFV------PsMLAVFENAATEILSSAQrqslpicr 1800
Cdd:PRK07798 230 hgaGQWAAFAALFSGQTVVLLP-DVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGPYDLSSLF-------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1801 VFCSGEALPTALAKS-FTEHF-SCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAIGYpvwNTQLyiLDQYLRPVPVGV 1878
Cdd:PRK07798 300 AIASGGALFSPSVKEaLLELLpNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP---RTVV--LDEDGNPVEPGS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1879 DGELYLA--GHqLAMGYLHRADLTASRFvanPFTAGQRMYRTGDIARWHADGSIQYIGRadDQLKIR--GQRIELGEIEQ 1954
Cdd:PRK07798 375 GEIGWIArrGH-IPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1955 QLRLISGL-DVVVHAISSEQ-NKANVQLVAyLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK07798 449 ALKAHPDVaDALVVGVPDERwGQEVVAVVQ-LREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1102-1405 |
9.82e-23 |
|
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: 103.94 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKGMLFLSQVE-NQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeEPVFIYSLHPTQAWPVQ 1180
Cdd:cd20484 3 PLSEGQKGLWMLQKMSpEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEE---DGVPFQKIEPSKPLSFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1181 ---FCSVTPDLLEQTIQEALQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQTNQ-- 1254
Cdd:cd20484 80 eedISSLKESEIIAYLREKAKEPFVLENgP--LMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQgk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1255 ---QLPVLEHSYETVI---KALSGRDHETSKVIWQRDLADLQP-LILFNQ-----AQQAVQET-SYRLSAELGAKLQHKL 1321
Cdd:cd20484 158 qptLASSPASYYDFVAweqDMLAGAEGEEHRAYWKQQLSGTLPiLELPADrprssAPSFEGQTyTRRLPSELSNQIKSFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1322 RQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRsaPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQQLHVE 1401
Cdd:cd20484 238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR--PEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLD 315
|
....
gi 490930577 1402 HLEH 1405
Cdd:cd20484 316 GLDH 319
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1558-2028 |
1.20e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 104.06 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLV-IGE 1636
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIfVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 QKDLAAIvhpsiatfafnelfdetkvdlssykttvitpqhpaylIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05914 88 EDDVALI-------------------------------------NYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTP------CTFDvsvweFFWSYLVGARLVIApidaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSS 1790
Cdd:cd05914 131 DKILSILPlhhiypLTFT-----LLLPLLNGAHVVFL----DKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 A------QRQSLPI--------------------CRVFCSGEA-LPTALAKSFTEHFSCELHNlYGPTEAAVDVSYmdat 1843
Cdd:cd05914 202 LtlkkfkFKLAKKInnrkirklafkkvheafggnIKEFVIGGAkINPDVEEFLRTIGFPYTIG-YGMTETAPIISY---- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1844 lglHPEESCV--AIGYPVWNTQLYILDqylrPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDI 1921
Cdd:cd05914 277 ---SPPNRIRlgSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1922 ARWHADGSIQYIGRADDQLKI-RGQRIELGEIEQQlrlISGLDVVVHAISSEQNKaNVQLVAYLQTTA--------PVDI 1992
Cdd:cd05914 344 GKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAK---INNMPFVLESLVVVQEK-KLVALAYIDPDFldvkalkqRNII 419
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 490930577 1993 DQLK----KQLAKHLPAYMVPTHYMLV-EQFPLSHNGKLDR 2028
Cdd:cd05914 420 DAIKwevrDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1570-2049 |
1.36e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 105.88 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG-AAYLPIDLQHPTERiKFMLQDAKSKLVI--GEQKDLAAivhP 1646
Cdd:PRK06060 43 LGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvMAFLANPELHRDDH-ALAARNTEPALVVtsDALRDRFQ---P 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1647 SIATFAFNELFDETKVDLSSYKttVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWM-QSEYPLSATDTILQKTPC 1725
Cdd:PRK06060 119 SRVAEAAELMSEAARVAPGGYE--PMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDTGLCSARM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1726 TFDVSVWEFFWSYL-VGARLVIAPIDAHRDPLALLSliQKYQVTTLHFVPSMLAvfenaatEILSSAQRQSLPICR-VFC 1803
Cdd:PRK06060 197 YFAYGLGNSVWFPLaTGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPNFFA-------RVIDSCSPDSFRSLRcVVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTALAKSFTEHFScELHNLYGPTEAAVDVSYMDATLGlhpEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELY 1883
Cdd:PRK06060 268 AGEALELGLAERLMEFFG-GIPILDGIGSTEVGQTFVSNRVD---EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLW 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1884 LAGHQLAMGYLHRADltasrfvanPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlRLISGLD 1963
Cdd:PRK06060 344 VRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVE---RLIIEDE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1964 VVVHA--ISSEQNKANVQLVAYLQTTAPVDIDQ-----LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL----- 2031
Cdd:PRK06060 412 AVAEAavVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsp 491
|
490
....*....|....*...
gi 490930577 2032 PQPHLTPSNTEKQYATSA 2049
Cdd:PRK06060 492 TKPIWELSLTEPGSGVRA 509
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
503-986 |
3.19e-22 |
|
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: 102.04 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDypidrmqmmcedanplfvLTTQ 582
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR------------------LTPN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQQLpqniqqlhldqegvqtqirkqdasdipaENRKFDFQDVAYVIFTSGSTGRPKGVMNT---H-----GSLLNLIL 654
Cdd:cd05912 64 ELAFQL----------------------------KDSDVKLDDIATIMYTSGTTGKPKGVQQTfgnHwwsaiGSALNLGL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 655 SHKPTiyWpvLEAVnerfpdrPLraahthsfsFDSSWLQVFW--MLWGQELHIFDenmRRDAFGLVQEIQQRQIDTLdlp 732
Cdd:cd05912 116 TEDDN--W--LCAL-------PL---------FHISGLSILMrsVIYGMTVYLVD---KFDAEQVLHLINSGKVTII--- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 733 pSFCAQMMTNGLFVENQHHPS---LILIGGEAAPLALWQQLnAQPALFAHNLYGPTEYT--VDTFRAELKQTARPVIGNP 807
Cdd:cd05912 170 -SVVPTMLQRLLEILGEGYPNnlrCILLGGGPAPKPLLEQC-KEKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 808 IGNTQAYVldRHLQRCPTGViGELYISGFGIANGYLGRADLSAARFVANPFEhgqrmyrTGDLVRWNSAGKLEFMGRCDD 887
Cdd:cd05912 248 LFPVELKI--EDDGQPPYEV-GEILLKGPNVTKGYLNRPDATEESFENGWFK-------TGDIGYLDEEGFLYVLDRRSD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 888 QIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNshrlLGYCVVKDIELDEKTSEQlsqQYLSQLRQNLPEYMVPSAL 967
Cdd:cd05912 318 LIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDK----WGQVPVAFVVSERPISEE---ELIAYCSEKLAKYKVPKKI 390
|
490
....*....|....*....
gi 490930577 968 TVMSEFPRNVSGKVDKKAL 986
Cdd:cd05912 391 YFVDELPRTASGKLLRHEL 409
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
503-986 |
3.94e-22 |
|
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: 101.79 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYW 662
Cdd:cd05935 82 EL---------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQ---SAVW 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 663 PVLEAVNERFPDRPLraahTHSFSFDSSWLQVfwMLWGQE---LHIFDENMRRDAfglvqeiqqrqIDTLDLPPSFCAQM 739
Cdd:cd05935 120 TGLTPSDVILACLPL----FHVTGFVGSLNTA--VYVGGTyvlMARWDRETALEL-----------IEKYKVTFWTNIPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 740 MTNGLF--VENQHH--PSLILIGGEAAPL--ALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQA 813
Cdd:cd05935 183 MLVDLLatPEFKTRdlSSLKVLTGGGAPMppAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 814 YVLD-RHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVanpFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIR 892
Cdd:cd05935 263 RVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 893 GYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQLSQQYlsqLRQNLPEYMVPSALTVMSE 972
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEEDIIEW---AREQMAAYKYPREVEFVDE 416
|
490
....*....|....
gi 490930577 973 FPRNVSGKVDKKAL 986
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1545-2031 |
3.99e-22 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 103.93 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1545 TPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqH-- 1616
Cdd:cd05967 64 RGDQIALiydspvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAI-------Hsv 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 ------PTE---RIkfmlQDAKSKLVIG-----------EQKDL--AAI---VHPSIATFAFNElfDETKVDLSSYKTTV 1671
Cdd:cd05967 137 vfggfaAKElasRI----DDAKPKLIVTascgiepgkvvPYKPLldKALelsGHKPHHVLVLNR--PQVPADLTKPGRDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1672 ----------------ITPQHPAYLIYTSGTTGQPKGVMVS---HQAIVNrilW-MQSEYPLSATDTILqktpCTFDVSv 1731
Cdd:cd05967 211 dwsellakaepvdcvpVAATDPLYILYTSGTTGKPKGVVRDnggHAVALN---WsMRNIYGIKPGDVWW----AASDVG- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1732 WEFFWSYLV------GARLVI---APiDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEIlSSAQRQSLPICRV- 1801
Cdd:cd05967 283 WVVGHSYIVygpllhGATTVLyegKP-VGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDG-KYIKKYDLSSLRTl 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1802 FCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEESCVAiGYPVWNTQLYILDQYLRPVPVGVDGE 1881
Cdd:cd05967 361 FLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSP-GKPVPGYQVQVLDEDGEPVGPNELGN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1882 LYLAGhQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlRLISG 1961
Cdd:cd05967 440 IVIKL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE--SVLSH 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1962 LDVVVHAI--SSEQNKANVQLVAY-LQTTAPVDIDQLKKQLAKH----LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05967 517 PAVAECAVvgVRDELKGQVPLGLVvLKEGVKITAEELEKELVALvreqIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
624-983 |
1.18e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 98.87 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 624 QDVAYVIFTSGSTGRPKGVMNTHGSL---LNLILSHkptiywpVLEAVNERFPDRPLRAAHthsfSFDSSWLQVFwMLWG 700
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFfavPDILQKE-------GLNWVVGDVTYLPLPATH----IGGLWWILTC-LIHG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 701 QELHIFDENMRRDAFglVQEIQQRQIDTLDLPPSFCAQMmTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFA 778
Cdd:cd17635 69 GLCVTGGENTTYKSL--FKILTTNAVTTTCLVPTLLSKL-VSELKSANATVPSLrlIGYGGSRAIAADVRFIEATGLTNT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 779 HNLYGPTEytvdTFRAELKQTARPVI-----GNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:cd17635 146 AQVYGLSE----TGTALCLPTDDDSIeinavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 854 VANPFehgqrmyRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVV 933
Cdd:cd17635 222 IDGWV-------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490930577 934 KDIELDEKTSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17635 295 ASAELDENAIRALKH----TIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1538-2031 |
1.26e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 101.09 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKDLAAI--------VHPSIATFAFNELFDETKVDLSSYkttviTPQHPAYLIYTSGTTG 1688
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEKTFQNMAlsmqkvsyVQRVISITSLKEIEDRKIDNFVEK-----NESASFIICYTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1689 QPKGVMVSHQAI----VNRILWMQseypLSATDTILQKTPCTFDVSVWEF-FWSYLVGARLVIApidAHRDPLALLSLIQ 1763
Cdd:PRK06839 163 KPKGAVLTQENMfwnaLNNTFAID----LTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVP---RKFEPTKALSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQVTTLHFVPSMLAVFENAateilSSAQRQSLPICRVFCSGEA-LPTALAKSFTEHfSCELHNLYGPTEAAVDVsYMDA 1842
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINC-----SKFETTNLQSVRWFYNGGApCPEELMREFIDR-GFLFGQGFGMTETSPTV-FMLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 tlglhpEESCV----AIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASrfvanpfTAGQRMYRT 1918
Cdd:PRK06839 309 ------EEDARrkvgSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE-------TIQDGWLCT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1919 GDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKK 1997
Cdd:PRK06839 376 GDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVyEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIE 455
|
490 500 510
....*....|....*....|....*....|....
gi 490930577 1998 QLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06839 456 HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1556-2031 |
2.40e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 100.83 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG 1635
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQ------KDLAAIVHPSIAT--------FAFNELfdeTKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:PLN02246 129 QScyvdklKGLAEDDGVTVVTiddppegcLHFSEL---TQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1702 NRIL-WMQSEYP---LSATDTILQKTPcTFDV----SVweFFWSYLVGARLVIAPidaHRDPLALLSLIQKYQVTTLHFV 1773
Cdd:PLN02246 206 TSVAqQVDGENPnlyFHSDDVILCVLP-MFHIyslnSV--LLCGLRVGAAILIMP---KFEIGALLELIQRHKVTIAPFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PS-MLAVFENAATEI--LSSAqrqslpicRVFCSGEAlptALAKSFTEHFSCELHNL-----YGPTEAAvDVSYMDATLG 1845
Cdd:PLN02246 280 PPiVLAIAKSPVVEKydLSSI--------RMVLSGAA---PLGKELEDAFRAKLPNAvlgqgYGMTEAG-PVLAMCLAFA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1846 LHPEE----SCvaiGYPVWNTQLYILDqylrP-----VPVGVDGELYLAGHQLAMGYLHRADLTAsrfvanpftagqrmy 1916
Cdd:PLN02246 348 KEPFPvksgSC---GTVVRNAELKIVD----PetgasLPRNQPGEICIRGPQIMKGYLNDPEATA--------------- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRaDDQL----------KIRGQRIELGEIEQQlrLISGLDVVVHAISSEQNKANVQL-VAYLQ 1985
Cdd:PLN02246 406 NTIDKDGWLHTGDIGYIDD-DDELfivdrlkeliKYKGFQVAPAELEAL--LISHPSIADAAVVPMKDEVAGEVpVAFVV 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 490930577 1986 TTAPVDI--DQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN02246 483 RSNGSEIteDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1570-2035 |
3.59e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 99.98 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDlQHPT-ERIKFMLQDAKSKLVIGEQkDLAAIVHPSI 1648
Cdd:PRK08276 24 LAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPIN-WHLTaAEIAYIVDDSGAKVLIVSA-ALADTAAELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1649 ATF----AFNELFDETKVDLSSYKTTVitPQHPAYLI----------YTSGTTGQPKGVMVSHQAIvnrilwmQSEYPLS 1714
Cdd:PRK08276 102 AELpagvPLLLVVAGPVPGFRSYEEAL--AAQPDTPIadetagadmlYSSGTTGRPKGIKRPLPGL-------DPDEAPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1715 ATDTILQKTPCTFDVSVweffwsYLVGARLV-IAP---------------IDAHRDPLALLSLIQKYQVTTLHFVPSM-- 1776
Cdd:PRK08276 173 MMLALLGFGMYGGPDSV------YLSPAPLYhTAPlrfgmsalalggtvvVMEKFDAEEALALIERYRVTHSQLVPTMfv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1777 --LAvfenaateiLSSAQRQSLPIC---RVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAvDVSYMDATLGL-HPEe 1850
Cdd:PRK08276 247 rmLK---------LPEEVRARYDVSslrVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGG-GVTVITSEDWLaHPG- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1851 scvAIGYPvWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVanpftaGQRMYRTGDIARWHADGSI 1930
Cdd:PRK08276 316 ---SVGKA-VLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGWVTVGDVGYLDEDGYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1931 QYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVV----HAISSEQNKANVQLVAylQTTAPVDI-DQLKKQLAKHLP 2004
Cdd:PRK08276 386 YLTDRKSDMIISGGVNIYPQEIENLLVTHPKvADVAVfgvpDEEMGERVKAVVQPAD--GADAGDALaAELIAWLRGRLA 463
|
490 500 510
....*....|....*....|....*....|.
gi 490930577 2005 AYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK08276 464 HYKCPRSIDFEDELPRTPTGKLYKRRLRDRY 494
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1530-2040 |
6.09e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 99.87 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:PLN02860 5 SQAHICQCLTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKF-MLQDAKSKLVIGEQKDLAAIVH-----PSIATFAF-NELFDETKVDLSSYKTT------VITPQH 1676
Cdd:PLN02860 85 APLNYRWSFEEAKSaMLLVRPVMLVTDETCSSWYEELqndrlPSLMWQVFlESPSSSVFIFLNSFLTTemlkqrALGTTE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAY--------LI-YTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIA 1747
Cdd:PLN02860 165 LDYawapddavLIcFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 P-IDAHrdplALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSlpICRVFCSGEALPTALAKSFTEHFSC-ELH 1825
Cdd:PLN02860 245 PkFDAK----AALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPS--VRKILNGGGSLSSRLLPDAKKLFPNaKLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTEAAVDVSYM---DATL-----------------GLHPEESCVaiGYPVWNTQLYI-LDQYLRpvpvgvDGELYL 1884
Cdd:PLN02860 319 SAYGMTEACSSLTFMtlhDPTLespkqtlqtvnqtksssVHQPQGVCV--GKPAPHVELKIgLDESSR------VGRILT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1885 AGHQLAMGYLHRADLTASRFVANPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LD 1963
Cdd:PLN02860 391 RGPHVMLGYWGQNSETASVLSNDGWLD------TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGvAS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1964 VVVHAISSEQNKANVQLVAYLQ---TTAPVDIDQLKKQLA------------KHLPAYMVPTHYML-VEQFPLSHNGK-- 2025
Cdd:PLN02860 465 VVVVGVPDSRLTEMVVACVRLRdgwIWSDNEKENAKKNLTlssetlrhhcreKNLSRFKIPKLFVQwRKPFPLTTTGKir 544
|
570
....*....|....*...
gi 490930577 2026 ---LDRKALPQPHLTPSN 2040
Cdd:PLN02860 545 rdeVRREVLSHLQSLPSN 562
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1547-2034 |
8.18e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 98.52 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1547 EQTALSDENHQLSFSEVRLQVCALAQQLQRAgvqagDIVAV-ALPrSVKLSIAILAVIEAGAAYLPIDLQH-PTERiKFM 1624
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAGAATAVAERVAGA-----RRVAVlATP-TLATVLAVVGALIAGVPVVPVPPDSgVAER-RHI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1625 LQDAKSKLVIGE-QKDLAAIvhPSIatfafnelfdetKVDL---SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:PRK07787 88 LADSGAQAWLGPaPDDPAGL--PHV------------PVRLharSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRILWMQSEYPLSATDTILQKTPcTFDVS--VWEFFWSYLVGARLV----IAPiDAHRDPLALLSliqkyqvtTLHF-V 1773
Cdd:PRK07787 154 AADLDALAEAWQWTADDVLVHGLP-LFHVHglVLGVLGPLRIGNRFVhtgrPTP-EAYAQALSEGG--------TLYFgV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1774 PSM---LAVFENAAtEILSSAqrqslpicRVFCSGEA-LPTALAKSFTEHFSCELHNLYGPTEAAVDVS-YMDAtlglhp 1848
Cdd:PRK07787 224 PTVwsrIAADPEAA-RALRGA--------RLLVSGSAaLPVPVFDRLAALTGHRPVERYGMTETLITLStRADG------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1849 EESCVAIGYPVWNTQLYILDQYLRPVPVGVD--GELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHA 1926
Cdd:PRK07787 289 ERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1927 DGSIQYIGR-ADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISSE------QnkanvQLVAYLQTTAPVDIDQLKKQL 1999
Cdd:PRK07787 363 DGMHRIVGReSTDLIKSGGYRIGAGEIETA--LLGHPGVREAAVVGVpdddlgQ-----RIVAYVVGADDVAADELIDFV 435
|
490 500 510
....*....|....*....|....*....|....*
gi 490930577 2000 AKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQP 2034
Cdd:PRK07787 436 AQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1533-2031 |
9.88e-21 |
|
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: 98.89 E-value: 9.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQAR------ITPEQTALSDENhqLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG 1606
Cdd:cd05906 11 TLLELLLRAAErgptkgITYIDADGSEEF--QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 aaYLPIDL---------QHPTERIKFMLQDAKSKLVIGEQKDLAAI-------VHPSIATFAFNELFDEtkvdLSSYKTT 1670
Cdd:cd05906 89 --FVPAPLtvpptydepNARLRKLRHIWQLLGSPVVLTDAELVAEFagletlsGLPGIRVLSIEELLDT----AADHDLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctFD--VSVWEF--FWSYLvGARLVI 1746
Cdd:cd05906 163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP--LDhvGGLVELhlRAVYL-GCQQVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1747 APIDA-HRDPLALLSLIQKYQVtTLHFVPS-MLAVFENAATEIlsSAQRQSLPICRVFCS-GEALPTALAKSFTEHFscE 1823
Cdd:cd05906 240 VPTEEiLADPLRWLDLIDRYRV-TITWAPNfAFALLNDLLEEI--EDGTWDLSSLRYLVNaGEAVVAKTIRRLLRLL--E 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1824 LHNL--------YGPTE--AAVDVSYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGY 1893
Cdd:cd05906 315 PYGLppdairpaFGMTEtcSGVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1894 LHRADLTASRFVANPFtagqrmYRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGLDVVVH------ 1967
Cdd:cd05906 395 YNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPsftaaf 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1968 AISSEQNKANVQLVAYLQTTAPVD-----IDQLKKQLAKHL---PAYMVPTHYmlvEQFPLSHNGKLDRKAL 2031
Cdd:cd05906 465 AVRDPGAETEELAIFFVPEYDLQDalsetLRAIRSVVSREVgvsPAYLIPLPK---EEIPKTSLGKIQRSKL 533
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
502-893 |
2.34e-20 |
|
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: 97.69 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 502 HLSFAELAVKVNQLTRFLQENGARKQTVIAGAiPRSIDSVVVMLSVLNSGASFLPLDLDYP---IDRMQMMCEDANPLFV 578
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVGKPGDRVLLLA-PPGLDFVAAFLGCLYAGAIAVPLPPPTPgrhAERLAAILADAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 579 LTTQALAQQLPQniqQLHLDQEGVQTQIRKQDASDI----PAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-Nli 653
Cdd:cd05931 103 LTTAAALAAVRA---FAASRPAAGTPRLLVVDLLPDtsaaDWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLaN-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 654 lshkptiywpvLEAVNERFPDRPlraaHTHSFsfdsSWLQVF--------------------WM----------LWGQEL 703
Cdd:cd05931 178 -----------VRQIRRAYGLDP----GDVVV----SWLPLYhdmgligglltplysggpsvLMspaaflrrplRWLRLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 704 ------HIFDENMrrdAFGL-VQEIQQRQIDTLDLppsfcaqmmtnglfvenqHHPSLILIGGE---AAPLALWQQ---- 769
Cdd:cd05931 239 sryratISAAPNF---AYDLcVRRVRDEDLEGLDL------------------SSWRVALNGAEpvrPATLRRFAEafap 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 770 --LNAQpALFAHnlYG-------------PTEYTVDTF-RAELKQTARPVI------------GNPIGNTQAYVLDR-HL 820
Cdd:cd05931 298 fgFRPE-AFRPS--YGlaeatlfvsggppGTGPVVLRVdRDALAGRAVAVAaddpaarelvscGRPLPDQEVRIVDPeTG 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490930577 821 QRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDL-VRWNsaGKLEFMGRCDDQIKIRG 893
Cdd:cd05931 375 RELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLgFLHD--GELYITGRLKDLIIVRG 446
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1529-2028 |
2.66e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 97.54 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1529 VRQSTLQQLLREQARITPEQTALSDENHQLSFSEVRL--QVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG 1606
Cdd:PRK12583 15 LLTQTIGDAFDATVARFPDREALVVRHQALRYTWRQLadAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 AAYLPIDLQHPTERIKFMLQDAKSKLVIG----EQKDLAAIVH---PSIATFAFNELFDE-------------------- 1659
Cdd:PRK12583 95 AILVNINPAYRASELEYALGQSGVRWVICadafKTSDYHAMLQellPGLAEGQPGALACErlpelrgvvslapapppgfl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1660 ------------TKVDLSSyKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIlWMQSEyPLSATDTILQKTPctf 1727
Cdd:PRK12583 175 awhelqargetvSREALAE-RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNG-YFVAE-SLGLTEHDRLCVP--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1728 dVSVWEFFWSYL-------VGARLVIaPIDAHrDPLALLSLIQKYQVTTLHFVPSMLaVFEnaateiLSSAQRQSLPICR 1800
Cdd:PRK12583 249 -VPLYHCFGMVLanlgcmtVGACLVY-PNEAF-DPLATLQAVEEERCTALYGVPTMF-IAE------LDHPQRGNFDLSS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1801 V---FCSGEALPTALAKSFTEHFSC-ELHNLYGPTEAAvDVSYMDATlgLHPEESCVA-IGYPVWNTQLYILDQYLRPVP 1875
Cdd:PRK12583 319 LrtgIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETS-PVSLQTTA--ADDLERRVEtVGRTQPHLEVKVVDPDGATVP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1876 VGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrMYrTGDIARWHADGSIQYIGRADDQLkIR-GQRIELGEIEQ 1954
Cdd:PRK12583 396 RGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMI-IRgGENIYPREIEE 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1955 QLRLISGL-DVVVHAISSEqnKANVQLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:PRK12583 469 FLFTHPAVaDVQVFGVPDE--KYGEEIVAWvrLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
480-920 |
2.74e-20 |
|
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: 97.31 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 480 YEQVKKYPERTAIVSGerPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDL 559
Cdd:cd05904 12 FLFASAHPSRPALIDA--ATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 560 DYPIDRMQMMCEDANPLFVLTTQALAQQLPQN------IQQLHLDQEGVQTQIRKQDASDIPAENRKFDfqDVAYVIFTS 633
Cdd:cd05904 90 LSTPAEIAKQVKDSGAKLAFTTAELAEKLASLalpvvlLDSAEFDSLSFSDLLFEADEAEPPVVVIKQD--DVAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 634 GSTGRPKGVMNTHGSLLNLILSHKPtiywpvLEAVNERFPDR-----PLraahTHSFSFdsSWLQVFWMLWGQELHIfde 708
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIAMVAQFVA------GEGSNSDSEDVflcvlPM----FHIYGL--SSFALGLLRLGATVVV--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 709 nMRR-DAFGLVQEIQQRQIDTLDL-PPSFCAqmMTNGLFVENQHHPSLILIGGEAAPLalwqqlnaQPAL---FAHNL-- 781
Cdd:cd05904 233 -MPRfDLEELLAAIERYKVTHLPVvPPIVLA--LVKSPIVDKYDLSSLRQIMSGAAPL--------GKELieaFRAKFpn 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 782 ------YGPTEYT--VDTFRAELKQTARPV-IGNPIGNTQAYVLD----RHLqrcPTGVIGELYISGFGIANGYLGRADL 848
Cdd:cd05904 302 vdlgqgYGMTESTgvVAMCFAPEKDRAKYGsVGRLVPNVEAKIVDpetgESL---PPNQTGELWIRGPSIMKGYLNNPEA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 849 SAARFVanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd05904 379 TAATID------KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYP 444
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1533-2031 |
3.58e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 97.06 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDENHQLSFSEVRLQvcALAQQLQRA-------GVQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIFESSGGVVRRYSYL--ELNEEINRTanlfyslGIRKGDKVALHLDNCPEFIFCWFGLAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GAAYLPIDLQHPTERIKFMLQDAKSKLVIGE-----------QKDLAAIVHPSIA---------TFAFNELFDETKVDLS 1665
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLVTSaqfypmyrqiqQEDATPLRHICLTrvalpaddgVSSFTQLKAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 syKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTP-------CTFDVSVweffwsY 1738
Cdd:PRK08008 166 --YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPafhidcqCTAAMAA------F 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 LVGARLVIAPIDAHRdplALLSLIQKYQVTTLHFVPSMLavfenaATEILSSAQrqslPICRVFCSGE-----ALPTALA 1813
Cdd:PRK08008 238 SAGATFVLLEKYSAR---AFWGQVCKYRATITECIPMMI------RTLMVQPPS----ANDRQHCLREvmfylNLSDQEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1814 KSFTEHFSCELHNLYGPTEAAVDVsymdatLGLHP--EESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYL---AGHQ 1888
Cdd:PRK08008 305 DAFEERFGVRLLTSYGMTETIVGI------IGDRPgdKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1889 LAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISG----LDV 1964
Cdd:PRK08008 379 IFKEYYLDPKATAKVLEADGW------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELEN---IIAThpkiQDI 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1965 VV----HAISSEQNKANVQLVAylqtTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK08008 450 VVvgikDSIRDEAIKAFVVLNE----GETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1541-2031 |
7.94e-20 |
|
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: 96.55 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1541 QARITPEQTAL---SDENHQ---LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAA------ 1608
Cdd:TIGR02188 66 HLEARPDKVAIiweGDEPGEvrkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIhsvvfg 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 -YLPIDLQhptERIkfmlQDAKSKLVI--------GEQKDLAAIVHPSIA------------------TFAFNE----LF 1657
Cdd:TIGR02188 146 gFSAEALA---DRI----NDAGAKLVItadeglrgGKVIPLKAIVDEALEkcpvsvehvlvvrrtgnpVVPWVEgrdvWW 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1658 DETKVDLSSY-KTTVITPQHPAYLIYTSGTTGQPKGVMVShqaivnrilwmQSEYPLSATDTilQKTpcTFDVSVWEFFW 1736
Cdd:TIGR02188 219 HDLMAKASAYcEPEPMDSEDPLFILYTSGSTGKPKGVLHT-----------TGGYLLYAAMT--MKY--VFDIKDGDIFW 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1737 -----------SYLV------GARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSL 1796
Cdd:TIGR02188 284 ctadvgwitghSYIVygplanGATTVMfegVP--TYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1797 picRVFCS-GEALptalaksftehfSCE----LHNLYGPTEAA-VDVSYMDATLG--LHPEESCVAI-----GYPVWNTQ 1863
Cdd:TIGR02188 362 ---RLLGSvGEPI------------NPEawmwYYKVVGKERCPiVDTWWQTETGGimITPLPGATPTkpgsaTLPFFGIE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPvGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:TIGR02188 427 PAVVDEEGNPVE-GPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVS 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1944 GQRIELGEIEQQlrLISGLDV----VV---HAISSEqnkANVQLVAYLQTTAPVD--IDQLKKQLAKHLPAYMVPTHYML 2014
Cdd:TIGR02188 506 GHRLGTAEIESA--LVSHPAVaeaaVVgipDDIKGQ---AIYAFVTLKDGYEPDDelRKELRKHVRKEIGPIAKPDKIRF 580
|
570
....*....|....*..
gi 490930577 2015 VEQFPLSHNGKLDRKAL 2031
Cdd:TIGR02188 581 VPGLPKTRSGKIMRRLL 597
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1101-1501 |
1.19e-19 |
|
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: 94.36 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQ-SNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHFDSElAEEPVFIYSlhPTQAWPV 1179
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEgSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWID--PYTPVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPD-----LLEQTIQEALQQPIHLDQPyGLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ--T 1252
Cdd:cd19533 79 RHIDLSGDpdpegAAQQWMQEDLRKPLPLDND-PLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTAllK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1253 NQQLPV-LEHSYETVI---KALSGRDH-ETSKVIWQRDLADLQPLILFNQAQQAVQETSYRLSAELGAKLQHKLRQQ--- 1324
Cdd:cd19533 158 GRPAPPaPFGSFLDLVeeeQAYRQSERfERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAaea 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1325 -GITLNVFMQMIWAmtlnIYAHR----EDIVFGTPVSGRsapINGLEQQI-GLFLNTIPVRVKLNMQQTLWEQLPQL--- 1395
Cdd:cd19533 238 hGASWPSFFIALVA----AYLHRltgaNDVVLGVPVMGR---LGAAARQTpGMVANTLPLRLTVDPQQTFAELVAQVsre 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1396 -------QQLHVEHLEHDgLGLSAIQQliaqgNLFDSLLVVENYpdnQYlQQKLGDAAiskLTNRGYSHYP---LALLVI 1465
Cdd:cd19533 311 lrsllrhQRYRYEDLRRD-LGLTGELH-----PLFGPTVNYMPF---DY-GLDFGGVV---GLTHNLSSGPtndLSIFVY 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 490930577 1466 P--DH---QIElLLEQRGVIDQPE---HfLERMIQLIEIALNEP 1501
Cdd:cd19533 378 DrdDEsglRID-FDANPALYSGEDlarH-QERLLRLLEEAAADP 419
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1100-1464 |
1.33e-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: 94.04 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1100 ILPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNgdiDPVRLQ---QALITVLKRHpqlgghfD-------SELAEEPVfi 1168
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDpYLLRSLLAFD---SRARLDaflAALQQVIDRH-------DilrtailWEGLSEPV-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1169 yslhptQA-W-----PVQFCSVTP--DLLEQTIQ--EALQQPIHLDQ-PygLIRATLIQHAPEQS-ELLIMVHHLLTDgw 1236
Cdd:cd19544 69 ------QVvWrqaelPVEELTLDPgdDALAQLRArfDPRRYRLDLRQaP--LLRAHVAEDPANGRwLLLLLFHHLISD-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1237 STPL-FLQDFIKAYQQTN-QQLPVLEhSYETVI-KALSGRDHETSKVIWQRDLADL-QPLILFNQAQ-----QAVQETSY 1307
Cdd:cd19544 139 HTSLeLLLEEIQAILAGRaAALPPPV-PYRNFVaQARLGASQAEHEAFFREMLGDVdEPTAPFGLLDvqgdgSDITEARL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1308 RLSAELGAKLQHKLRQQGITLNVFMQMIWAMTLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNmQQT 1387
Cdd:cd19544 218 ALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1388 LWEQLPQLQQLHVEHLEHDGLGLSAIQQ---LIAQGNLFDSLLvveNY---PDNQYLQQKLGDAAISKLTNRGYSHYPLA 1461
Cdd:cd19544 297 VREAVRQTHARLAELLRHEHASLALAQRcsgVPAPTPLFSALL---NYrhsAAAAAAAALAAWEGIELLGGEERTNYPLT 373
|
...
gi 490930577 1462 LLV 1464
Cdd:cd19544 374 LSV 376
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1525-2031 |
1.36e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 95.47 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1525 TQYyvrqSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIE 1604
Cdd:PRK07059 20 SQY----PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1605 AGAA-------YLPIDLQHP-----TERIkFMLQDAKSKL------------VIGEQKDL----AAIVH----------P 1646
Cdd:PRK07059 96 AGYVvvnvnplYTPRELEHQlkdsgAEAI-VVLENFATTVqqvlaktavkhvVVASMGDLlgfkGHIVNfvvrrvkkmvP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1647 --SIATF-AFNELFDETKVdlSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIL----WMQSEYPLSATDTI 1719
Cdd:PRK07059 175 awSLPGHvRFNDALAEGAR--QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLqmeaWLQPAFEKKPRPDQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1720 LQkTPCT------FDVSVwEFFWSYLVGARLVIAPidAHRDPLALLSLIQKYQVttlHFVPSMLAVFeNAateILSSAQR 1793
Cdd:PRK07059 253 LN-FVCAlplyhiFALTV-CGLLGMRTGGRNILIP--NPRDIPGFIKELKKYQV---HIFPAVNTLY-NA---LLNNPDF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1794 QSL---PICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAA--VDVSYMDATlglhpeESCVAIGYPVWNTQLYILD 1868
Cdd:PRK07059 322 DKLdfsKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpvATCNPVDAT------EFSGTIGLPLPSTEVSIRD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1869 QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIE 1948
Cdd:PRK07059 396 DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVY 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1949 LGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDiDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK07059 470 PNEIEEVVASHPGvLEVAAVGVPDEHSGEAVKLFVVKKDPALTE-EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKIL 548
|
....
gi 490930577 2028 RKAL 2031
Cdd:PRK07059 549 RREL 552
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1542-2033 |
1.39e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 94.55 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERI 1621
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQ--DAKSKLVIGEQKDLAAIVHPSIATFAfnelfDETKVDLSsykttvitPQHPAYLIYTSGTTGQPKGVMVSHQA 1699
Cdd:PRK09029 93 EELLPslTLDFALVLEGENTFSALTSLHLQLVE-----GAHAVAWQ--------PQRLATMTLTSGSTGLPKAAVHTAQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1700 IVNRILWMQSEYPLSATDTILQKTPcTFDVS----VWEffWsYLVGARLVIapidahRDPLALLSLIQkyQVTTLHFVPS 1775
Cdd:PRK09029 160 HLASAEGVLSLMPFTAQDSWLLSLP-LFHVSgqgiVWR--W-LYAGATLVV------RDKQPLEQALA--GCTHASLVPT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 MLavfenaaTEILSSAQrQSLPICRVFCSGEALPTALAKSFTEH-FSCELHnlYGPTEAA--VDVSYMDATLGlhpeesc 1852
Cdd:PRK09029 228 QL-------WRLLDNRS-EPLSLKAVLLGGAAIPVELTEQAEQQgIRCWCG--YGLTEMAstVCAKRADGLAG------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1853 vaIGYPVWNTQLYIldqylrpvpvgVDGELYLAGHQLAMGYLHRADLTasrfvanPFTAGQRMYRTGDIARWHaDGSIQY 1932
Cdd:PRK09029 291 --VGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1933 IGRADDQLKIRGQRIELGEIEqqlRLISGLDVVVHAISSEQnkANVQL----VAYLQTTAPVDIDQLKKQLAKHLPAYMV 2008
Cdd:PRK09029 350 LGRLDNLFFSGGEGIQPEEIE---RVINQHPLVQQVFVVPV--ADAEFgqrpVAVVESDSEAAVVNLAEWLQDKLARFQQ 424
|
490 500
....*....|....*....|....*
gi 490930577 2009 PTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK09029 425 PVAYYLLPPELKNGGIKISRQALKE 449
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1546-2031 |
2.31e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.52 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTALSD--ENHQLSFSEVRLQVCALAQQL-QRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID-LQHPTErI 1621
Cdd:PLN02574 53 NGDTALIDssTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNpSSSLGE-I 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1622 KFMLQDAKSKLVIGEQKD---LAAIVHPSIATfAFNELFDETKVDLSSYKTT-----------VITPQHPAYLIYTSGTT 1687
Cdd:PLN02574 132 KKRVVDCSVGLAFTSPENvekLSPLGVPVIGV-PENYDFDSKRIEFPKFYELikedfdfvpkpVIKQDDVAAIMYSSGTT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1688 GQPKGVMVSHQAIVNRI-LWMQ---SEYPLSATDTILQKTPCTFDVSVWEFFWSYLV---GARLVIAPIDAHRdplaLLS 1760
Cdd:PLN02574 211 GASKGVVLTHRNLIAMVeLFVRfeaSQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLslgSTIVVMRRFDASD----MVK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1761 LIQKYQVTTLHFVPSMLAVFENAAteilSSAQRQSLPICRVFCSGEA-LPTALAKSFTEHFS-CELHNLYGPTE-AAVdv 1837
Cdd:PLN02574 287 VIDRFKVTHFPVVPPILMALTKKA----KGVCGEVLKSLKQVSCGAApLSGKFIQDFVQTLPhVDFIQGYGMTEsTAV-- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1838 symdATLGLHPEE--SCVAIGYPVWNTQLYILDQYLRP-VPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqr 1914
Cdd:PLN02574 361 ----GTRGFNTEKlsKYSSVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW----- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1915 mYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQlrLISGLDVVVHAISSEQNKA----NVQLVAYLQTTApV 1990
Cdd:PLN02574 432 -LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAV--LISHPEIIDAAVTAVPDKEcgeiPVAFVVRRQGST-L 507
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 490930577 1991 DIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN02574 508 SQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1532-2031 |
2.88e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 94.44 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQR-AGVQAGDIVAVALPRSVKLSIAILAVIEAG---- 1606
Cdd:PRK05677 24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGlivv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 ---AAYLPIDLQHpteriKFMLQDAKSKLVIGEQKDLAAIV-----------------HPSIATFAFNELFDETKVDLSS 1666
Cdd:PRK05677 104 ntnPLYTAREMEH-----QFNDSGAKALVCLANMAHLAEKVlpktgvkhvivtevadmLPPLKRLLINAVVKHVKKMVPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YK-------TTVI--------TPQHP-----AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQseyPLSAT------DTIL 1720
Cdd:PRK05677 179 YHlpqavkfNDALakgagqpvTEANPqaddvAVLQYTGGTTGVAKGAMLTHRNLVANMLQCR---ALMGSnlnegcEILI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1721 QKTPC------TFDVSVweffwSYLVGARLVIapIDAHRDPLALLSLIQKYQVT------TLhFVpsmlAVFENAATEIL 1788
Cdd:PRK05677 256 APLPLyhiyafTFHCMA-----MMLIGNHNIL--ISNPRDLPAMVKELGKWKFSgfvglnTL-FV----ALCNNEAFRKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1789 S-SAQRQSLPicrvfcSGEALPTALAKSFTEHFSCELHNLYGPTEAA--VDVSYMDAT-LGlhpeescvAIGYPVWNTQL 1864
Cdd:PRK05677 324 DfSALKLTLS------GGMALQLATAERWKEVTGCAICEGYGMTETSpvVSVNPSQAIqVG--------TIGIPVPSTLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:PRK05677 390 KVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHN 2023
Cdd:PRK05677 464 FNVYPNELEDVLAALPGvLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNV 543
|
....*...
gi 490930577 2024 GKLDRKAL 2031
Cdd:PRK05677 544 GKILRREL 551
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
484-986 |
3.92e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 93.41 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 484 KKYPERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:PRK06145 13 RRTPDRAALVYRD----QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 564 DRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDqEGVQTQIRKQDASDIP-AENRKFDFQDVAYVIFTSGSTGRPKGV 642
Cdd:PRK06145 89 DEVAYILGDAGAKLLLVDEEFDAIVALETPKIVID-AAAQADSRRLAQGGLEiPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 643 MNTHGSLlnlilshkptiYWPVLE---AVNERFPDRPLRAAHT-HSFSFDSSWLQVFWMlwGQELHIfdenMRR-DAFGL 717
Cdd:PRK06145 168 MHSYGNL-----------HWKSIDhviALGLTASERLLVVGPLyHVGAFDLPGIAVLWV--GGTLRI----HREfDPEAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 718 VQEIQQRQIDTLDLPPSFCAQMMTnglfVENQHHPSL-----ILIGGEAAPlalWQQLNAQPALFAH----NLYGPTEyT 788
Cdd:PRK06145 231 LAAIERHRLTCAWMAPVMLSRVLT----VPDRDRFDLdslawCIGGGEKTP---ESRIRDFTRVFTRaryiDAYGLTE-T 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 789 V--DTFRAELKQTAR-PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmy 865
Cdd:PRK06145 303 CsgDTLMEAGREIEKiGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 866 RTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVKD---IELDEK 941
Cdd:PRK06145 376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPgatLTLEAL 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 490930577 942 TseqlsqqylSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06145 456 D---------RHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1107-1387 |
5.07e-19 |
|
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: 92.13 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1107 QKGMLFLSQ-VENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHF--DSELAEepvfiyslhPTQA----WPV 1179
Cdd:cd19532 8 QSRFWFLQQyLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGE---------PMQGvlasSPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1180 QFCSVTPDLlEQTIQEALQQpIHlDQPYGL-----IRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQqtNQ 1254
Cdd:cd19532 79 RLEHVQISD-EAEVEEEFER-LK-NHVYDLesgetMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--GQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1255 QLPVLEHSY----ETVIKALSGRDHETSKVIWQRDLADL-QPLILFNQAQQAV---------QETSYRLSAELGAKLQHK 1320
Cdd:cd19532 154 PLLPPPLQYldfaARQRQDYESGALDEDLAYWKSEFSTLpEPLPLLPFAKVKSrppltrydtHTAERRLDAALAARIKEA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1321 LRQQGIT-LNVFMQMIWAMtLNIYAHREDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQT 1387
Cdd:cd19532 234 SRKLRVTpFHFYLAALQVL-LARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQT 298
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1554-2038 |
8.37e-19 |
|
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: 92.11 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1554 ENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqhpTERIKFMLQDAkskl 1632
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------PAFINYNLSGD---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 vigeqkdlaAIVHpsiatfafnelfdetKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVShqaivNRILWMQSEyp 1712
Cdd:cd05937 69 ---------PLIH---------------CLKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAIS-----WRRTLVTSN-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1713 LSATDTILQKTPCTFD--------VSVWEFFWSYLVGARLVIAPIDAHRDplaLLSLIQKYQVTTLHFVPSMLAVFENAA 1784
Cdd:cd05937 118 LLSHDLNLKNGDRTYTcmplyhgtAAFLGACNCLMSGGTLALSRKFSASQ---FWKDVRDSGATIIQYVGELCRYLLSTP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1785 TEILSSAQRqslpiCRVfCSGEALPTALAKSFTEHFSC-ELHNLYGPTE---AAVDVSYMDATLGlhpeescvAIGYPVW 1860
Cdd:cd05937 195 PSPYDRDHK-----VRV-AWGNGLRPDIWERFRERFNVpEIGEFYAATEgvfALTNHNVGDFGAG--------AIGHHGL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1861 NTQLYILDQYL-------------RP-------VPVGVDGE----LYLAGHQLAMGYLHRADLTASRFVANPFTAGQRMY 1916
Cdd:cd05937 261 IRRWKFENQVVlvkmdpetddpirDPktgfcvrAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNK-----ANVQLVAYLQTTAPV 1990
Cdd:cd05937 341 RTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDiAEANVYGVKVPGHDgragcAAITLEESSAVPTEF 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 490930577 1991 DIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTP 2038
Cdd:cd05937 421 TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1557-2009 |
8.53e-19 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 92.03 E-value: 8.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAaylpidlqhPTERIKFMLQdaksklvige 1636
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAALINYNLR---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 qkdLAAIVHpsiatfafnelfdetKVDLSSYKTTVITPqhpAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05940 64 ---GESLAH---------------CLNVSSAKHLVVDA---ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTPCTFDVSVWEFFWSYLV-GARLVIAPIDAHRDplaLLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRqs 1795
Cdd:cd05940 123 DVLYTCLPLYHSTALIVGWSACLAsGATLVIRKKFSASN---FWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHK-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 lpiCRVFCsGEALPTALAKSFTEHFSC-ELHNLYGPTE---AAVDVSYMDATLGLHPEESCVAIGYPV----WNTQLYIL 1867
Cdd:cd05940 198 ---VRMIF-GNGLRPDIWEEFKERFGVpRIAEFYAATEgnsGFINFFGKPGAIGRNPSLLRKVAPLALvkydLESGEPIR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1868 DQ--YLRPVPVGVDGELYLAGHQLA--MGYLHRADLTASRfVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR 1943
Cdd:cd05940 274 DAegRCIKVPRGEPGLLISRINPLEpfDGYTDPAATEKKI-LRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1944 GQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAY-LQTTAPVDIDQLKKQLAKHLPAYMVP 2009
Cdd:cd05940 353 GENVSTTEVAAVLGAFPGvEEANVYGVQVPGTDGRAGMAAIvLQPNEEFDLSALAAHLEKNLPGYARP 420
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1534-2031 |
8.56e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 92.80 E-value: 8.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLVIGEQ--KDLAAIVHPSIATFAFNELFDETKVDLS-----------SYKTTVITPQHPAYL 1680
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHAdfPEHAAAVRAASPDLTHVVAIGGARAGLDyealvarhlgaRVANAAVDHDDPCWF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1681 IYTSGTTGQPKGVMVSHQ----AIVNRILWMqseYP-LSATDTILQKTPCTFDVSVweffwSYLV----GARLVIAPIDA 1751
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHGqmafVITNHLADL---MPgTTEQDASLVVAPLSHGAGI-----HQLCqvarGAATVLLPSER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1752 HrDPLALLSLIQKYQVTTLHFVPSMLAVFenaaTEILSSAQRQ--SL--------PICRvfcsgEALPTALAKsftehFS 1821
Cdd:PRK07470 241 F-DPAEVWALVERHRVTNLFTVPTILKML----VEHPAVDRYDhsSLryviyagaPMYR-----ADQKRALAK-----LG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 CELHNLYGPTEAAVDVSYMDATlgLHPEE--------SCvaiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGY 1893
Cdd:PRK07470 306 KVLVQYFGLGEVTGNITVLPPA--LHDAEdgpdarigTC---GFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1894 LHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLrlisgldvVVHAISSEQ 1973
Cdd:PRK07470 381 YNNPEANAKAFRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKL--------LTHPAVSEV 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1974 NKANVQ---------LVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07470 446 AVLGVPdpvwgevgvAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
477-986 |
1.01e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 92.30 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:PRK08316 15 DILRRSARRYPDKTALVFGDR----SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 557 L-------DLDYPIDrmqmmceDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDAS-------------DIPA 616
Cdd:PRK08316 91 VnfmltgeELAYILD-------HSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPggwldfadwaeagSVAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 617 ENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYWPVLEAvnerfPDRPLraahtHSFS-FDSSWLQVF 695
Cdd:PRK08316 164 PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVS---CIVAGDMSA-----DDIPL-----HALPlYHCAQLDVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 696 WM--LW-GQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMtnglfvenqHHP--------SL--ILIGGEAA 762
Cdd:PRK08316 231 LGpyLYvGATNVILD---APDPELILRTIEAERITSFFAPPTVWISLL---------RHPdfdtrdlsSLrkGYYGASIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 763 PLALWQQLNAQ-PALFAHNLYGPTE----YTVdtFRAElKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF 836
Cdd:PRK08316 299 PVEVLKELRERlPGLRFYNCYGQTEiaplATV--LGPE-EHLRRPgSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 837 GIANGYLGRADLSAArfvanPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVV 916
Cdd:PRK08316 376 QLMLGYWDDPEKTAE-----AFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 917 IAEPinnsHRLLGYCVVKDIELdeKTSEQLS-QQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08316 449 IGLP----DPKWIEAVTAVVVP--KAGATVTeDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
485-988 |
1.01e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 92.68 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 485 KYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIaGAIPR-SIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:PRK07788 61 RAPDRAALIDERGT----LTYAELDEQSNALARGLLALGVRAGDGV-AVLARnHRGFVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 564 DRMQMMC--EDANPLFV---LTtqALAQQLPQNIQQLH---LDQEGVQTQ----------IRKQDASDIPAEnRKFDFQd 625
Cdd:PRK07788 136 PQLAEVAarEGVKALVYddeFT--DLLSALPPDLGRLRawgGNPDDDEPSgstdetlddlIAGSSTAPLPKP-PKPGGI- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 626 vayVIFTSGSTGRPKGVMNTHGSLLN---LILSHKPtiyWPVLEAVNerfpdrpLRAAHTHSFSFdsSWLQVFWMLwGQE 702
Cdd:PRK07788 212 ---VILTSGTTGTPKGAPRPEPSPLAplaGLLSRVP---FRAGETTL-------LPAPMFHATGW--AHLTLAMAL-GST 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 703 LhifdeNMRR--DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPS---LILIGGEAAPLALWQQLNAQ--PA 775
Cdd:PRK07788 276 V-----VLRRrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSslkIIFVSGSALSPELATRALEAfgPV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 776 LfaHNLYGPTEYTVDTF--RAELKQ---TA-RPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADls 849
Cdd:PRK07788 351 L--YNLYGSTEVAFATIatPEDLAEapgTVgRPPKG-----VTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD-- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 850 aarfvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLL 928
Cdd:PRK07788 422 ------KQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVvEAAVIGVDDEEFGQRLR 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 929 GYCVVKDIEldEKTSEQLsQQYLsqlRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:PRK07788 494 AFVVKAPGA--ALDEDAI-KDYV---RDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1528-1956 |
1.35e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 92.32 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1528 YVRQSTLQQLLReQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:PRK08162 15 YVPLTPLSFLER-AAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 AYLPIDLQHPTERIKFMLQDAKSKLVIGEQkDLAAIVHPSIAtfafneLFDETK-----VDLSSYKTT----------VI 1672
Cdd:PRK08162 94 VLNTLNTRLDAASIAFMLRHGEAKVLIVDT-EFAEVAREALA------LLPGPKplvidVDDPEYPGGrfigaldyeaFL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1673 TPQHPAY-------------LIYTSGTTGQPKGVMVSHQ-----AIVNRILWMQSEYPlsatdTILQKTPcTFDVSVWEF 1734
Cdd:PRK08162 167 ASGDPDFawtlpadewdaiaLNYTSGTTGNPKGVVYHHRgaylnALSNILAWGMPKHP-----VYLWTLP-MFHCNGWCF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1735 FWSYLVGA------RLViapidahrDPLALLSLIQKYQVTtlHF-----VPSMLAvfeNAATEILSSAQRQslpiCRVFC 1803
Cdd:PRK08162 241 PWTVAARAgtnvclRKV--------DPKLIFDLIREHGVT--HYcgapiVLSALI---NAPAEWRAGIDHP----VHAMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTA-LAKsfTEHFSCELHNLYGPTEaavdvSYMDATLGL-HPEESCVAIG------------YPVwNTQLYILD- 1868
Cdd:PRK08162 304 AGAAPPAAvIAK--MEEIGFDLTHVYGLTE-----TYGPATVCAwQPEWDALPLDeraqlkarqgvrYPL-QEGVTVLDp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1869 QYLRPVPvgVD----GELYLAGHQLAMGYLHRADLTASRFvanpftAGQrMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:PRK08162 376 DTMQPVP--ADgetiGEIMFRGNIVMKGYLKNPKATEEAF------AGG-WFHTGDLAVLHPDGYIKIKDRSKDIIISGG 446
|
490
....*....|..
gi 490930577 1945 QRIELGEIEQQL 1956
Cdd:PRK08162 447 ENISSIEVEDVL 458
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1538-1935 |
1.48e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 91.88 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1538 LREQARITPEQTALSDENH----------QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 AYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAA----------IVH------------PSIATFafnelfdETKVDLS 1665
Cdd:PRK09274 92 VPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKAHLArrlfgwgkpsVRRlvtvggrllwggTTLATL-------LRDGAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 SYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILqktpCTFDVSVwefFWSYLVGARLV 1745
Cdd:PRK09274 165 PFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDL----PTFPLFA---LFGPALGMTSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1746 IAPIDAHR----DPLALLSLIQKYQVTTLhFV-PSMLAVFENAATeilssAQRQSLP-ICRVFCSGEALPTALAKSFTEH 1819
Cdd:PRK09274 238 IPDMDPTRpatvDPAKLFAAIERYGVTNL-FGsPALLERLGRYGE-----ANGIKLPsLRRVISAGAPVPIAVIERFRAM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1820 FS--CELHNLYGPTEaAVDVSY--MDATLGLHPEES------CVaiGYPVWNTQLYILD---------QYLRPVPVGVDG 1880
Cdd:PRK09274 312 LPpdAEILTPYGATE-ALPISSieSREILFATRAATdngagiCV--GRPVDGVEVRIIAisdapipewDDALRLATGEIG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1881 ELYLAGHQLAMGYLHRADLTASRFVANPftAGQRMYRTGDIARWHADGSIQYIGR 1935
Cdd:PRK09274 389 EIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGR 441
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1541-2031 |
1.82e-18 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 92.24 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1541 QARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILA---------VIEA 1605
Cdd:cd05966 62 HLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 G--AAYLpidlqhpTERIkfmlQDAKSKLVI--------GEQKDLAAIVH------PSI----------ATFAFNE---- 1655
Cdd:cd05966 142 GfsAESL-------ADRI----NDAQCKLVItadggyrgGKVIPLKEIVDealekcPSVekvlvvkrtgGEVPMTEgrdl 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 LFDETKVDLSSY-KTTVITPQHPAYLIYTSGTTGQPKGVMVSHqaivnrilwmqSEYPLSATDTilQKTpcTFDVSVWEF 1734
Cdd:cd05966 211 WWHDLMAKQSPEcEPEWMDSEDPLFILYTSGSTGKPKGVVHTT-----------GGYLLYAATT--FKY--VFDYHPDDI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1735 FW-----------SYLV------GARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQ 1794
Cdd:cd05966 276 YWctadigwitghSYIVygplanGATTVMfegTP--TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1795 SLpicRVFCS-GEAL-PTALaKSFTEH---FSCELHNLYGPTEAAvdvSYMDATL-GLHPEE--SCvaiGYPVWNTQLYI 1866
Cdd:cd05966 354 SL---RVLGSvGEPInPEAW-MWYYEVigkERCPIVDTWWQTETG---GIMITPLpGATPLKpgSA---TRPFFGIEPAI 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1867 LDQYLRPVPVGVDGelYLAGHQ----LAMGyLHRADltaSRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKI 1942
Cdd:cd05966 424 LDEEGNEVEGEVEG--YLVIKRpwpgMART-IYGDH---ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINV 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1943 RGQRIELGEIEQQlrLISGLDV----VV---HAIsseqnKANVqLVAYL-----QTTAPVDIDQLKKQLAKHLPAYMVPT 2010
Cdd:cd05966 498 SGHRLGTAEVESA--LVAHPAVaeaaVVgrpHDI-----KGEA-IYAFVtlkdgEEPSDELRKELRKHVRKEIGPIATPD 569
|
570 580
....*....|....*....|.
gi 490930577 2011 HYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05966 570 KIQFVPGLPKTRSGKIMRRIL 590
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1557-1935 |
2.01e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 90.98 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGE 1636
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 QKDLaaivhpsiatfafnelfdetkvdlssykttvitpqHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:cd05910 82 PKAD-----------------------------------EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTP--CTFDVsvweffwsyLVGARLVIAPIDAHR----DPLALLSLIQKYQVTTLHFVPSMLAVFENAAteilsS 1790
Cdd:cd05910 127 EVDLATFPlfALFGP---------ALGLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYC-----A 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 AQRQSLP-ICRVFCSGEALPTALAKSFTEHFS--CELHNLYGPTEA----AVDVSYMDATLGLHPEE-SCVAIGYPVWNT 1862
Cdd:cd05910 193 QHGITLPsLRRVLSAGAPVPIALAARLRKMLSdeAEILTPYGATEAlpvsSIGSRELLATTTAATSGgAGTCVGRPIPGV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1863 QLYILD---------QYLRPVPVGVDGELYLAGHQLAMGYLHRADltASRFVANPFTAGQRMYRTGDIARWHADGSIQYI 1933
Cdd:cd05910 273 RVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPV--ATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFC 350
|
..
gi 490930577 1934 GR 1935
Cdd:cd05910 351 GR 352
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
475-986 |
2.35e-18 |
|
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: 90.85 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 475 VLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQtviagaiprsiDSVVVMLsvlnsgasf 554
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDGDR----RLTYRELDRRADRLAAGLRGLGIRPG-----------DRVVVQL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 555 lPLDLDypidrmqmmcedanplFVLTTQALAQQ-------LPQniqQLHLDQEGVQTQIRKQdASDIPAENRKFDFQ--- 624
Cdd:cd05920 73 -PNVAE----------------FVVLFFALLRLgavpvlaLPS---HRRSELSAFCAHAEAV-AYIVPDRHAGFDHRala 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 --------DVAYVIFTSGSTGRPKGVMNTHGSLLNLI--------LSHKpTIYWPVLEAvnerfpdrplraahTHSFSFD 688
Cdd:cd05920 132 relaesipEVALFLLSGGTTGTPKLIPRTHNDYAYNVrasaevcgLDQD-TVYLAVLPA--------------AHNFPLA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 689 SSwlQVFWMLWGQELHIFDENMRRD-AFGLvqeIQQRQIDTLDLPPSFcAQMMTNGLFVENQHHPSLILIGGEAAPLAlw 767
Cdd:cd05920 197 CP--GVLGTLLAGGRVVLAPDPSPDaAFPL---IEREGVTVTALVPAL-VSLWLDAAASRRADLSSLRLLQVGGARLS-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 768 qqlnAQPALFAHNLYGPTEYTVdtF-RAE--LKQTArpvIGNP---IGNTQAY---------VLDRHLQRCPTGVIGELY 832
Cdd:cd05920 269 ----PALARRVPPVLGCTLQQV--FgMAEglLNYTR---LDDPdevIIHTQGRpmspddeirVVDEEGNPVPPGEEGELL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 833 ISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVE 912
Cdd:cd05920 340 TRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVH 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 913 SAVVIAEPinnsHRLLG-----YCVVKDIELDektseqlsqqyLSQLRQNLPE-----YMVPSALTVMSEFPRNVSGKVD 982
Cdd:cd05920 414 DAAVVAMP----DELLGerscaFVVLRDPPPS-----------AAQLRRFLRErglaaYKLPDRIEFVDSLPLTAVGKID 478
|
....
gi 490930577 983 KKAL 986
Cdd:cd05920 479 KKAL 482
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
487-986 |
2.73e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 90.71 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIvsgERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRM 566
Cdd:PRK07514 16 RDAPFI---ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 567 QMMCEDANP-LFVLTT------QALAQQLP-QNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDfqDVAYVIFTSGSTGR 638
Cdd:PRK07514 93 DYFIGDAEPaLVVCDPanfawlSKIAAAAGaPHVETLDADGTGSLLEAAAAAPDDFETVPRGAD--DLAAILYTSGTTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 639 PKGVMNTHGSLL-NLILSHKptiYWpvleavneRF-PDRPLRAA----HTHSFsFDSSWLQVFW---MLWgqeLHIFD-- 707
Cdd:PRK07514 171 SKGAMLSHGNLLsNALTLVD---YW--------RFtPDDVLIHAlpifHTHGL-FVATNVALLAgasMIF---LPKFDpd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 708 ---ENMRR-DAFGLVQEIQQRQIDTLDLPPSFCAQMMtngLFvenqhhpslilIGGEAAPLA----LWQQLNAQPALfah 779
Cdd:PRK07514 236 avlALMPRaTVMMGVPTFYTRLLQEPRLTREAAAHMR---LF-----------ISGSAPLLAethrEFQERTGHAIL--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 780 NLYGPTEYTVDT---FRAElkqtARP-VIGNPIGNTQAYVLDRHL-QRCPTGVIGELYISGFGIANGYLGRADLSAARFV 854
Cdd:PRK07514 299 ERYGMTETNMNTsnpYDGE----RRAgTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 855 ANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAvVIAEPinnsHRLLGYCVV 933
Cdd:PRK07514 375 ADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVvESA-VIGVP----HPDFGEGVT 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 934 ------KDIELDEKTseqlsqqYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07514 444 avvvpkPGAALDEAA-------ILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1678-2031 |
2.84e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 89.08 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDV--SVWEFFWSYLVGARLVIAPIDAHRDP 1755
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLP-LFHVngSVVTLLTPLASGAHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1756 LA---LLSLIQKYQVTTLHFVPSMLAvfenAATEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTE 1832
Cdd:cd05944 84 GLfdnFWKLVERYRITSLSTVPTVYA----ALLQVPVNADISSLRF--AMSGAAPLPVELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1833 A--AVDVSYMDATLGLhpeeSCVAIGYPVWNTQLYILD---QYLRPVPVGVDGELYLAGHQLAMGYLHRADltasrfvAN 1907
Cdd:cd05944 158 AtcLVAVNPPDGPKRP----GSVGLRLPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTEG-------NK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1908 PFTAGQRMYRTGDIARWHADGSIQYIGRADDqLKIR-GQRIELGEIEQQlrLISGLDV-VVHAISSEQNKANVQLVAYLQ 1985
Cdd:cd05944 227 NAFVADGWLNTGDLGRLDADGYLFITGRAKD-LIIRgGHNIDPALIEEA--LLRHPAVaFAGAVGQPDAHAGELPVAYVQ 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490930577 1986 TT--APVDIDQLKKQLAKHLPAY-MVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05944 304 LKpgAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
475-986 |
3.85e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 90.88 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 475 VLDIFYEQVKKYPERTAIVS--GERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA 552
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAvrLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 553 SFLPLdldYPIDRMQ----MMCEDANPLFVL-----------TTQALAQQLPQNIQQLHLDQEG------VQTQIRKQDA 611
Cdd:PRK13295 106 VLNPL---MPIFRERelsfMLKHAESKVLVVpktfrgfdhaaMARRLRPELPALRHVVVVGGDGadsfeaLLITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 612 SDIPA--ENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILshkptiywPVLEAVNERFPDRPLRA---AHTHSFS 686
Cdd:PRK13295 183 PDAPAilARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIV--------PYAERLGLGADDVILMAspmAHQTGFM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 687 F---------DSSWLQVFWmlwgqelhifdenmrrDAFGLVQEIQQRQID-TLDLPPsFCAQMMTNglfVENQHH--PSL 754
Cdd:PRK13295 255 YglmmpvmlgATAVLQDIW----------------DPARAAELIRTEGVTfTMASTP-FLTDLTRA---VKESGRpvSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 755 --ILIGGEAAPLALWQQlnAQPALFAH--NLYGPTE---YTVDTFRAELKQtARPVIGNPIGNTQAYVLDRHLQRCPTGV 827
Cdd:PRK13295 315 rtFLCAGAPIPGALVER--ARAALGAKivSAWGMTEngaVTLTKLDDPDER-ASTTDGCPLPGVEVRVVDADGAPLPAGQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 828 IGELYISGFGIANGYLGRADLSAARFvanpfehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIRG-YRVEIGEVENALS 906
Cdd:PRK13295 392 IGRLQVRGCSNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADGYIRISGRSKDVI-IRGgENIPVVEIEALLY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 907 ILTNVESAVVIAEPinnsHRLLG----YCVV----KDIELDEKT----SEQLSQQYLsqlrqnlpeymvPSALTVMSEFP 974
Cdd:PRK13295 463 RHPAIAQVAIVAYP----DERLGeracAFVVprpgQSLDFEEMVeflkAQKVAKQYI------------PERLVVRDALP 526
|
570
....*....|..
gi 490930577 975 RNVSGKVDKKAL 986
Cdd:PRK13295 527 RTPSGKIQKFRL 538
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1547-1956 |
3.90e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 90.72 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1547 EQTAL----SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIK 1622
Cdd:PRK04319 59 DKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1623 FMLQDAKSK-----------------------LVIGEQKDLAAivhpsiATFAFNELFDETKvdlSSYKTTVITPQHPAY 1679
Cdd:PRK04319 139 DRLEDSEAKvlittpallerkpaddlpslkhvLLVGEDVEEGP------GTLDFNALMEQAS---DEFDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQAIVNRilWMQSEYPLSatdtiLQKTP---CTFDVSvWEFFWSY------LVGARLViapID 1750
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLQH--YQTGKYVLD-----LHEDDvywCTADPG-WVTGTSYgifapwLNGATNV---ID 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1751 AHR-DPLALLSLIQKYQVTTLHFVPSMLAVFENAATEIlssAQRQSLPICRVFCS-GEAL-PTAL--AKsftEHFSCELH 1825
Cdd:PRK04319 279 GGRfSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDL---VKKYDLSSLRHILSvGEPLnPEVVrwGM---KVFGLPIH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTE--AAVDVSY--MDATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAM--GYLHRADL 1899
Cdd:PRK04319 353 DNWWMTEtgGIMIANYpaMDIKPG--------SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMmrGIWNNPEK 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 1900 TASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:PRK04319 425 YESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKL 474
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1534-2031 |
5.93e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 90.09 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1534 LQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID 1613
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 LQHPTERIKFMLQDAKSKLV------------IGEQKDLAAIVHPSIATF---AFNELFD---------ETKVDLS---- 1665
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVIlcldlvfprvtnVQSATKIEHVIVTRIADFlpfPKNLLYPfvqkkqsnlVVKVSESetih 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 -------SYKTTVITPQHP----AYLIYTSGTTGQPKGVMVSHQAIV-NRILWMQSEYPLSATDTILqktpctfdVSVWE 1733
Cdd:PRK06710 186 lwnsvekEVNTGVEVPCDPendlALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVV--------LGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1734 FFWSYLVGARLVIAPIDAHR-------DPLALLSLIQKYQVTTLHFVPSMLAVFENAAteILSSAQRQSLPICrvfCSGE 1806
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKmvlipkfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSP--LLKEYDISSIRAC---ISGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 A-LPTALAKSFTEHFSCELHNLYGPTEAAvDVSYMDAtlgLHPEESCVAIGYPVWNTQLYILD----QYLRPvpvGVDGE 1881
Cdd:PRK06710 333 ApLPVEVQEKFETVTGGKLVEGYGLTESS-PVTHSNF---LWEKRVPGSIGVPWPDTEAMIMSletgEALPP---GEIGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1882 LYLAGHQLAMGYLHRADLTASrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG 1961
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEK 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1962 L-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06710 479 VqEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
503-988 |
6.64e-18 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 89.11 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedanplFVlttq 582
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL-------------------FT---- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAqqlPQNIQQlHLDQEGVQTQIrkqdasdIPAENR-KFDfQDVAYVIFTSGSTGRPKGV------MNTHGSLLNLILS 655
Cdd:cd05973 58 AFG---PKAIEH-RLRTSGARLVV-------TDAANRhKLD-SDPFVMMFTSGTTGLPKGVpvplraLAAFGAYLRDAVD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 656 HKP-TIYWPVLE---------AVNErfpdrPLRAAHTH-----SFSFDSSWlqvfwmlwgqelhifdENMRRdaFGlvqe 720
Cdd:cd05973 126 LRPeDSFWNAADpgwayglyyAITG-----PLALGHPTillegGFSVESTW----------------RVIER--LG---- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 721 iqqrqIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLA----LWqqLNAQPALFAHNLYGPTEytVDTFRAEL 796
Cdd:cd05973 179 -----VTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTpeviRW--FDAALGVPIHDHYGQTE--LGMVLANH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 797 KQTARPV----IGNPIGNTQAYVLDRHLQRCPTGVIGELYI----SGFGIANGYLGRADLSAArfvanpfehgQRMYRTG 868
Cdd:cd05973 250 HALEHPVhagsAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdianSPLMWFRGYQLPDTPAID----------GGYYLTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVkdIELDEKTSEQLSQ 948
Cdd:cd05973 320 DTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVV--LRGGHEGTPALAD 397
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 490930577 949 QYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05973 398 ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
625-983 |
9.21e-18 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 86.69 E-value: 9.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYwpvLEAVNERFPDRPLraAHTHSFSfdsSWLQVFWMlwGQELH 704
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFN---ISGEDAILAPGPL--SHSLFLY---GAISALYL--GGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 705 IfdenMRR-DAFGLVQEIQQRQIDTLDLPPSfcaqmMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQ-PALFAHN 780
Cdd:cd17633 71 G----QRKfNPKSWIRKINQYNATVIYLVPT-----MLQALARTLEPESKIksIFSSGQKLFESTKKKLKNIfPKANLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 781 LYGPTEYTVDTFRAElkQTARPV--IGNPIGNTQAYVLDRHlqrcpTGVIGELYISGFGIANGYLGRADLSAARFvanpf 858
Cdd:cd17633 142 FYGTSELSFITYNFN--QESRPPnsVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 859 ehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIEL 938
Cdd:cd17633 210 ------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP----DARFGEIAVALYSG 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490930577 939 DEKTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17633 280 DKLTYKQL----KRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
489-986 |
9.41e-18 |
|
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: 88.69 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 489 RTAIVSGERpnlqHLSFAELAVKVNQLTRFLQ-ENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA------SFL-PLDLD 560
Cdd:cd05958 1 RTCLRSPER----EWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAiavatmPLLrPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 561 YPIDRmqmmcedANPLFVLTTQALAqqlpqniqqlhldqegvqtqirkqdASDipaenrkfdfqDVAYVIFTSGSTGRPK 640
Cdd:cd05958 77 YILDK-------ARITVALCAHALT-------------------------ASD-----------DICILAFTSGTTGAPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 641 GVMNTHGSLLnlilshkptiywpvleAVNERFPDRPLRAAHTH--------SFSFDSSWLQVFWMLWGQELHIFDENMRR 712
Cdd:cd05958 114 ATMHFHRDPL----------------ASADRYAVNVLRLREDDrfvgspplAFTFGLGGVLLFPFGVGASGVLLEEATPD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 713 DAFGLVQEiqQRQIDTLDLPPSFCAqmMTNGLFVENQHHPSLILI--GGEAAPLALWQQLNAQPALFAHNLYGPTEyTVD 790
Cdd:cd05958 178 LLLSAIAR--YKPTVLFTAPTAYRA--MLAHPDAAGPDLSSLRKCvsAGEALPAALHRAWKEATGIPIIDGIGSTE-MFH 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 791 TFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGfgiANGYLGRADLSAARFVANPFEHgqrmyrTGD 869
Cdd:cd05958 253 IFISARPGDARPgATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGGWNI------TGD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 870 LVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNshRLL---GYCVVKDielDEKTSEQL 946
Cdd:cd05958 324 TYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDES--RGVvvkAFVVLRP---GVIPGPVL 398
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 490930577 947 SQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05958 399 ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1562-2032 |
1.02e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 88.17 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1562 EVRLQVCALAQQLQRAgvqAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVigeqkdla 1641
Cdd:PRK08308 15 DLRLQRYEEMEQFQEA---AGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGL-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1642 aivhpsiatfafneLFDETKVDLSSYKTTviTPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQ 1721
Cdd:PRK08308 84 --------------LYGESDFTKLEAVNY--LAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1722 KTPCTFdvsvweffwSY------LVGARLVIAP-IDAHRDPLALLSLIQKYQVTTLHFVPSMLavfenaatEILSSAQRQ 1794
Cdd:PRK08308 148 ACPVTH---------SYglicgvLAALTRGSKPvIITNKNPKFALNILRNTPQHILYAVPLML--------HILGRLLPG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1795 SLPICRVFCSGEALPTALAKSFTEHfSCELHNLYGPTEAAvdvsymdatlglhpeesCVAIGYPVwntqlyildqylrpv 1874
Cdd:PRK08308 211 TFQFHAVMTSGTPLPEAWFYKLRER-TTYMMQQYGCSEAG-----------------CVSICPDM--------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1875 pvgvdgelylAGHqLAMGY-LHRADLTASRFVANP----FTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIEL 1949
Cdd:PRK08308 258 ----------KSH-LDLGNpLPHVSVSAGSDENAPeeivVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1950 GEIEQQLRLISGL-DVVV----HAISSEQNKAnvQLVAylqtTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNG 2024
Cdd:PRK08308 327 IEVEDVMLRLPGVqEAVVyrgkDPVAGERVKA--KVIS----HEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANG 400
|
....*...
gi 490930577 2025 KLDRKALP 2032
Cdd:PRK08308 401 KVSRKLLE 408
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1680-2028 |
1.18e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 86.55 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPcTFDVSVWEF-FWSYLVGARLVIAPidaHRDPLAL 1758
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLP-LFHIAGLNLaLATFHAGGANVVME---KFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1759 LSLIQKYQVTTLHFVPSMLAVFENAATEilSSAQRQSLPICrvfcSGEALPtALAKSFTEHFSCELHNLYGPTEAAVDVS 1838
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEK--SGVDLSSLRHV----LGLDAP-ETIQRFEETTGATFWSLYGQTETSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 YMDAtlglhpEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFvanpftagqR--MY 1916
Cdd:cd17637 154 LSPY------RERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1917 RTGDIARWHADGSIQYIGR--ADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTTAPVDID 1993
Cdd:cd17637 219 HTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIaEVCVIGVPDPKWGEGIKAVCVLKPGATLTAD 298
|
330 340 350
....*....|....*....|....*....|....*
gi 490930577 1994 QLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDR 2028
Cdd:cd17637 299 ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
475-1003 |
1.19e-17 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 89.04 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 475 VLDIFYEQVKKYPERTAIVS--GERpnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA 552
Cdd:PRK06087 25 LADYWQQTARAMPDKIAVVDnhGAS-----YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 553 SFLPL-------DLDYPIDRMQ---MMCED--ANPLFVLTTQALAQQLPQNIQQLHLDQEGVQT------QIRKQD---A 611
Cdd:PRK06087 100 VSVPLlpswreaELVWVLNKCQakmFFAPTlfKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATsslslsQIIADYeplT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 612 SDIPAenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGsllNLILSHKPtiYWPVLEAvnerfpdrplraahthsfsfdsSW 691
Cdd:PRK06087 180 TAITT-----HGDELAAVLFTSGTEGLPKGVMLTHN---NILASERA--YCARLNL----------------------TW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 692 LQVFWM------------------LWGQE---LHIFdenmrRDAFGLVQEIQQRQIDTLDLPPsFCAQMMTNglfVENQH 750
Cdd:PRK06087 228 QDVFMMpaplghatgflhgvtapfLIGARsvlLDIF-----TPDACLALLEQQRCTCMLGATP-FIYDLLNL---LEKQP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 751 H--PSL--ILIGGEAAPLALWQQLNAQPALFAhNLYGPTEYTVDTFRAELKQTARPVI--GNPIGNTQAYVLDRHLQRCP 824
Cdd:PRK06087 299 AdlSALrfFLCGGTTIPKKVARECQQRGIKLL-SVYGSTESSPHAVVNLDDPLSRFMHtdGYAAAGVEIKVVDEARKTLP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 825 TGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDqIKIRG-YRVEIGEVEN 903
Cdd:PRK06087 378 PGCEGEEASRGPNVFMGYLDEPELTARALDEEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRGgENISSREVED 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 904 ALSILTNVESAVVIAEPINN-SHRLLGYCVVKDIELDEKTSEQLSqqYLSqlRQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:PRK06087 451 ILLQHPKIHDACVVAMPDERlGERSCAYVVLKAPHHSLTLEEVVA--FFS--RKRVAKYKYPEHIVVIDKLPRTASGKIQ 526
|
570 580
....*....|....*....|.
gi 490930577 983 KKALPKPQIRAHSRMAETPEQ 1003
Cdd:PRK06087 527 KFLLRKDIMRRLTQDVCEEIE 547
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
21-265 |
1.33e-17 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 84.71 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 21 LASTQLGIFladHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIELNNQVQFQIEEFDF 100
Cdd:COG4908 1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 101 CHLTPKKAQQRLWDWMPSDRQcaKSLKAGETQLFRQVLF-TTHDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQEGK 179
Cdd:COG4908 78 SALPEPEREAELEELVAEEAS--RPFDLARGPLLRAALIrLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 180 DLSVSPF-IGVNEVISERQAYENSHQFKIDQAFWKAYCEDLPSPISLST-HHLAAKTTATFVKHQLRFSTGILEQIQALA 257
Cdd:COG4908 156 PPPLPELpIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTdRPRPAVQTFRGATLSFTLPAELTEALKALA 235
|
....*...
gi 490930577 258 AQTKLALN 265
Cdd:COG4908 236 KAHGATVN 243
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
625-982 |
1.35e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 87.05 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHG----SLLNLILSHKP---TIYWPVLEAVNE----RFPDRPLraahTHSfsfDSSWLQ 693
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEdifrMLMGGADFGTGeftPSEDAHKAAAAAagtvMFPAPPL----MHG---TGSWTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 694 VFWMLWGQELHIFDEnmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-PSLILIGGEAAPLALW---QQ 769
Cdd:cd05924 77 FGGLLGGQTVVLPDD--RFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDlSSLFAISSGGALLSPEvkqGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 770 LNAQPALFAHNLYGPTE-----YTVDTFRAELKQTARPVignpigNTQAYVLDRHLQRCPTGVIGELYISGFG-IANGYL 843
Cdd:cd05924 155 LELVPNITLVDAFGSSEtgftgSGHSAGSGPETGPFTRA------NPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 844 GRADLSAARFvanPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinn 923
Cdd:cd05924 229 GDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRP--- 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 924 SHRlLGYCVVKDIELDEKTSEQLsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:cd05924 303 DER-WGQEVVAVVQLREGAGVDL-EELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
487-986 |
1.44e-17 |
|
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: 88.72 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGERpnlQH-LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL-------D 558
Cdd:cd05923 15 PDACAIADPAR---GLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALInprlkaaE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 559 LDYPIDRMQM----MCEDANPlfvltTQALAQQLpqnIQQLHLDQEgVQTQIRKQDASDIPAenRKFDFQDVAYVIFTSG 634
Cdd:cd05923 92 LAELIERGEMtaavIAVDAQV-----MDAIFQSG---VRVLALSDL-VGLGEPESAGPLIED--PPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 635 STGRPKGV-------------MNTHGSLL----NLILSHKPtIYWPVleavnerfpdrPLRAAHTHSFSFDSSWLQVfwm 697
Cdd:cd05923 161 TTGLPKGAvipqraaesrvlfMSTQAGLRhgrhNVVLGLMP-LYHVI-----------GFFAVLVAALALDGTYVVV--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 698 lwgqelhifDENMRRDAFGLvqeIQQRQIDTLDLPPSFCAQMMTNGLF----VENQHHpslILIGGEAAPLALWQQLN-A 772
Cdd:cd05923 226 ---------EEFDPADALKL---IEQERVTSLFATPTHLDALAAAAEFaglkLSSLRH---VTFAGATMPDAVLERVNqH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 773 QPALFAhNLYGPTEYTVDTFRAELKQTARpviGNPIGNTQ---AYVLDRHLQRCPTGVIGELYISGFGIA--NGYLGRAD 847
Cdd:cd05923 291 LPGEKV-NIYGTTEAMNSLYMRDARTGTE---MRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 848 LSAARFVanpfehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRL 927
Cdd:cd05923 367 ATAKKLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQS 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 928 LGYCVVkdIELDEKTSEQLSQQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05923 440 VTACVV--PREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1101-1380 |
2.56e-17 |
|
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: 87.09 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1101 LPLLPLQKGMLFLSQVENQSN-YNAFTRLSLNGDIDPVRLQQALITVLKRH-------PQLGGhfdselaeEPV-FIysL 1171
Cdd:cd19540 2 IPLSFAQQRLWFLNRLDGPSAaYNIPLALRLTGALDVDALRAALADVVARHeslrtvfPEDDG--------GPYqVV--L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1172 HPTQAWP-VQFCSVTPDLLEQTIQEALQQPIHL--DQPyglIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKA 1248
Cdd:cd19540 72 PAAEARPdLTVVDVTEDELAARLAEAARRGFDLtaELP---LRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1249 Y----QQTNQQLPVLEHSYetvikA--------LSGRDHETSKVI------WQRDLADL-QPLIL-FNQAQQAVQetSYR 1308
Cdd:cd19540 149 YaarrAGRAPDWAPLPVQY-----AdyalwqreLLGDEDDPDSLAarqlayWRETLAGLpEELELpTDRPRPAVA--SYR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1309 -------LSAELGAKLQHKLRQQGITLnvFM--QMIWAMTLniyaHR----EDIVFGTPVSGRSAPinGLEQQIGLFLNT 1375
Cdd:cd19540 222 ggtveftIDAELHARLAALAREHGATL--FMvlHAALAVLL----SRlgagDDIPIGTPVAGRGDE--ALDDLVGMFVNT 293
|
....*
gi 490930577 1376 IPVRV 1380
Cdd:cd19540 294 LVLRT 298
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1530-2031 |
4.22e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 87.42 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAILAVIEAGAA 1608
Cdd:PRK08974 21 RYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1609 -------YLPIDLQHpterikfMLQDAKSKlvigeqkdlaAIVhpSIATFA--FNELFDETKVD----------LSSYKT 1669
Cdd:PRK08974 101 vvnvnplYTPRELEH-------QLNDSGAK----------AIV--IVSNFAhtLEKVVFKTPVKhviltrmgdqLSTAKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1670 TV---------------------------------------ITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSE 1710
Cdd:PRK08974 162 TLvnfvvkyikrlvpkyhlpdaisfrsalhkgrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1711 Y-PLSATDTILQKTPC----TFDVSVWEFFWSYLVGARLVIA-PidahRDPLALLSLIQKYQVTTLHFVPSMLavfeNAa 1784
Cdd:PRK08974 242 YgPLLHPGKELVVTALplyhIFALTVNCLLFIELGGQNLLITnP----RDIPGFVKELKKYPFTAITGVNTLF----NA- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1785 teILSSAQRQSLPICRVFCS---GEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLGLHPEescvAIGYPVWN 1861
Cdd:PRK08974 313 --LLNNEEFQELDFSSLKLSvggGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSG----SIGLPVPS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1862 TQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASrFVANPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLK 1941
Cdd:PRK08974 387 TEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMIL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1942 IRGQRIELGEIEQQLRLISG-LDVVV----HAISSEQNKANVqlvayLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVE 2016
Cdd:PRK08974 460 VSGFNVYPNEIEDVVMLHPKvLEVAAvgvpSEVSGEAVKIFV-----VKKDPSLTEEELITHCRRHLTGYKVPKLVEFRD 534
|
570
....*....|....*
gi 490930577 2017 QFPLSHNGKLDRKAL 2031
Cdd:PRK08974 535 ELPKSNVGKILRREL 549
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
779-989 |
4.39e-17 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 87.12 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 779 HNLYGPTEY------TVDTFRAELKQTARPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADlsaar 852
Cdd:PRK13382 341 YNNYNATEAgmiataTPADLRAAPDTAGRPAEG-----TEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 853 fvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLLGYC 931
Cdd:PRK13382 411 ---KDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVaEAAVIGVDDEQYGQRLAAFV 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 932 VVKDIEldEKTSEQLSQQylsqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:PRK13382 486 VLKPGA--SATPETLKQH----VRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1532-1998 |
4.45e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 87.31 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTALS---------DENHQLSFSEVRLQVCALAQQLQRAGVqAGDIVAVALPRSVKLSIAILAV 1602
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAFTfidyeqdpaGVAETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1603 IEAGAAYLPIDLQHP---TERIKFMLQDAKSKLVIGEQKDLAAIV-----HPSIATFAFNELfDetKVDLSSYKTTVITP 1674
Cdd:PRK05850 80 LQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSAVVDDVTeyvapQPGQSAPPVIEV-D--LLDLDSPRGSDARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1675 Q-HP--AYLIYTSGTTGQPKGVMVSHQ-AIVNRILWMQSEYPlsATDTILqkTPCTFDVSvWEFFW---SYLVGarlVIA 1747
Cdd:PRK05850 157 RdLPstAYLQYTSGSTRTPAGVMVSHRnVIANFEQLMSDYFG--DTGGVP--PPDTTVVS-WLPFYhdmGLVLG---VCA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1748 PIDAHRdPLALLS---LIQKyqvttlhfvPS----MLA----VFE---NAATEIlsSAQRQS--------LPICRVFCSG 1805
Cdd:PRK05850 229 PILGGC-PAVLTSpvaFLQR---------PArwmqLLAsnphAFSaapNFAFEL--AVRKTSdddmagldLGGVLGIISG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1806 -EALPTALAKSFTEHFSceLHNL--------YGPTEAAVDVSymDATLGLHPE--------------ESCVA------IG 1856
Cdd:PRK05850 297 sERVHPATLKRFADRFA--PFNLretairpsYGLAEATVYVA--TREPGQPPEsvrfdyeklsaghaKRCETgggtplVS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1857 YPV-WNTQLYILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVA-----NPFTAGQRMYRTGDIARWHaDGS 1929
Cdd:PRK05850 373 YGSpRSPTVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpSPGTPEGPWLRTGDLGFIS-EGE 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1930 IQYIGRADDQLKIRGQRIELGEIEQQLRLISGLDVVvhAISSEQNKANvQLVAylqttapvdIDQLKKQ 1998
Cdd:PRK05850 452 LFIVGRIKDLLIVDGRNHYPDDIEATIQEITGGRVA--AISVPDDGTE-KLVA---------IIELKKR 508
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1532-2036 |
6.81e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 86.76 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARI----------TPEQTALSDENHQLSFSEVRLQVCALAQQLQRA-GVQAGDIVAVALPRSVKLSIAIL 1600
Cdd:PRK05620 3 STMQDVPLSLTRIleygstvhgdTTVTTWGGAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1601 AVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQK--------------------------DLAAIVHPS-IATFAF 1653
Cdd:PRK05620 83 AVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRlaeqlgeilkecpcvravvfigpsdaDSAAAHMPEgIKVYSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1654 NELFDETKVDlssYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHqaivnRILWMQSeYPLSATDTILQKTPCTFDVSV-- 1731
Cdd:PRK05620 163 EALLDGRSTV---YDWPELDETTAAAICYSTGTTGAPKGVVYSH-----RSLYLQS-LSLRTTDSLAVTHGESFLCCVpi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1732 -----WEF-FWSYLVGARLVIAPIDAhrDPLALLSLIQKYQVTTLHFVPS-----MLAVFENaateilsSAQRQSLPicR 1800
Cdd:PRK05620 234 yhvlsWGVpLAAFMSGTPLVFPGPDL--SAPTLAKIIATAMPRVAHGVPTlwiqlMVHYLKN-------PPERMSLQ--E 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1801 VFCSGEALPTALAKSFTEHFSCELHNLYGPTEAavdvsymdATLGL--HPeESCVAiGYPVWNtqlYILDQYLRPVPV-- 1876
Cdd:PRK05620 303 IYVGGSAVPPILIKAWEERYGVDVVHVWGMTET--------SPVGTvaRP-PSGVS-GEARWA---YRVSQGRFPASLey 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1877 ----------GVD---GELYLAGHQLAMGYLH----RADLTASRFVANPFTAGQRMY------RTGDIARWHADGSIQYI 1933
Cdd:PRK05620 370 rivndgqvmeSTDrneGEIQVRGNWVTASYYHspteEGGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1934 GRADDQLKIRGQRIELGEIEQqlrLISGLDVVVHA--ISSEQNK------ANVQLVAYLQTTAPVdIDQLKKQLAKHLPA 2005
Cdd:PRK05620 450 DRARDVIRSGGEWIYSAQLEN---YIMAAPEVVECavIGYPDDKwgerplAVTVLAPGIEPTRET-AERLRDQLRDRLPN 525
|
570 580 590
....*....|....*....|....*....|.
gi 490930577 2006 YMVPTHYMLVEQFPLSHNGKLDRKALPQpHL 2036
Cdd:PRK05620 526 WMLPEYWTFVDEIDKTSVGKFDKKDLRQ-HL 555
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
487-986 |
1.10e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 85.68 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGErpnlQHLSFAELAVKVNQLTRFLQ-ENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:PRK06839 16 PDRIAIITEE----EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 566 MQMMCEDANplfvlTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIpaENRKFD-----FQDVAYVI-FTSGSTGRP 639
Cdd:PRK06839 92 LIFQLKDSG-----TTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEI--EDRKIDnfvekNESASFIIcYTSGTTGKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 640 KG-VMNTHGSLLNLILShkptiywpvLEAVNERFPDR-----PL-RAAHTHSFSFDSswlqvfwMLWGQELHIFDenmRR 712
Cdd:PRK06839 165 KGaVLTQENMFWNALNN---------TFAIDLTMHDRsivllPLfHIGGIGLFAFPT-------LFAGGVIIVPR---KF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 713 DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVE-NQHHPSLILIGGEAAPLALWQQLNAQPALFAHNlYGPTEYTVDT 791
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETtNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQG-FGMTETSPTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 792 FRAELKQTARPV--IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAarfvaNPFEHGqrMYRTGD 869
Cdd:PRK06839 305 FMLSEEDARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE-----ETIQDG--WLCTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 870 LVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYcVVKDIELDEKTSEQLSQQ 949
Cdd:PRK06839 378 LARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQ----HVKWGE-IPIAFIVKKSSSVLIEKD 452
|
490 500 510
....*....|....*....|....*....|....*..
gi 490930577 950 YLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06839 453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1541-2026 |
1.53e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 85.45 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1541 QARITPEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPT 1618
Cdd:PRK13390 6 HAQIAPDRPAVivAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1619 ERIKFMLQDAKSKLVIGEQ--KDLAAIV-HPSIATFAFNELFDetkvDLSSYKTTVITPQHP-------AYLIYTSGTTG 1688
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAalDGLAAKVgADLPLRLSFGGEID----GFGSFEAALAGAGPRlteqpcgAVMLYSSGTTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1689 QPKGVmvshqaivnrilwmQSEYPLSATDT----ILQKTPCTFDVSVWEFFWS----------------YLVGARLVIAp 1748
Cdd:PRK13390 162 FPKGI--------------QPDLPGRDVDApgdpIVAIARAFYDISESDIYYSsapiyhaaplrwcsmvHALGGTVVLA- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 idAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSsaqRQSLPICR-VFCSGEALPTALAKSFTEHFSCELHNL 1827
Cdd:PRK13390 227 --KRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRT---RYDVSSLRaVIHAAAPCPVDVKHAMIDWLGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAAvDVSYMDATLGL-HPEescvAIGYPVWNTqLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTA-SRFV 1905
Cdd:PRK13390 302 YSSTEAH-GMTFIDSPDWLaHPG----SVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAaAQHP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1906 ANPFTAgqrmyRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISS----EQNKANVQL 1980
Cdd:PRK13390 376 AHPFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVhDVAVIGVPDpemgEQVKAVIQL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 490930577 1981 VAYLQTTapvdiDQLKKQLAKHLPA----YMVPTHYMLVEQFPLSHNGKL 2026
Cdd:PRK13390 451 VEGIRGS-----DELARELIDYTRSriahYKAPRSVEFVDELPRTPTGKL 495
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
625-983 |
1.75e-16 |
|
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: 83.32 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiyWPVLEAVNErfPDRPLRA-AHTHSFSFDSSWLQVfwMLWGQEL 703
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAA------WADCADLTE--DDRYLIInPFFHTFGYKAGIVAC--LLTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 704 H---IFDenmrrdAFGLVQEIQQRQIDTLDLPPSfcaqmmtngLFVENQHHPSL----------ILIGGEAAPLALWQQL 770
Cdd:cd17638 71 VpvaVFD------VDAILEAIERERITVLPGPPT---------LFQSLLDHPGRkkfdlsslraAVTGAATVPVELVRRM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 771 NAQ-PALFAHNLYGPTEYTVDTF--RAELKQTARPVIGNPIGNTQAYVLDRhlqrcptgviGELYISGFGIANGYLGRAD 847
Cdd:cd17638 136 RSElGFETVLTAYGLTEAGVATMcrPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 848 LSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRL 927
Cdd:cd17638 206 ATAEAIDADGWLH------TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEV 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 928 LGYCVV--KDIELDEktseqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd17638 280 GKAFVVarPGVTLTE-------EDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1532-2134 |
4.78e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.61 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARITPEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGvQAGDIVAVALPRSVKLSIAILAVIEA 1605
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1606 GA----AYLPIDL-QHPTERIKFMLQDAKSKLVI---GEQKDLAAIVHPSIAtfAFNELFDETKVDLS---SYKTTVITP 1674
Cdd:PRK05691 88 GViavpAYPPESArRHHQERLLSIIADAEPRLLLtvaDLRDSLLQMEELAAA--NAPELLCVDTLDPAlaeAWQEPALQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1675 QHPAYLIYTSGTTGQPKGVMVSHQAIV-NRILWMQS-EYPLSATDTILQKTPCTFDVSvweffwsyLVGARL-------- 1744
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVaNEQLIRHGfGIDLNPDDVIVSWLPLYHDMG--------LIGGLLqpifsgvp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 --VIAPIDAHRDPLALLSLIQKYQvTTLHFVPSMlaVFENAATEILSSA-QRQSLPICRVFCSG-EALPTALAKSFTEHF 1820
Cdd:PRK05691 238 cvLMSPAYFLERPLRWLEAISEYG-GTISGGPDF--AYRLCSERVSESAlERLDLSRWRVAYSGsEPIRQDSLERFAEKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1821 S-C-----ELHNLYGPTEAAVDVS-------------YMDATLGLHPEE-------SCvaiGYPVWNTQLYILD-QYLRP 1873
Cdd:PRK05691 315 AaCgfdpdSFFASYGLAEATLFVSggrrgqgipalelDAEALARNRAEPgtgsvlmSC---GRSQPGHAVLIVDpQSLEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1874 VPVGVDGELYLAGHQLAMGYLHRADLTASRFVANpftAGQRMYRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:PRK05691 392 LGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH---DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1954 QQLRliSGLDVV----VHAISSEQNKAN-----VQLVAYLQTTAPVD--IDQLKKQLAKhlpAYM-VPTHYMLVE--QFP 2019
Cdd:PRK05691 468 KTVE--REVEVVrkgrVAAFAVNHQGEEgigiaAEISRSVQKILPPQalIKSIRQAVAE---ACQeAPSVVLLLNpgALP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2020 LSHNGKLDRKALPQPH---------LTPSNTEKQYATSA-----FEHELTRIFQQILNTDQnIGVNEDFFAIGGHSILVM 2085
Cdd:PRK05691 543 KTSSGKLQRSACRLRLadgsldsyaLFPALQAVEAAQTAasgdeLQARIAAIWCEQLKVEQ-VAADDHFFLLGGNSIAAT 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 490930577 2086 KLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQERLAEVEQTGMQPI 2134
Cdd:PRK05691 622 QVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAAIARL 670
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
482-986 |
6.08e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 83.32 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 482 QVKKYPERTA---IVSGERpnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLD 558
Cdd:PRK09088 4 HARLQPQRLAavdLALGRR-----WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 559 LDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNiqqlhLDQEGVQTQIrkqDASDiPAENRKFDFQDVAYVIFTSGSTGR 638
Cdd:PRK09088 79 WRLSASELDALLQDAEPRLLLGDDAVAAGRTDV-----EDLAAFIASA---DALE-PADTPSIPPERVSLILFTSGTSGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 639 PKGVMNTHGSLLNLilshkptiywpvleAVNerFpDRPLRAAHTHSFSFDSSWLQVFWMLwgqelhifdENMR------- 711
Cdd:PRK09088 150 PKGVMLSERNLQQT--------------AHN--F-GVLGRVDAHSSFLCDAPMFHIIGLI---------TSVRpvlavgg 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 712 ----RDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvenQHHPSL----------ILIGG--EAAPLALWQQLNAQPA 775
Cdd:PRK09088 204 silvSNGFEPKRTLGRLGDPALGITHYFCVPQMAQAF----RAQPGFdaaalrhltaLFTGGapHAAEDILGWLDDGIPM 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 776 LFAhnlYGPTE------YTVDTFRAELKQTArpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLS 849
Cdd:PRK09088 280 VDG---FGMSEagtvfgMSVDCDVIRAKAGA---AGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQAT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 850 AARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV-IAEPINNShrl 927
Cdd:PRK09088 354 ARAFTGDGW------FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIrECAVVgMADAQWGE--- 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 928 LGYCVVKDIELDEKTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK09088 425 VGYLAIVPADGAPLDLERI----RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
455-986 |
6.34e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 83.78 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 455 TALTQSGIGPRVShpeqynnvlDIFYEQVKKYPERTA-IVSGERPNLqhlSFAELAVKVNQLTRFLQENGARKQTVIAGA 533
Cdd:PRK05852 7 AAPMASDFGPRIA---------DLVEVAATRLPEAPAlVVTADRIAI---SYRDLARLVDDLAGQLTRSGLLPGDRVALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 534 IPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVL--------TTQALAQQLPQNIQQLHLDQEGVQTQ 605
Cdd:PRK05852 75 MGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidadgphdRAEPTTRWWPLTVNVGGDSGPSGGTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 606 IRKQDASDIPAENRKFDF---QDVAYVIFTSGSTGRPKGVMNTHGsllNLILSHKPTIYWPVLEAVNERFPDRPLraAHT 682
Cdd:PRK05852 155 SVHLDAATEPTPATSTPEglrPDDAMIMFTGGTTGLPKMVPWTHA---NIASSVRAIITGYRLSPRDATVAVMPL--YHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 683 HSF-----SFDSSWLQVFWMLWGQ-ELHIFDENMRRDA---FGLVQEIQQRQIDTLDLPPSfcaqmmtnglfveNQHHPS 753
Cdd:PRK05852 230 HGLiaallATLASGGAVLLPARGRfSAHTFWDDIKAVGatwYTAVPTIHQILLERAATEPS-------------GRKPAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 754 LILIGGEAAPL------ALWQQLNAqPALFAhnlYGPTEYT--VDTFRAE-LKQTARPVIGN-PIGNT---QAYVLDRHL 820
Cdd:PRK05852 297 LRFIRSCSAPLtaetaqALQTEFAA-PVVCA---FGMTEAThqVTTTQIEgIGQTENPVVSTgLVGRStgaQIRIVGSDG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 821 QRCPTGVIGELYISGFGIANGYLGRADLSAARFVanpfeHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGE 900
Cdd:PRK05852 373 LPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-----DG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPER 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 901 VENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIeLDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGK 980
Cdd:PRK05852 446 VEGVLASHPNVMEAAVFGVP----DQLYGEAVAAVI-VPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGS 520
|
....*.
gi 490930577 981 VDKKAL 986
Cdd:PRK05852 521 LDRRAV 526
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
481-988 |
1.15e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 82.52 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 481 EQVKKY----PERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENgARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLP 556
Cdd:PRK07638 5 KEYKKHaslqPNKIAIKENDR----VLTYKDWFESVCKVANWLNEK-ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 557 LDLDYPIDRMQMMCEDANPLFVLTTQALAQQLP-QNIQQLHLDQEGVQTQIRKQD-ASDIPAENRKFdfqdvaYVIFTSG 634
Cdd:PRK07638 80 LDIKWKQDELKERLAISNADMIVTERYKLNDLPdEEGRVIEIDEWKRMIEKYLPTyAPIENVQNAPF------YMGFTSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 635 STGRPKGVMNTHGSLLNlilSHKPTIywpvlEAVNERFPDRPLRAA---HTHsFSFDSswlqVFWMLWGQELHIfdenMR 711
Cdd:PRK07638 154 STGKPKAFLRAQQSWLH---SFDCNV-----HDFHMKREDSVLIAGtlvHSL-FLYGA----ISTLYVGQTVHL----MR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 712 R-DAFGLVQEIQQRQIDTLDLPPSfcaqmMTNGLFVENQ--HHPSLILIGGEAAPLALWQQLNAQ-PALFAHNLYGPTEY 787
Cdd:PRK07638 217 KfIPNQVLDKLETENISVMYTVPT-----MLESLYKENRviENKMKIISSGAKWEAEAKEKIKNIfPYAKLYEFYGASEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 788 TVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLsaarfvanPFEHGQRMYR 866
Cdd:PRK07638 292 SFVTALVDEESERRPnSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVL--------ARELNADGWM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 867 TGDLVRW-NSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIEldektSEQ 945
Cdd:PRK07638 364 TVRDVGYeDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVP----DSYWGEKPVAIIK-----GSA 434
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 490930577 946 LSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:PRK07638 435 TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
477-986 |
1.26e-15 |
|
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: 82.50 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARK-QTVIAgAIPRSIDSVVVMLSVLNSGAsfL 555
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGER----RLSYAELDRRADRLAAGLLALGLRPgDRVVV-QLPNVAEFVIVFFALFRAGA--I 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 556 PL---------DLDYPIDRMQ---MMCEDANPLFvlTTQALAQQLPQNIQQL-HL----DQEGVQ--TQIRKQDASDIPA 616
Cdd:COG1021 102 PVfalpahrraEISHFAEQSEavaYIIPDRHRGF--DYRALARELQAEVPSLrHVlvvgDAGEFTslDALLAAPADLSEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 617 ENrkfDFQDVAYVIFTSGSTGRPKGVMNTHGS-LLNLILS------HKPTIYWPVLEAVnerfpdrplraahtHSFSFdS 689
Cdd:COG1021 180 RP---DPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSVRASaeicglDADTVYLAALPAA--------------HNFPL-S 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 690 S--WLQVFW------MLwgqelhifdENMRRD-AFGLvqeIQQRQIDTLDLPPSFcAQMMTNglFVENQHH--PSL--IL 756
Cdd:COG1021 242 SpgVLGVLYaggtvvLA---------PDPSPDtAFPL---IERERVTVTALVPPL-ALLWLD--AAERSRYdlSSLrvLQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 757 IGGeaAPLAlwQQLNAQ--PAL--FAHNLYGPTE----YTvdtfraelkqtaRPviGNP---IGNTQAY---------VL 816
Cdd:COG1021 307 VGG--AKLS--PELARRvrPALgcTLQQVFGMAEglvnYT------------RL--DDPeevILTTQGRpispddevrIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 817 DRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIkIRGyrv 896
Cdd:COG1021 369 DEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG--- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 897 eiGE------VENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKDIELdekTSEQLsQQYLSQlrQNLPEYMVPS 965
Cdd:COG1021 439 --GEkiaaeeVENLLLAHPAVHDAAVVAMP----DEYLGerscaFVVPRGEPL---TLAEL-RRFLRE--RGLAAFKLPD 506
|
570 580
....*....|....*....|.
gi 490930577 966 ALTVMSEFPRNVSGKVDKKAL 986
Cdd:COG1021 507 RLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
483-920 |
1.39e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 82.34 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 483 VKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPL----- 557
Cdd:PRK06188 22 LKRYPDRPALVLGDT----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALhplgs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 558 --DLDYPID--RMQMMCEDANPlFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDF-QDVAYVIFT 632
Cdd:PRK06188 98 ldDHAYVLEdaGISTLIVDPAP-FVERALALLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALpPDIAGLAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 633 SGSTGRPKGVMNTHGSLLNLILSHKPTIYWPvleaVNERFpdrpLRAAhthSFSFDSSWLQVFWMLWGQELHI---FDEn 709
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWP----ADPRF----LMCT---PLSHAGGAFFLPTLLRGGTVIVlakFDP- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 710 mrrDAFglVQEIQQRQIDTLDLPPSfcaqmMTNGLFvenQHHPS---------LILIGGEA-APLALWQQLNAQPALFAH 779
Cdd:PRK06188 245 ---AEV--LRAIEEQRITATFLVPT-----MIYALL---DHPDLrtrdlssleTVYYGASPmSPVRLAEAIERFGPIFAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 780 nLYGPTE--YTVDTFRAELKQTARPVI----GNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:PRK06188 312 -YYGQTEapMVITYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 854 vANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:PRK06188 391 -RDGWLH------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVP 450
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1683-2003 |
1.40e-15 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 81.73 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1683 TSGTTGQPKGVMVSHQAI------VNRILWMQseyPLSATDTILqktpCTFDVSVWEFFWSYLVGAR----LVIaPIDAh 1752
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLdrwaelFARSLRAA---GVRPGDRVQ----NAFGYGLFTGGLGLHYGAErlgaTVI-PAGG- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 RDPLALLSLIQKYQVTTLHFVPSMLAVfenaateILSSAQRQ-----SLPICRVFCSGEALPTALAKSFTEHFSCELHNL 1827
Cdd:COG1541 162 GNTERQLRLMQDFGPTVLVGTPSYLLY-------LAEVAEEEgidprDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAAVDVSYMDATL-GLHpeescvaigypVWNTQLY--ILD-QYLRPVPVGVDGELYlaghqlamgylhradltasr 1903
Cdd:COG1541 235 YGLTEVGPGVAYECEAQdGLH-----------IWEDHFLveIIDpETGEPVPEGEEGELV-------------------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1904 fvanpFTAGQRM------YRTGDIARWHADGS--------IQYI-GRADDQLKIRGQRIELGEIEQQLRLISGLD----V 1964
Cdd:COG1541 284 -----VTTLTKEamplirYRTGDLTRLLPEPCpcgrthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpeyqI 358
|
330 340 350
....*....|....*....|....*....|....*....
gi 490930577 1965 VVhaissEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHL 2003
Cdd:COG1541 359 VV-----DREGGLDELTVRVELAPGASLEALAEAIAAAL 392
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
561-986 |
2.05e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 82.04 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 561 YPIDRmQMMCEDANPL---FVLTTQALAQQLPQNIQQLhLDQEGVQTQIRKQDASDipaenrkfdfqDVAYVIFTSGSTG 637
Cdd:PRK08008 120 YPMYR-QIQQEDATPLrhiCLTRVALPADDGVSSFTQL-KAQQPATLCYAPPLSTD-----------DTAEILFTSGTTS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 638 RPKGVMNTHGSLL----------NLilsHKPTIYWPVLEAVNERFPDRPLRAAhthsFSFDSSWLQV-------FWmlwg 700
Cdd:PRK08008 187 RPKGVVITHYNLRfagyysawqcAL---RDDDVYLTVMPAFHIDCQCTAAMAA----FSAGATFVLLekysaraFW---- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 701 qelhifdenmrrdafglvqeiqqRQIDTLDLPPSFCAQMMTNGLFV------ENQHHPSLILIG---GEAAPLALWQQLN 771
Cdd:PRK08008 256 -----------------------GQVCKYRATITECIPMMIRTLMVqppsanDRQHCLREVMFYlnlSDQEKDAFEERFG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 772 AQpaLFahNLYGPTEYTVDTFRAELKQTAR-PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF---GIANGYLGRAD 847
Cdd:PRK08008 313 VR--LL--TSYGMTETIVGIIGDRPGDKRRwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 848 LSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAepinnshrl 927
Cdd:PRK08008 389 ATAKVLEADGWLH------TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVG--------- 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 928 lgycvVKDIELDE--------KTSEQLSQ-QYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08008 454 -----IKDSIRDEaikafvvlNEGETLSEeEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
474-982 |
2.06e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 81.86 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 474 NVLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGAS 553
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDR----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 554 FLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQlpqnIQQLHLDQEGVQTQIRKQDASDIPAENRKFDFQDVA------ 627
Cdd:PRK07798 80 PVNVNYRYVEDELRYLLDDSDAVALVYEREFAPR----VAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALaagspe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 628 -----------YVIFTSGSTGRPKGVMNTHGSL-------LNLILSHKPTIYWPVLEAVNE-----RFPDRPLRAAHTHS 684
Cdd:PRK07798 156 rdfgerspddlYLLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGEPIEDEEELAKRAAAgpgmrRFPAPPLMHGAGQW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 685 FSFDSswlqvfwMLWGQELhIFDENMRRDAFGLVQEIQQRQ---------------IDTLDLPPSFCAqmmtnglfvenq 749
Cdd:PRK07798 236 AAFAA-------LFSGQTV-VLLPDVRFDADEVWRTIEREKvnvitivgdamarplLDALEARGPYDL------------ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 750 hhPSLILIGGEAAPL--ALWQQLNAQ-PALFAHNLYGPTE----YTVDTFRAELKqTARPVIgNPIGNTQayVLDRHLQR 822
Cdd:PRK07798 296 --SSLFAIASGGALFspSVKEALLELlPNVVLTDSIGSSEtgfgGSGTVAKGAVH-TGGPRF-TIGPRTV--VLDEDGNP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 823 CPTG--VIGELYISGFgIANGYLGRADLSAARF-VANpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIG 899
Cdd:PRK07798 370 VEPGsgEIGWIARRGH-IPLGYYKDPEKTAETFpTID----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 900 EVENALSILTNVESAVVIAEPinnSHRlLGYCVVKDIELDEKTSEQLsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSG 979
Cdd:PRK07798 445 EVEEALKAHPDVADALVVGVP---DER-WGQEVVAVVQLREGARPDL-AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAG 519
|
...
gi 490930577 980 KVD 982
Cdd:PRK07798 520 KAD 522
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
21-437 |
4.84e-15 |
|
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: 79.80 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 21 LASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYSSDPSQPFIEL-NNQVQFQIEEFD 99
Cdd:cd19536 4 LSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVvHRQAQVPVTELD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 100 FCHLTPKKAQQRLWdwmpSDRQCAKSLKAGETQLFRQVLF--TTHDKVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQE 177
Cdd:cd19536 84 LTPLEEQLDPLRAY----KEETKIRRFDLGRAPLVRAALVrkDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 178 GKDLSVSPFIGVNEVISERQAYENSHQfkiDQAFWKAYCEDLPSPislSTHHLAAKTTATFVKH-QLRFSTGILEQIQAL 256
Cdd:cd19536 160 YKPLSLPPAQPYRDFVAHERASIQQAA---SERYWREYLAGATLA---TLPALSEAVGGGPEQDsELLVSVPLPVRSRSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 257 AAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRL-GSKAIRSTL-PTVNVLPVKFKVAEkDSWVSLAQHVQEQLR 334
Cdd:cd19536 234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeETTGAERLLgLFLNTLPLRVTLSE-ETVEDLLKRAQEQEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 335 EIRPHQKYDaeqiLRDLNSIDIHERMYGPILNYKAFDQD----LVIDGEKVKTH--HISTGPIDDFEFSFIVQDHELIIE 408
Cdd:cd19536 313 ESLSHEQVP----LADIQRCSEGEPLFDSIVNFRHFDLDfglpEWGSDEGMRRGllFSEFKSNYDVNLSVLPKQDRLELK 388
|
410 420
....*....|....*....|....*....
gi 490930577 409 LRADSQRYTQDELfnhgQRLTLLLEQALI 437
Cdd:cd19536 389 LAYNSQVLDEEQA----QRLAAYYKSAIA 413
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
799-1075 |
5.71e-15 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 77.87 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 799 TARPVIGNPIGNTQAY-VLDRHLQRCPTGVIGElYISGFGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAG 877
Cdd:COG3433 13 PDEPPPVIPPAIVQARaLLLIVDLQGYFGGFGG-EGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 878 KLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAE--PINNSHRLLGYCVVKDIELDEKTSEQLSQQYLsqlr 955
Cdd:COG3433 92 GLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaaLRGAGVGLLLIVGAVAALDGLAAAAALAALDK---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 956 qnLPEYMVPSALTVMSEFPRNVSGKVDKKALPKPQIRAHSRMAETPE--------QQLLCQITASVLKL--DAIGIDDDF 1025
Cdd:COG3433 168 --VPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPApaletaltEEELRADVAELLGVdpEEIDPDDNL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490930577 1026 FMTGGDSISAIMLCTQLRQRGYSLRPSDVFQFKTVAAMAPQLTRLDEQQA 1075
Cdd:COG3433 246 FDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
484-981 |
6.87e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 80.39 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 484 KKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQ-ENGARK------------QTVIAG-AIPRSiDSVVVMLSVLN 549
Cdd:PRK08314 21 RRYPDKTAIVFYGR----AISYRELLEEAERLAGYLQqECGVRKgdrvllymqnspQFVIAYyAILRA-NAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 550 sgasfLPLDLDYPIdrmqmmcEDANPLFVLTTQALAQQLPQNIQQLHLDQ-------------------EGVQTQIRKQD 610
Cdd:PRK08314 96 -----REEELAHYV-------TDSGARVAIVGSELAPKVAPAVGNLRLRHvivaqysdylpaepeiavpAWLRAEPPLQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 611 -------------ASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYW------PVLEAVNER 671
Cdd:PRK08314 164 lapggvvawkealAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVG---SVLWsnstpeSVVLAVLPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 672 FpdrplraahtHSFSFDSSWLQVFWMlwGQELHI---FDenmrRDAFGlvQEIQQRQIDTLDLPPSFCAQMMTNGLFvEN 748
Cdd:PRK08314 241 F----------HVTGMVHSMNAPIYA--GATVVLmprWD----REAAA--RLIERYRVTHWTNIPTMVVDFLASPGL-AE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 749 QHHPSLILIGGEAAPL--ALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLD-RHLQRCPT 825
Cdd:PRK08314 302 RDLSSLRYIGGGGAAMpeAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 826 GVIGELYISGFGIANGYLGRADLSAARFVAnpFEhGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENAL 905
Cdd:PRK08314 382 GEVGEIVVHGPQVFKGYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLL 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 906 SILTNVESAVVIAEPinNSHR---LLGYCVVKDiELDEKTSEqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKV 981
Cdd:PRK08314 459 YKHPAIQEACVIATP--DPRRgetVKAVVVLRP-EARGKTTE---EEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1553-1967 |
7.65e-15 |
|
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: 79.95 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1553 DENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGaayLPIDLQHPTerikfmlqdakskl 1632
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAT-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 vIGEqkdlAAIVHPsiatfafnelFDETKVdlssykTTVIT---PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQS 1709
Cdd:cd17639 64 -LGE----DALIHS----------LNETEC------SAIFTdgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1710 EYP--LSATDTILQKTPCT----FDVSVWEFFWsylvGARLviapidAHRDPLALLSLIQK--------YQVTTLHFVPs 1775
Cdd:cd17639 123 RVPelLGPDDRYLAYLPLAhifeLAAENVCLYR----GGTI------GYGSPRTLTDKSKRgckgdlteFKPTLMVGVP- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1776 mlAVFENAATEILS-----SAQRQSL------------------PIC----------------RVFCSGEALPTALAKSF 1816
Cdd:cd17639 192 --AIWDTIRKGVLAklnpmGGLKRTLfwtayqsklkalkegpgtPLLdelvfkkvraalggrlRYMLSGGAPLSADTQEF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFSCELHNLYGPTE---AAVDVSYMDATLGlhpeescvAIGYPVWNTQLYILD------QYLRPVPvgvDGELYLAGH 1887
Cdd:cd17639 270 LNIVLCPVIQGYGLTEtcaGGTVQDPGDLETG--------RVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1888 QLAMGYLHRADLTASRFvanpftAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR-GQRIELGEIEQQLR---LISGLD 1963
Cdd:cd17639 339 NVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRsnpLVNNIC 412
|
....
gi 490930577 1964 VVVH 1967
Cdd:cd17639 413 VYAD 416
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
485-987 |
1.25e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 79.27 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 485 KYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPID 564
Cdd:PRK13383 47 RWPGRTAIIDDDGA----LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 565 RMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRkfdfqdvaYVIFTSGSTGRPKGVMN 644
Cdd:PRK13383 123 ALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGR--------IVLLTSGTTGKPKGVPR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 645 THGsllnliLSHKPTIYWPVLEAVNERFPDR-PLRAAHTHSFSFDSSWLQVfwMLWGQEL---HiFDENM--------RR 712
Cdd:PRK13383 195 APQ------LRSAVGVWVTILDRTRLRTGSRiSVAMPMFHGLGLGMLMLTI--ALGGTVLthrH-FDAEAalaqaslhRA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 713 DAFGLVQEIQQRqidTLDLPPSFCAQmmtNGLfvenqhhPSL--ILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVD 790
Cdd:PRK13383 266 DAFTAVPVVLAR---ILELPPRVRAR---NPL-------PQLrvVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 791 TFR--AELKQtARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGradlSAARFVANPfehgqrMYRTG 868
Cdd:PRK13383 333 ALAtpADLRD-APETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDG------MTSTG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 869 DLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVK---DIELDektse 944
Cdd:PRK13383 402 DMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERfGHRLAAFVVLHpgsGVDAA----- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 490930577 945 qlsqQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PRK13383 477 ----QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1558-1956 |
1.29e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 78.76 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 kdlaaivhpsiATFAfnelfdetkvdlssykttvitpQHPAYLIYTSGTTGQPKGVMVSHQAivnrilwmqseYPLSATD 1717
Cdd:cd05974 81 -----------NTHA----------------------DDPMLLYFTSGTTSKPKLVEHTHRS-----------YPVGHLS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1718 TI----LQKTPCTFDVS-------VWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFenaate 1786
Cdd:cd05974 117 TMywigLKPGDVHWNISspgwakhAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRML------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1787 ILSSAQRQSLPICRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVsymdatlGLHPEESCVA--IGYPVWNTQL 1864
Cdd:cd05974 191 IQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV-------GNSPGQPVKAgsMGRPLPGYRV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQYLRPVPvgvDGELYL---AGHQLAM--GYLHRADLTASrfvanpfTAGQRMYRTGDIARWHADGSIQYIGRADDQ 1939
Cdd:cd05974 264 ALLDPDGAPAT---EGEVALdlgDTRPVGLmkGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDV 333
|
410
....*....|....*..
gi 490930577 1940 LKIRGQRIELGEIEQQL 1956
Cdd:cd05974 334 FKSSDYRISPFELESVL 350
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
470-986 |
2.05e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 78.77 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 470 EQYNNVLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFL-QENGARKQTVIAGAIPRSIDSVVVMLSVL 548
Cdd:PRK08751 22 EQFRTVAEVFATSVAKFADRPAYHSFGKT----ITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 549 -----------------------NSGASFLPLdLDYPIDRMQMMCEDANPLFVLTTQ----------ALAQQLPQNIQQL 595
Cdd:PRK08751 98 ragltvvnvnplytprelkhqliDSGASVLVV-IDNFGTTVQQVIADTPVKQVITTGlgdmlgfpkaALVNFVVKYVKKL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 596 HLDQEgVQTQIRKQDASDIPAENR----KFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-NLILSHKPTIYWPVLEAVNE 670
Cdd:PRK08751 177 VPEYR-INGAIRFREALALGRKHSmptlQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQAHQWLAGTGKLEEGCE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 671 R-FPDRPLraahTHSFSFDSSWLqVFwMLWGQELHIFDENmrRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLFVENQ 749
Cdd:PRK08751 256 VvITALPL----YHIFALTANGL-VF-MKIGGCNHLISNP--RDMPGFVKELKKTR---------FTAFTGVNTLFNGLL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 750 HHP----------SLILIGGEAAPLAL---WQQLNAQPALFAhnlYGPTEYTVDTFRAELK-QTARPVIGNPIGNTQAYV 815
Cdd:PRK08751 319 NTPgfdqidfsslKMTLGGGMAVQRSVaerWKQVTGLTLVEA---YGLTETSPAACINPLTlKEYNGSIGLPIPSTDACI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 816 LDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYR 895
Cdd:PRK08751 396 KDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLH------TGDIARMDEQGFVYIVDRKKDMILVSGFN 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 896 VEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVV-KDIELdekTSEQLSqqylSQLRQNLPEYMVPSALTVMSEFP 974
Cdd:PRK08751 470 VYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVkKDPAL---TAEDVK----AHARANLTGYKQPRIIEFRKELP 542
|
570
....*....|..
gi 490930577 975 RNVSGKVDKKAL 986
Cdd:PRK08751 543 KTNVGKILRREL 554
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1537-2031 |
2.22e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 78.91 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PLN03102 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEqKDLAAIV--------------HPSI--------ATFAFNELFD--------ETKVDLSS 1666
Cdd:PLN03102 99 DATSIAAILRHAKPKILFVD-RSFEPLArevlhllssedsnlNLPVifiheidfPKRPSSEELDyecliqrgEPTPSLVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQ-----AIVNRILWMQSEYPLsatdtILQKTPcTFDVSVWEFFWSylVG 1741
Cdd:PLN03102 178 RMFRIQDEHDPISLNYTSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPV-----YLWTLP-MFHCNGWTFTWG--TA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1742 ARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSaqrQSLPIcRVFCSGEALPTALAKSfTEHFS 1821
Cdd:PLN03102 250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSP---RSGPV-HVLTGGSPPPAALVKK-VQRLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 CELHNLYGPTEAAVDV---SYMDATLGLhPEESCVAIGYPVWNTQLYILD------QYLRPVPVG--VDGELYLAGHQLA 1890
Cdd:PLN03102 325 FQVMHAYGLTEATGPVlfcEWQDEWNRL-PENQQMELKARQGVSILGLADvdvknkETQESVPRDgkTMGEIVIKGSSIM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1891 MGYLHRADLTASRFvanpftaGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR-----LISGLDVV 1965
Cdd:PLN03102 404 KGYLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYkypkvLETAVVAM 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1966 VHAISSEQNKANVQLVAYlQTTAPVDIDQL---KKQLAKH----LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN03102 477 PHPTWGETPCAFVVLEKG-ETTKEDRVDKLvtrERDLIEYcrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1570-2035 |
2.32e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 78.38 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAI-----V 1644
Cdd:PRK07514 41 LANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLskiaaA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1645 HPSIATFAFNE-----LFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTI 1719
Cdd:PRK07514 121 AGAPHVETLDAdgtgsLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1720 LQKTP------------CTFdvsvweffwsyLVGARLVIAPidaHRDPLALLSLIQkyQVTTLHFVPSMLavfenaaTEI 1787
Cdd:PRK07514 201 IHALPifhthglfvatnVAL-----------LAGASMIFLP---KFDPDAVLALMP--RATVMMGVPTFY-------TRL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1788 LSSAQ--RQSLPICRVFCSGEAlPTaLAKSFTEHFSCELHNL---YGPTEAAVDVSymdatlglHP---EESCVAIGYPV 1859
Cdd:PRK07514 258 LQEPRltREAAAHMRLFISGSA-PL-LAETHREFQERTGHAIlerYGMTETNMNTS--------NPydgERRAGTVGFPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1860 WNTQLYILDQYL-RPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADD 1938
Cdd:PRK07514 328 PGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYVHIVGRGKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1939 qLKIRGqrielG------EIEQqlrLISGLDVVV--------HAISSEQnkanVQLVAYLQTTAPVD----IDQLKKQLA 2000
Cdd:PRK07514 402 -LIISG-----GynvypkEVEG---EIDELPGVVesavigvpHPDFGEG----VTAVVVPKPGAALDeaaiLAALKGRLA 468
|
490 500 510
....*....|....*....|....*....|....*
gi 490930577 2001 KhlpaYMVPTHYMLVEQFPLSHNGKLDRKALPQPH 2035
Cdd:PRK07514 469 R----FKQPKRVFFVDELPRNTMGKVQKNLLREQY 499
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1556-1953 |
2.48e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 78.59 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQ-HPtERIKFMLQDAKSKLVI 1634
Cdd:PRK07008 38 HRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFP-EQIAYIVNHAEDRYVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1635 GEQKDLAAI--VHPSIATF-AFNELFDETK-----VDLSSYKTtVITPQHPAY------------LIYTSGTTGQPKGVM 1694
Cdd:PRK07008 117 FDLTFLPLVdaLAPQCPNVkGWVAMTDAAHlpagsTPLLCYET-LVGAQDGDYdwprfdenqassLCYTSGTTGNPKGAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQAIVnrILWMQSEYP----LSATDTILQKTPcTFDVSVWEFFWSY-LVGARLVI-APidaHRDPLALLSLIQKYQVT 1768
Cdd:PRK07008 196 YSHRSTV--LHAYGAALPdamgLSARDAVLPVVP-MFHVNAWGLPYSApLTGAKLVLpGP---DLDGKSLYELIEAERVT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1769 TLHFVPS---MLAVFENAATEILSSAQrqslpicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAA---VDVSYMDA 1842
Cdd:PRK07008 270 FSAGVPTvwlGLLNHMREAGLRFSTLR-------RTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKWK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1843 TLGLhPEESCVAI----GYPVWNTQLYILDQYLRPVPV-GVD-GELYLAGHQLAMGYLhRADltasrfvANPFTAGqrMY 1916
Cdd:PRK07008 343 HSQL-PLDEQRKLlekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYF-RGD-------ASPLVDG--WF 411
|
410 420 430
....*....|....*....|....*....|....*..
gi 490930577 1917 RTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:PRK07008 412 PTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIE 448
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
624-988 |
2.66e-14 |
|
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: 78.28 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 624 QDVAYVIFTSGSTGRPKGVMNTHGSL-LNLILSHKptiYWpvleavnerfpdRPLRAAHTHSFSFDSSWLQVFWML---- 698
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGR---YW------------LDLTASDIMWNTSDTGWIKSAWSSlfep 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 699 WGQELHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPS----FCAQMMTNGLFVENQHhpslILIGGEAAPLALWQQLNAQ 773
Cdd:cd05928 239 WIQGACVFVHHLPRfDPLVILKTLSSYPITTFCGAPTvyrmLVQQDLSSYKFPSLQH----CVTGGEPLNPEVLEKWKAQ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 774 PALFAHNLYGPTEyTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYIS-----GFGIANGYLGRAD 847
Cdd:cd05928 315 TGLDIYEGYGQTE-TGLICANFKGMKIKPgSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 848 LSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIA-EPINNsh 925
Cdd:cd05928 394 KTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVvESAVVSSpDPIRG-- 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 926 RLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05928 465 EVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
487-986 |
2.82e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 78.54 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIV-SGerpnlQHLSFAELAvkvNQLTRF---LQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDldyP 562
Cdd:PRK06178 47 PQRPAIIfYG-----HVITYAELD---ELSDRFaalLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS---P 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 563 IDR-MQMMCE--DANPLFVLTTQALAQ-----------------------------QLPQNIQQLHLDQEGVQTQIRKQD 610
Cdd:PRK06178 116 LFReHELSYElnDAGAEVLLALDQLAPvveqvraetslrhvivtsladvlpaeptlPLPDSLRAPRLAAAGAIDLLPALR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 611 ASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiYWPVleAVNERFPDRPLraahthsfsfdsS 690
Cdd:PRK06178 196 ACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAA-----AYAV--AVVGGEDSVFL------------S 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 691 WLQVFWmlwgqelhIFDENM----------------RRDAFGLVQEIQQRQIDTLdlppsfcaqMMTNGLFVENQHHP-- 752
Cdd:PRK06178 257 FLPEFW--------IAGENFgllfplfsgatlvllaRWDAVAFMAAVERYRVTRT---------VMLVDNAVELMDHPrf 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 753 ------SLILIGGEAAPLAL-------WQQLNAqpALFAHNLYGPTE-YTVDTFRAELkQT------ARPV-IGNPIGNT 811
Cdd:PRK06178 320 aeydlsSLRQVRVVSFVKKLnpdyrqrWRALTG--SVLAEAAWGMTEtHTCDTFTAGF-QDddfdllSQPVfVGLPVPGT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 812 QAYVLDRHLQR-CPTGVIGELYISGFGIANGYLGRADLSAARFVANpfehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIK 890
Cdd:PRK06178 397 EFKICDFETGElLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 891 IRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELdeKTSEQLSQQYLSQ-LRQNLPEYMVPSaLTV 969
Cdd:PRK06178 470 VNGMSVFPSEVEALLGQHPAVLGSAVVGRP----DPDKGQVPVAFVQL--KPGADLTAAALQAwCRENMAVYKVPE-IRI 542
|
570
....*....|....*..
gi 490930577 970 MSEFPRNVSGKVDKKAL 986
Cdd:PRK06178 543 VDALPMTATGKVRKQDL 559
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1557-2048 |
2.86e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 78.51 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLqhPT---------ERIKFMLQD 1627
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPL--PMgfggresyiAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1628 AKSKLVIG--EQKD-LAAIVHPSIATFAF-NELFD---ETKVDLSsykttVITPQHPAYLIYTSGTTGQPKGVMVSHQAI 1700
Cdd:PRK09192 127 AQPAAIITpdELLPwVNEATHGNPLLHVLsHAWFKalpEADVALP-----RPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRilwmqseypLSA-TDTILQKTPCTFDVSvWEFFwsY----LVGarLVIAPI------------DAHRDPLALLSLIQ 1763
Cdd:PRK09192 202 MAN---------LRAiSHDGLKVRPGDRCVS-WLPF--YhdmgLVG--FLLTPVatqlsvdylptrDFARRPLQWLDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1764 KYQvTTLHFVPSMlaVFENAATEIlSSAQRQSLPICR---VFCSGEALPTALAKSFTEHFS-----------CelhnlYG 1829
Cdd:PRK09192 268 RNR-GTISYSPPF--GYELCARRV-NSKDLAELDLSCwrvAGIGADMIRPDVLHQFAEAFApagfddkafmpS-----YG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1830 PTEAAVDVSYMDATLGLHPEE-----------------------SCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAG 1886
Cdd:PRK09192 339 LAEATLAVSFSPLGSGIVVEEvdrdrleyqgkavapgaetrrvrTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1887 HQLAMGYLHRADLTASRFVANpftagqrMYRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEIE----QQLRLISGl 1962
Cdd:PRK09192 419 PSLMSGYFRDEESQDVLAADG-------WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEwiaeQEPELRSG- 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1963 DVVVHAISSEQNKANVQLVaYLQTTAPVDIDQLKKQLAKHLPAY--------MVPTHYMlveqfPLSHNGKLDRKALPQP 2034
Cdd:PRK09192 490 DAAAFSIAQENGEKIVLLV-QCRISDEERRGQLIHALAALVRSEfgveaaveLVPPHSL-----PRTSSGKLSRAKAKKR 563
|
570
....*....|....
gi 490930577 2035 HLTPSNTEKQYATS 2048
Cdd:PRK09192 564 YLSGAFASLDVAAS 577
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
578-988 |
2.96e-14 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 78.09 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 578 VLTTQALAQQL-PQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDfqDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSh 656
Cdd:cd05906 122 VLTDAELVAEFaGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 657 kptiywpvLEAVNERFPDR------PLRAA----HTHSFSFDsswlqvfwmLWGQELHIFDENMRRDAFGLVQEIQQRQI 726
Cdd:cd05906 199 --------KIQHNGLTPQDvflnwvPLDHVgglvELHLRAVY---------LGCQQVHVPTEEILADPLRWLDLIDRYRV 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 727 dTLDLPPSFCAQMMTNGLFVENQHHPSL-----ILIGGEA-------APLALWQQLNAQPALFaHNLYGPTE------YT 788
Cdd:cd05906 262 -TITWAPNFAFALLNDLLEEIEDGTWDLsslryLVNAGEAvvaktirRLLRLLEPYGLPPDAI-RPAFGMTEtcsgviYS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 789 VDTFRAELKQTARPV-IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRT 867
Cdd:cd05906 340 RSFPTYDHSQALEFVsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 868 GDLVrWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAepinNSHRLLG-----YCV--VKDIELDE 940
Cdd:cd05906 414 GDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAA----FAVRDPGaeteeLAIffVPEYDLQD 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 490930577 941 KTSEQLS--QQYLSQLRQNLPEYMVPSAltvMSEFPRNVSGKVDKKALPK 988
Cdd:cd05906 489 ALSETLRaiRSVVSREVGVSPAYLIPLP---KEEIPKTSLGKIQRSKLKA 535
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1557-2031 |
3.45e-14 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 78.40 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI-- 1634
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVItc 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1635 -GEQKDLAAIVHPSIATFAFNELFDE-TKVDL-----------------------------SSYKTTV----ITPQHPAY 1679
Cdd:PLN02654 200 nAVKRGPKTINLKDIVDAALDESAKNgVSVGIcltyenqlamkredtkwqegrdvwwqdvvPNYPTKCevewVDAEDPLF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVM-VSHQAIVNRILWMQSEYPLSATDTILqktpCTFDVSvWEFFWSY------LVGARLVI---APi 1749
Cdd:PLN02654 280 LLYTSGSTGKPKGVLhTTGGYMVYTATTFKYAFDYKPTDVYW----CTADCG-WITGHSYvtygpmLNGATVLVfegAP- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1750 dAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpicRVFCS-GEAL-PTALAKSF--TEHFSCELH 1825
Cdd:PLN02654 354 -NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSL---RVLGSvGEPInPSAWRWFFnvVGDSRCPIS 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTEAAvdvSYMDATL-GLHPEESCVAIgYPVWNTQLYILDQYlrpvPVGVDGEL--YLAGHQLAMGYLHRADLTAS 1902
Cdd:PLN02654 430 DTWWQTETG---GFMITPLpGAWPQKPGSAT-FPFFGVQPVIVDEK----GKEIEGECsgYLCVKKSWPGAFRTLYGDHE 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1903 RFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRL--------ISGLDvvvHAISSEQN 1974
Cdd:PLN02654 502 RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVShpqcaeaaVVGIE---HEVKGQGI 578
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1975 KANVQLVAYLQTTapvdiDQLKKQLA----KHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PLN02654 579 YAFVTLVEGVPYS-----EELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
625-986 |
4.05e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 77.88 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVNERFPdrPLRAAHTHSFSFDSswlqVFWMLWGQElH 704
Cdd:PRK05677 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIA--PLPLYHIYAFTFHC----MAMMLIGNH-N 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 705 IFDENmRRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLFVENQHHPS----------LILIGGEAAPLA---LWQQLN 771
Cdd:PRK05677 281 ILISN-PRDLPAMVKELGKWK---------FSGFVGLNTLFVALCNNEAfrkldfsalkLTLSGGMALQLAtaeRWKEVT 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 772 AQPALFAhnlYGPTE----YTVDTFRAELKQTarpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRAD 847
Cdd:PRK05677 351 GCAICEG---YGMTEtspvVSVNPSQAIQVGT----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 848 LSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRL 927
Cdd:PRK05677 424 ATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 928 LGYCVVKdieldeKTSEQLS-QQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK05677 498 IKVFVVV------KPGETLTkEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
486-986 |
6.57e-14 |
|
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: 76.90 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 486 YPERTaIVSGERPNLQH-LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPID 564
Cdd:cd12119 9 HGDRE-IVSRTHEGEVHrYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 565 RMQMMCEDA-------NPLFVLTTQALAQQLP--QNIQQLHLDQEGVQTQIRKQDASD--IPAENRKFDFQDV----AYV 629
Cdd:cd12119 88 QIAYIINHAedrvvfvDRDFLPLLEAIAPRLPtvEHVVVMTDDAAMPEPAGVGVLAYEelLAAESPEYDWPDFdentAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 630 I-FTSGSTGRPKGVMNTHGSLL--NLILSHKPTIYWPVLEAVnerFPDRPLRAAHTHSFSFDSSWLQVFWMLWGQELhif 706
Cdd:cd12119 168 IcYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVV---LPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYL--- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 707 denmrrDAFGLVQEIQQRQidtldlpPSFCA------QMMTNGLFVENQHHPSL--ILIGGEAAPLALWQQLNAQPALFA 778
Cdd:cd12119 242 ------DPASLAELIEREG-------VTFAAgvptvwQGLLDHLEANGRDLSSLrrVVIGGSAVPRSLIEAFEERGVRVI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 779 HnLYGPTEY----TVDTFRAEL-------KQTARPVIGNPIGNTQAYVLDRHLQRCP-TGV-IGELYISGFGIANGYLgR 845
Cdd:cd12119 309 H-AWGMTETsplgTVARPPSEHsnlsedeQLALRAKQGRPVPGVELRIVDDDGRELPwDGKaVGELQVRGPWVTKSYY-K 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 846 ADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsH 925
Cdd:cd12119 387 NDEESEALTEDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVP----H 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 926 -----RLLGYCVVKDIEldEKTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd12119 457 pkwgeRPLAVVVLKEGA--TVTAEEL----LEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1540-2009 |
1.03e-13 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 76.84 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1540 EQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTE 1619
Cdd:PRK08279 45 EAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1620 RIKFMLQDAKSKLVIGEQKDLAAI--------VHPSIATFAFNELFD-ETKVDLSSYKTTV----------ITPQHPAYL 1680
Cdd:PRK08279 125 VLAHSLNLVDAKHLIVGEELVEAFeearadlaRPPRLWVAGGDTLDDpEGYEDLAAAAAGApttnpasrsgVTAKDTAFY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1681 IYTSGTTGQPKGVMVSHqaivNRIL----WMQSEYPLSATDTILQKTPC---TFDVSVWEffwSYLV-GARLVIAP-IDA 1751
Cdd:PRK08279 205 IYTSGTTGLPKAAVMSH----MRWLkamgGFGGLLRLTPDDVLYCCLPLyhnTGGTVAWS---SVLAaGATLALRRkFSA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1752 HR---DplallslIQKYQVTTLHFVPSMLAVFENAATEILSSAQRqslpiCRVFCsGEALPTALAKSFTEHFS----CEl 1824
Cdd:PRK08279 278 SRfwdD-------VRRYRATAFQYIGELCRYLLNQPPKPTDRDHR-----LRLMI-GNGLRPDIWDEFQQRFGipriLE- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1825 hnLYGPTEAAV---DVSYMDATLGLHP--EESCVAI-------GYPVWNTqlyilDQYLRPVPVGVDGELylaghqLAM- 1891
Cdd:PRK08279 344 --FYAASEGNVgfiNVFNFDGTVGRVPlwLAHPYAIvkydvdtGEPVRDA-----DGRCIKVKPGEVGLL------IGRi 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 -------GYLHRADlTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-D 1963
Cdd:PRK08279 411 tdrgpfdGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVeE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 490930577 1964 VVVHAISSEQNKANVQLVAY-LQTTAPVDIDQLKKQLAKHLPAYMVP 2009
Cdd:PRK08279 490 AVVYGVEVPGTDGRAGMAAIvLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
467-992 |
1.34e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 76.23 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 467 SHPEQYNNVLDIFYEQVKKYPERTAIVSGERPNLQHL----SFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVV 542
Cdd:PRK06710 10 SYPEEIPSTISYDIQPLHKYVEQMASRYPEKKALHFLgkdiTFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 543 VMLSVL-----------------------NSGAS-FLPLDLDYP---------------IDRMQMMCEDANPLFVLTTQA 583
Cdd:PRK06710 90 GYYGTLlaggivvqtnplytereleyqlhDSGAKvILCLDLVFPrvtnvqsatkiehviVTRIADFLPFPKNLLYPFVQK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 584 LAQQLPQNIQQLHLDQEGVQTQIRKQDASDIPAENRkfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkpTIYWP 663
Cdd:PRK06710 170 KQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPE----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLM---GVQWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 664 VLEAVNERFPDRPLRAAHTHSFS--FDSSWLQVFWMLWgqeLHIFDENMrrdafgLVQEIQQRQIDTLDLPPSFCAQMMT 741
Cdd:PRK06710 243 YNCKEGEEVVLGVLPFFHVYGMTavMNLSIMQGYKMVL---IPKFDMKM------VFEAIKKHKVTLFPGAPTIYIALLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 742 NGLFVENQHHPSLILIGGEAA-PLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRH 819
Cdd:PRK06710 314 SPLLKEYDISSIRACISGSAPlPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPgSIGVPWPDTEAMIMSLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 820 L-QRCPTGVIGELYISGFGIANGYLGRADLSAArFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:PRK06710 394 TgEALPPGEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGWLH------TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 899 GEVENALSILTNVESAVVIAEPinNSHR---LLGYCVVKDielDEKTSEQLSQQYLsqlRQNLPEYMVPSALTVMSEFPR 975
Cdd:PRK06710 467 REVEEVLYEHEKVQEVVTIGVP--DPYRgetVKAFVVLKE---GTECSEEELNQFA---RKYLAAYKVPKVYEFRDELPK 538
|
570
....*....|....*..
gi 490930577 976 NVSGKVDKKALPKPQIR 992
Cdd:PRK06710 539 TTVGKILRRVLIEEEKR 555
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1550-2031 |
1.48e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 76.01 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1550 ALSDENHQLSFSEVRLQVCALAQQLQR-AGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDA 1628
Cdd:PRK12492 42 AFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1629 KSKLVI-----GE--QKDLA--AIVH----------PSIATFAFNELFDETKVDLSSY--------------------KT 1669
Cdd:PRK12492 122 GARALVylnmfGKlvQEVLPdtGIEYlieakmgdllPAAKGWLVNTVVDKVKKMVPAYhlpqavpfkqalrqgrglslKP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1670 TVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDtilqktpctfDVSVWEffwsylVGARLVIAP- 1748
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPD----------GQPLMK------EGQEVMIAPl 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 ------------------------IDAHRDPLALLSLIQKYQVTTLHFVPSM-LAVFENAATEILSSAQRQSlpicrVFC 1803
Cdd:PRK12492 266 plyhiyaftancmcmmvsgnhnvlITNPRDIPGFIKELGKWRFSALLGLNTLfVALMDHPGFKDLDFSALKL-----TNS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVS---YMD-ATLGlhpeescvAIGYPVWNTQLYILDQYLRPVPVGVD 1879
Cdd:PRK12492 341 GGTALVKATAERWEQLTGCTIVEGYGLTETSPVAStnpYGElARLG--------TVGIPVPGTALKVIDDDGNELPLGER 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1880 GELYLAGHQLAMGYLHRADLTASRFVAnpftagQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEqqlrli 1959
Cdd:PRK12492 413 GELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE------ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1960 sglDVVV-H---------AISSEQNKANVQLVAYLQTTApVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRK 2029
Cdd:PRK12492 481 ---DVVMaHpkvancaaiGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRR 556
|
..
gi 490930577 2030 AL 2031
Cdd:PRK12492 557 EL 558
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1579-2031 |
1.63e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.07 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1579 VQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDA-KSKLVIGE------QKDLAAIVHPSIATF 1651
Cdd:PRK08751 73 LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSgASVLVVIDnfgttvQQVIADTPVKQVITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1652 AFNELFDETKVDLSSY----------------------------KTTV----ITPQHPAYLIYTSGTTGQPKGVMVSHQA 1699
Cdd:PRK08751 153 GLGDMLGFPKAALVNFvvkyvkklvpeyringairfrealalgrKHSMptlqIEPDDIAFLQYTGGTTGVAKGAMLTHRN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1700 IVNRIL----WMQSEYPL-SATDTILQKTPctfdvsVWEFFwsYLVGARLVIAPIDA--H-----RDPLALLSLIQKYQV 1767
Cdd:PRK08751 233 LVANMQqahqWLAGTGKLeEGCEVVITALP------LYHIF--ALTANGLVFMKIGGcnHlisnpRDMPGFVKELKKTRF 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1768 TTLHFVPSMLAVFENaaTEILSSAQRQSLPIcrVFCSGEALPTALAKSFTEHFSCELHNLYGPTEAAVDVSYMDATLglh 1847
Cdd:PRK08751 305 TAFTGVNTLFNGLLN--TPGFDQIDFSSLKM--TLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTL--- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1848 pEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHAD 1927
Cdd:PRK08751 378 -KEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQ 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1928 GSIQYIGRADDQLKIRGQRIELGEIEQQLRLISG-LDVVVHAISSEQNKANVQLVAYLQTTApVDIDQLKKQLAKHLPAY 2006
Cdd:PRK08751 451 GFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGvLEVAAVGVPDEKSGEIVKVVIVKKDPA-LTAEDVKAHARANLTGY 529
|
490 500
....*....|....*....|....*
gi 490930577 2007 MVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK08751 530 KQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1671-2031 |
2.06e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 75.49 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFF--------WSYLVGA 1742
Cdd:PRK07867 148 VADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMP---------LFhsnavmagWAVALAA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1743 RLVIApIDAHRDPLALLSLIQKYQVTTLHFVPSMLAVfenaateILSSAQR---QSLPIcRVFCSGEALPTALAKsFTEH 1819
Cdd:PRK07867 219 GASIA-LRRKFSASGFLPDVRRYGATYANYVGKPLSY-------VLATPERpddADNPL-RIVYGNEGAPGDIAR-FARR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1820 FSCELHNLYGPTEAAVDVSYMDATlglhPEEscvAIGYPVWNTQlyILD-QYLRPVPVGVD------------GELY-LA 1885
Cdd:PRK07867 289 FGCVVVDGFGSTEGGVAITRTPDT----PPG---ALGPLPPGVA--IVDpDTGTECPPAEDadgrllnadeaiGELVnTA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1886 GHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DV 1964
Cdd:PRK07867 360 GPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAtEV 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1965 VVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKH--LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07867 433 AVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1566-1935 |
2.34e-13 |
|
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: 75.33 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1566 QVCALAQQLQRAGVQAG------DIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIgeqkd 1639
Cdd:cd05927 10 EVAERADNIGSALRSLGgkpapaSFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1640 laaiVHPSIATFAFNELFDETKVDLssYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIlwmqseyplSATDTI 1719
Cdd:cd05927 85 ----CDAGVKVYSLEEFEKLGKKNK--VPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNV---------AGVFKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1720 LQKTPC--TFDVSVweffwSYLVGA----RLVIAPIDAH--------RDPLALLSLIQKYQVTTLHFVPSML-----AVF 1780
Cdd:cd05927 150 LEILNKinPTDVYI-----SYLPLAhifeRVVEALFLYHgakigfysGDIRLLLDDIKALKPTVFPGVPRVLnriydKIF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 E-------------NAATEI----LSSAQRQSLPI----------------CRVFCSGEALPTALAKSFTEH-FSCELHN 1826
Cdd:cd05927 225 NkvqakgplkrklfNFALNYklaeLRSGVVRASPFwdklvfnkikqalggnVRLMLTGSAPLSPEVLEFLRVaLGCPVLE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1827 LYGPTE--AAVDVSYMDATLGLHpeescvaIGYPVWNTQLYILD----QYLRPVPVGvDGELYLAGHQLAMGYLHRADLT 1900
Cdd:cd05927 305 GYGQTEctAGATLTLPGDTSVGH-------VGGPLPCAEVKLVDvpemNYDAKDPNP-RGEVCIRGPNVFSGYYKDPEKT 376
|
410 420 430
....*....|....*....|....*....|....*
gi 490930577 1901 ASRFVANPFtagqrmYRTGDIARWHADGSIQYIGR 1935
Cdd:cd05927 377 AEALDEDGW------LHTGDIGEWLPNGTLKIIDR 405
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1128-1383 |
2.40e-13 |
|
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: 74.53 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1128 LSLNGDIDPVRLQQALITVLKRHPQLGGHFdSELAEEPVFIYSLHPTQawpVQFCSVTpDLLEQtiqealqqpihLDQPY 1207
Cdd:cd19537 30 CRLSGDVDRDRLASAWNTVLARHRILRSRY-VPRDGGLRRSYSSSPPR---VQRVDTL-DVWKE-----------INRPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1208 GLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQtNQQLPVLEHSYETVIKALSGRDHETSkvIWQRDLA 1287
Cdd:cd19537 94 DLEREDPIRVFISPDTLLVVMSHIICDLTTLQLLLREVSAAYNG-KLLPPVRREYLDSTAWSRPASPEDLD--FWSEYLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1288 DLQPLILFNQ-AQQAVQETS--YRLSAELGAKLQHKLRQQGITLNvfmQMIWA---MTLNIYAHREDIVFGTPVSGRSAP 1361
Cdd:cd19537 171 GLPLLNLPRRtSSKSYRGTSrvFQLPGSLYRSLLQFSTSSGITLH---QLALAavaLALQDLSDRTDIVLGAPYLNRTSE 247
|
250 260
....*....|....*....|..
gi 490930577 1362 inGLEQQIGLFLNTIPVRVKLN 1383
Cdd:cd19537 248 --EDMETVGLFLEPLPIRIRFP 267
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1542-1953 |
2.46e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.42 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPE--QTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPidLQHPTE 1619
Cdd:PRK07768 12 ARTSPRgmVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTM--LHQPTP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1620 RIKFML--QDAKSKL--------VIGEQKDLAAIV--HPSIATFAFNELFDETKVDlssykTTVITPQHPAYLIYTSGTT 1687
Cdd:PRK07768 90 RTDLAVwaEDTLRVIgmigakavVVGEPFLAAAPVleEKGIRVLTVADLLAADPID-----PVETGEDDLALMQLTSGST 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1688 GQPKGVMVSHQAIVNRILWMQSEYPLSA-TDTILQKTPCTFDVSVWEFFWSYL-VGARLV-IAPIDAHRDPLALLSLIQK 1764
Cdd:PRK07768 165 GSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPMyFGAELVkVTPMDFLRDPLLWAELISK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1765 YQVTTL---HFVPSMLA-VFENAATEI---LSSaqrqslpiCRVFCSG---------EALPTAlAKSFTEHFSCELhNLY 1828
Cdd:PRK07768 245 YRGTMTaapNFAYALLArRLRRQAKPGafdLSS--------LRFALNGaepidpadvEDLLDA-GARFGLRPEAIL-PAY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEAAVDVSYMDATLGLHPEESC---------------------VAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGH 1887
Cdd:PRK07768 315 GMAEATLAVSFSPCGAGLVVDEVDadllaalrravpatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1888 QLAMGYlhradLTASRFVanPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:PRK07768 395 SVTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1674-2033 |
3.37e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 74.83 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWS--------YLVGARLV 1745
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLApliagmnqYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1746 IapidahRDPLALLSLIQKYQVTTL---HFVPSMLAVFENAATeilssAQRQSLPICRVFCSG-EALPTALAKSFTEHFS 1821
Cdd:cd05908 185 I------RRPILWLKKASEHKATIVsspNFGYKYFLKTLKPEK-----ANDWDLSSIRMILNGaEPIDYELCHEFLDHMS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1822 C------ELHNLYGPTEAAVDVSYMDA-----TLGLH--------PEE----------SCVAIGYPVWNTQLYILDQYLR 1872
Cdd:cd05908 254 KyglkrnAILPVYGLAEASVGASLPKAqspfkTITLGrrhvthgePEPevdkkdseclTFVEVGKPIDETDIRICDEDNK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1873 PVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFTagqrmyRTGDIArWHADGSIQYIGRADDQLKIRGQRIELGEI 1952
Cdd:cd05908 334 ILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDI 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1953 EQQLRLISGLD---VVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAY-------MVPthymlVEQFPLSH 2022
Cdd:cd05908 407 ERIAEELEGVElgrVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRggwqineVLP-----IRRIPKTT 481
|
410
....*....|.
gi 490930577 2023 NGKLDRKALPQ 2033
Cdd:cd05908 482 SGKVKRYELAQ 492
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1532-2033 |
4.36e-13 |
|
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: 74.49 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1532 STLQQLLREQARItPEQTALSDENH--QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAY 1609
Cdd:cd17642 18 EQLHKAMKRYASV-PGTIAFTDAHTgvNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1610 LPIDLQHPTERIKFMLQDAKSKLVIGEQKDLAAIVH-PSIATFAFNELFDETKVDLSSYKT--TVITPQHP--------- 1677
Cdd:cd17642 97 APTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNvQKKLKIIKTIIILDSKEDYKGYQClyTFITQNLPpgfneydfk 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 ----------AYLIYTSGTTGQPKGVMVSHQAIVNRIlwmqseypLSATDTIL--QKTPCTFDVSVWEFFWSY------- 1738
Cdd:cd17642 177 ppsfdrdeqvALIMNSSGSTGLPKGVQLTHKNIVARF--------SHARDPIFgnQIIPDTAILTVIPFHHGFgmfttlg 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1739 --LVGARLVIAPidaHRDPLALLSLIQKYQVTTLHFVPSMLAVFenAATEILSSAQRQSLPIcrVFCSGEALPTALAKSF 1816
Cdd:cd17642 249 ylICGFRVVLMY---KFEEELFLRSLQDYKVQSALLVPTLFAFF--AKSTLVDKYDLSNLHE--IASGGAPLSKEVGEAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1817 TEHFSCE-LHNLYGPTEAAVDVSymdatlgLHPEESCV--AIGYPVWNTQLYILDQYLRPVpVGVD--GELYLAGHQLAM 1891
Cdd:cd17642 322 AKRFKLPgIRQGYGLTETTSAIL-------ITPEGDDKpgAVGKVVPFFYAKVVDLDTGKT-LGPNerGELCVKGPMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQ-QLRLISGLDVVVHAI- 1969
Cdd:cd17642 394 GYVNNPEATKALIDKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESiLLQHPKIFDAGVAGIp 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1970 ---SSEQNKANVQLVAYLQTTAPVDIDQLKKQL--AKHLPAYMVpthymLVEQFPLSHNGKLDRKALPQ 2033
Cdd:cd17642 468 dedAGELPAAVVVLEAGKTMTEKEVMDYVASQVstAKRLRGGVK-----FVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1672-2031 |
6.76e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 73.91 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1672 ITPQHPAYLIYTSGTTGQPKGVMVSHqAIVNRILWMQSE-YPLSATDTILQKTPcTFDVSVWEFFWSYLV--GARLVIAP 1748
Cdd:PRK13388 147 VDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFAGRALTErFGLTRDDVCYVSMP-LFHSNAVMAGWAPAVasGAAVALPA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 -IDAHRdplaLLSLIQKYQVTTLHFVPSMLAVfenaateILSSAQR---QSLPICRVFcSGEALPTALAKsFTEHFSCEL 1824
Cdd:PRK13388 225 kFSASG----FLDDVRRYGATYFNYVGKPLAY-------ILATPERpddADNPLRVAF-GNEASPRDIAE-FSRRFGCQV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1825 HNLYGPTEAAVDVSYMDATlglhPEEScvaIGYPVWNTQLYILDQyLRPVPVGV-D------------GELY-LAGHQLA 1890
Cdd:PRK13388 292 EDGYGSSEGAVIVVREPGT----PPGS---IGRGAPGVAIYNPET-LTECAVARfDahgallnadeaiGELVnTAGAGFF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1891 MGYLHRADLTASRFvanpftagqR--MYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVVH 1967
Cdd:PRK13388 364 EGYYNNPEATAERM---------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILlRHPAINRVAVY 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1968 AISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKH--LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK13388 435 AVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1533-1923 |
7.04e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.93 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1533 TLQQLLREQARITPEQTALSDEN------HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAG 1606
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1607 AAYLPID-----LQHPTERIKFMLQDAKSKLVIGEQ-----KDLAA-------IVHPS-----IATFAFNELFDETKVDL 1664
Cdd:PRK12582 130 VPAAPVSpayslMSHDHAKLKHLFDLVKPRVVFAQSgapfaRALAAldlldvtVVHVTgpgegIASIAFADLAATPPTAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1665 SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTIlqktPCTFDvsvWeFFWSYLVGARL 1744
Cdd:PRK12582 210 VAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP----PVSLD---W-MPWNHTMGGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1745 VIAP---------IDAHRdPLAllSLIQKyQVTTLHFV-PSmlaVFEN--AATEILSSAQRQSLPICRVFCS-------- 1804
Cdd:PRK12582 282 NFNGllwgggtlyIDDGK-PLP--GMFEE-TIRNLREIsPT---VYGNvpAGYAMLAEAMEKDDALRRSFFKnlrlmayg 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1805 GEALPT-------ALAKSFTEHfSCELHNLYGPTEAAvdvsymDATLGLH-PEESCVAIGYPVWNTQLYIldqylrpVPV 1876
Cdd:PRK12582 355 GATLSDdlyermqALAVRTTGH-RIPFYTGYGATETA------PTTTGTHwDTERVGLIGLPLPGVELKL-------APV 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 490930577 1877 GVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIAR 1923
Cdd:PRK12582 421 GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAAR 461
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1556-2031 |
7.05e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 74.02 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG 1635
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQK---DLAAIVH--PSIATF------------------AFNELFDETKVDlSSYKTtvITPQHPAYLIYTSGTTGQPKG 1692
Cdd:PRK06018 118 DLTfvpILEKIADklPSVERYvvltdaahmpqttlknavAYEEWIAEADGD-FAWKT--FDENTAAGMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1693 VMVSHQA-IVNRILWMQSE-YPLSATDTILQKTPcTFDVSVWEF-FWSYLVGARLVIApiDAHRDPLALLSLIQKYQVTT 1769
Cdd:PRK06018 195 VLYSHRSnVLHALMANNGDaLGTSAADTMLPVVP-LFHANSWGIaFSAPSMGTKLVMP--GAKLDGASVYELLDTEKVTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1770 LHFVPSM-LAVFENAATEILssaqrqSLP-ICRVFCSGEALPTALAKSFtEHFSCELHNLYGPTEaavdVSYMDATLGLH 1847
Cdd:PRK06018 272 TAGVPTVwLMLLQYMEKEGL------KLPhLKMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTE----MSPLGTLAALK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1848 PEESCVAI----------GYPVWNTQLYILDQYLRPVPvgVDGE----LYLAGHQLAMGYLhRADltASRFVANPFtagq 1913
Cdd:PRK06018 341 PPFSKLPGdarldvlqkqGYPPFGVEMKITDDAGKELP--WDGKtfgrLKVRGPAVAAAYY-RVD--GEILDDDGF---- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1914 rmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGLDVVVHA--ISSEQNKAN------VQLvAYLQ 1985
Cdd:PRK06018 412 --FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEN---LAVGHPKVAEAavIGVYHPKWDerplliVQL-KPGE 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 490930577 1986 TTAPVDI-DQLKKQLAKhlpaYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06018 486 TATREEIlKYMDGKIAK----WWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
481-979 |
7.56e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 73.62 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 481 EQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLD 560
Cdd:PRK06164 18 AHARARPDAVALIDEDRP----LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 561 Y------------------------PID---RMQMMCEDANP----LFVL--TTQALAQQLPQNIQQL--HLDQEGVQTQ 605
Cdd:PRK06164 94 YrshevahilgrgrarwlvvwpgfkGIDfaaILAAVPPDALPplraIAVVddAADATPAPAPGARVQLfaLPDPAPPAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 606 IRKQDASDIPAenrkfdfqdVAYVifTSGSTGRPKGVMNTHGSLLnlilSHKptiyWPVLEAVNERfPDRPLRAAHTHSF 685
Cdd:PRK06164 174 GERAADPDAGA---------LLFT--TSGTTSGPKLVLHRQATLL----RHA----RAIARAYGYD-PGAVLLAALPFCG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 686 SFDSSWLQVFwMLWGQELH---IFD-----ENMRRD----AFGlVQEIQQRQIDTLDLPPSFcaqmmtnglfvenqhhPS 753
Cdd:PRK06164 234 VFGFSTLLGA-LAGGAPLVcepVFDaartaRALRRHrvthTFG-NDEMLRRILDTAGERADF----------------PS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 754 LILIG-----GEAAPLALWQQLNAQPAlfaHNLYGPTEYT--VDTFRAELKQTARPVIGNPIGNTQAYVLDRHLQR---C 823
Cdd:PRK06164 296 ARLFGfasfaPALGELAALARARGVPL---TGLYGSSEVQalVALQPATDPVSVRIEGGGRPASPEARVRARDPQDgalL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 824 PTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN 903
Cdd:PRK06164 373 PDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEH 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 904 ALSILTNVESAVVIAEPINNSHRLLGYCVVKD-IELDEktseqlsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSG 979
Cdd:PRK06164 447 ALEALPGVAAAQVVGATRDGKTVPVAFVIPTDgASPDE-------AGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1677-2031 |
7.89e-13 |
|
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: 73.57 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQA----IVNRILWmQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPidaH 1752
Cdd:cd05929 127 GWKMLYSGGTTGRPKGIKRGLPGgppdNDTLMAA-ALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME---K 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 RDPLALLSLIQKYQVTTLHFVPSM----LAVFENA-ATEILSSAQRqslpicrVFCSGEALPTALAKSFTEHFSCELHNL 1827
Cdd:cd05929 203 FDPEEFLRLIERYRVTFAQFVPTMfvrlLKLPEAVrNAYDLSSLKR-------VIHAAAPCPPWVKEQWIDWGGPIIWEY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1828 YGPTEAaVDVSYMDATLGL-HPEescvAIGYPVwNTQLYILDQYLRPVPVGVDGELYLAGHQlAMGYLHRADLTASRFVA 1906
Cdd:cd05929 276 YGGTEG-QGLTIINGEEWLtHPG----SVGRAV-LGKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1907 NPFTAgqrmyrTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL-RLISGLDVVV----HAISSEQNKANVQlV 1981
Cdd:cd05929 349 GGWST------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALiAHPKVLDAAVvgvpDEELGQRVHAVVQ-P 421
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490930577 1982 AYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05929 422 APGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
467-656 |
8.69e-13 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 73.60 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 467 SHPEQYNNVLDIFYEQVKKYPERTAIVSGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLS 546
Cdd:COG1022 5 SDVPPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 547 VLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLT-TQALAQQLPQNIQQLH-------LDQEGVQTQIRKQDASDIPAEN 618
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPslrhivvLDPRGLRDDPRLLSLDELLALG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490930577 619 RKFDFQ-------------DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSH 656
Cdd:COG1022 165 REVADPaelearraavkpdDLATIIYTSGTTGRPKGVMLTHRNLLSNARAL 215
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
755-989 |
1.33e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 72.72 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 755 ILIGGEAA-PLALWQQLNAQPALFAHNLYGPTEyTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGV--IGE 830
Cdd:PRK07787 245 LLVSGSAAlPVPVFDRLAALTGHRPVERYGMTE-TLITLSTRADGERRPgWVGLPLAGVETRLVDEDGGPVPHDGetVGE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 831 LYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGR-CDDQIKIRGYRVEIGEVENALSILT 909
Cdd:PRK07787 324 LQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 910 NVESAVVIAEPINN-SHRLLGYCV----VKDIELDEKTSEQLSQqylsqlrqnlpeYMVPSALTVMSEFPRNVSGKVDKK 984
Cdd:PRK07787 398 GVREAAVVGVPDDDlGQRIVAYVVgaddVAADELIDFVAQQLSV------------HKRPREVRFVDALPRNAMGKVLKK 465
|
....*
gi 490930577 985 ALPKP 989
Cdd:PRK07787 466 QLLSE 470
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
625-986 |
1.36e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 73.16 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKpTIYWPVLeAVNERFPDRPLRAAHThsFSFDSSWLqVFWMLWGQELH 704
Cdd:PRK08974 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAK-AAYGPLL-HPGKELVVTALPLYHI--FALTVNCL-LFIELGGQNLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 705 IFDEnmrRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLF---VENQHHPSL------ILIGG----EAAPLALWQQLN 771
Cdd:PRK08974 282 ITNP---RDIPGFVKELKKYP---------FTAITGVNTLFnalLNNEEFQELdfsslkLSVGGgmavQQAVAERWVKLT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 772 AQPALFAhnlYGPTE---------YTVDTFRAElkqtarpvIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGY 842
Cdd:PRK08974 350 GQYLLEG---YGLTEcsplvsvnpYDLDYYSGS--------IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGY 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 843 LGRADLSAarfvaNPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPIN 922
Cdd:PRK08974 419 WQRPEATD-----EVIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSE 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 923 NSHRLLGYCVV-KDIELdekTSEQLsqqyLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08974 492 VSGEAVKIFVVkKDPSL---TEEEL----ITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
469-916 |
1.66e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 72.98 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 469 PEQYNNVLDIFYEQVKKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSV- 547
Cdd:PRK08279 33 PDSKRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 548 --------LNSGASFLPL----------------DLDYPIDRMQMMCEDANPLFVLTTQALAQqlPQNIQQLHLDQEGVQ 603
Cdd:PRK08279 109 klgavvalLNTQQRGAVLahslnlvdakhlivgeELVEAFEEARADLARPPRLWVAGGDTLDD--PEGYEDLAAAAAGAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 604 TQiRKQDASDIPAEnrkfdfqDVAYVIFTSGSTGRPKGVMNTHGSLLN--------LILSHKPTIYWPVleavnerfpdr 675
Cdd:PRK08279 187 TT-NPASRSGVTAK-------DTAFYIYTSGTTGLPKAAVMSHMRWLKamggfgglLRLTPDDVLYCCL----------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 676 PLraahTHSFSFDSSWLQV-----------------FWmlwgqelhifDENMRRDA--FGLVQEIQqRQIdtLDLPPSfc 736
Cdd:PRK08279 248 PL----YHNTGGTVAWSSVlaagatlalrrkfsasrFW----------DDVRRYRAtaFQYIGELC-RYL--LNQPPK-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 737 AQmmtnglfvENQHHPSLIlIGGEAAPlALWQQLNAQpalFA----HNLYGPTE-----YTVDTFR-------AELKQTA 800
Cdd:PRK08279 309 PT--------DRDHRLRLM-IGNGLRP-DIWDEFQQR---FGipriLEFYAASEgnvgfINVFNFDgtvgrvpLWLAHPY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 801 RPV-----IGNPIGNTqayvlDRHLQRCPTGVIGELY--ISGFGIANGYLGRADlSAARFVANPFEHGQRMYRTGDLVRW 873
Cdd:PRK08279 376 AIVkydvdTGEPVRDA-----DGRCIKVKPGEVGLLIgrITDRGPFDGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRD 449
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 490930577 874 NSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVV 916
Cdd:PRK08279 450 DGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVV 492
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1546-2031 |
2.21e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 72.67 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1546 PEQTAL------SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqHP-- 1617
Cdd:PRK10524 67 PEQLALiavsteTDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAI-------HSvv 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1618 ---------TERIkfmlQDAKSKLVIG------------------EQKDLAA-------IVHPSIATFAFNELFDetkVD 1663
Cdd:PRK10524 140 fggfashslAARI----DDAKPVLIVSadagsrggkvvpykplldEAIALAQhkprhvlLVDRGLAPMARVAGRD---VD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1664 LSSYKTTVITPQ---------HPAYLIYTSGTTGQPKGVM--VSHQAIVnrilwmqseypLSAT-DTILQKTP-----CT 1726
Cdd:PRK10524 213 YATLRAQHLGARvpvewlesnEPSYILYTSGTTGKPKGVQrdTGGYAVA-----------LATSmDTIFGGKAgetffCA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1727 FDVSvWEFFWSYLVGARLvIA----------PIdaHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSL 1796
Cdd:PRK10524 282 SDIG-WVVGHSYIVYAPL-LAgmatimyeglPT--RPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1797 PicRVFCSGEALPTALAKSFTEHFSCELHNLYGPTE-------AAVDVSYMDATLGlhpeescvAIGYPVWNTQLYILDQ 1869
Cdd:PRK10524 358 R--ALFLAGEPLDEPTASWISEALGVPVIDNYWQTEtgwpilaIARGVEDRPTRLG--------SPGVPMYGYNVKLLNE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1870 YL-RPVPVGVDGELYLAGhQL---AMGYLHRADltaSRFVANPFTA-GQRMYRTGDIARWHADGSIQYIGRADDQLKIRG 1944
Cdd:PRK10524 428 VTgEPCGPNEKGVLVIEG-PLppgCMQTVWGDD---DRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAG 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1945 QRIELGEIEQqlrlisgldvvvhAISSEQNKANVQLV--------------AYLQTTAPVDID--------QLKKQLAKH 2002
Cdd:PRK10524 504 HRLGTREIEE-------------SISSHPAVAEVAVVgvkdalkgqvavafVVPKDSDSLADRearlalekEIMALVDSQ 570
|
570 580
....*....|....*....|....*....
gi 490930577 2003 LPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK10524 571 LGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
475-986 |
2.41e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 72.35 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 475 VLDIFYEQVKKYPERTAIVSGErpNLQHLSFAELAVKVNQLTRFLQENGARKQT---VIAGAIPRSIDSVvvmLSVLNSG 551
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRRCD--GTSALRYRELVAEVGGLAADLRAQSVSRGSrvlVISDNGPETYLSV---LACAKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 552 ASFLPLDLDYPIDRMQMMCEDANPLFVLTTQAL---AQQLPQ---NIQQLHLDQEGVQTQIRKQDASDIPAENRKFDFQD 625
Cdd:PRK05857 91 AIAVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEalhSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 626 VAYVIFTSGSTGRPKGVMNTHGSLLNL--ILSHKPT--IYWPVLEAVNErfpdrPLRAAHTHSFsfdssWLQVFWMLWGQ 701
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVLLANRTFFAVpdILQKEGLnwVTWVVGETTYS-----PLPATHIGGL-----WWILTCLMHGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 702 ELHIFDENmrrdAFGLVQEIQQRQIDTLDLPPSFCAQMMTNgLFVENQHHPSLILI--GGEAAPLALWQQLNAQPALFAH 779
Cdd:PRK05857 241 LCVTGGEN----TTSLLEILTTNAVATTCLVPTLLSKLVSE-LKSANATVPSLRLVgyGGSRAIAADVRFIEATGVRTAQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 780 nLYGPTEY--------TVDTFRAELKQTArpvIGNPIGNTQAYVLDRH------LQRCPTGVIGELYISGFGIANGYLGr 845
Cdd:PRK05857 316 -VYGLSETgctalclpTDDGSIVKIEAGA---VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWN- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 846 adlsaarfvaNPFEHGQRM----YRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPI 921
Cdd:PRK05857 391 ----------NPERTAEVLidgwVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 922 NNSHRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK05857 461 EEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1537-2009 |
2.53e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 72.18 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1537 LLREQARITPEQTALSDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQH 1616
Cdd:PLN02479 25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1617 PTERIKFMLQDAKSKLVIGEQKD-----------------------LAAIVHPSIATFAFNELFDETKVDLSSYKTTvit 1673
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFftlaeealkilaekkkssfkpplLIVIGDPTCDPKSLQYALGKGAIEYEKFLET--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 pQHPAY-------------LIYTSGTTGQPKGVMVSHQ-----AIVNRILWMQSEyplsatDTILQKTPCTFDVSVWEFF 1735
Cdd:PLN02479 182 -GDPEFawkppadewqsiaLGYTSGTTASPKGVVLHHRgaylmALSNALIWGMNE------GAVYLWTLPMFHCNGWCFT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1736 WSY--LVGARLVIAPIDAHrdplALLSLIQKYQVTTLHFVPSMLAVFENAateilsSAQRQSLPICR---VFCSGEALPT 1810
Cdd:PLN02479 255 WTLaaLCGTNICLRQVTAK----AIYSAIANYGVTHFCAAPVVLNTIVNA------PKSETILPLPRvvhVMTAGAAPPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1811 AL-----AKSFTEHFSCELHNLYGPTEAAV-----DVSYMDATLGLHPEESCVAIGYpvwnTQLYILD-QYLRPVPV--G 1877
Cdd:PLN02479 325 SVlfamsEKGFRVTHTYGLSETYGPSTVCAwkpewDSLPPEEQARLNARQGVRYIGL----EGLDVVDtKTMKPVPAdgK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1878 VDGELYLAGHQLAMGYLHRADLTASRFvANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR 1957
Cdd:PLN02479 401 TMGEIVMRGNMVMKGYLKNPKANEEAF-ANGW------FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVY 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1958 LISG-LDVVVHAISSEQ-NKANVQLVAYLQTTAPVDIDQLKKQLAK----HLPAYMVP 2009
Cdd:PLN02479 474 THPAvLEASVVARPDERwGESPCAFVTLKPGVDKSDEAALAEDIMKfcreRLPAYWVP 531
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1838-2117 |
2.53e-12 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 70.16 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1838 SYMDATLGLHPEESCVAIGYPVWNTQLYILDQYLRPVPVGVDGELYLAGhqLAMGYLHRADLTASRFVANPFTAGQ---R 1914
Cdd:COG3433 3 IATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLG--AGLLLRIRLLAAAARAPFIPVPYPAqpgR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1915 MYRTGDIARWHADGSIQYIGRADDQLKIRG-QRIELGEIEQQLRLISGLDVVVHAISSEQNKANVQLVAYLQTTAPVDID 1993
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAeRGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1994 QLKKQLakHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPSNTEKQYATSA-----FEHELTRIFQQILNTD-QN 2067
Cdd:COG3433 161 ALAALD--KVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPAletalTEEELRADVAELLGVDpEE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490930577 2068 IGVNEDFFAIGGHSILVMKLAIEIRKVFkRTIPIGQLMSHVTIQRLAALL 2117
Cdd:COG3433 239 IDPDDNLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPTLAAWWALL 287
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1674-2027 |
3.44e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 72.31 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPctfdvsvweFFWSYLVGARLViapidahr 1753
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALP---------VFHSFGLTGGLV-------- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1754 dpLALLSLIQKYQV-TTLHF--VPSMlaVFENAATEI------LSSAQRQSLP-----ICRVFCSGEALPTALAKSFTEH 1819
Cdd:PRK06814 855 --LPLLSGVKVFLYpSPLHYriIPEL--IYDTNATILfgtdtfLNGYARYAHPydfrsLRYVFAGAEKVKEETRQTWMEK 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1820 FSCELHNLYGPTEAAvdvsymdatlglhPeesCVAIGYPVWN---TQLYIL---DQYLRPVPvGVD--GELYLAGHQLAM 1891
Cdd:PRK06814 931 FGIRILEGYGVTETA-------------P---VIALNTPMHNkagTVGRLLpgiEYRLEPVP-GIDegGRLFVRGPNVML 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLhRADltaSRFVANPFTAGqrMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQqlrLISGLDV-VVHAIS 1970
Cdd:PRK06814 994 GYL-RAE---NPGVLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE---LAAELWPdALHAAV 1064
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1971 SEQN-KANVQLVayLQTTAPvDIDQ---LKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK06814 1065 SIPDaRKGERII--LLTTAS-DATRaafLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
627-986 |
6.40e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 70.96 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 627 AYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVNerFPDRPLraahTHSFSFDSswLQVFWMLWG----QE 702
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVG--FVGVPL----FHIAGIGS--MLPGLLLGAptviYP 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 703 LHIFDENMRRDAfglvqeIQQRQIDTLDLPP----SFCAQMMTNGlfvenqHHPSLILIGGEAAPL--ALWQQLNAQ-PA 775
Cdd:PRK07786 249 LGAFDPGQLLDV------LEAEKVTGIFLVPaqwqAVCAEQQARP------RDLALRVLSWGAAPAsdTLLRQMAATfPE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 776 LFAHNLYGPTEYTVDTFRAELKQTARPV--IGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARF 853
Cdd:PRK07786 317 AQILAAFGQTEMSPVTCMLLGEDAIRKLgsVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 854 VANPFEhgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG---- 929
Cdd:PRK07786 397 AGGWFH-------SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRA----DEKWGevpv 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 930 YCVVKDIELDEKTSEQLSQQylsqLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07786 466 AVAAVRNDDAALTLEDLAEF----LTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
487-986 |
9.53e-12 |
|
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: 70.60 E-value: 9.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIV-SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:cd05968 75 RTRPALRwEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 566 MQMMCEDANPLFVLTTQALAQQ-----LPQNIQQLHLDQEGVQTQI--RKQDASDIPAENR----------------KFD 622
Cdd:cd05968 155 AATRLQDAEAKALITADGFTRRgrevnLKEEADKACAQCPTVEKVVvvRHLGNDFTPAKGRdlsydeeketagdgaeRTE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 623 FQDVAYVIFTSGSTGRPKGVMNTHGSLlnlilshkptiywpvleavnerfpdrPLRAAHTHSFSF------------DSS 690
Cdd:cd05968 235 SEDPLMIIYTSGTTGKPKGTVHVHAGF--------------------------PLKAAQDMYFQFdlkpgdlltwftDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 691 WLQVFWMLWG-----QELHIFDENMRRDAFGLVQEIQQR-QIDTLDLPPSFCAQMMTNG-LFVENQHHPSLILIGGEAAP 763
Cdd:cd05968 289 WMMGPWLIFGglilgATMVLYDGAPDHPKADRLWRMVEDhEITHLGLSPTLIRALKPRGdAPVNAHDLSSLRVLGSTGEP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 764 lalWqqlNAQPA--LFAH---------NLYGPTEYTVDTFRAELKQTARPVIGN-PIGNTQAYVLDRHLQRCPtGVIGEL 831
Cdd:cd05968 369 ---W---NPEPWnwLFETvgkgrnpiiNYSGGTEISGGILGNVLIKPIKPSSFNgPVPGMKADVLDESGKPAR-PEVGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 832 YISG--FGIANGYLGRADlsaaRFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILT 909
Cdd:cd05968 442 VLLApwPGMTRGFWRDED----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHP 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 910 NV-ESAVV-IAEPINNShRLLGYCVVKDielDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05968 518 AVlESAAIgVPHPVKGE-AIVCFVVLKP---GVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1677-2019 |
1.08e-11 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 68.48 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1677 PAYLIYTSGTTGQPKGVMVSHQAIVNR---ILWMQSeypLSATDTILQKTPcTFDVSVWEF-FWSYLVGARLVIAPidah 1752
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQALLAQalvLAVLQA---IDEGTVFLNSGP-LFHIGTLMFtLATFHAGGTNVFVR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 R-DPLALLSLIQKYQVT-TLHFVPSMLAVFE-NAATEI-LSSAQRQSLPICRVFCSgEALPTALAKSFtehfscelhNLY 1828
Cdd:cd17636 74 RvDAEEVLELIEAERCThAFLLPPTIDQIVElNADGLYdLSSLRSSPAAPEWNDMA-TVDTSPWGRKP---------GGY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1829 GPTEaavdVSYMDATLGLHPEESCVAiGYPVWNTQLYILDQYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVAnp 1908
Cdd:cd17636 144 GQTE----VMGLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1909 ftagqRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKANVQLVAYLQTT 1987
Cdd:cd17636 217 -----GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVaDAAVIGVPDPRWAQSVKAIVVLKPG 291
|
330 340 350
....*....|....*....|....*....|..
gi 490930577 1988 APVDIDQLKKQLAKHLPAYMVPTHYMLVEQFP 2019
Cdd:cd17636 292 ASVTEAELIEHCRARIASYKKPKSVEFADALP 323
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
822-986 |
1.79e-11 |
|
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: 69.00 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 822 RCPTGVIGELYISGF----GIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVE 897
Cdd:cd05937 293 RAPVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 898 IGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNV 977
Cdd:cd05937 373 TTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTD 452
|
....*....
gi 490930577 978 SGKVDKKAL 986
Cdd:cd05937 453 NHKQQKGVL 461
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1557-1956 |
2.94e-11 |
|
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: 68.65 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIdlqHPT---ERIKFMLQDAKSK-L 1632
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSESKaL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 VIGEQKDLAAIVH------PSIATFAFNEL-FDETKVDL-----SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSH--- 1697
Cdd:cd05932 83 FVGKLDDWKAMAPgvpeglISISLPPPSAAnCQYQWDDLiaqhpPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFgsf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1698 ----QAIVNRIlwmqseyPLSATDTILQKTP-CTFDVSVWEFFWSYLVGARLVIA-PIDahrdplALLSLIQKYQVTTLH 1771
Cdd:cd05932 163 awaaQAGIEHI-------GTEENDRMLSYLPlAHVTERVFVEGGSLYGGVLVAFAeSLD------TFVEDVQRARPTLFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1772 FVPSMLAVFENAATEILSSAQRQ---SLPI-----------------CRVFCSGEA-LPTALAkSFTEHFSCELHNLYGP 1830
Cdd:cd05932 230 SVPRLWTKFQQGVQDKIPQQKLNlllKIPVvnslvkrkvlkglgldqCRLAGCGSApVPPALL-EWYRSLGLNILEAYGM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1831 TEaavdvSYMDATLGLHPEESCVAIGYPVWNTQLYILDqylrpvpvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFt 1910
Cdd:cd05932 309 TE-----NFAYSHLNYPGRDKIGTVGNAGPGVEVRISE----------DGEILVRSPALMMGYYKDPEATAEAFTADGF- 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 490930577 1911 agqrmYRTGDIARWHADGSIQYIGRADDQLKI-RGQRIELGEIEQQL 1956
Cdd:cd05932 373 -----LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKL 414
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1102-1408 |
2.97e-11 |
|
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: 68.06 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKGMLFLSQ-VENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQLGGHF---DSELAEEPVFIYSLHptqaW 1177
Cdd:cd20483 3 PMSTFQRRLWFLHNfLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYfegDDFGEQQVLDDPSFH----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1178 PVQFCSVTPD---LLEQTIQEALQQPIHLDQpyG-LIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQ--- 1250
Cdd:cd20483 79 IVIDLSEAADpeaALDQLVRNLRRQELDIEE--GeVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDalr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1251 -QTNQQlPVLEHSYETVIKALSGRDHETSKVI------WQRDLADLQP---LILF--------NQAQQAVQETSyrLSAE 1312
Cdd:cd20483 157 aGRDLA-TVPPPPVQYIDFTLWHNALLQSPLVqplldfWKEKLEGIPDaskLLPFakaerppvKDYERSTVEAT--LDKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1313 LGAKLQHKLRQQGITlnVFMQMIWAMTLNIYAH--REDIVFGTPVSGRSAPinGLEQQIGLFLNTIPVRVKLNMQQTLWE 1390
Cdd:cd20483 234 LLARMKRICAQHAVT--PFMFLLAAFRAFLYRYteDEDLTIGMVDGDRPHP--DFDDLVGFFVNMLPIRCRMDCDMSFDD 309
|
330
....*....|....*...
gi 490930577 1391 QLPQLQQLHVEHLEHDGL 1408
Cdd:cd20483 310 LLESTKTTCLEAYEHSAV 327
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1554-1948 |
3.56e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 68.60 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1554 ENHQLSFSEVRLQVCALAQQLQRAGvQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI-DLQHP--TERIKFMLQDAKS 1630
Cdd:PRK07769 52 VARDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1631 KlVIGEQKDLAAIVHPSIATFAFNELFDETKVDL------SSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRI 1704
Cdd:PRK07769 131 S-AILTTTDSAEGVRKFFRARPAKERPRVIAVDAvpdevgATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1705 LWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYLVGARLVI-APIDAHRDP---LALLSLIQKYQVTTLHFVPSMlaVF 1780
Cdd:PRK07769 210 LQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFmSPAAFVRRPgrwIRELARKPGGTGGTFSAAPNF--AF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1781 ENAATEILSSAQRQSLPICRVFC---SGEALPTALAKSFTEHFS------CELHNLYGPTEAAVDVS-----------YM 1840
Cdd:PRK07769 288 EHAAARGLPKDGEPPLDLSNVKGllnGSEPVSPASMRKFNEAFApyglppTAIKPSYGMAEATLFVSttpmdeeptviYV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1841 DAT-LGLH-------------PEESCVAIGYPVWNTqlyILD-QYLRPVPVGVDGELYLAGHQLAMGYLHRADLTASRF- 1904
Cdd:PRK07769 368 DRDeLNAGrfvevpadapnavAQVSAGKVGVSEWAV---IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFq 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 1905 ------VANPFTAG----QRMYRTGDIARWHaDGSIQYIGRADDQLKIRG-----QRIE 1948
Cdd:PRK07769 445 nilksrLSESHAEGapddALWVRTGDYGVYF-DGELYITGRVKDLVIIDGrnhypQDLE 502
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
503-986 |
4.02e-11 |
|
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: 67.59 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLdldypidrmqmmcedanplfvlTTQ 582
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA----------------------TTL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQQLPQNIQQlhldqeGVQTQIRKQDASDIpaenrkfdfQDVAYVIFTSGSTGRPKGVMNTHGSllnLILSHKPTIYW 662
Cdd:cd05974 59 LTPDDLRDRVDR------GGAVYAAVDENTHA---------DDPMLLYFTSGTTSKPKLVEHTHRS---YPVGHLSTMYW 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 663 PVLEAVNERFP-DRPLRAAHTHSfsfdsswlqVFWMLWGQELHIFDENMRR-DAFGLVQEIQQRQIDTLDLPPSfCAQMM 740
Cdd:cd05974 121 IGLKPGDVHWNiSSPGWAKHAWS---------CFFAPWNAGATVFLFNYARfDAKRVLAALVRYGVTTLCAPPT-VWRML 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 741 TNGLFVENQHHPSLILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDRHL 820
Cdd:cd05974 191 IQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 821 QRCPTGVIGeLYISG---FGIANGYLGRADLSAARFvanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVE 897
Cdd:cd05974 271 APATEGEVA-LDLGDtrpVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRIS 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 898 IGEVENALSILTNVESAVVIAEPinNSHRLL---GYCVVKDielDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVmSEFP 974
Cdd:cd05974 343 PFELESVLIEHPAVAEAAVVPSP--DPVRLSvpkAFIVLRA---GYEPSPETALEIFRFSRERLAPYKRIRRLEF-AELP 416
|
490
....*....|..
gi 490930577 975 RNVSGKVDKKAL 986
Cdd:cd05974 417 KTISGKIRRVEL 428
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
628-986 |
4.32e-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: 67.79 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 628 YVIFTSGSTGRPKGVMNTHGSllnlilshkptiywpvleavnERFPDRPLRAAHTHS-FSFDSSWL----------QVFW 696
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPG---------------------GPPDNDTLMAAALGFgPGADSVYLspaplyhaapFRWS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 697 M---LWGQELHIfdenMRR-DAFGLVQEIQQRQIDTLDLPPSfcaqMMTNGLFV-ENQHH----PSLILIGGEAAPLALW 767
Cdd:cd05929 188 MtalFMGGTLVL----MEKfDPEEFLRLIERYRVTFAQFVPT----MFVRLLKLpEAVRNaydlSSLKRVIHAAAPCPPW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 768 --QQLNAQPALFAHNLYGPTEYTVDTF-RAELKQTARPVIGNPIGNtQAYVLDRHLQRCPTGVIGELYIS---GFGIANG 841
Cdd:cd05929 260 vkEQWIDWGGPIIWEYYGGTEGQGLTIiNGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAngpGFEYTND 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 842 YLGRAdlsAARFvanpfEHGqrmYRT-GDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd05929 339 PEKTA---AARN-----EGG---WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVP 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 921 innsHRLLGYCVVKDIE--LDEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05929 408 ----DEELGQRVHAVVQpaPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1542-1923 |
6.85e-11 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 67.46 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1542 ARITPEQTALSDEN-----HQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPID--- 1613
Cdd:cd05921 5 ARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpay 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1614 ---------LQHPTERIK---FMLQDAKSKlvigeQKDLAAIV--HPSIAtFAFNELFDETKVDLSSYKTT--------- 1670
Cdd:cd05921 85 slmsqdlakLKHLFELLKpglVFAQDAAPF-----ARALAAIFplGTPLV-VSRNAVAGRGAISFAELAATpptaavdaa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1671 --VITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATD--TILQKTPctfdvsvweffWSYLVGARLVI 1746
Cdd:cd05921 159 faAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLP-----------WNHTFGGNHNF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1747 AP---------IDAHRdPLALL---SLIQKYQV-TTLHF-VPsmlavfenAATEILSSAQRQSLPICR--------VFCS 1804
Cdd:cd05921 228 NLvlynggtlyIDDGK-PMPGGfeeTLRNLREIsPTVYFnVP--------AGWEMLVAALEKDEALRRrffkrlklMFYA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1805 GEALP-------TALAKSFTEHfSCELHNLYGPTEAAVdvsymDATLGLHPEESCVAIGYPVWNTQlyildqyLRPVPVG 1877
Cdd:cd05921 299 GAGLSqdvwdrlQALAVATVGE-RIPMMAGLGATETAP-----TATFTHWPTERSGLIGLPAPGTE-------LKLVPSG 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 490930577 1878 VDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIAR 1923
Cdd:cd05921 366 GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF------YCLGDAAK 405
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
481-986 |
7.00e-11 |
|
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: 67.55 E-value: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 481 EQVKKYPERTAIVSG-----ERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFL 555
Cdd:cd17642 18 EQLHKAMKRYASVPGtiaftDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 556 PLDLDYPIDRMQMMCEDANPLFVLTTQ-------ALAQQLP--QNIQQLHL--DQEGVQTqIRKQDASDIPAENRKFDF- 623
Cdd:cd17642 98 PTNDIYNERELDHSLNISKPTIVFCSKkglqkvlNVQKKLKiiKTIIILDSkeDYKGYQC-LYTFITQNLPPGFNEYDFk 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 624 -------QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYwpvleaVNERFPDRPLRAA---HtHSFSFDSSwlq 693
Cdd:cd17642 177 ppsfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIF------GNQIIPDTAILTVipfH-HGFGMFTT--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 694 VFWMLWGQE---LHIFDENMrrdafgLVQEIQQRQIDTLDLPPSFCAQMMTNGLfVENQHHPSLILIGGEAAPLA--LWQ 768
Cdd:cd17642 247 LGYLICGFRvvlMYKFEEEL------FLRSLQDYKVQSALLVPTLFAFFAKSTL-VDKYDLSNLHEIASGGAPLSkeVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 769 QLNAQPAL-FAHNLYGPTEYTVDTFRAELKQTARPVIGNPIGNTQAYVLDrhlqrCPTGVI------GELYISGFGIANG 841
Cdd:cd17642 320 AVAKRFKLpGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVD-----LDTGKTlgpnerGELCVKGPMIMKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 842 YLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPI 921
Cdd:cd17642 395 YVNNPEATKALIDKDGWLH------SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 922 NNSHRLLGYCVVKdiELDEKTSEQLSQQYLSQlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd17642 469 EDAGELPAAVVVL--EAGKTMTEKEVMDYVAS--QVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
503-986 |
7.56e-11 |
|
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: 67.36 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTViAGAIPRSIDSVVVMLSVLNSGAsfLPLDLDYP--IDRMQMMCEDANPLFVLT 580
Cdd:cd05909 8 LTYRKLLTGAIALARKLAKMTKEGENV-GVMLPPSAGGALANFALALSGK--VPVMLNYTagLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 581 TQALAQQLPQNIQQLHLDQ------EGVQTQIRKQD------ASDIPAENR-------KFDFQDVAYVIFTSGSTGRPKG 641
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYDarivylEDLRAKISKADkckaflAGKFPPKWLlrifgvaPVQPDDPAVILFTSGSEGLPKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 642 VMNTHGSLL-NlilshkptiywpvLEAVNERFP----DRPLRAAHT-HSFSFDSSwlqvFWMLWGQELHIFDENMRRDAF 715
Cdd:cd05909 165 VVLSHKNLLaN-------------VEQITAIFDpnpeDVVFGALPFfHSFGLTGC----LWLPLLSGIKVVFHPNPLDYK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 716 GLVQEIQQRQIDTLDLPPSFcaqMMTNGLFVENQHHPSL--ILIGGEAAPLAL---WQQLNAQPALFAhnlYGPTEytvd 790
Cdd:cd05909 228 KIPELIYDKKATILLGTPTF---LRGYARAAHPEDFSSLrlVVAGAEKLKDTLrqeFQEKFGIRILEG---YGTTE---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 791 tfraelkqtARPVI--------------GNPIGNTQAYVLDRH-LQRCPTGVIGELYISGFGIANGYLGRADLSAarfva 855
Cdd:cd05909 298 ---------CSPVIsvntpqspnkegtvGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS----- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 856 npFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALS-ILTNVESAVVIAEPinnsHRLLGYCVVk 934
Cdd:cd05909 364 --FAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSeILPEDNEVAVVSVP----DGRKGEKIV- 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 490930577 935 dIELDEKTSEQLS-QQYLSQlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:cd05909 437 -LLTTTTDTDPSSlNDILKN--AGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
501-989 |
8.63e-11 |
|
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: 67.00 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 501 QHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLT 580
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 581 tqalaqqlpqniqqlhldqegvqtqirkqdasdipaENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptI 660
Cdd:cd17640 84 ------------------------------------ENDS---DDLATIIYTSGTTGNPKGVMLTHANLLHQIRS----L 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 661 YWPVLEAVNERFpdrplraahthsFSFDSSW------LQVFWMLWGQELH-----IFDENMRR------DAFGLVQEIQQ 723
Cdd:cd17640 121 SDIVPPQPGDRF------------LSILPIWhsyersAEYFIFACGCSQAytsirTLKDDLKRvkphyiVSVPRLWESLY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 724 RQIDTLDLPPSFCAQMMTNGLFVENQHhpSLILIGGEAAPLALWQQLNAQ--PALfahNLYGPTEYTVDTFRAELKQTAR 801
Cdd:cd17640 189 SGIQKQVSKSSPIKQFLFLFFLSGGIF--KFGISGGGALPPHVDTFFEAIgiEVL---NGYGLTETSPVVSARRLKCNVR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 802 PVIGNPIGNTQAYVLDRHLQRC-PTGVIGELYISGFGIANGYLgrADLSAARFVANP---FEhgqrmyrTGDLVRWNSAG 877
Cdd:cd17640 264 GSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYY--KNPEATSKVLDSdgwFN-------TGDLGWLTCGG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 878 KLEFMGRCDDQIKIR-GYRVEIGEVENALSILTNVESAVVIAEpinnSHRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQ 956
Cdd:cd17640 335 ELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQ----DQKRLGALIVPNFEELEKWAKESGVKLANDRSQ 410
|
490 500 510
....*....|....*....|....*....|...
gi 490930577 957 NLpeymvpSALTVMSEFPRNVSGKVDKKALPKP 989
Cdd:cd17640 411 LL------ASKKVLKLYKNEIKDEISNRPGFKS 437
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1133-1407 |
1.16e-10 |
|
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: 66.36 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1133 DIDPVRLQQALITVLKRHPQLGGHFDS----ELAEEPvfiyslhPTQAWPVQFCSvtpDLLEQTIQEALQQpihldqpyg 1208
Cdd:cd19535 36 DLDPDRLERAWNKLIARHPMLRAVFLDdgtqQILPEV-------PWYGITVHDLR---GLSEEEAEAALEE--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1209 lIRATLIQH--APEQSELL-IMVHH--------------LLTDGWSTPLFLQDFIKAYQQTNQQLPVLEHS---YETVIK 1268
Cdd:cd19535 97 -LRERLSHRvlDVERGPLFdIRLSLlpegrtrlhlsidlLVADALSLQILLRELAALYEDPGEPLPPLELSfrdYLLAEQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1269 ALSGRDHETSKVIWQRDLADLQ-----PLIlfnQAQQAVQET-----SYRLSAELGAKLQHKLRQQGITLNVFMQMIWAM 1338
Cdd:cd19535 176 ALRETAYERARAYWQERLPTLPpapqlPLA---KDPEEIKEPrftrrEHRLSAEQWQRLKERARQHGVTPSMVLLTAYAE 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1339 TLNIYAHREDIVFGTPVSGRSAPINGLEQQIGLFLNTIPVRVKLNMQQTLWEQLPQLQ-QLH--VEHLEHDG 1407
Cdd:cd19535 253 VLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQqQLWedLDHSSYSG 324
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
1558-1954 |
1.30e-10 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 67.03 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI-DLQHPTErIKFMLQDAKSK----- 1631
Cdd:PLN03052 209 MTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIaDSFAPSE-IATRLKISKAKaiftq 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1632 -LVIGEQKDLA------------AIVHPSIATFAFNELFDEtkvDLS-----SYKTTVITPQH--PAYL--------IYT 1683
Cdd:PLN03052 288 dVIVRGGKSIPlysrvveakapkAIVLPADGKSVRVKLREG---DMSwddflARANGLRRPDEykAVEQpveaftniLFS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1684 SGTTGQPKGvmvshqaivnrILWMQSEyPL-SATDTILQKTPCTFDVSVWEFFWSYLVGARLVIAPIdAHRDPLALLS-- 1760
Cdd:PLN03052 365 SGTTGEPKA-----------IPWTQLT-PLrAAADAWAHLDIRKGDIVCWPTNLGWMMGPWLVYASL-LNGATLALYNgs 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1761 --------LIQKYQVTTLHFVPSMLAVFENaaTEILSSAQRQSLpicRVFCS-GEA---------LPTALAKSFTEhfSC 1822
Cdd:PLN03052 432 plgrgfakFVQDAKVTMLGTVPSIVKTWKN--TNCMAGLDWSSI---RCFGStGEAssvddylwlMSRAGYKPIIE--YC 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1823 elhnlyGPTEAAvdVSYMDATLgLHPeESCVAIGYPVWNTQLYILDQYLRPVP--VGVDGELYLAGHQL-AMGYLHRADL 1899
Cdd:PLN03052 505 ------GGTELG--GGFVTGSL-LQP-QAFAAFSTPAMGCKLFILDDSGNPYPddAPCTGELALFPLMFgASSTLLNADH 574
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1900 TASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQ 1954
Cdd:PLN03052 575 YKVYFKGMPVFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIER 629
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
486-888 |
1.41e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 66.05 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 486 YPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDR 565
Cdd:PRK09029 16 RPQAIALRLNDEV----LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 566 MQMMCEDANPLFVLTTQALAQqlPQNIQQLHLDQEGVQTQIRkqdasdipaenrkFDFQDVAYVIFTSGSTGRPKGVMNT 645
Cdd:PRK09029 92 LEELLPSLTLDFALVLEGENT--FSALTSLHLQLVEGAHAVA-------------WQPQRLATMTLTSGSTGLPKAAVHT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 646 HgsllnlilshkptiywpvleavnerfpdrplrAAHTHS---------FSFDSSW---LQVF----------WMLWGQEL 703
Cdd:PRK09029 157 A--------------------------------QAHLASaegvlslmpFTAQDSWllsLPLFhvsgqgivwrWLYAGATL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 704 HIfdenmrRDAFGLVQEIQ------------QRqidtldlppsfcaqmmtngLFVENQHHPSL--ILIGGEAAPLALWQQ 769
Cdd:PRK09029 205 VV------RDKQPLEQALAgcthaslvptqlWR-------------------LLDNRSEPLSLkaVLLGGAAIPVELTEQ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 770 LNAQpALFAHNLYGPTEY--TVDTFRAElkqtARPVIGNPIGNtqayvldRHLQRcptgVIGELYISGFGIANGYLGRAD 847
Cdd:PRK09029 260 AEQQ-GIRCWCGYGLTEMasTVCAKRAD----GLAGVGSPLPG-------REVKL----VDGEIWLRGASLALGYWRQGQ 323
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 490930577 848 LsaarfvaNPFEHGQRMYRTGDLVRWNSaGKLEFMGRCDDQ 888
Cdd:PRK09029 324 L-------VPLVNDEGWFATRDRGEWQN-GELTILGRLDNL 356
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1558-2002 |
1.61e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 66.32 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAylpidlqHP-----------TERIkfmlQ 1626
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV-------HSvvfggfsaealADRI----I 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1627 DAKSKLVI--------GEQKDLAAIV------HPSIAT------------------FAFNELFDETKVDlssykttvITP 1674
Cdd:PRK00174 168 DAGAKLVItadegvrgGKPIPLKANVdealanCPSVEKvivvrrtggdvdwvegrdLWWHELVAGASDE--------CEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1675 Q-----HPAYLIYTSGTTGQPKGVM-----------VSHQAIV----NRILWmqseyplsatdtilqktpCTFDVSvwef 1734
Cdd:PRK00174 240 EpmdaeDPLFILYTSGSTGKPKGVLhttggylvyaaMTMKYVFdykdGDVYW------------------CTADVG---- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1735 fW----SYLV------GARLVI---API--DAHRdplaLLSLIQKYQVTTLHFVPSMLAVFENAATEILSSAQRQSLpic 1799
Cdd:PRK00174 298 -WvtghSYIVygplanGATTLMfegVPNypDPGR----FWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSL--- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1800 RVFCS-GEAL-PTALaksftEHFscelHNLYG----P-------TEAAvdvSYMDATL-GLHPEE--SCvaiGYPVWNTQ 1863
Cdd:PRK00174 370 RLLGSvGEPInPEAW-----EWY----YKVVGgercPivdtwwqTETG---GIMITPLpGATPLKpgSA---TRPLPGIQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVGVDGelYLAghqlamgylhradLTAS-------------RFVANPFTAGQRMYRTGDIARWHADGSI 1930
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGG--NLV-------------IKDPwpgmmrtiygdheRFVKTYFSTFKGMYFTGDGARRDEDGYY 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1931 QYIGRADDQLKIRGQRIELGEIEqqlrliSGLdvVVHAISSEqnkANV----------QLVAY--LQTTAPVDiDQLKKQ 1998
Cdd:PRK00174 500 WITGRVDDVLNVSGHRLGTAEIE------SAL--VAHPKVAE---AAVvgrpddikgqGIYAFvtLKGGEEPS-DELRKE 567
|
....
gi 490930577 1999 LAKH 2002
Cdd:PRK00174 568 LRNW 571
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
625-992 |
1.81e-10 |
|
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: 65.19 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGS------LLNLILSHKPTiywPVLeavnerFPDRPLraahthsFSFDSSWLQVFWML 698
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNevynawMLALNSLFDPD---DVL------LCGLPL-------FHVNGSVVTLLTPL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 699 W-GQELHIFDENMRRDAfGLVQE----IQQRQIDTLDLPPSFCAQMMTNGLfveNQHHPSL--ILIGGEAAPLALWQQLN 771
Cdd:cd05944 67 AsGAHVVLAGPAGYRNP-GLFDNfwklVERYRITSLSTVPTVYAALLQVPV---NADISSLrfAMSGAAPLPVELRARFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 772 AQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQA--YVLD---RHLQRCPTGVIGELYISGFGIANGYLgR 845
Cdd:cd05944 143 DATGLPVVEGYGLTEATCLVAVNPPDGPKRPgSVGLRLPYARVriKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYL-Y 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 846 ADLSAARFVanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIR-GYRVEIGEVENALSILTNVESAVVIAEPinNS 924
Cdd:cd05944 222 TEGNKNAFV------ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQP--DA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 925 HRllGYCVVKDIELDEKTSEQlSQQYLSQLRQNLPEY-MVPSALTVMSEFPRNVSGKVDKKALPKPQIR 992
Cdd:cd05944 293 HA--GELPVAYVQLKPGAVVE-EEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADAIH 358
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1556-1707 |
2.37e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 65.92 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1556 HQLSFSEVRLQVCALAQQLQRAgVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPI---DLQHPTERIKFMLQDAKSKL 1632
Cdd:PRK12476 67 VELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1633 VIGEQ-------KDLAAIVH---PSIatFAFNELFDETKVDlssYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVN 1702
Cdd:PRK12476 146 VLTTTaaaeaveGFLRNLPRlrrPRV--IAIDAIPDSAGES---FVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGT 220
|
....*
gi 490930577 1703 RILWM 1707
Cdd:PRK12476 221 NLVQM 225
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1530-2025 |
3.02e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 65.60 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1530 RQSTLQQLLREQARITPEQTAL--SDENHQLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGA 1607
Cdd:PRK08315 14 LEQTIGQLLDRTAARYPDREALvyRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1608 -------AYLPIDLQHP-----------TERIKF-----MLQDAKSKLVIGEQKDLAAIVHPSIAT------------FA 1652
Cdd:PRK08315 94 ilvtinpAYRLSELEYAlnqsgckaliaADGFKDsdyvaMLYELAPELATCEPGQLQSARLPELRRviflgdekhpgmLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1653 FNELF----DETKVDLSSYKTT-----VITPQhpayliYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKT 1723
Cdd:PRK08315 174 FDELLalgrAVDDAELAARQATldpddPINIQ------YTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1724 P---CtfdvsvwefFWSYL-------VGARLVIaPIDAHrDPLALLSLIQKYQVTTLHFVPSM-LAVFENA--ATEILSS 1790
Cdd:PRK08315 248 PlyhC---------FGMVLgnlacvtHGATMVY-PGEGF-DPLATLAAVEEERCTALYGVPTMfIAELDHPdfARFDLSS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1791 ------AqrqslpicrvfcsGEALPTALAKSFTE--HFScELHNLYGPTEAAvDVSYM---DATLglhpEESCVAIGYPV 1859
Cdd:PRK08315 317 lrtgimA-------------GSPCPIEVMKRVIDkmHMS-EVTIAYGMTETS-PVSTQtrtDDPL----EKRVTTVGRAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1860 WNTQLYILDQYL-RPVPVGVDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrMyRTGDIARWHADGSIQYIGRADD 1938
Cdd:PRK08315 378 PHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-----M-HTGDLAVMDEEGYVNIVGRIKD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1939 QLkIR-GQRIELGEIEQQLRLISG-LDVVVHAISSEqnKANVQLVAYL-----QTTAPVDI-DQLKKQLAKhlpaYMVPT 2010
Cdd:PRK08315 452 MI-IRgGENIYPREIEEFLYTHPKiQDVQVVGVPDE--KYGEEVCAWIilrpgATLTEEDVrDFCRGKIAH----YKIPR 524
|
570
....*....|....*
gi 490930577 2011 HYMLVEQFPLSHNGK 2025
Cdd:PRK08315 525 YIRFVDEFPMTVTGK 539
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
861-987 |
3.09e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 64.67 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 861 GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDe 940
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID- 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 490930577 941 ktSEQLSQqylsQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PRK08308 368 --PVQLRE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1680-2026 |
3.19e-10 |
|
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: 64.06 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSH-QAIVNRILWMQSEyPLSATDTILQKTPctfdvsvweFFWSY----------LVGARLViaP 1748
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINP---------FFHTFgykagivaclLTGATVV--P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IdAHRDPLALLSLIQKYQVTtlhFVPSMLAVFENaateILSSAQRQS--LPICRVFCSGEA-LPTALAKSFTEHFSCE-L 1824
Cdd:cd17638 73 V-AVFDVDAILEAIERERIT---VLPGPPTLFQS----LLDHPGRKKfdLSSLRAAVTGAAtVPVELVRRMRSELGFEtV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1825 HNLYGPTEAAVdvsymdATLgLHPEESCVAI----GYPVWNTQLYILDqylrpvpvgvDGELYLAGHQLAMGYLHRADLT 1900
Cdd:cd17638 145 LTAYGLTEAGV------ATM-CRPGDDAETVattcGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEAT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1901 ASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQ----NK 1975
Cdd:cd17638 208 AEAIDADGW------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVaQVAVIGVPDERmgevGK 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1976 ANVqlVAYLQTTapVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKL 2026
Cdd:cd17638 282 AFV--VARPGVT--LTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
18-352 |
3.25e-10 |
|
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: 65.03 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 18 RFELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNE---ADTVIASYSSDPSQpFIELNNQVQFQ 94
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQhpiLKSVIEEEDGVPFQ-KIEPSKPLSFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 95 IEefDFCHLTPkkaqqrlWDWMPSDRQCAK---SLKAGEtqLFRQVLFTTHDKVYWYQ-RYHHIMLDGFSMINLTKRIVE 170
Cdd:cd20484 80 EE--DISSLKE-------SEIIAYLREKAKepfVLENGP--LMRVHLFSRSEQEHFVLiTIHHIIFDGSSSLTLIHSLLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 171 LYQQLQEGKDLSVSPFIGV-NEVISERQAYENSHQFKIDQAFWKAYCE------DLPSPislSTHHLAAKTTATfvKHQL 243
Cdd:cd20484 149 AYQALLQGKQPTLASSPASyYDFVAWEQDMLAGAEGEEHRAYWKQQLSgtlpilELPAD---RPRSSAPSFEGQ--TYTR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 244 RFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWV 323
Cdd:cd20484 224 RLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFS 303
|
330 340
....*....|....*....|....*....
gi 490930577 324 SLAQHVQEQLREIRPHQKYDAEQILRDLN 352
Cdd:cd20484 304 DFIRKLQLTVLDGLDHAAYPFPAMVRDLN 332
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
625-884 |
3.49e-10 |
|
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: 64.79 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKpTIYWPVLEAVNerFPDRPLRAahthsfsfdsswlqVFWMLWGQELH 704
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALR-QLYGIRPGEVD--LATFPLFA--------------LFGPALGLTSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 705 IFDENMRR----DAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLfvENQHH-PSL--ILIGGEAAPLALWQQLNA--QPA 775
Cdd:cd05910 149 IPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCA--QHGITlPSLrrVLSAGAPVPIALAARLRKmlSDE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 776 LFAHNLYGPTE---------YTVDTFRAELKQTARPV-IGNPIGNTQAYVL-----------DRHlqRCPTGVIGELYIS 834
Cdd:cd05910 227 AEILTPYGATEalpvssigsRELLATTTAATSGGAGTcVGRPIPGVRVRIIeiddepiaewdDTL--ELPRGEIGEITVT 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490930577 835 GFGIANGYLGRADlsAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGR 884
Cdd:cd05910 305 GPTVTPTYVNRPV--ATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGR 352
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
503-997 |
3.96e-10 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 65.25 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFL-QENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTT 581
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 582 QALAQQL-PQNIQQLHLDQEGVQTQIRKQDASDIPAENRKFDF--------QDVAYVIFTSGSTGRPKGVMNTHGsllNL 652
Cdd:PLN02574 147 PENVEKLsPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDFvpkpvikqDDVAAIMYSSGTTGASKGVVLTHR---NL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 653 ILSHKPTIywpvleavneRFpdrplRAAHTHSFSFDSSWLQVFWMLWGQELHIFDEN----------MRR-DAFGLVQEI 721
Cdd:PLN02574 224 IAMVELFV----------RF-----EASQYEYPGSDNVYLAALPMFHIYGLSLFVVGllslgstivvMRRfDASDMVKVI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 722 QQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAAPLA---LWQQLNAQPALFAHNLYGPTEYT-VDTFRAELK 797
Cdd:PLN02574 289 DRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSgkfIQDFVQTLPHVDFIQGYGMTESTaVGTRGFNTE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 798 QTAR-PVIGNPIGNTQAYVLDRHLQRC-PTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNS 875
Cdd:PLN02574 369 KLSKySSVGLLAPNMQAKVVDWSTGCLlPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLR------TGDIAYFDE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 876 AGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVVKdieldeKTSEQLSQ-QYLSQL 954
Cdd:PLN02574 443 DGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVR------RQGSTLSQeAVINYV 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490930577 955 RQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPKP-QIRAHSRM 997
Cdd:PLN02574 517 AKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSlTNSVSSRL 560
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
479-986 |
4.36e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 65.33 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 479 FYEQVKKYPERTAIVSGERPNLQHLSFAELAVkvnQLTRFLQENGARKQTViaGAI-PRSIDSVVVMLSVLNSGAsfLPL 557
Cdd:PRK08633 621 WIDTAKRNWSRLAVADSTGGELSYGKALTGAL---ALARLLKRELKDEENV--GILlPPSVAGALANLALLLAGK--VPV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 558 DLDYPI--DRMQMMCEDANPLFVLTTQALAQQLPQNIQQLHLDQ-------EGVQTQIRKQD-------ASDIPA----- 616
Cdd:PRK08633 694 NLNYTAseAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPEnvkviylEDLKAKISKVDkltallaARLLPArllkr 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 617 -ENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLIlshkptiywpvlEAVNERFP----DR-----PLraahTHSFS 686
Cdd:PRK08633 774 lYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNI------------EQISDVFNlrndDVilsslPF----FHSFG 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 687 FDSSwlqvfwmLWGQELhifdENMR-------RDAFGLVQEIQQRQIDTLDLPPSFCaqmmtnGLFVENQH-HP------ 752
Cdd:PRK08633 838 LTVT-------LWLPLL----EGIKvvyhpdpTDALGIAKLVAKHRATILLGTPTFL------RLYLRNKKlHPlmfasl 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 753 SLILIGGEAAPLALWQQLNAQpalFAHNL---YGPTEYT-V------DTFRAE-LKQTA--RPVIGNPIGNTQAYVLD-R 818
Cdd:PRK08633 901 RLVVAGAEKLKPEVADAFEEK---FGIRIlegYGATETSpVasvnlpDVLAADfKRQTGskEGSVGMPLPGVAVRIVDpE 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 819 HLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVAnpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:PRK08633 978 TFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPL 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 899 GEVENALSILTNVESAVVIAEPINNSHRllGYCVVKDIELDEKTSEQLSQQYLSqlrQNLPEYMVPSALTVMSEFPRNVS 978
Cdd:PRK08633 1055 GAVEEELAKALGGEEVVFAVTAVPDEKK--GEKLVVLHTCGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGS 1129
|
....*...
gi 490930577 979 GKVDKKAL 986
Cdd:PRK08633 1130 GKLDLKGL 1137
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
2148-2265 |
4.86e-10 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 61.47 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2148 FYPGSGsAWQYTVLNRYLHSDLPIIGLQSP--RPDGLLAnsTDMDELVEKQLEIMRKQQPTGPYTLLGYSLGGTVAYAVA 2225
Cdd:smart00824 6 TAAPSG-PHEYARLAAALRGRRDVSALPLPgfGPGEPLP--ASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHAVA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490930577 2226 AKLTEQGEKVDYLGLLDTYPAE---IHQWLDLSVEEMNAEAEQ 2265
Cdd:smart00824 83 ARLEARGIPPAAVVLLDTYPPGdpaPEGWLPELLRGVFEREDS 125
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
616-981 |
7.84e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 64.25 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 616 AENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-NLI--------LSHKPTIYWPVLeavnerfpdrPLraahTHSFS 686
Cdd:PRK05605 211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAqgkawvpgLGDGPERVLAAL----------PM----FHAYG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 687 FdsSWLQVFWMLWGQELHIFD--------ENMRRD--AF---------GLVQEIQQRQID----------TLDLPPSFCA 737
Cdd:PRK05605 277 L--TLCLTLAVSIGGELVLLPapdidlilDAMKKHppTWlpgvpplyeKIAEAAEERGVDlsgvrnafsgAMALPVSTVE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 738 --QMMTNGLFVEnqhhpsliligG----EAAPLALWQQLNAqpalfahnlygpteytvdtfraelkqTARP-VIGNPIGN 810
Cdd:PRK05605 355 lwEKLTGGLLVE-----------GygltETSPIIVGNPMSD--------------------------DRRPgYVGVPFPD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 811 TQAYVLDRH-LQRC-PTGVIGELYISGFGIANGYLGRADLSAARFvanpfeHGQrMYRTGDLVRWNSAGKLEFMGRCDDQ 888
Cdd:PRK05605 398 TEVRIVDPEdPDETmPDGEEGELLVRGPQVFKGYWNRPEETAKSF------LDG-WFRTGDVVVMEEDGFIRIVDRIKEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 889 IKIRGYRVEIGEVENALSILTNVESAVVIAEPINNShrllGYCVVKDIELDEktSEQLSQQYLSQ-LRQNLPEYMVPSAL 967
Cdd:PRK05605 471 IITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDG----SEEVVAAVVLEP--GAALDPEGLRAyCREHLTRYKVPRRF 544
|
410
....*....|....
gi 490930577 968 TVMSEFPRNVSGKV 981
Cdd:PRK05605 545 YHVDELPRDQLGKV 558
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
487-980 |
1.06e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 63.83 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYP---- 562
Cdd:cd05943 83 DDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGvpgv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 563 IDRMQMMcedaNPLFVLT----------------TQALAQQLPQNIQQLHLD--QEGVQTQIRKQ-----------DASD 613
Cdd:cd05943 163 LDRFGQI----EPKVLFAvdaytyngkrhdvrekVAELVKGLPSLLAVVVVPytVAAGQPDLSKIakaltledflaTGAA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 614 IPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvLEAVNErfpdrplraahtHSFSFDSSWLQ 693
Cdd:cd05943 239 GELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTL--------------LQHLKE------------HILHCDLRPGD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 694 VF-------WMLW---------GQELHIFDEN-MRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-PSLI 755
Cdd:cd05943 293 RLfyyttcgWMMWnwlvsglavGATIVLYDGSpFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDlSSLR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 756 LIGGEAAPLA----LWQQLNAQPALFAHNLYGPTEyTVDTFraelkqtarpVIGNPI-----GNTQAYVLDRHLQ----- 821
Cdd:cd05943 373 TILSTGSPLKpesfDYVYDHIKPDVLLASISGGTD-IISCF----------VGGNPLlpvyrGEIQCRGLGMAVEafdee 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 822 -RCPTGVIGELYI-SGF-GIANGYLGRADlsAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:cd05943 442 gKPVWGEKGELVCtKPFpSMPVGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGT 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 899 GEVENALSILTNVESAVVIAE--PINNSHRLLGYCVVKDIELDektsEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRN 976
Cdd:cd05943 520 AEIYRVVEKIPEVEDSLVVGQewKDGDERVILFVKLREGVELD----DELRKRIRSTIRSALSPRHVPAKIIAVPDIPRT 595
|
....
gi 490930577 977 VSGK 980
Cdd:cd05943 596 LSGK 599
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
469-986 |
1.32e-09 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 63.50 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 469 PEQYNNVLDIFYEQVKKYPERTAIVSGERPnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVL 548
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPAFICMGKA----ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 549 NSGAS-------FLPLDLDYpidrmQMMCEDANPLFVLTTQA-LAQQLPQNIQQLHL------DQEGVQTQI-----RKQ 609
Cdd:PRK07059 95 RAGYVvvnvnplYTPRELEH-----QLKDSGAEAIVVLENFAtTVQQVLAKTAVKHVvvasmgDLLGFKGHIvnfvvRRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 610 D----ASDIP---------AENRKFDFQ-------DVAYVIFTSGSTGRPKGVMNTHGSLL-NLILSHKptiyWpvLEAV 668
Cdd:PRK07059 170 KkmvpAWSLPghvrfndalAEGARQTFKpvklgpdDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQMEA----W--LQPA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 669 NERFPDR---------PLraahTHSFSfdsswLQVFWMLwgqelhifdeNMR-----------RDAFGLVQEIQQRQIDT 728
Cdd:PRK07059 244 FEKKPRPdqlnfvcalPL----YHIFA-----LTVCGLL----------GMRtggrnilipnpRDIPGFIKELKKYQVHI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 729 ldlppsFCAqmmTNGLFVENQHHP--------SLIL-IGGEAA---PLA-LWQQLNAQPAlfaHNLYGPTE--------- 786
Cdd:PRK07059 305 ------FPA---VNTLYNALLNNPdfdkldfsKLIVaNGGGMAvqrPVAeRWLEMTGCPI---TEGYGLSEtspvatcnp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 787 YTVDTFRAelkqtarpVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYR 866
Cdd:PRK07059 373 VDATEFSG--------TIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 867 TGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNSHRLLGYCVV-KDIELDEktseq 945
Cdd:PRK07059 439 TGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVkKDPALTE----- 513
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 490930577 946 lsQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07059 514 --EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1676-2031 |
1.36e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 63.61 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1676 HPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFDVSVWEFFWSYL-VGARLV------IAP 1748
Cdd:PTZ00237 255 HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLsLGNTFVmfeggiIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IDAHRDplaLLSLIQKYQVTTLHFVPSMLAVFENA---ATEILSSAQRQSLPicRVFCSGEALPTALAKSFTEHFSCELH 1825
Cdd:PTZ00237 335 KHIEDD---LWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLK--EIWCGGEVIEESIPEYIENKLKIKSS 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1826 NLYGPTEAAVdvsymdatlglhpeesCVAIGYPVWNTQLYIL---DQYLRPVPVGVDG------ELYLAGHQLAM--GYl 1894
Cdd:PTZ00237 410 RGYGQTEIGI----------------TYLYCYGHINIPYNATgvpSIFIKPSILSEDGkelnvnEIGEVAFKLPMppSF- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1895 hradltASRFVANP------FTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQ-LRLISGLDVVVH 1967
Cdd:PTZ00237 473 ------ATTFYKNDekfkqlFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSiLKHPLVLECCSI 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1968 AISSeQNKANVqLVAYL-----QTTAPVDIDQLKKQ----LAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PTZ00237 547 GIYD-PDCYNV-PIGLLvlkqdQSNQSIDLNKLKNEinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2052-2111 |
1.45e-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: 56.03 E-value: 1.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 2052 HELTRIFQQILNTD-QNIGVNEDFFAIGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQ 2111
Cdd:pfam00550 1 ERLRELLAEVLGVPaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1536-1956 |
1.46e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 63.44 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1536 QLLReqARITPEQTAL-SDENH---QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYL- 1610
Cdd:cd05943 75 NLLR--HADADDPAAIyAAEDGertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSs 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1611 --P-------IDLQHPTE-RIKFM---------LQDAKSKL--VIGEQKDLAAIVHpsIATFAFNELFDETK----VDLS 1665
Cdd:cd05943 153 csPdfgvpgvLDRFGQIEpKVLFAvdaytyngkRHDVREKVaeLVKGLPSLLAVVV--VPYTVAAGQPDLSKiakaLTLE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1666 SYKTTVITPQ---------HPAYLIYTSGTTGQPKGVMVSH-----QAIVNRILwmQSEypLSATDTILQKTPCTFdvSV 1731
Cdd:cd05943 231 DFLATGAAGElefeplpfdHPLYILYSSGTTGLPKCIVHGAggtllQHLKEHIL--HCD--LRPGDRLFYYTTCGW--MM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1732 WEFFWSYL-VGARLVI---APidAHRDPLALLSLIQKYQVTTLHFVPSMLAVFENAAteiLSSAQRQSLPICRVFCS-GE 1806
Cdd:cd05943 305 WNWLVSGLaVGATIVLydgSP--FYPDTNALWDLADEEGITVFGTSAKYLDALEKAG---LKPAETHDLSSLRTILStGS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1807 ALPTALAKSFTEH--FSCELHNLYGPTEAAVDVSYMDATLGLHPEE-SCVAIGYPVwntqlYILDQYLRPVpVGVDGELY 1883
Cdd:cd05943 380 PLKPESFDYVYDHikPDVLLASISGGTDIISCFVGGNPLLPVYRGEiQCRGLGMAV-----EAFDEEGKPV-WGEKGELV 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490930577 1884 LAGHQLAM--GYLHRADltASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQL 1956
Cdd:cd05943 454 CTKPFPSMpvGFWNDPD--GSRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVV 526
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
474-884 |
1.69e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 62.99 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 474 NVLDIFYEQVKKYPERTAIV------SGERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSV 547
Cdd:PRK09274 7 NIARHLPRAAQERPDQLAVAvpggrgADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 548 LNSGAsfLPLDLDYPIDRMQMM-C-EDANPLfVLTTQALAQQL-------PQNIQQL-----HLDQEGVQ-TQIRkQDAS 612
Cdd:PRK09274 87 FKAGA--VPVLVDPGMGIKNLKqClAEAQPD-AFIGIPKAHLArrlfgwgKPSVRRLvtvggRLLWGGTTlATLL-RDGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 613 DIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNLIlshkptiywpvlEAVNERFPDRPlraahthsFSFDSSWL 692
Cdd:PRK09274 163 AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQI------------EALREDYGIEP--------GEIDLPTF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 693 QVFwmlwgqELH---------IFDENMRRDAFG----LVQEIQQRQIDTLdlppsFC--AQMMTNGLFVENQHH--PSL- 754
Cdd:PRK09274 223 PLF------ALFgpalgmtsvIPDMDPTRPATVdpakLFAAIERYGVTNL-----FGspALLERLGRYGEANGIklPSLr 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 755 -ILIGGEAAPLALWQQLNA---QPALFaHNLYGPTE---YTVDTFRAELKQTA------------RPVIG---------- 805
Cdd:PRK09274 292 rVISAGAPVPIAVIERFRAmlpPDAEI-LTPYGATEalpISSIESREILFATRaatdngagicvgRPVDGvevriiaisd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 806 NPIgntqayvldRHLQ---RCPTGVIGELYISGFGIANGYLGRADLSAARFVANPfeHGQRMYRTGDLVRWNSAGKLEFM 882
Cdd:PRK09274 371 API---------PEWDdalRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFC 439
|
..
gi 490930577 883 GR 884
Cdd:PRK09274 440 GR 441
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
482-986 |
2.02e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 62.85 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 482 QVKKYPERTAIVSGErpnlQHLSFAELAVKVNqltrflqengARKQTVIAGAIPRSiDSVVVMLS--------VLNS--- 550
Cdd:PRK06155 30 QAERYPDRPLLVFGG----TRWTYAEAARAAA----------AAAHALAAAGVKRG-DRVALMCGnriefldvFLGCawl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 551 GASFLPLDLDYPIDRMQMMCEDANP-LFVLTTQALA--QQLPQNIQQLH----LDQEGVQTQIRKQDASDIPAENRKFDF 623
Cdd:PRK06155 95 GAIAVPINTALRGPQLEHILRNSGArLLVVEAALLAalEAADPGDLPLPavwlLDAPASVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 624 QDV-----AYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiYWPVLEA----VNER---FPDRPLraAHTHSFSfdsSW 691
Cdd:PRK06155 175 AAVqpgdtAAILYTSGTTGPSKGVCCPHAQFY----------WWGRNSAedleIGADdvlYTTLPL--FHTNALN---AF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 692 LQVfwMLWGQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGeAAPLALWQQLN 771
Cdd:PRK06155 240 FQA--LLAGATYVLEP---RFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGP-GVPAALHAAFR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 772 AQPALFAHNLYGPTEYTVDTfrAELKQTARP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISG---FGIANGYLGRAD 847
Cdd:PRK06155 314 ERFGVDLLDGYGSTETNFVI--AVTHGSQRPgSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 848 LSAARFvANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRL 927
Cdd:PRK06155 392 KTVEAW-RNLWFH------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP----SEL 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 928 LGYCVVKDIELDEKTS---EQLSQQYLSQlrqnLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK06155 461 GEDEVMAAVVLRDGTAlepVALVRHCEPR----LAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
490-999 |
2.34e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 62.49 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 490 TAIVSGERPNLQHLSFAELAVKVNQLTRFLQEN-GARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQM 568
Cdd:PRK05620 26 TTVTTWGGAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 569 MCEDANPLFVLTTQALAQQLPQNIQQLhldqEGVQTQI----------RKQDASDIPAENRK---------FDFQDV--- 626
Cdd:PRK05620 106 IINHAEDEVIVADPRLAEQLGEILKEC----PCVRAVVfigpsdadsaAAHMPEGIKVYSYEalldgrstvYDWPELdet 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 627 --AYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvLEAVNERFPDRplrAAHTHSFSFDS--------SWLQVF- 695
Cdd:PRK05620 182 taAAICYSTGTTGAPKGVVYSHRSLY--------------LQSLSLRTTDS---LAVTHGESFLCcvpiyhvlSWGVPLa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 696 -WM------LWGQEL------HIFDENMRRDAFGLvqeiqqrqidtldlpPSFCAQMMTNGLfvenQHHP---SL--ILI 757
Cdd:PRK05620 245 aFMsgtplvFPGPDLsaptlaKIIATAMPRVAHGV---------------PTLWIQLMVHYL----KNPPermSLqeIYV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 758 GGEAAPLALWQQLNAQPALFAHNLYGPTEY-TVDTfraelkqTARPvignPIG-NTQAYVLDRHLQ-RCPTGV------- 827
Cdd:PRK05620 306 GGSAVPPILIKAWEERYGVDVVHVWGMTETsPVGT-------VARP----PSGvSGEARWAYRVSQgRFPASLeyrivnd 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 828 ----------IGELYISGFGIANGYL----GRADLSAARFVANPFEHGQRMY------RTGDLVRWNSAGKLEFMGRCDD 887
Cdd:PRK05620 375 gqvmestdrnEGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 888 QIKIRGYRVEIGEVENALSILTNVESAVVIAEPINN-SHRLLGYCVVKD-IELDEKTSEQLSqqylSQLRQNLPEYMVPS 965
Cdd:PRK05620 455 VIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLAVTVLAPgIEPTRETAERLR----DQLRDRLPNWMLPE 530
|
570 580 590
....*....|....*....|....*....|....
gi 490930577 966 ALTVMSEFPRNVSGKVDKKALpkpqiRAHSRMAE 999
Cdd:PRK05620 531 YWTFVDEIDKTSVGKFDKKDL-----RQHLADGD 559
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
501-986 |
2.58e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 62.23 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 501 QHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCED-------A 573
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDsgakvliV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 574 NPLFVLTTQALAQQLPQNIQQLHLDQEGVQTQIR------KQDASDIPAENRKFDFQdvayviFTSGSTGRPKGVMnthg 647
Cdd:PRK08276 90 SAALADTAAELAAELPAGVPLLLVVAGPVPGFRSyeealaAQPDTPIADETAGADML------YSSGTTGRPKGIK---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 648 sllnlilshkptiywpvleavnerfpdRPLRAAHTHSFSFDSSWLQVFWM--------------------LWGQELH--- 704
Cdd:PRK08276 160 ---------------------------RPLPGLDPDEAPGMMLALLGFGMyggpdsvylspaplyhtaplRFGMSALalg 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 705 ---IFDEnmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQH-HPSLILIGGEAAPLAlwQQLNAQ------P 774
Cdd:PRK08276 213 gtvVVME--KFDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYdVSSLRVAIHAAAPCP--VEVKRAmidwwgP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 775 ALfaHNLYGPTE---YTVDTFRAELKQ---TARPVIGnpigntQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADL 848
Cdd:PRK08276 289 II--HEYYASSEgggVTVITSEDWLAHpgsVGKAVLG------EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 849 SAARfvanpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIRGyRVEI--GEVENALSILTNVESAVVIAEPinnsHR 926
Cdd:PRK08276 361 TAAA------RNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISG-GVNIypQEIENLLVTHPKVADVAVFGVP----DE 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 927 LLGYCVVKDIELDEKT--SEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK08276 429 EMGERVKAVVQPADGAdaGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
624-986 |
2.79e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 62.15 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 624 QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILShkptiywpVLEAVNERFPD-------------RPLRAAHTHSFSFDSS 690
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQ--------VRACLSQLGPDgqplmkegqevmiAPLPLYHIYAFTANCM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 691 WLqvfwMLWGQElHIFDENmRRDAFGLVQEIQQRQidtldlppsFCAQMMTNGLFVENQHHPSLILI----------GGE 760
Cdd:PRK12492 279 CM----MVSGNH-NVLITN-PRDIPGFIKELGKWR---------FSALLGLNTLFVALMDHPGFKDLdfsalkltnsGGT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 761 A---APLALWQQLNAQPALFAhnlYGPTEYTVDTFRAELKQTAR-PVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGF 836
Cdd:PRK12492 344 AlvkATAERWEQLTGCTIVEG---YGLTETSPVASTNPYGELARlGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 837 GIANGYLGRADLSAARFVAnpfehgQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVV 916
Cdd:PRK12492 421 QVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAA 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 917 IAEPINNSHRLLGYCVVkdieldeKTSEQLSQQYLSQL-RQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK12492 495 IGVPDERSGEAVKLFVV-------ARDPGLSVEELKAYcKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
477-983 |
3.27e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 62.10 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSgeRPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA---- 552
Cdd:PRK12583 22 DAFDATVARFPDREALVV--RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAilvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 553 ---SFLPLDLDYPI-----------------DRMQMMCEDANPLFVLTTQALA-QQLPQNIQQLHLDQE---------GV 602
Cdd:PRK12583 100 inpAYRASELEYALgqsgvrwvicadafktsDYHAMLQELLPGLAEGQPGALAcERLPELRGVVSLAPApppgflawhEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 603 QTQIRKQDASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLNlilshkptIYWPVLEAVNERFPDR-----PL 677
Cdd:PRK12583 180 QARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILN--------NGYFVAESLGLTEHDRlcvpvPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 678 raahTHSFSFDSSWLQVfwMLWGQELHIFDENMrrDAFGLVQEIQQRQIDTL-DLPPSFCAQMmtnglfvenqHHP---- 752
Cdd:PRK12583 252 ----YHCFGMVLANLGC--MTVGACLVYPNEAF--DPLATLQAVEEERCTALyGVPTMFIAEL----------DHPqrgn 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 753 ----SLI--LIGGEAAPLALWQ----QLNAQPALFAhnlYGPTEYTVDTFraelkQTAR----PVIGNPIGNTQAY---- 814
Cdd:PRK12583 314 fdlsSLRtgIMAGAPCPIEVMRrvmdEMHMAEVQIA---YGMTETSPVSL-----QTTAaddlERRVETVGRTQPHlevk 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 815 VLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIkIRG- 893
Cdd:PRK12583 386 VVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMH------TGDLATMDEQGYVRIVGRSKDMI-IRGg 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 894 ---YRVEIgevENALSILTNVESAVVIAEPINNshrlLGYCVVKDIELdeKTSEQLSQQYLSQL-RQNLPEYMVPSALTV 969
Cdd:PRK12583 459 eniYPREI---EEFLFTHPAVADVQVFGVPDEK----YGEEIVAWVRL--HPGHAASEEELREFcKARIAHFKVPRYFRF 529
|
570
....*....|....
gi 490930577 970 MSEFPRNVSGKVDK 983
Cdd:PRK12583 530 VDEFPMTVTGKVQK 543
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
631-983 |
3.71e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 61.14 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 631 FTSGSTGRPKGVMNTHGSLLN--------LILSHKPTIYWPVleavnerfpdrPLraahTHSFSfdsSWLQVFWML-WGQ 701
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNngyfigerLGLTEQDRLCIPV-----------PL----FHCFG---SVLGVLACLtHGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 702 ELhIFDENMRrDAFGLVQEIQQRQIDTL-DLPPSFCAQMmtnglfvenqHHPSLI----------LIGGEAAPLALW--- 767
Cdd:cd05917 71 TM-VFPSPSF-DPLAVLEAIEKEKCTALhGVPTMFIAEL----------EHPDFDkfdlsslrtgIMAGAPCPPELMkrv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 768 -QQLNAQPALFAhnlYGPTEYTVDTFRAELKQTARPVI---GNPIGNTQAYVLD-RHLQRCPTGVIGELYISGFGIANGY 842
Cdd:cd05917 139 iEVMNMKDVTIA---YGMTETSPVSTQTRTDDSIEKRVntvGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 843 LGRADLSAARfvanpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIRG----YRVEIgevENALSILTNVESAVVIA 918
Cdd:cd05917 216 WNDPEKTAEA------IDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgeniYPREI---EEFLHTHPKVSDVQVVG 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490930577 919 EPinnsHRLLGYCVVKDIEL--DEKTSEQLSQQYLsqlRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:cd05917 286 VP----DERYGEEVCAWIRLkeGAELTEEDIKAYC---KGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
841-988 |
4.39e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 61.29 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 841 GYLGRADlSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd05939 328 GYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVE 406
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 921 INNSHRLLGYCVVKDIEldektsEQLSQQYLSQ-LRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05939 407 VPGVEGRAGMAAIVDPE------RKVDLDRFSAvLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
822-964 |
5.08e-09 |
|
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: 61.22 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 822 RCPTGVIGEL--YISGFGIANGYLGRADlSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIG 899
Cdd:cd05940 281 KVPRGEPGLLisRINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTT 359
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 900 EVENALSILTNVESAVVIAEPINNSHrllGYCVVKDIELDEKTSEQLSQqyLSQ-LRQNLPEYMVP 964
Cdd:cd05940 360 EVAAVLGAFPGVEEANVYGVQVPGTD---GRAGMAAIVLQPNEEFDLSA--LAAhLEKNLPGYARP 420
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
625-994 |
5.83e-09 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 61.35 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiywpvLEAVNERFPDRPLRAA---HTHSFSfdsswlQVFWMLWGQ 701
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALIVQSLAK--------IAIVGYGEDDVYLHTAplcHIGGLS------SALAMLMVG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 702 ELHIFDENMrrDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQH-HPSL--ILIGGEAAPLALWQ---QLNAQPA 775
Cdd:PLN02860 239 ACHVLLPKF--DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKvFPSVrkILNGGGSLSSRLLPdakKLFPNAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 776 LFAhnLYGPTE------------YTVDTFRAELKQTARPV-------IGNPIGNTQAYVldrHLQRCPTGV--IGELYIS 834
Cdd:PLN02860 317 LFS--AYGMTEacssltfmtlhdPTLESPKQTLQTVNQTKsssvhqpQGVCVGKPAPHV---ELKIGLDESsrVGRILTR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 835 GFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESA 914
Cdd:PLN02860 392 GPHVMLGYWGQNSETASVLSNDGW------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 915 VVIAEPinnSHRlLGYCVVKDIEL------------DEKTSEQLSQQYLSQ--LRQNLPEYMVPSALTVMSE-FPRNVSG 979
Cdd:PLN02860 466 VVVGVP---DSR-LTEMVVACVRLrdgwiwsdnekeNAKKNLTLSSETLRHhcREKNLSRFKIPKLFVQWRKpFPLTTTG 541
|
410
....*....|....*
gi 490930577 980 KVdKKALPKPQIRAH 994
Cdd:PLN02860 542 KI-RRDEVRREVLSH 555
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
828-992 |
5.87e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 61.19 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 828 IGELYISGFGIANGYLgradlSAARFVANPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PLN03102 392 MGEIVIKGSSIMKGYL-----KNPKATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 908 LTNVESAVVIAEPinnsHRLLGY--CVVKDIELDEKTSEQLSQQYLSQ-------LRQNLPEYMVPSALTVMSEFPRNVS 978
Cdd:PLN03102 465 YPKVLETAVVAMP----HPTWGEtpCAFVVLEKGETTKEDRVDKLVTRerdlieyCRENLPHFMCPRKVVFLQELPKNGN 540
|
170
....*....|....
gi 490930577 979 GKVdkkalPKPQIR 992
Cdd:PLN03102 541 GKI-----LKPKLR 549
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1004-1062 |
7.89e-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: 53.72 E-value: 7.89e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 1004 QLLCQITASVLKLDA--IGIDDDFFMTGGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAA 1062
Cdd:pfam00550 1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
805-988 |
7.89e-09 |
|
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: 60.79 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 805 GNPIGNTQAYVLDRHLQRCPTGVIGELYISGfGIANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGR 884
Cdd:cd05967 414 GKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 885 CDDQIKIRGYRVEIGEVENALSILTNV-ESAVVIAEPINNSHRLLGYCVVKdiELDEKTSEQLSQQYLSQLRQNLPEYMV 963
Cdd:cd05967 493 TDDVINVAGHRLSTGEMEESVLSHPAVaECAVVGVRDELKGQVPLGLVVLK--EGVKITAEELEKELVALVREQIGPVAA 570
|
170 180
....*....|....*....|....*
gi 490930577 964 PSALTVMSEFPRNVSGKVDKKALPK 988
Cdd:cd05967 571 FRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1535-1772 |
1.68e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 59.81 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1535 QQLLREQAritPEQTAL--SDENH---QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILA-------- 1601
Cdd:PRK03584 90 ENLLRHRR---DDRPAIifRGEDGprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLAtaslgaiw 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1602 -----------VIE-----------AGAAYL----PIDLqhpTERIKFMLQDAKS--KLVIGEQKDLAAIVHPSIATFAF 1653
Cdd:PRK03584 167 sscspdfgvqgVLDrfgqiepkvliAVDGYRyggkAFDR---RAKVAELRAALPSleHVVVVPYLGPAAAAAALPGALLW 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1654 NELfdetkvdLSSYKTTVITPQ-----HPAYLIYTSGTTGQPKGVMVSHQAIV-NRILWMQSEYPLSATDTILQKTPCTf 1727
Cdd:PRK03584 244 EDF-------LAPAEAAELEFEpvpfdHPLWILYSSGTTGLPKCIVHGHGGILlEHLKELGLHCDLGPGDRFFWYTTCG- 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490930577 1728 dvsvWeFFWSYLV-----GARLVI---APidAHRDPLALLSLIQKYQVTtlHF 1772
Cdd:PRK03584 316 ----W-MMWNWLVsgllvGATLVLydgSP--FYPDPNVLWDLAAEEGVT--VF 359
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1678-2031 |
1.91e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 58.90 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVNrilwmqseyplSATDT---------ILQKTPCTFDVSVWEFFWSYLVGARLVIAP 1748
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTA-----------SADAThdrlggpgqWLLALPAHHIAGLQVLVRSVIAGSEPVELD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IDAHRDPLALLSLIQ------KYqvTTLhfVPSML--AVFENAATEILSSaqrqslpICRVFCSGEALPTALAKSftehf 1820
Cdd:PRK07824 107 VSAGFDPTALPRAVAelgggrRY--TSL--VPMQLakALDDPAATAALAE-------LDAVLVGGGPAPAPVLDA----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1821 scelhnlygPTEAAVDV--SY-MDATLGlhpeeSCVAIGYPVWNTQLYIldqylrpvpvgVDGELYLAGHQLAMGYLHRA 1897
Cdd:PRK07824 171 ---------AAAAGINVvrTYgMSETSG-----GCVYDGVPLDGVRVRV-----------EDGRIALGGPTLAKGYRNPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1898 DltasrfvaNPFTAGQRMYRTGDIARWHaDGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAISSEQNKA 1976
Cdd:PRK07824 226 D--------PDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVaDCAVFGLPDDRLGQ 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 1977 NVqLVAYLQTTAPVD-IDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:PRK07824 297 RV-VAAVVGDGGPAPtLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
997-1064 |
3.05e-08 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 52.55 E-value: 3.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 997 MAETPEQQLLCQITASVLKLDA--IGIDDDFFMT-GGDSISAIMLCTQLRQR-GYSLRPSDVFQFKTVAAMA 1064
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDPeeITPDDSFFEDlGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLA 72
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1558-2031 |
3.22e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 58.67 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1558 LSFSEVRLQVCALAQQLQRagvQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGEQ 1637
Cdd:PRK06334 46 LSYNQVRKAVIALATKVSK---YPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1638 K--DLAAIVHPSIATFAFNELFDET---------KVDLSSYKTTVIT------------PQHPAYLIYTSGTTGQPKGVM 1694
Cdd:PRK06334 123 QlmQHLAQTHGEDAEYPFSLIYMEEvrkelsfweKCRIGIYMSIPFEwlmrwfgvsdkdPEDVAVILFTSGTEKLPKGVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1695 VSHQA-IVNRILWMQSEYPLSaTDTILQKTP---------CTFdvsvweffWSYLVGARLVIA--PIDAHRdplaLLSLI 1762
Cdd:PRK06334 203 LTHANlLANQRACLKFFSPKE-DDVMMSFLPpfhaygfnsCTL--------FPLLSGVPVVFAynPLYPKK----IVEMI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1763 QKYQVTTLHFVPSMLAVfenaateILSSAQRQ--SLPICR-VFCSGEALPTALAKSFTEHF-SCELHNLYGPTEAAVDVS 1838
Cdd:PRK06334 270 DEAKVTFLGSTPVFFDY-------ILKTAKKQesCLPSLRfVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTECSPVIT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1839 YMDATLGLHpeESCVaiGYPVWNTQLYILDQYLR-PVPVGVDGELYLAGHQLAMGYLHrADLTASrFVAnpfTAGQRMYR 1917
Cdd:PRK06334 343 INTVNSPKH--ESCV--GMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLG-EDFGQG-FVE---LGGETWYV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1918 TGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGLD-------VVVHAISSEQnkanVQLVayLQTTAPV 1990
Cdd:PRK06334 414 TGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNaadhagpLVVCGLPGEK----VRLC--LFTTFPT 487
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 490930577 1991 DIDQLKKQLAKHLPAYMVPTHYM-LVEQFPLSHNGKLDRKAL 2031
Cdd:PRK06334 488 SISEVNDILKNSKTSSILKISYHhQVESIPMLGTGKPDYCSL 529
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
90-340 |
3.50e-08 |
|
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: 58.37 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 90 QVQFQIEEFDFCHLTPKKAQQRLWDWMPSDRQcaKSLKAGETQLFRQVLFTTHDKVYWY-QRYHHIMLDGFSMINLTKRI 168
Cdd:cd19543 74 DRKLPWRELDLSHLSEAEQEAELEALAEEDRE--RGFDLARAPLMRLTLIRLGDDRYRLvWSFHHILLDGWSLPILLKEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 169 VELYQQLQEGKDLS---VSPFigvneviSERQAYENSHQFKIDQAFWKAYCEDLPSPISLSTHHLA-AKTTATFVKHQLR 244
Cdd:cd19543 152 FAIYAALGEGQPPSlppVRPY-------RDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPAdADGSYEPGEVSFE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 245 FSTGILEQIQALAAQTKLALNDMMM---SLSLHyiyKMTDKAELVNGI-----PfmrrlgskairSTLPTV--------N 308
Cdd:cd19543 225 LSAELTARLQELARQHGVTLNTVVQgawALLLS---RYSGRDDVVFGTtvsgrP-----------AELPGIetmvglfiN 290
|
250 260 270
....*....|....*....|....*....|..
gi 490930577 309 VLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQ 340
Cdd:cd19543 291 TLPVRVRLDPDQTVLELLKDLQAQQLELREHE 322
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
474-981 |
4.03e-08 |
|
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: 58.73 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 474 NVLDifyEQVKKYPERTAIV-SGERPN-LQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVML------ 545
Cdd:cd05966 57 NCLD---RHLKERGDKVAIIwEGDEPDqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLacarig 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 546 ---SVLNSGASFLPLdldypIDRMqmmcEDANPLFVLTT-----------------QALaQQLP--QNI---QQLHLD-- 598
Cdd:cd05966 134 avhSVVFAGFSAESL-----ADRI----NDAQCKLVITAdggyrggkviplkeivdEAL-EKCPsvEKVlvvKRTGGEvp 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 599 -QEGV----QTQIRKQDAsDIPAEnrKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvleavnerfp 673
Cdd:cd05966 204 mTEGRdlwwHDLMAKQSP-ECEPE--WMDSEDPLFILYTSGSTGKPKGVVHTTGGYL----------------------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 674 drpLRAAHTHSFSFDSSWLQVFW------------------MLWGQELHIFDENMRRDAFGLVQEIQQR-QIDTLDLPPS 734
Cdd:cd05966 258 ---LYAATTFKYVFDYHPDDIYWctadigwitghsyivygpLANGATTVMFEGTPTYPDPGRYWDIVEKhKVTIFYTAPT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 735 FCAQMMTNG-LFVENQHHPSLILIG--GEaaPLalwqqlNAQPALFAHNLYGPTEYT-VDTFRaelkQT----------- 799
Cdd:cd05966 335 AIRALMKFGdEWVKKHDLSSLRVLGsvGE--PI------NPEAWMWYYEVIGKERCPiVDTWW----QTetggimitplp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 800 ----------ARPVIGnpignTQAYVLDRHLQRCPTGVIGELYISGF--GIANGYLGradlSAARFVANPFEHGQRMYRT 867
Cdd:cd05966 403 gatplkpgsaTRPFFG-----IEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYG----DHERYEDTYFSKFPGYYFT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 868 GDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHRLLG-----YCVVKDielDEKT 942
Cdd:cd05966 474 GDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRP----HDIKGeaiyaFVTLKD---GEEP 546
|
570 580 590
....*....|....*....|....*....|....*....
gi 490930577 943 SEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKV 981
Cdd:cd05966 547 SDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI 585
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
604-992 |
4.17e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 58.81 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 604 TQIRKQDASDIPAEnRKFDFQDVAYVIFTSGSTGRPKGVMNTHGS------LLNLILSHKP--TIYWPV-LEAVNerfpd 674
Cdd:PRK07529 194 AELARQPGDRLFSG-RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanawLGALLLGLGPgdTVFCGLpLFHVN----- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 675 rplrAAHTHSFSFDSSWLQVfwmLWGQELHIFDENMRRDAFGLVQeiqQRQIDTLDLPPSFCAQMM---TNGLFVEnqhh 751
Cdd:PRK07529 268 ----ALLVTGLAPLARGAHV---VLATPQGYRGPGVIANFWKIVE---RYRINFLSGVPTVYAALLqvpVDGHDIS---- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 752 pSL-ILIGGEAA-PLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQAYVL-----DRHLQRC 823
Cdd:PRK07529 334 -SLrYALCGAAPlPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIgSVGLRLPYQRVRVVilddaGRYLRDC 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 824 PTGVIGELYISGFGIANGYLgRADLSAARFVanpfehGQRMYRTGDLVRWNSAGKLEFMGRCDDQIkIR-GYRVEIGEVE 902
Cdd:PRK07529 413 AVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 903 NALSILTNVESAVVIAEPinNSHRllGYCVVKDIELDEKTSEQlSQQYLSQLRQNLPE-YMVPSALTVMSEFPRNVSGKV 981
Cdd:PRK07529 485 EALLRHPAVALAAAVGRP--DAHA--GELPVAYVQLKPGASAT-EAELLAFARDHIAErAAVPKHVRILDALPKTAVGKI 559
|
410
....*....|.
gi 490930577 982 DKKALPKPQIR 992
Cdd:PRK07529 560 FKPALRRDAIR 570
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
2138-2232 |
6.20e-08 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 56.01 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2138 RSGSGHPLFCFYPGSGSAWQYTVLNRYLHSDLPIIGLQSP-----RPDGLLansTDMDELVEKQLEIMRkQQPTGPYTLL 2212
Cdd:COG3208 2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPgrgdrLGEPPL---TSLEELADDLAEELA-PLLDRPFALF 77
|
90 100
....*....|....*....|
gi 490930577 2213 GYSLGGTVAYAVAAKLTEQG 2232
Cdd:COG3208 78 GHSMGALLAFELARRLERRG 97
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
488-655 |
8.22e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 57.83 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 488 ERTAIVSGERPNLQHLSFAE----LAVKV--NQLTRFLQENGARKQTV------IAGAIPRSIDSVVVMLSVLNSGASFL 555
Cdd:PRK12476 41 ERNIANVGDTVAYRYLDHSHsaagCAVELtwTQLGVRLRAVGARLQQVagpgdrVAILAPQGIDYVAGFFAAIKAGTIAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 556 PL---DLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQNIQQL-HLDQEGVQT--QIRKQDASD-IPAEnrkFDFQDVAY 628
Cdd:PRK12476 121 PLfapELPGHAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLpRLRRPRVIAidAIPDSAGESfVPVE---LDTDDVSH 197
|
170 180 190
....*....|....*....|....*....|.
gi 490930577 629 VIFTSGSTGRPKGVMNTHGS----LLNLILS 655
Cdd:PRK12476 198 LQYTSGSTRPPVGVEITHRAvgtnLVQMILS 228
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1667-1965 |
8.51e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 57.72 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1667 YKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRI-----LWMQSEYPLSATDTILQKTPCT--FDVSVWEFFWSyl 1739
Cdd:PLN02614 215 YDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIagvirLLKSANAALTVKDVYLSYLPLAhiFDRVIEECFIQ-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1740 VGARLVIAPIDAHrdplALLSLIQKYQVTTLHFVPSML-------------------AVFENAATEILSSAQR-----QS 1795
Cdd:PLN02614 293 HGAAIGFWRGDVK----LLIEDLGELKPTIFCAVPRVLdrvysglqkklsdggflkkFVFDSAFSYKFGNMKKgqshvEA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1796 LPIC----------------RVFCSGEALPTALAKSFTEHFSCeLHNL--YGPTEAAVdvsymdATLGLHPEESCV--AI 1855
Cdd:PLN02614 369 SPLCdklvfnkvkqglggnvRIILSGAAPLASHVESFLRVVAC-CHVLqgYGLTESCA------GTFVSLPDELDMlgTV 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1856 GYPVWNtqlyiLDQYLRPVP-VGVD-------GELYLAGHQLAMGYLHRADLTASRFVANpftagqrMYRTGDIARWHAD 1927
Cdd:PLN02614 442 GPPVPN-----VDIRLESVPeMEYDalastprGEICIRGKTLFSGYYKREDLTKEVLIDG-------WLHTGDVGEWQPN 509
|
330 340 350
....*....|....*....|....*....|....*....
gi 490930577 1928 GSIQYIGRADDQLKI-RGQRIELGEIEQQLRLISGLDVV 1965
Cdd:PLN02614 510 GSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSV 548
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1519-2039 |
8.92e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 57.30 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1519 IQKTNQTQYYVR----------QSTLQQLLREQARITPEQTALSDE--NHQLSFSEVRLQVCALAQQLQRAGVQAGDIVA 1586
Cdd:PLN02330 5 IQKQEDNEHIFRsrypsvpvpdKLTLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1587 VALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVI------GEQKDLAAIV----HPSIAT-FAFNE 1655
Cdd:PLN02330 85 VVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVtndtnyGKVKGLGLPVivlgEEKIEGaVNWKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 LFDETKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILwmqSEYPLSATDTILQKTpctfDVSVWEFF 1735
Cdd:PLN02330 165 LLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLC---SSLFSVGPEMIGQVV----TLGLIPFF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1736 WSYLV-----------GARLVIAPIDAHrdplALLSLIQKYQVTTLHFVPS-MLAVFENAATEILSSAQrqsLPICRVFC 1803
Cdd:PLN02330 238 HIYGItgiccatlrnkGKVVVMSRFELR----TFLNALITQEVSFAPIVPPiILNLVKNPIVEEFDLSK---LKLQAIMT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1804 SGEALPTALAKSFTEHF-SCELHNLYGPTE-AAVDVSYMDATLGlHPEESCVAIGYPVWNTQLYILD-QYLRPVPVGVDG 1880
Cdd:PLN02330 311 AAAPLAPELLTAFEAKFpGVQVQEAYGLTEhSCITLTHGDPEKG-HGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1881 ELYLAGHQLAMGYLHRADLTASRFVAnpftagQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLIS 1960
Cdd:PLN02330 390 ELCVRSQCVMQGYYNNKEETDRTIDE------DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1961 GL-DVVVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQPHLTPS 2039
Cdd:PLN02330 464 SVeDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
487-986 |
1.44e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.56 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGERPnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGA-------SFLPLDL 559
Cdd:PRK13390 11 PDRPAVIVAETG--EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLyitainhHLTAPEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 560 DYpidrmqMMCEDANPLFVLTT--QALAQQLPQNIQqLHLDQEGVQTQIRKQDASDIPAENRKFDFQDVAYVIFTSGSTG 637
Cdd:PRK13390 89 DY------IVGDSGARVLVASAalDGLAAKVGADLP-LRLSFGGEIDGFGSFEAALAGAGPRLTEQPCGAVMLYSSGTTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 638 RPKGVMnthgsllnlilshkptiywPVLEAVNERFPDRPLRAAHTHSFSFDSSwlQVFW----------MLWGQELHIFD 707
Cdd:PRK13390 162 FPKGIQ-------------------PDLPGRDVDAPGDPIVAIARAFYDISES--DIYYssapiyhaapLRWCSMVHALG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 708 ENM----RRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-PSLILIGGEAAPL------ALWQQLNaqPAL 776
Cdd:PRK13390 221 GTVvlakRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDvSSLRAVIHAAAPCpvdvkhAMIDWLG--PIV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 777 FAHnlYGPTEY----TVDT--FRAELKQTARPVIGNpigntqAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSA 850
Cdd:PRK13390 299 YEY--YSSTEAhgmtFIDSpdWLAHPGSVGRSVLGD------LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 851 -ARFVANPFehgqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNshrlLG 929
Cdd:PRK13390 371 aAQHPAHPF-----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPE----MG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 930 YCVVKDIELDE--KTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK13390 442 EQVKAVIQLVEgiRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1525-1942 |
1.63e-07 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 56.69 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1525 TQYYVRQSTLQQLLReqaRITpeqtalsdenhqLSFSEVRLQVCALAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVI 1603
Cdd:cd17632 50 TDPATGRTTLRLLPR---FET------------ITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1604 EAGAAYLPIDLQHPTERIKFMLQDAKSKL--VIGEQKDLA------AIVHPSIATFAFNELFDETKVDLSSYKT------ 1669
Cdd:cd17632 115 RLGAVSVPLQAGASAAQLAPILAETEPRLlaVSAEHLDLAveavleGGTPPRLVVFDHRPEVDAHRAALESARErlaavg 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1670 -TVIT----------------------PQHPAYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSE---YPLSAtdTILQKT 1723
Cdd:cd17632 195 iPVTTltliavrgrdlppaplfrpepdDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIqdiRPPAS--ITLNFM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1724 PCTfdvSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIQKYQVTTLHFVP---SML-------------------AVFE 1781
Cdd:cd17632 273 PMS---HIAGRISLYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPrvcDMLfqryqaeldrrsvagadaeTLAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1782 NAATEIlssaqRQSLPICRV---FCSGEALpTALAKSFTEH-FSCELHNLYGPTEAAVDV--------SYMDATLGLHPE 1849
Cdd:cd17632 350 RVKAEL-----RERVLGGRLlaaVCGSAPL-SAEMKAFMESlLDLDLHDGYGSTEAGAVIldgvivrpPVLDYKLVDVPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1850 escvaIGYpvwntqlYILDqylRPVPvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDI-ARWHADg 1928
Cdd:cd17632 424 -----LGY-------FRTD---RPHP---RGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVmAELGPD- 478
|
490
....*....|....
gi 490930577 1929 SIQYIGRADDQLKI 1942
Cdd:cd17632 479 RLVYVDRRNNVLKL 492
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
503-988 |
1.73e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 56.83 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQ 582
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 583 ALAQQLP----QNIQQLHLD---QEGVQTQI--RKQDASDIPAENRKF------------------------DFQDVAYV 629
Cdd:PLN02654 201 AVKRGPKtinlKDIVDAALDesaKNGVSVGIclTYENQLAMKREDTKWqegrdvwwqdvvpnyptkcevewvDAEDPLFL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 630 IFTSGSTGRPKGVMNTHGSLLnlilshkptIYwpvleavnerfpdrplrAAHTHSFSFDSSWLQVFW------------- 696
Cdd:PLN02654 281 LYTSGSTGKPKGVLHTTGGYM---------VY-----------------TATTFKYAFDYKPTDVYWctadcgwitghsy 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 697 -----MLWGQELHIFDENMRRDAFGLVQEIQQR-QIDTLDLPPSFCAQMMTNGL-FVENQHHPSLILIGGEAAPLalwqq 769
Cdd:PLN02654 335 vtygpMLNGATVLVFEGAPNYPDSGRCWDIVDKyKVTIFYTAPTLVRSLMRDGDeYVTRHSRKSLRVLGSVGEPI----- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 770 lNAQPALFAHNLYGPTEYTV-DTFRaelkQTAR------PVIGN----------PIGNTQAYVLDRHLQRCPTGVIGELY 832
Cdd:PLN02654 410 -NPSAWRWFFNVVGDSRCPIsDTWW----QTETggfmitPLPGAwpqkpgsatfPFFGVQPVIVDEKGKEIEGECSGYLC 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 833 ISGF--GIANGYLGRADlsaaRFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENAL-SILT 909
Cdd:PLN02654 485 VKKSwpGAFRTLYGDHE----RYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALvSHPQ 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 910 NVESAVVIAEpinnsHRLLGYCVVKDIELDEKT--SEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKALP 987
Cdd:PLN02654 561 CAEAAVVGIE-----HEVKGQGIYAFVTLVEGVpySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
.
gi 490930577 988 K 988
Cdd:PLN02654 636 K 636
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1892-2031 |
1.98e-07 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 56.28 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1892 GYLHRADlTASRFVANPFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRLISGL-DVVVHAIS 1970
Cdd:cd05939 328 GYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLeDVVVYGVE 406
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1971 SEQNKANVQLVAYLQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKAL 2031
Cdd:cd05939 407 VPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
491-996 |
2.22e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 56.25 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 491 AIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMC 570
Cdd:PRK12406 4 TIISGDR----RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 571 EDANPLfVLTTQA-----LAQQLPQNIQQL------------------------HLDQEGVQTQIRKQDASDIPAEnrkf 621
Cdd:PRK12406 80 EDSGAR-VLIAHAdllhgLASALPAGVTVLsvptppeiaaayrispalltppagAIDWEGWLAQQEPYDGPPVPQP---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 622 dfqdvAYVIFTSGSTGRPKGVmnthgsllnlilshkptiywpvleavnERFPDRPLRAAhthsfsfdsSWLQVFWMLWGQ 701
Cdd:PRK12406 155 -----QSMIYTSGTTGHPKGV---------------------------RRAAPTPEQAA---------AAEQMRALIYGL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 702 ELHI----------------------FDENM----RRDAFGLVQEIQQRQIDT-----------LDLPPSFCAQMMTNGL 744
Cdd:PRK12406 194 KPGIralltgplyhsapnayglragrLGGVLvlqpRFDPEELLQLIERHRITHmhmvptmfirlLKLPEEVRAKYDVSSL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 745 fvenqhhpSLILIGGEAAPLALWQQLNAQPALFAHNLYGPTEYTVDTFRAELKQTARP-VIGNPIGNTQAYVLDRHLQRC 823
Cdd:PRK12406 274 --------RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALSHPgTVGKAAPGAELRFVDEDGRPL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 824 PTGVIGELYISGFGIAN-GYLG----RADLSAARFVAnpfehgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEI 898
Cdd:PRK12406 346 PQGEIGEIYSRIAGNPDfTYHNkpekRAEIDRGGFIT-----------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYP 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 899 GEVENALSILTNVESAVVIAEPinnsHRLLGYCVVKDIELDEKTSeqLSQQYL-SQLRQNLPEYMVPSALTVMSEFPRNV 977
Cdd:PRK12406 415 AEIEAVLHAVPGVHDCAVFGIP----DAEFGEALMAVVEPQPGAT--LDEADIrAQLKARLAGYKVPKHIEIMAELPRED 488
|
570
....*....|....*....
gi 490930577 978 SGKVDKKALPKPQIRAHSR 996
Cdd:PRK12406 489 SGKIFKRRLRDPYWANAGR 507
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
502-650 |
2.66e-07 |
|
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: 55.53 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 502 HLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTT 581
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 582 qalaqqlpqniqqlhldqegvqtqirkqdasdipaenrkfDFQDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:cd05914 87 ----------------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIV 115
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1674-2027 |
3.20e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.87 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1674 PQHP---AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPC--TFDVSVwEFFWSYLVGARLVIAP 1748
Cdd:PRK08043 361 KQQPedaALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1749 IDAHrdplallsliqkYQVttlhfVPSMlaVFENAATEI------LSSAQRQSLP-----ICRVFCSGEALPTALAKSFT 1817
Cdd:PRK08043 440 SPLH------------YRI-----VPEL--VYDRNCTVLfgtstfLGNYARFANPydfarLRYVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1818 EHFSCELHNLYGPTEAAvdvsymdatlglhpeeSCVAIGYPVW---NTQLYIL---DQYLRPVPvGVD--GELYLAGHQL 1889
Cdd:PRK08043 501 DKFGLRILEGYGVTECA----------------PVVSINVPMAakpGTVGRILpgmDARLLSVP-GIEqgGRLQLKGPNI 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1890 AMGYLHradltasrfVANPF---------TAGQR---MYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLR 1957
Cdd:PRK08043 564 MNGYLR---------VEKPGvlevptaenARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL 634
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1958 LISGLDvvVHAISSEQNKANVQLVAYLQTTAPVDIDQLKKQLAKH-LPAYMVPTHYMLVEQFPLSHNGKLD 2027
Cdd:PRK08043 635 GVSPDK--QHATAIKSDASKGEALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1908-2033 |
3.55e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 55.39 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1908 PFTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIRGQRIELGEIEQQLRlISGL--DVVVHAISSEQnkANVQLVA-YL 1984
Cdd:PRK07445 318 QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAIL-ATGLvqDVCVLGLPDPH--WGEVVTAiYV 394
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490930577 1985 QTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGKLDRKALPQ 2033
Cdd:PRK07445 395 PKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2051-2120 |
3.83e-07 |
|
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: 49.47 E-value: 3.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 2051 EHELTRIFQQILNTD-QNIGVNEDFFA-IGGHSILVMKLAIEIRKVFKRTIPIGQLMSHVTIQRLAALLLTQ 2120
Cdd:COG0236 7 EERLAEIIAEVLGVDpEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
483-986 |
3.97e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 55.08 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 483 VKKYPERTAIV---SGERpnlqhLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSG------AS 553
Cdd:PRK13391 7 AQTTPDKPAVImasTGEV-----VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGlyytcvNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 554 FL-PLDLDYPIDrmqmmceDANPLFVLTTQA-------LAQQLPQNIQQLHLDQ-------EGVQTQIRKQDASDIPAEN 618
Cdd:PRK13391 82 HLtPAEAAYIVD-------DSGARALITSAAkldvaraLLKQCPGVRHRLVLDGdgelegfVGYAEAVAGLPATPIADES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 619 RKFDFQdvayviFTSGSTGRPKGVMnthGSLLNLILSHKPTIYWPVLEAVNERFPDRPLRAA---HTHSFSFDSSWLQVf 695
Cdd:PRK13391 155 LGTDML------YSSGTTGRPKGIK---RPLPEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAplyHSAPQRAVMLVIRL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 696 wmlwGQELHIFDenmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHHPSLILIGGEAA---PLALWQQLNA 772
Cdd:PRK13391 225 ----GGTVIVME---HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAapcPPQVKEQMID 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 773 QPALFAHNLYGPTEYTVDTF-RAE--LKQ---TARPVIGNPigntqaYVLDRHLQRCPTGVIGELYISGfGIANGYLGRA 846
Cdd:PRK13391 298 WWGPIIHEYYAATEGLGFTAcDSEewLAHpgtVGRAMFGDL------HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 847 DLSAARFVANPfehgqRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPinnsHR 926
Cdd:PRK13391 371 AKTAEARHPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP----NE 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490930577 927 LLG---YCVVKDIELDEKTSEqLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK13391 442 DLGeevKAVVQPVDGVDPGPA-LAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
629-920 |
4.03e-07 |
|
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: 54.62 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 629 VIFTSGSTGRPKGVMNTHGSLLnlilshkptiywpvLEAVNerfpdrplrAAHTHSFSFDSSWLQV-------FWMLWGQ 701
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALL--------------AQALV---------LAVLQAIDEGTVFLNSgplfhigTLMFTLA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 702 ELHIFDEN--MRR-DAFGLVQEIQQRQIDTLDLPPSFCAQMMTnglFVENQHHPSLILIGGEAAPLalWQQL-NAQPALF 777
Cdd:cd17636 62 TFHAGGTNvfVRRvDAEEVLELIEAERCTHAFLLPPTIDQIVE---LNADGLYDLSSLRSSPAAPE--WNDMaTVDTSPW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 778 AHNL--YGPTEYT-VDTFRAeLKQTARPVIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAARFV 854
Cdd:cd17636 137 GRKPggYGQTEVMgLATFAA-LGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 855 AnpfehgqRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd17636 216 G-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVP 274
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1102-1260 |
4.35e-07 |
|
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: 54.95 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1102 PLLPLQKgMLFLSQVENQSNYNAFTRLSLNGDIDPVRLQQALITVLKRHPQL--------GGH--FDSELAEEPVFIYSL 1171
Cdd:cd19534 3 PLTPIQR-WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALrmrfrredGGWqqRIRGDVEELFRLEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1172 hptqawpvqfcSVTPDLLEQTIQEA---LQQPIHLDQ-PygLIRATLIQHAPEQSELLIMVHHLLTDGWSTPLFLQDFIK 1247
Cdd:cd19534 82 -----------DLSSLAQAAAIEALaaeAQSSLDLEEgP--LLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEA 148
|
170
....*....|....
gi 490930577 1248 AYQQ-TNQQLPVLE 1260
Cdd:cd19534 149 AYEQaLAGEPIPLP 162
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
474-918 |
7.79e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 54.67 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 474 NVLDIFYEQVKKYPERTAIVSGERPNLQ--HLSFAELAVKVNQLTRFLQENGA---RKQTVIAGaipRSIDSVVVMLSVL 548
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPGHGQwrKVTYGEAKRAVDALAQALLDLGLdpgRPVMILSG---NSIEHALMTLAAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 549 NSGASFLPLDLDYpidrmQMMCEDANPL---FVLTTQAL--AQQLPQNIQQLH-LDQEGVQTQIRKQDASDIPAenrkFD 622
Cdd:PRK12582 127 QAGVPAAPVSPAY-----SLMSHDHAKLkhlFDLVKPRVvfAQSGAPFARALAaLDLLDVTVVHVTGPGEGIAS----IA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 623 FQD---------------------VAYVIFTSGSTGRPKGVMNTHGSLLNLIlshkptiywPVLEAVNERFPDRPlraah 681
Cdd:PRK12582 198 FADlaatpptaavaaaiaaitpdtVAKYLFTSGSTGMPKAVINTQRMMCANI---------AMQEQLRPREPDPP----- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 682 tHSFSFDsswlqvfWMLW----------------GQELHI---------FDENMR--RD----AFGLVQEIQQRQIDTLD 730
Cdd:PRK12582 264 -PPVSLD-------WMPWnhtmggnanfngllwgGGTLYIddgkplpgmFEETIRnlREisptVYGNVPAGYAMLAEAME 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 731 LPPSFCAQMMTNglfvenqhhPSLILIGGEAAPLALWQQLNAQP-ALFAHNL-----YGPTE---YTVDTFRAelkqTAR 801
Cdd:PRK12582 336 KDDALRRSFFKN---------LRLMAYGGATLSDDLYERMQALAvRTTGHRIpfytgYGATEtapTTTGTHWD----TER 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 802 P-VIGNPIGNTQayvldrhLQRCPTGVIGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRW----NSA 876
Cdd:PRK12582 403 VgLIGLPLPGVE-------LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFvdpdDPE 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 490930577 877 GKLEFMGRCDDQIKI-RGYRVEIGEVE-NALSILTNVESAVVIA 918
Cdd:PRK12582 470 KGLIFDGRVAEDFKLsTGTWVSVGTLRpDAVAACSPVIHDAVVA 513
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
829-986 |
9.04e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 53.51 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 829 GELYISGFGIANGYLGRADlsaarfvANPF-EHGqrMYRTGDLVRWNSaGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PRK07824 208 GRIALGGPTLAKGYRNPVD-------PDPFaEPG--WFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 908 LTNVESAVVIAEPinnsHRLLGYCVVKDIELDEKTSEQLSQqYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK07824 278 HPAVADCAVFGLP----DDRLGQRVVAAVVGDGGPAPTLEA-LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1570-1806 |
1.16e-06 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 53.89 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1570 LAQQLQ-RAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLV-------IGEQKDLA 1641
Cdd:cd05905 27 IAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVAltveaclKGLPKKLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1642 AIVHPS-IATF-AFNELFDETKVDLS-SYKTTVITPQHP------AYLIYTSGTTGQPKGVMVSHQAIVN--RILWMQSE 1710
Cdd:cd05905 107 KSKTAAeIAKKkGWPKILDFVKIPKSkRSKLKKWGPHPPtrdgdtAYIEYSFSSDGSLSGVAVSHSSLLAhcRALKEACE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1711 YplSATDTILQKTPCTFDVSVWefFW---SYLVGAR-LVIAPIDAHRDPLALLSLIQKYQVTTLhFVPS--MLAVFENAA 1784
Cdd:cd05905 187 L--YESRPLVTVLDFKSGLGLW--HGcllSVYSGHHtILIPPELMKTNPLLWLQTLSQYKVRDA-YVKLrtLHWCLKDLS 261
|
250 260
....*....|....*....|....*.
gi 490930577 1785 TEILSSAQR----QSLPICRVFCSGE 1806
Cdd:cd05905 262 STLASLKNRdvnlSSLRMCMVPCENR 287
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
476-920 |
1.28e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 53.75 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 476 LDIFYEQVKKYPE-----RTAI--VSGERPnlQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVL 548
Cdd:PRK04319 42 VNIAYEAIDRHADggrkdKVALryLDASRK--EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 549 NSGASFLPLDLDY---PI-DRMqmmcEDANPLFVLTTQAL-----AQQLPQNIQQLHLDQEG------VQTQIRKQDASD 613
Cdd:PRK04319 120 KNGAIVGPLFEAFmeeAVrDRL----EDSEAKVLITTPALlerkpADDLPSLKHVLLVGEDVeegpgtLDFNALMEQASD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 614 ---IPAENRkfdfQDVAYVIFTSGSTGRPKGVMNTHgsllNLILSHKPTIYWpVLEavnerfpdrpLRAAhthsfsfdss 690
Cdd:PRK04319 196 efdIEWTDR----EDGAILHYTSGSTGKPKGVLHVH----NAMLQHYQTGKY-VLD----------LHED---------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 691 wlQVFWM-------------LWGQELH----IFDENmRRDAFGLVQEIQQRQIDTLDLPPSFCAQMMTNGLFVENQHH-P 752
Cdd:PRK04319 247 --DVYWCtadpgwvtgtsygIFAPWLNgatnVIDGG-RFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDlS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 753 SL--ILIGGEaaPL---ALW--QQLNAQPalfAHNLYGPTE---YTVDTFRAelkQTARP-VIGNPIGNTQAYVLDRHLQ 821
Cdd:PRK04319 324 SLrhILSVGE--PLnpeVVRwgMKVFGLP---IHDNWWMTEtggIMIANYPA---MDIKPgSMGKPLPGIEAAIVDDQGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 822 RCPTGVIGELYI-----SGFgiaNGYLGradlsaarfvaNP------FEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIK 890
Cdd:PRK04319 396 ELPPNRMGNLAIkkgwpSMM---RGIWN-----------NPekyesyFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIK 459
|
490 500 510
....*....|....*....|....*....|
gi 490930577 891 IRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:PRK04319 460 TSGERVGPFEVESKLMEHPAVAEAGVIGKP 489
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
464-986 |
1.63e-06 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 53.44 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 464 PRVSHPEQYNnVLDIFYEQVKKYPERTAIVsgERPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVV 543
Cdd:PLN02330 20 PSVPVPDKLT-LPDFVLQDAELYADKVAFV--EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 544 MLSVLNSGASFLPLDLDYPIDRMQMMCEDANPLFVLTTQALAQQLPQ-NIQQLHLDQEGVQTQIRKQD-------ASDIP 615
Cdd:PLN02330 97 ALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGlGLPVIVLGEEKIEGAVNWKElleaadrAGDTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 616 AeNRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLL-NLILShkptiywpvleavneRFPDRPLRAAHTHSFSfdsswLQV 694
Cdd:PLN02330 177 D-NEEILQTDLCALPFSSGTTGISKGVMLTHRNLVaNLCSS---------------LFSVGPEMIGQVVTLG-----LIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 695 FWMLWG--------------------QELHIFDENMrrdafgLVQEIQQRQIdtldLPPSFCAqmMTNGLFVENQHHPSL 754
Cdd:PLN02330 236 FFHIYGitgiccatlrnkgkvvvmsrFELRTFLNAL------ITQEVSFAPI----VPPIILN--LVKNPIVEEFDLSKL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 755 IL--IGGEAAPLA--LWQQLNAQ-PALFAHNLYGPTEYTVDTFRAELKQTARPV-----IGNPIGNTQAYVLDRHL-QRC 823
Cdd:PLN02330 304 KLqaIMTAAAPLApeLLTAFEAKfPGVQVQEAYGLTEHSCITLTHGDPEKGHGIakknsVGFILPNLEVKFIDPDTgRSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 824 PTGVIGELYISGFGIANGYLGRADLSAARFVANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN 903
Cdd:PLN02330 384 PKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLH------TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 904 ALSILTNVESAVVIAEPINNSHRLLGYCVVKDIELDEKtseqlSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDK 983
Cdd:PLN02330 458 ILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKES-----EEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMR 532
|
...
gi 490930577 984 KAL 986
Cdd:PLN02330 533 RLL 535
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1557-1953 |
1.72e-06 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 53.20 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1557 QLSFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIGE 1636
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1637 QKDLaAIVHPSIATFAFnelFDETKVDLSSYKT------------TVITPQ---HPAYLIYTSGTTGQPKGVMVSHQ-AI 1700
Cdd:cd05915 104 PNLL-PLVEAIRGELKT---VQHFVVMDEKAPEgylayeealgeeADPVRVperAACGMAYTTGTTGLPKGVVYSHRaLV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1701 VNRI-LWMQSEYPLSATDTILQKTPcTFDVSVWEFFWSYLVGARLVIAPIDAHRDPLALLSLIqKYQVTTLHFVPSMLAV 1779
Cdd:cd05915 180 LHSLaASLVDGTALSEKDVVLPVVP-MFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFD-GEGVTFTAGVPTVWLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1780 FENAATEIlssaqRQSLP-ICRVFCSGEALPTALAK-----SFTEHFSCELHNLYGPTEAAVDVSYMDATlglhPEESCV 1853
Cdd:cd05915 258 LADYLEST-----GHRLKtLRRLVVGGSAAPRSLIArfermGVEVRQGYGLTETSPVVVQNFVKSHLESL----SEEEKL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 AI----GYPVWNTQLYILDQYLRPVPvgVDGE----LYLAGHQLAMGYLHRADLTAsrfvANPFTAGqrMYRTGDIARWH 1925
Cdd:cd05915 329 TLkaktGLPIPLVRLRVADEEGRPVP--KDGKalgeVQLKGPWITGGYYGNEEATR----SALTPDG--FFRTGDIAVWD 400
|
410 420
....*....|....*....|....*...
gi 490930577 1926 ADGSIQYIGRADDQLKIRGQRIELGEIE 1953
Cdd:cd05915 401 EEGYVEIKDRLKDLIKSGGEWISSVDLE 428
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
625-919 |
2.38e-06 |
|
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: 52.60 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLLNLILSHkptiywpvLEAVNERFPDR-----PLraahTHSFSfDSSWLQVFWMLW 699
Cdd:cd05907 88 DLATIIYTSGTTGRPKGVMLSHRNILSNALAL--------AERLPATEGDRhlsflPL----AHVFE-RRAGLYVPLLAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 700 GQELHIFDENMRRDAFglvQEIQqrqidtldlPPSFCA-----QMMTNGLFVENQhhPSL------ILIGGE-------A 761
Cdd:cd05907 155 ARIYFASSAETLLDDL---SEVR---------PTVFLAvprvwEKVYAAIKVKAV--PGLkrklfdLAVGGRlrfaasgG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 762 APLAlwqqlnAQPALFAHNL-------YGPTE----YTVDTFRAELKQTarpvIGNPIGNTQAYVLDRhlqrcptgviGE 830
Cdd:cd05907 221 APLP------AELLHFFRALgipvyegYGLTEtsavVTLNPPGDNRIGT----VGKPLPGVEVRIADD----------GE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 831 LYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDLVRWNSAGKLEFMGRCDDQIKIR-GYRVEIGEVENALSILT 909
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASP 354
|
330
....*....|
gi 490930577 910 NVESAVVIAE 919
Cdd:cd05907 355 LISQAVVIGD 364
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
828-997 |
4.68e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 52.00 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 828 IGE--LYISGFGiANGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYR---VEIGEVE 902
Cdd:PLN03052 553 TGElaLFPLMFG-ASSTLLNADHYKVYFKGMPVFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGIKvssVEIERVC 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 903 NAL--SILtnvESAVVIAEPINNS-HRLLGYCVVKDIELDEKTSEQLSQQYLSQLRQNL-PEYMVpSALTVMSEFPRNVS 978
Cdd:PLN03052 632 NAAdeSVL---ETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLnPLFKV-SAVVIVPSFPRTAS 707
|
170 180
....*....|....*....|.
gi 490930577 979 GKVDKKALPK--PQIRAHSRM 997
Cdd:PLN03052 708 NKVMRRVLRQqlAQELSRSKL 728
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
523-646 |
5.97e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 51.65 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 523 GARKQTV------IAGAIPRSIDSVVVMLSVLNSGASFLPL-DLDYP--IDRMQMMCEDANPLFVLTTQALAQQLPQNIQ 593
Cdd:PRK07769 69 GARLQQVtkpgdrVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRKFFR 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 594 QLHLDQegvQTQIRKQDAsdIPAE------NRKFDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:PRK07769 149 ARPAKE---RPRVIAVDA--VPDEvgatwvPPEANEDTIAYLQYTSGSTRIPAGVQITH 202
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
829-932 |
7.44e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 51.27 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 829 GELYISGFGIANGYLGRADLSAARFVANpfEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIR-GYRVEIGEVENALSI 907
Cdd:PLN02387 503 GEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSV 580
|
90 100
....*....|....*....|....*
gi 490930577 908 LTNVESAVVIAEPINNshrllgYCV 932
Cdd:PLN02387 581 SPYVDNIMVHADPFHS------YCV 599
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
484-656 |
8.07e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 51.20 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 484 KKYPERTAIVSGERpnlqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLSVLNSGASFLPLDLDYPI 563
Cdd:PRK07470 18 RRFPDRIALVWGDR----SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 564 DRMQ----------MMCEDANPLFVLTTQALAQQLPQNIQQLHLDQE-GVQTQIRkqDASDIPAENRKFDFQDVAYVIFT 632
Cdd:PRK07470 94 DEVAylaeasgaraMICHADFPEHAAAVRAASPDLTHVVAIGGARAGlDYEALVA--RHLGARVANAAVDHDDPCWFFFT 171
|
170 180
....*....|....*....|....
gi 490930577 633 SGSTGRPKGVMNTHGSLLNLILSH 656
Cdd:PRK07470 172 SGTTGRPKAAVLTHGQMAFVITNH 195
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
900-980 |
8.72e-06 |
|
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: 45.61 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 900 EVENALSILTNVESAVVIAEPINNS-HRLLGYCVVKDieldekTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVS 978
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKgEAPVAFVVLKP------GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRS 74
|
..
gi 490930577 979 GK 980
Cdd:pfam13193 75 GK 76
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
624-655 |
8.94e-06 |
|
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: 51.06 E-value: 8.94e-06
10 20 30
....*....|....*....|....*....|..
gi 490930577 624 QDVAYVIFTSGSTGRPKGVMNTHGSLLNLILS 655
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSNVAG 145
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
126-352 |
1.08e-05 |
|
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: 50.53 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 126 LKAGETqlFRQVLFTTHDKVYW----YqryHHIMLDGFSMINLTKRIVELYQqlqeGKDLSVSPFIGVNEVISERQAYEn 201
Cdd:cd19532 105 LESGET--MRIVLLSLSPTEHYlifgY---HHIAMDGVSFQIFLRDLERAYN----GQPLLPPPLQYLDFAARQRQDYE- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 202 SHQFKIDQAFWKAYCEDLPSPISL-STHHLAAKTTATFVKH---QLRFSTGILEQIQALAAQTK-------LAlndmmms 270
Cdd:cd19532 175 SGALDEDLAYWKSEFSTLPEPLPLlPFAKVKSRPPLTRYDThtaERRLDAALAARIKEASRKLRvtpfhfyLA------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 271 lSLH-YIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQK--YDAeqI 347
Cdd:cd19532 248 -ALQvLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRvpFDV--L 324
|
....*
gi 490930577 348 LRDLN 352
Cdd:cd19532 325 LDELG 329
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
597-650 |
1.45e-05 |
|
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: 50.29 E-value: 1.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490930577 597 LDQEGVQTQIRKQDASDIPAENRKfdfQDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:cd17639 64 LGEDALIHSLNETECSAIFTDGKP---DDLACIMYTSGSTGNPKGVMLTHGNLV 114
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1670-1701 |
1.48e-05 |
|
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: 50.43 E-value: 1.48e-05
10 20 30
....*....|....*....|....*....|....*
gi 490930577 1670 TVITPQHP---AYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:cd05933 142 AIISSQKPnqcCTLIYTSGTTGMPKGVMLSHDNIT 176
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1680-1942 |
2.02e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 49.84 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1680 LIYTSGTTGQPKGVMVSHQAIVNRIlwMQSEYPLSATDTIlqktpCTFDVSvwefFWSYLVGARLVIAPIDAH------- 1752
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEV--LSTDHLLKVTDRV-----ATEEDS----YFSYLPLAHVYDQVIETYciskgas 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1753 -----RDPLALLSLIQKYQVTTLHFVPSMLAVFENAATEILSSA------------------------QRQSLPI----- 1798
Cdd:PLN02861 294 igfwqGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGgmlrkklfdfaynyklgnlrkglkQEEASPRldrlv 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1799 -----------CRVFCSGEALPTALAKSFTEHFSCE-LHNLYGPTEAA-------VDVSYMDATLGLHPE------ESCV 1853
Cdd:PLN02861 374 fdkikeglggrVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCggcftsiANVFSMVGTVGVPMTtiearlESVP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1854 AIGYPVwntqlyildqyLRPVPvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmyRTGDIARWHADGSIQYI 1933
Cdd:PLN02861 454 EMGYDA-----------LSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLIDGWF-------HTGDIGEWQPNGAMKII 512
|
....*....
gi 490930577 1934 GRADDQLKI 1942
Cdd:PLN02861 513 DRKKNIFKL 521
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1656-1948 |
2.10e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 50.10 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1656 LFDE-TKVDLSSYKTTVITPQHPAYLIYTSGTTGQPKGVMVSHQAIVNRIlwmqseYPLSATDTILQKTPCT----FDVS 1730
Cdd:PTZ00342 284 LFDDmTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTV------VPLCKHSIFKKYNPKThlsyLPIS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1731 -VWE---FFWSYLVGARLVIAPIDahrdpLALLSL-IQKYQVTTLHFVPSMLA-VFENAATEIlssaqrQSLPICRVFCS 1804
Cdd:PTZ00342 358 hIYErviAYLSFMLGGTINIWSKD-----INYFSKdIYNSKGNILAGVPKVFNrIYTNIMTEI------NNLPPLKRFLV 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1805 GEALptALAKS--------FTE---HFSC--------------------------ELHNL--------YGPTEAAVDVSY 1839
Cdd:PTZ00342 427 KKIL--SLRKSnnnggfskFLEgitHISSkikdkvnpnlevilngggklspkiaeELSVLlnvnyyqgYGLTETTGPIFV 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1840 MDATlGLHPEescvAIGYPVWNTQLYIL---DQY----LRPvpvgvDGELYLAGHQLAMGYLHRADLTASRFVANPFtag 1912
Cdd:PTZ00342 505 QHAD-DNNTE----SIGGPISPNTKYKVrtwETYkatdTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY--- 571
|
330 340 350
....*....|....*....|....*....|....*..
gi 490930577 1913 qrmYRTGDIARWHADGSIQYIGRADDQLKI-RGQRIE 1948
Cdd:PTZ00342 572 ---FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
629-920 |
2.24e-05 |
|
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: 49.19 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 629 VIFTSGSTGRPKGVMNTHGsllNLILSHKPTIY-WPVLEAvnerfpDR---PLRAAHTHSFSFDSSWLQVfwmlWGQELh 704
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHG---NLIAANLQLIHaMGLTEA------DVylnMLPLFHIAGLNLALATFHA----GGANV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 705 ifdeNMRR-DAFGLVQEIQQRQIdTL--DLPPsfcaqMMTNGLFVENQHH---PSLILIGGEAAP--LALWQQLNaqPAL 776
Cdd:cd17637 71 ----VMEKfDPAEALELIEEEKV-TLmgSFPP-----ILSNLLDAAEKSGvdlSSLRHVLGLDAPetIQRFEETT--GAT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 777 FaHNLYGPTE----YTVDTFRAelkqtaRP-VIGNPIGNTQAYVLDRHLQRCPTGVIGELYISGFGIANGYLGRADLSAA 851
Cdd:cd17637 139 F-WSLYGQTEtsglVTLSPYRE------RPgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 852 RFvANPFEHgqrmyrTGDLVRWNSAGKLEFMGRC--DDQIKIRGYRVEIGEVENALSILTNVESAVVIAEP 920
Cdd:cd17637 212 TF-RNGWHH------TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP 275
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
625-649 |
3.86e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 49.20 E-value: 3.86e-05
10 20
....*....|....*....|....*
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:PTZ00216 265 DLALIMYTSGTTGDPKGVMHTHGSL 289
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
625-650 |
3.96e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 48.96 E-value: 3.96e-05
10 20
....*....|....*....|....*.
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHGNIV 276
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
503-646 |
4.23e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 48.79 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 503 LSFAELAVKVNQLTRFLQENGARKQTVIAGAiPRSIDSVVVMLSVLNSGASFLPLDLDYP---IDRMQMMCEDANPLFVL 579
Cdd:PRK05850 36 LTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVL 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 580 TTQALAQQLPQNIQQlhlDQEGVQTQIRKQDASDIPAEN----RKFDFQDVAYVIFTSGSTGRPKGVMNTH 646
Cdd:PRK05850 115 TTSAVVDDVTEYVAP---QPGQSAPPVIEVDLLDLDSPRgsdaRPRDLPSTAYLQYTSGSTRTPAGVMVSH 182
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
828-986 |
6.34e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 48.30 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 828 IGELYISGFGIANGYLGRADLSAARFvANPFEHgqrmyrTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSI 907
Cdd:PLN02479 402 MGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFH------SGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 908 LTNVESAVVIAEPINN-SHRLLGYCVVKDiELDEKTSEQLSQQYLSQLRQNLPEYMVPSALtVMSEFPRNVSGKVDKKAL 986
Cdd:PLN02479 475 HPAVLEASVVARPDERwGESPCAFVTLKP-GVDKSDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
626-983 |
6.54e-05 |
|
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: 48.25 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 626 VAYVIFTSGSTGRPKGVMNTHGSLLNLILSHKPTIYWPVLEAVNERFPdrplraaHTHSFSFDSSWLQVFWMLWGQELHI 705
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMP-------LTHDMGLIAFHLAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 706 FDENMRRDAFGLVQeIQQRQIDTLDLP----PSFCAQMMTNGLFVENQHHPSLILIGGEAAPLALWQQLNAQPALFA--- 778
Cdd:cd05908 181 TRLFIRRPILWLKK-ASEHKATIVSSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkr 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 779 ---HNLYGPTEYTVDTFRAELKQTARPVI----------------------------GNPIGNTQAYVLDRHLQRCPTGV 827
Cdd:cd05908 260 naiLPVYGLAEASVGASLPKAQSPFKTITlgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKILPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 828 IGELYISGFGIANGYLGRADLSAARFVANPFehgqrmYRTGDL--VRwnsAGKLEFMGRCDDQIKIRGYRVEIGEVENAL 905
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLgfIR---NGRLVITGREKDIIFVNGQNVYPHDIERIA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 906 SILTNVESAVVIAEPINNSH----RLLGYCVVKD-----IELDEKTSEQLSQQYLSQLRQNLPeymvpsaltvMSEFPRN 976
Cdd:cd05908 411 EELEGVELGRVVACGVNNSNtrneEIFCFIEHRKseddfYPLGKKIKKHLNKRGGWQINEVLP----------IRRIPKT 480
|
....*..
gi 490930577 977 VSGKVDK 983
Cdd:cd05908 481 TSGKVKR 487
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1559-1957 |
7.29e-05 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 48.19 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1559 SFSEVRLQVCALAQQLQRAGVQAGDIVAVALPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG--- 1635
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAede 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1636 EQKD----LAAIVH------------------PSIATFA----------------FNELFDETKvdlssykttvitPQHP 1677
Cdd:cd17641 93 EQVDklleIADRIPsvryviycdprgmrkyddPRLISFEdvvalgraldrrdpglYEREVAAGK------------GEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSATDTILQKTPCTFdvsVWEFFwsYLVGARLVIA-PIDAHRDPL 1756
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW---IGEQM--YSVGQALVCGfIVNFPEEPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1757 ALLSLIQKYQVttlHFVPSMLAVFENAATEILSSAQrQSLPICRVF---------------CSGEALPTALAK------- 1814
Cdd:cd17641 236 TMMEDLREIGP---TFVLLPPRVWEGIAADVRARMM-DATPFKRFMfelgmklglraldrgKRGRPVSLWLRLaswlada 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1815 ------------------------------SFTEHFSCELHNLYGPTEAAVdVSYMDATLGLHPEescvAIGYPVWNTQL 1864
Cdd:cd17641 312 llfrplrdrlgfsrlrsaatggaalgpdtfRFFHAIGVPLKQLYGQTELAG-AYTVHRDGDVDPD----TVGVPFPGTEV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1865 YILDQylrpvpvgvdGELYLAGHQLAMGYLHRADLTASRFVANPFtagqrmYRTGDIARWHADGSIQYIGRADDQLKI-R 1943
Cdd:cd17641 387 RIDEV----------GEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAKDVGTTsD 450
|
490
....*....|....
gi 490930577 1944 GQRIELGEIEQQLR 1957
Cdd:cd17641 451 GTRFSPQFIENKLK 464
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1951-2025 |
9.52e-05 |
|
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: 42.53 E-value: 9.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1951 EIEQQLRLISG-LDVVVHAISSEQnKANVqLVAY--LQTTAPVDIDQLKKQLAKHLPAYMVPTHYMLVEQFPLSHNGK 2025
Cdd:pfam13193 1 EVESALVSHPAvAEAAVVGVPDEL-KGEA-PVAFvvLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
861-1005 |
1.35e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 47.12 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 861 GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENAL--SILTNVESAVVIAEPINNSHRLLgYCVVKDIEL 938
Cdd:PLN03051 355 GMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACdrAVAGIAETAAVGVAPPDGGPELL-VIFLVLGEE 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490930577 939 ----DEKTSEQLSQQYLSQLRQNL-PEYMVpSALTVMSEFPRNVSGKVDKKALpkpqiRAHSRMAETPEQQL 1005
Cdd:PLN03051 434 kkgfDQARPEALQKKFQEAIQTNLnPLFKV-SRVKIVPELPRNASNKLLRRVL-----RDQLKKELSGRSKL 499
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
625-649 |
1.35e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 47.18 E-value: 1.35e-04
10 20
....*....|....*....|....*
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:PRK08180 210 TIAKFLFTSGSTGLPKAVINTHRML 234
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
487-649 |
1.50e-04 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 47.04 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 487 PERTAIVSGERPN-LQHLSFAELAVKVNQLTRFLQENG---ARKQTVIAGaipRSIDSVVVMLSVLNSGASFLPLDLDYP 562
Cdd:cd05921 9 PDRTWLAEREGNGgWRRVTYAEALRQVRAIAQGLLDLGlsaERPLLILSG---NSIEHALMALAAMYAGVPAAPVSPAYS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 563 I-----DRMQMMCEDANPLFVLTT------QALAQQLPQNIQQLHL--DQEGVQTQIRKQDAS-----DIPAENRKFDFQ 624
Cdd:cd05921 86 LmsqdlAKLKHLFELLKPGLVFAQdaapfaRALAAIFPLGTPLVVSrnAVAGRGAISFAELAAtpptaAVDAAFAAVGPD 165
|
170 180
....*....|....*....|....*
gi 490930577 625 DVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:cd05921 166 TVAKFLFTSGSTGLPKAVINTQRML 190
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
19-224 |
1.93e-04 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 46.54 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 19 FELASTQLGIFLADHLSSIEDLYTIAHCLELPKTVDIPTFKKAIQIGLNEADTVIASYS-SDPSQPFIELNNQVQFQIEE 97
Cdd:cd19547 2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDDLAPPWAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 98 FDFCHLTPKKAQQRLWDWMPSDRQCAKSLKAgeTQLFRQVLFTTHD-KVYWYQRYHHIMLDGFSMINLTKRIVELYQQLQ 176
Cdd:cd19547 82 LDWSGEDPDRRAELLERLLADDRAAGLSLAD--CPLYRLTLVRLGGgRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490930577 177 EGKDLSVSPFIGVNEVISERQAyeNSHQFKIDQAFWKAYCEDL-PSPIS 224
Cdd:cd19547 160 HGREPQLSPCRPYRDYVRWIRA--RTAQSEESERFWREYLRDLtPSPFS 206
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1872-1968 |
2.00e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 46.65 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1872 RPVPvgvDGELYLAGHQLAMGYLHRADLTASRFVANpfTAGQRMYRTGDIARWHADGSIQYIGRADDQLKIR-GQRIELG 1950
Cdd:PLN02387 498 KPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD--ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLG 572
|
90
....*....|....*....
gi 490930577 1951 EIEQQLRLISGLD-VVVHA 1968
Cdd:PLN02387 573 KVEAALSVSPYVDnIMVHA 591
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
1589-1954 |
2.39e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 46.35 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1589 LPRSVKLSIAILAVIEAGAAYLPIDLQHPTERIKFMLQDAKSKLVIG------------------EQKDLAAIVHPSIAT 1650
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTqdvvlrggralplyskvvEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1651 FAFNELF--DETKVDL--SSYKTTVITPQH--PAYL--------IYTSGTTGQPKGVMVSHQAIVNRILWMQSEYPLSAT 1716
Cdd:PLN03051 81 PVAVPLReqDLSWCDFlgVAAAQGSVGGNEysPVYApvesvtniLFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1717 DTILQKTPCTFDVSVWEFFWSYLVGARLVIApidaHRDPLA--LLSLIQKYQVTTLHFVPSMLAVFENAATeilSSAQRQ 1794
Cdd:PLN03051 161 DVVCWPTNLGWMMGPWLLYSAFLNGATLALY----GGAPLGrgFGKFVQDAGVTVLGLVPSIVKAWRHTGA---FAMEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1795 SLPICRVFCS-GEA----------LPTALAKSFTEHfsCelhnlyGPTEAAVdvSYMDATLgLHPEeSCVAIGYPVWNTQ 1863
Cdd:PLN03051 234 DWSKLRVFAStGEAsavddvlwlsSVRGYYKPVIEY--C------GGTELAS--GYISSTL-LQPQ-APGAFSTASLGTR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1864 LYILDQYLRPVPVG--VDGELYLAghQLAMGYLHR---ADLTASRFVANPF--TAGQRMYRTGDIARWHADGSIQYIGRA 1936
Cdd:PLN03051 302 FVLLNDNGVPYPDDqpCVGEVALA--PPMLGASDRllnADHDKVYYKGMPMygSKGMPLRRHGDIMKRTPGGYFCVQGRA 379
|
410
....*....|....*...
gi 490930577 1937 DDQLKIRGQRIELGEIEQ 1954
Cdd:PLN03051 380 DDTMNLGGIKTSSVEIER 397
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
829-982 |
2.64e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.50 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 829 GELYISGFGIANGYLgRADlsaARFVANPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSIL 908
Cdd:PRK06814 982 GRLFVRGPNVMLGYL-RAE---NPGVLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAEL 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 909 TNVESAVVIAEPinnshrllgycvvkdielDEKTSEQL----------SQQYLSQLRQN-LPEYMVPSALTVMSEFPRNV 977
Cdd:PRK06814 1056 WPDALHAAVSIP------------------DARKGERIillttasdatRAAFLAHAKAAgASELMVPAEIITIDEIPLLG 1117
|
....*
gi 490930577 978 SGKVD 982
Cdd:PRK06814 1118 TGKID 1122
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
829-1004 |
3.60e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 45.86 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 829 GELYISGFGIANGYL-----GRADLSAARFVANPFEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVEN 903
Cdd:PRK08043 554 GRLQLKGPNIMNGYLrvekpGVLEVPTAENARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQ 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 904 -ALSILTNVESAVVIAEPINNSHRLLGYcvVKDIELdekTSEQLSQQYLSqlrQNLPEYMVPSALTVMSEFPRNVSGKVD 982
Cdd:PRK08043 632 lALGVSPDKQHATAIKSDASKGEALVLF--TTDSEL---TREKLQQYARE---HGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
170 180
....*....|....*....|..
gi 490930577 983 KKALpkpqirahSRMAETPEQQ 1004
Cdd:PRK08043 704 FVTL--------KSMVDEPEQH 717
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
851-986 |
3.64e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 45.71 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 851 ARFVANPFEH-GQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNV-ESAVV-IAEPInNSHRL 927
Cdd:PRK10524 460 DRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVaEVAVVgVKDAL-KGQVA 538
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490930577 928 LGYCVVKDIEL--DEKTSEQLSQQYLSQLRQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK10524 539 VAFVVPKDSDSlaDREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
477-651 |
3.71e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 45.57 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 477 DIFYEQVKKYPERTAIVSGERpNLqHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLS---------- 546
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDQ-GL-RWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFAtakigailvt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 547 ------------VLN-SGASFLPL-----DLDYpidrMQMMCEDANPLFVLTTQAL-AQQLPQNIQQLHLDQEG------ 601
Cdd:PRK08315 98 inpayrlseleyALNqSGCKALIAadgfkDSDY----VAMLYELAPELATCEPGQLqSARLPELRRVIFLGDEKhpgmln 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490930577 602 ---VQTQIRKQDASDIPAENRKFDFQDVAYVIFTSGSTGRPKGVMNTHGSLLN 651
Cdd:PRK08315 174 fdeLLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILN 226
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1672-1719 |
4.13e-04 |
|
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: 45.36 E-value: 4.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490930577 1672 ITPQHPAYLIYTSGTTGQPKGVMVSHQaivnRILWMQSEYPLS---ATDTI 1719
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISHL----RVLQCSGFLSLCgvtADDVI 187
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
480-649 |
7.92e-04 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 44.59 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 480 YEQVKKYPERTAIVSGerPNLQHLSFAELAVKVNQLTRFLQENGARKQTVIAGAIPRSIDSVVVMLsvlnsGASFLpldl 559
Cdd:PLN02246 30 FERLSEFSDRPCLIDG--ATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFL-----GASRR---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 560 dypidrmQMMCEDANPLFvlTTQALAQQL-----------PQNIQQL--HLDQEGVQ--------------TQIRKQDAS 612
Cdd:PLN02246 99 -------GAVTTTANPFY--TPAEIAKQAkasgakliitqSCYVDKLkgLAEDDGVTvvtiddppegclhfSELTQADEN 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 490930577 613 DIPAEnrKFDFQDVAYVIFTSGSTGRPKGVMNTHGSL 649
Cdd:PLN02246 170 ELPEV--EISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
496-650 |
1.39e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.19 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 496 ERPNLQHLSFAELAVKVNQLTRFLQENGARKQTViaGA-IPRSIDSVVVMLSVLNSGasFLPLDLDYP--IDRMQMMCED 572
Cdd:PRK06814 652 EDPVNGPLTYRKLLTGAFVLGRKLKKNTPPGENV--GVmLPNANGAAVTFFALQSAG--RVPAMINFSagIANILSACKA 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 573 ANPLFVLTT---------QALAQQLPQNIQQLHLdqEGVQTQIRKQD---------ASDIPAENRKFDfqDVAYVIFTSG 634
Cdd:PRK06814 728 AQVKTVLTSrafiekarlGPLIEALEFGIRIIYL--EDVRAQIGLADkikgllagrFPLVYFCNRDPD--DPAVILFTSG 803
|
170
....*....|....*.
gi 490930577 635 STGRPKGVMNTHGSLL 650
Cdd:PRK06814 804 SEGTPKGVVLSHRNLL 819
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
151-383 |
1.64e-03 |
|
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: 43.40 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 151 YHHIMLDGFSMINLTKRIVELYQQLQEGKDLSVSPFIGVN--EVISERQAYENSHQFKIDQAFWKAYCEDLPSPISL--- 225
Cdd:cd20483 131 SHHIAWDRGSSKSIFEQFTALYDALRAGRDLATVPPPPVQyiDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKLlpf 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 226 -STHHLAAKTTATfVKHQLRFSTGILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTL 304
Cdd:cd20483 211 aKAERPPVKDYER-STVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 305 PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLN-----------SIDIHERMYGPILNYKAFDQD 373
Cdd:cd20483 290 FFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPFDYIVDALDvprstshfpigQIAVNYQVHGKFPEYDTGDFK 369
|
250
....*....|.
gi 490930577 374 LV-IDGEKVKT 383
Cdd:cd20483 370 FTdYDHYDIPT 380
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
305-439 |
1.86e-03 |
|
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: 43.06 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 305 PTVNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLNSiDIHERMYGPILNYK-AFDQDLVIDGEKVKT 383
Cdd:cd19542 265 PCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGL-WPSGTLFNTLVSYQnFEASPESELSGSSVF 343
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 384 HHISTGPIDDFEFSFIVQDH--ELIIELRADSQRYTQDELFNHGQRLTLLLEQALIRP 439
Cdd:cd19542 344 ELSAAEDPTEYPVAVEVEPSgdSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1674-1701 |
1.88e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.55 E-value: 1.88e-03
10 20
....*....|....*....|....*...
gi 490930577 1674 PQHPAYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLI 247
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
612-662 |
1.91e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.59 E-value: 1.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490930577 612 SDIPAEnrKFDFQDVAYVIFTSGSTGRPKGVM-NTHGSLLNLILSH------KPT-IYW 662
Cdd:PRK00174 235 DECEPE--PMDAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAAMTMkyvfdyKDGdVYW 291
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
782-986 |
1.95e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 43.48 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 782 YGPTEYTVDTFRAElkQTARPVIGNPIGNTQAYVLDRhLQRCPTGV-------------IGELY-ISGFGIANGYLGRAD 847
Cdd:PRK13388 295 YGSSEGAVIVVREP--GTPPGSIGRGAPGVAIYNPET-LTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 848 LSAARFvanpfEHGqrMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAEPINNShrl 927
Cdd:PRK13388 372 ATAERM-----RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV--- 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490930577 928 lGYCVVKDIELDEKTS-------EQLSQQylsqlrQNLPEYMVPSALTVMSEFPRNVSGKVDKKAL 986
Cdd:PRK13388 442 -GDQVMAALVLRDGATfdpdafaAFLAAQ------PDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
2141-2252 |
2.37e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 41.91 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 2141 SGHPLFCF--YPGSGSAWQYTVlnRYLHSDLPIIGL------QSPRPDGllanSTDMDELVEkQLEIMRKQQPTGPYTLL 2212
Cdd:COG0596 22 DGPPVVLLhgLPGSSYEWRPLI--PALAAGYRVIAPdlrghgRSDKPAG----GYTLDDLAD-DLAALLDALGLERVVLV 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 490930577 2213 GYSLGGTVAYAVAAKlteQGEKVDYLGLLDTYPAEIHQWL 2252
Cdd:COG0596 95 GHSMGGMVALELAAR---HPERVAGLVLVDEVLAALAEPL 131
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
1122-1329 |
2.65e-03 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 42.77 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1122 YNAFTRLS--LNGDIDPVRLQQALITVLKRHPQLGGHFDSElaeepvfiyslhPTQAWPVQFCSVTPDLLEQTIQEALQQ 1199
Cdd:PRK09294 20 YEAFTGYTahLRGVLDIDALSDAFDALLRAHPVLAAHLEQD------------SDGGWELVADDLLHPGIVVVDGDAARP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 1200 PIH--LDQPYGLIRATLIQHApEQSELLIMVHHLLTDGWSTPLFLQDFIKAYQQ---TNQQLPVLEH----SYETVI--- 1267
Cdd:PRK09294 88 LPElqLDQGVSLLALDVVPDD-GGARVTLYIHHSIADAHHSASLLDELWSRYTDvvtTGDPGPIRPQpapqSLEAVLaqr 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490930577 1268 ----KALSGRDhETSKVIWQRDLADLQPLILFNQAQ--QAVQETSYRLSAELGAKLQHKLRQQGITLN 1329
Cdd:PRK09294 167 girrQALSGAE-RFMPAMYAYELPPTPTAAVLAKPGlpQAVPVTRCRLSKAQTSSLAAFGRRHRLTVN 233
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
624-650 |
2.73e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 43.16 E-value: 2.73e-03
10 20
....*....|....*....|....*..
gi 490930577 624 QDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLL 391
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
152-352 |
3.17e-03 |
|
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: 42.37 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 152 HHIMLDGFSMINLTKRIVELYQQLQEGK--DLSVSPFIGVNEVISERQAYEnSHQFKIDQAFWKAYCEDLpSPISLSTHH 229
Cdd:cd19539 134 HHTAFDAWSLDVFARDLAALYAARRKGPaaPLPELRQQYKEYAAWQREALA-APRAAELLDFWRRRLRGA-EPTALPTDR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 230 LAAKTTAtFVKHQLRFST--GILEQIQALAAQTKLALNDMMMSLSLHYIYKMTDKAELVNGIPFMRRLGSKAIRSTLPTV 307
Cdd:cd19539 212 PRPAGFP-YPGADLRFELdaELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFV 290
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490930577 308 NVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDLN 352
Cdd:cd19539 291 NLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELP 335
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
840-972 |
3.89e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 42.28 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 840 NGYLGRADLSAARFVANPFEHGQRMYRTGDLVRWNSAGKLEFMGRCDDQIKIRGYRVEIGEVENALSILTNVESAVVIAE 919
Cdd:cd05938 363 LGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490930577 920 PINNSHRLLGYCVVKdieLDEKTSEQLSQQYlSQLRQNLPEYMVPSALTVMSE 972
Cdd:cd05938 443 TVPGHEGRIGMAAVK---LKPGHEFDGKKLY-QHVREYLPAYARPRFLRIQDS 491
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
624-650 |
4.25e-03 |
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long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.39 E-value: 4.25e-03
10 20
....*....|....*....|....*..
gi 490930577 624 QDVAYVIFTSGSTGRPKGVMNTHGSLL 650
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLI 247
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| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1678-1701 |
5.75e-03 |
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acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 41.89 E-value: 5.75e-03
10 20
....*....|....*....|....
gi 490930577 1678 AYLIYTSGTTGQPKGVMVSHQAIV 1701
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHGSLT 290
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| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
865-958 |
8.04e-03 |
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Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 41.29 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 865 YRTGDLVRWNSA----G----KLEF-MGRCDDQIKIRG---YRVEIGEVENALSILTnvESAVVIAEPINNSHRLlgycV 932
Cdd:COG1541 297 YRTGDLTRLLPEpcpcGrthpRIGRiLGRADDMLIIRGvnvFPSQIEEVLLRIPEVG--PEYQIVVDREGGLDEL----T 370
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90 100
....*....|....*....|....*..
gi 490930577 933 VKdIELDEKTS-EQLSQQYLSQLRQNL 958
Cdd:COG1541 371 VR-VELAPGASlEALAEAIAAALKAVL 396
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| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
93-351 |
9.34e-03 |
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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: 40.93 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 93 FQIEEFDFCHLTPKKAQQRLWDWmpsdRQcAKS---LKAGETQLFRQVLFTTHDKVYwyqRYH----HIMLDGFSMINLT 165
Cdd:cd19535 75 YGITVHDLRGLSEEEAEAALEEL----RE-RLShrvLDVERGPLFDIRLSLLPEGRT---RLHlsidLLVADALSLQILL 146
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 166 KRIVELYQQlqEGKDLsvsPFIGVN---EVISERQAYENSHQfkIDQAFWKAYCEDLPSPISLSthhLAAK----TTATF 238
Cdd:cd19535 147 RELAALYED--PGEPL---PPLELSfrdYLLAEQALRETAYE--RARAYWQERLPTLPPAPQLP---LAKDpeeiKEPRF 216
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490930577 239 VKHQLRFSTGILEQIQALAAQTKLALNDMMMSlslhyIYkmtdkAE-----------LVNgIP-FMRRLGSKAIRS---- 302
Cdd:cd19535 217 TRREHRLSAEQWQRLKERARQHGVTPSMVLLT-----AY-----AEvlarwsgqprfLLN-LTlFNRLPLHPDVNDvvgd 285
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 490930577 303 -TlptvNVLPVKFKVAEKDSWVSLAQHVQEQLREIRPHQKYDAEQILRDL 351
Cdd:cd19535 286 fT----SLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRRL 331
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