|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-1737 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 671.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 19 PAVFAEWVGRR----PDAVALRTVAATGIDD--WTYQRLWDHVREIRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAA 92
Cdd:PRK05691 8 PLTLVQALQRRaaqtPDRLALRFLADDPGEGvvLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 93 GLIPVPVYLPSTREPQRfLARAQHILRDCEPSAVYTCGELvevleRDPILGALPIRTPAS----TADGLAPHPG-GTTAD 167
Cdd:PRK05691 88 GVIAVPAYPPESARRHH-QERLLSIIADAEPRLLLTVADL-----RDSLLQMEELAAANApellCVDTLDPALAeAWQEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 168 ADHGEHVAFLQYSSGSTGKPKGVVNTH------QSILRQAaFAANVwnGDDDMhMVSWLPLYHDMGIFWGVFMPLLNGGC 241
Cdd:PRK05691 162 ALQPDDIAFLQYTSGSTALPKGVQVSHgnlvanEQLIRHG-FGIDL--NPDDV-IVSWLPLYHDMGLIGGLLQPIFSGVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 TTLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAA 321
Cdd:PRK05691 238 CVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAAC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 322 GLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDADALERGIAVEvaqpnpadGRSRALVSCGDGAFGWDIQIVDPDRH 401
Cdd:PRK05691 318 GFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEP--------GTGSVLMSCGRSQPGHAVLIVDPQSL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 402 MTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARtaDGlGPYLRTGDAGFRYQGELYVCGRYRDLIIVGGRNHFPNDI 481
Cdd:PRK05691 390 EVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH--DG-RTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 482 EKTVEEAHCGVAPG--GACAVQPDAPQANGewwLVLETGSPVEDL---DDLSRILRRRILAHHETAPERVVWVPCRTLPT 556
Cdd:PRK05691 467 EKTVEREVEVVRKGrvAAFAVNHQGEEGIG---IAAEISRSVQKIlppQALIKSIRQAVAEACQEAPSVVLLLNPGALPK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 557 TTSGKIRRRETLNRLTAGQLE--VVHEVSPRAQAPDTPAAPDDPPTELAQHLAAMLGVEpyELAPDADLTTLGLTSMMTA 634
Cdd:PRK05691 544 TSSGKLQRSACRLRLADGSLDsyALFPALQAVEAAQTAASGDELQARIAAIWCEQLKVE--QVAADDHFFLLGGNSIAAT 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 635 QIV-EWSSSQSRRLDFADLYAEPTLRSW----QRLFDAAPPVQTGTSSVAASGPWPTTPLQQAYWV-----GRGAEQPLG 704
Cdd:PRK05691 622 QVVaRLRDELGIDLNLRQLFEAPTLAAFsaavARQLAGGGAAQAAIARLPRGQALPQSLAQNRLWLlwqldPQSAAYNIP 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 705 GvGCQTYFELvgarvDAGRLAAALDALTRRHPMLRATFPD----PGRCLITPEAVrlPLAVHDLTDAPVTTRDTHLAEIR 780
Cdd:PRK05691 702 G-GLHLRGEL-----DEAALRASFQRLVERHESLRTRFYErdgvALQRIDAQGEF--ALQRIDLSDLPEAEREARAAQIR 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 781 RRLRTHRFDIETGDTWTVELTRL---PHGCIVHFavDLIIADVTSIGTMLRDL----AASYRGE--KLPAPSATFADLIQ 851
Cdd:PRK05691 774 EEEARQPFDLEKGPLLRVTLVRLddeEHQLLVTL--HHIVADGWSLNILLDEFsrlyAAACQGQtaELAPLPLGYADYGA 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 852 -----------------------STSPPPQACADRlpegpqlPRVQEADISFLRHQHTLSALATKAIDDACHNHGVTRAA 908
Cdd:PRK05691 852 wqrqwlaqgeaarqlaywkaqlgDEQPVLELATDH-------PRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFM 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 909 VLLAAYTLVLRRWASQDDFLVNVTTFGR-SPEVSDVVGDFTETHLYRAQLDGQISFvdqAQVTQKGLRTALRAAPAPDLL 987
Cdd:PRK05691 925 VLLAAFQALLHRYSGQGDIRIGVPNANRpRLETQGLVGFFINTQVLRAQLDGRLPF---TALLAQVRQATLGAQAHQDLP 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 988 ATQLRSGTGHS---GIVPVVFTYAADSplLSAEDANTLGAIDEVVSMTPQVLIDHQACRLGDD---VVLSWDYRAGCFPP 1061
Cdd:PRK05691 1002 FEQLVEALPQAreqGLFQVMFNHQQRD--LSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRngrLTLSFDYAAELFDA 1079
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1062 GVVDDMFEAYVTLLERLGGHDWSTPATPGLSAHSRLARAHRNATTTPAPAG-LLYDAFRENAATHPARLALRWrpddyrg 1140
Cdd:PRK05691 1080 ATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQaWLPELLNEQARQTPERIALVW------- 1152
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1141 erhgdviaqDRSQLTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRI 1219
Cdd:PRK05691 1153 ---------DGGSLDYAELHAQANRLAHYLRDKGVGPDVcVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYM 1223
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1220 CARSAmAGLIRTDSD-----TQDAGVAVSDITAM-IECAPTDPIRIDPHDA--AYVIYTSGSTGEPKGVLVSHAAALNTI 1291
Cdd:PRK05691 1224 LADSG-VELLLTQSHllerlPQAEGVSAIALDSLhLDSWPSQAPGLHLHGDnlAYVIYTSGSTGQPKGVGNTHAALAERL 1302
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1292 VDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAA 1371
Cdd:PRK05691 1303 QWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEP 1382
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1372 GdkAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAI----WSNEFvvddvdPDWASIPYGYPLANQMF 1447
Cdd:PRK05691 1383 L--AAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAInvthWQCQA------EDGERSPIGRPLGNVLC 1454
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1448 RVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIR 1524
Cdd:PRK05691 1455 RVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPlgeDGARLYRTGDRARWNADGALEYLGRLDQQVKLR 1534
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1525 GHRVECGEIEHALRGHPLVAAATVVpIHNcTALGAGIVVTGSGAEQFDDStPGALRAHLAVRLPQYMIPKVFVSCPELPL 1604
Cdd:PRK05691 1535 GFRVEPEEIQARLLAQPGVAQAAVL-VRE-GAAGAQLVGYYTGEAGQEAE-AERLKAALAAELPEYMVPAQLIRLDQMPL 1611
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1605 TANGKVDRGKIAARLEAAARAPQPldtsstLTVVERLVAEVWSDVLGAPITGREDNFFAQGGDSLRATEAVARLTRRGVA 1684
Cdd:PRK05691 1612 GPSGKLDRRALPEPVWQQREHVEP------RTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDV 1685
|
1770 1780 1790 1800 1810
....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1685 GAEVGQLLSHQTLGQFSAACVLADPASEASESAA----DVGEPVtpgegfPLTRLQQ 1737
Cdd:PRK05691 1686 ELPLRALFEASELGAFAEQVARIQAAGERNSQGAiarvDRSQPV------PLSYSQQ 1736
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
666-1973 |
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: 653.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 666 DAAPPVQTGTSSVAASGPWPTTPLQQAYWVGRGAEQPLGGVGCQTYFELVGARVDAGRLAAALDALTRRHPMLRATFPDP 745
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 746 GRCLITPEAVRLPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRLPHGC-IVHFAVDLIIADVTSIG 824
Cdd:COG1020 81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLlLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 825 TMLRDLAASY------RGEKLPAPSATFADL-----IQSTSPPPQACADR-------LPEGPQLP----RVQEADISFLR 882
Cdd:COG1020 161 LLLAELLRLYlaayagAPLPLPPLPIQYADYalwqrEWLQGEELARQLAYwrqqlagLPPLLELPtdrpRPAVQSYRGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 883 HQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQI 961
Cdd:COG1020 241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPrPELEGLVGFFVNTLPLRVDLSGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 962 SFVDQAQVTQKGLRTALR--AAPAPDLL-ATQLRSGTGHSGIVPVVFTYAADSPLLSAEDANTLGAIdEVVSMTPQVLID 1038
Cdd:COG1020 321 SFAELLARVRETLLAAYAhqDLPFERLVeELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPL-ELDSGTAKFDLT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1039 HQACRLGDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLERL-GGHDWSTPATPGLSAHSRLA-RAHRNATTTPAPA-GLLY 1115
Cdd:COG1020 400 LTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALaADPDQPLGDLPLLTAAERQQlLAEWNATAAPYPAdATLH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1116 DAFRENAATHPARLALRWrpddyrGERhgdviaqdrsQLTYGELDE--------LARSVARAvaarhaaGSVIGIQLPKG 1187
Cdd:COG1020 480 ELFEAQAARTPDAVAVVF------GDQ----------SLTYAELNAranrlahhLRALGVGP-------GDLVGVCLERS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1188 PSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIrTDSDTQD------AGVAVSDITAMIECAPTDPIR-ID 1260
Cdd:COG1020 537 LEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVL-TQSALAArlpelgVPVLALDALALAAEPATNPPVpVT 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1261 PHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARR 1340
Cdd:COG1020 616 PDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARR 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1341 DAFHWLSLTTEFGITVWNSVPGLMDMLLIAAgdkAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIW 1420
Cdd:COG1020 696 DPAALAELLARHRVTVLNLTPSLLRALLDAA---PEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVD 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1421 SNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWY 1497
Cdd:COG1020 773 STYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPfgfPGARLY 852
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1498 RTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNctALGAGIVVTGSGAEQFDDSTPG 1577
Cdd:COG1020 853 RTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARED--APGDKRLVAYVVPEAGAAAAAA 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1578 ALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKIAARLEAAARAPQPldtssTLTVVERLVAEVWSDVLGAPITGR 1657
Cdd:COG1020 931 LLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAA-----PPAEEEEEEAALALLLLLVVVVGD 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1658 EDNFFAQGGDSLRATEAVARLTRRGVAGAEVGQLLSHQTLGQFSAACVLADPASEASESAADVGEPVTPGEGFPLTRLQQ 1737
Cdd:COG1020 1006 DDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLA 1085
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1738 AYTLGAAGLNGSTCAPTYFAVVLAAAPESAGIDLDR-------FARVVTRCVDEFAMLRCALDADTTQRVQVDAGPVPVH 1810
Cdd:COG1020 1086 LLLLLALLALLALLLLLLLLLLLLALLLLLALLLALlaalrarRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAA 1165
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1811 DLDIQDDPDLLLRRMAAAPFDPHSVPVIQCFAPSRSPRHVGLLISYLGLDARSLSTVVTTIIAEYQSQPRPRQVDPTAAV 1890
Cdd:COG1020 1166 ELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAA 1245
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1891 FARFASESAWGENDVDNSVAGPPLLPLHDQRRDPFERVTFARRSFTIEEQAAATLREHAAHLGVTPTALVFEAFAHALAS 1970
Cdd:COG1020 1246 LLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLL 1325
|
...
gi 2181016861 1971 IGA 1973
Cdd:COG1020 1326 LAL 1328
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1147-1612 |
0e+00 |
|
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: 568.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1147 IAQDRSQLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAm 1225
Cdd:cd12114 6 VICGDGTLTYGELAERARRVAGAlKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1226 AGLIRTDSDTQDAGVAVSDITAMIECA-----PTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRI 1300
Cdd:cd12114 85 ARLVLTDGPDAQLDVAVFDVLILDLDAlaapaPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1301 DTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPT 1380
Cdd:cd12114 165 GPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1381 LRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDY 1460
Cdd:cd12114 245 LRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1461 VAGELWIGGAGVALGYHNAPELTSDRFVHDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGH 1540
Cdd:cd12114 325 VPGELWIGGRGVALGYLGDPELTAARFVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAH 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 1541 PLVAAATVVPIHNC--TALGAGIVVTGSGAEqfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd12114 405 PGVARAVVVVLGDPggKRLAAFVVPDNDGTP----IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
24-573 |
5.77e-144 |
|
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: 461.32 E-value: 5.77e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 24 EWVGRRPDAVALRTVA--ATGIDDWTYQRLWDHVREI----RDVAfsglSAGIRIPMALPGGADYVAGMLAALAAGLIPV 97
Cdd:cd05931 1 RRAAARPDRPAYTFLDdeGGREETLTYAELDRRARAIaarlQAVG----KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 98 PVYLPstrEPQRFLARAQHILRDCEPSAVYTCGE----LVEVLERDPILGALPIRTPASTADGLAPHPGGTTADADHgeh 173
Cdd:cd05931 77 PLPPP---TPGRHAERLAAILADAGPRVVLTTAAalaaVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDD--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDFVRN 253
Cdd:cd05931 151 IAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 254 PRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLRDDVMAPQYG 333
Cdd:cd05931 231 PLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 334 LAEAGLGVTGSQTVRVWVEKSFDADALERGIAVEVAQPNPAdgrsRALVSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIW 413
Cdd:cd05931 311 LAEATLFVSGGPPGTGPVVLRVDRDALAGRAVAVAADDPAA----RELVSCGRPLPDQEVRIVDPETGRELPDGEVGEIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 414 VGGPGLPDGYWRQPEQTATTFGARTADGLGPYLRTGDAGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEAHCGVA 493
Cdd:cd05931 387 VRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 494 PGGACAVqpdAPQANGEWWLV----LETGSPVEDLDDLSRILRRRILAHHETAPERVVWVPCRTLPTTTSGKIRRRETLN 569
Cdd:cd05931 467 PGCVAAF---SVPDDGEERLVvvaeVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRA 543
|
....
gi 2181016861 570 RLTA 573
Cdd:cd05931 544 AYLD 547
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1150-1612 |
1.80e-134 |
|
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: 429.64 E-value: 1.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1150 DRSQLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRIcarsamagl 1228
Cdd:cd05930 9 GDQSLTYAELDARANRLARYlRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1229 irtdsdTQDAGVAVsditamiecaptdpIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLA 1308
Cdd:cd05930 80 ------LEDSGAKL--------------VLTDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1309 LSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAgsLPTLRSVFLSG 1388
Cdd:cd05930 140 FTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1389 DWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIG 1468
Cdd:cd05930 218 EALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1469 GAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAA 1546
Cdd:cd05930 298 GAGLARGYLNRPELTAERFVPNPfgPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREA 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 1547 TVVPIHNCTA---LGAGIVvtgsgAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05930 378 AVVAREDGDGekrLVAYVV-----PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-1739 |
8.29e-130 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 461.17 E-value: 8.29e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 8 PPALHDGDRSVPAVFAEWVGRRPDAVALrtvaATGIDDWTYQRLWDHVREIRDVAF-SGLSAGIRIPMALPGGADYVAGM 86
Cdd:PRK12467 504 APATEYAPDCVHQLIEAQARQHPERPAL----VFGEQVLSYAELNRQANRLAHVLIaAGVGPDVLVGIAVERSIEMVVGL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 87 LAALAAGLIPVPVylpstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLERDPILGALPIRTPAstaDGLAPHPGGTTA 166
Cdd:PRK12467 580 LAVLKAGGAYVPL------DPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPA---DLLCGYSGHNPE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 167 DADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN--GDDDMHMVSwlPLYHDMGIfWGVFMPLLNGGCTTL 244
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQlaADDSMLMVS--TFAFDLGV-TELFGALASGATLHL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 245 IPPhDFVRNPRIWLETVSRFRGNWIGGPDFAYRrcieAFDGTALQSLDLSCLRLATNG-AEPVrgttlrDFTAKFRAAGL 323
Cdd:PRK12467 728 LPP-DCARDAEAFAALMADQGVTVLKIVPSHLQ----ALLQASRVALPRPQRALVCGGeALQV------DLLARVRALGP 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 324 RDDVMApQYGLAEAGLGVTgsqtvrVWVEKSFDADALergiAVEVAQPNPADGrsralvscgdgafgwdIQIVDPDRHMt 403
Cdd:PRK12467 797 GARLIN-HYGPTETTVGVS------TYELSDEERDFG----NVPIGQPLANLG----------------LYILDHYLNP- 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 404 LTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGLGP----YLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFP 478
Cdd:PRK12467 849 VPVGVVGELYIGGAGLARGYHRRPALTAERF---VPDPFGAdggrLYRTGDlARYRADGVIEYLGRMDHQVKIRGFRIEL 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 479 NDIEKT------VEEAHCGVAPGGACA-----VQPDAPqangewwlvLETGSPVEDLDDLSRILRRRILAHheTAPERVV 547
Cdd:PRK12467 926 GEIEARllaqpgVREAVVLAQPGDAGLqlvayLVPAAV---------ADGAEHQATRDELKAQLRQVLPDY--MVPAHLL 994
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 548 WVpcRTLPTTTSGKIRRRETlnrltagqlevvheVSPRAQAPDtpAAPDDPPTELAQHLAAM----LGVEPYELapDADL 623
Cdd:PRK12467 995 LL--DSLPLTPNGKLDRKAL--------------PKPDASAVQ--ATFVAPQTELEKRLAAIwadvLKVERVGL--TDNF 1054
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 624 TTLGLTSMMTAQIVewsSSQSRRLD----FADLYAEPTLRSW-QRLFDAAPPVQTGTSSVAASGPWPTTPLQQAYWVGRG 698
Cdd:PRK12467 1055 FELGGHSLLATQVI---SRVRQRLGiqvpLRTLFEHQTLAGFaQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQ 1131
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 699 AEQPLGGVGCQTYFELVGArVDAGRLAAALDALTRRHPMLRATFPDPG---RCLITPE-AVRLPLAVHDLTDAPVTTRDT 774
Cdd:PRK12467 1132 LEPGSAAYHIPQALRLKGP-LDIEALERSFDALVARHESLRTTFVQEDgrtRQVIHPVgSLTLEEPLLLAADKDEAQLKV 1210
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 775 HLAEIRRRLrthrFDIETGDTWTVELTRL-PHGCIVHFAVDLIIADVTSIGTMLRDLAASYRGE------KLPAPSATFA 847
Cdd:PRK12467 1211 YVEAEARQP----FDLEQGPLLRVGLLRLaADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYsqgqslQLPALPIQYA 1286
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 848 DL-------IQSTSPPPQAC--ADRL-PEGP--QLP--RVQEADISFL--RHQHTLSALATKAIDDACHNHGVTRAAVLL 911
Cdd:PRK12467 1287 DYavwqrqwMDAGERARQLAywKAQLgGEQPvlELPtdRPRPAVQSHRgaRLAFELPPALAEGLRALARREGVTLFMLLL 1366
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 912 AAYTLVLRRWASQDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFvdqAQVTQKGLRTALRAAPAPDLLATQ 990
Cdd:PRK12467 1367 ASFQTLLHRYSGQDDIRVGVPIANRNrAETEGLIGFFVNTQVLRAEVDGQASF---QQLLQQVKQAALEAQAHQDLPFEQ 1443
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 991 L-------RSgTGHSGIVPVVFTY-------AADSPLLSAEDantlgaidevvsmtpqvlidhqacrlgddvvLSWDYRA 1056
Cdd:PRK12467 1444 LvealqpeRS-LSHSPLFQVMFNHqrddhqaQAQLPGLSVES-------------------------------LSWESQT 1491
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1057 GCF---------PPGV------VDDMFEAyvTLLERLGGHdW-----STPATPG--LSAHSRLARAHR-------NATTT 1107
Cdd:PRK12467 1492 AQFdltldtyesSEGLqasltyATDLFEA--STIERLAGH-WlnllqGLVADPErrLGELDLLDEAERrqilegwNATHT 1568
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1108 PAPAG-LLYDAFRENAATHPARLALRWrpddyrGERhgdviaqdrsQLTYGELDELARSVARAVAARHAAGSV-IGIQLP 1185
Cdd:PRK12467 1569 GYPLArLVHQLIEDQAAATPEAVALVF------GEQ----------ELTYGELNRRANRLAHRLIALGVGPEVlVGIAVE 1632
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1186 KGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAmAGLIRTDSDTQD-----AGV---AVSDITAMIECAP-TDP 1256
Cdd:PRK12467 1633 RSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSG-IELLLTQSHLQArlplpDGLrslVLDQEDDWLEGYSdSNP 1711
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1257 I-RIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIP 1335
Cdd:PRK12467 1712 AvNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAP 1791
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1336 EHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSlPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGAT 1415
Cdd:PRK12467 1792 PGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHP-LSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPT 1870
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1416 EAAIWSNEFVVDDVDPD-WASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP--- 1491
Cdd:PRK12467 1871 ETAVDVTHWTCRRKDLEgRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPfgt 1950
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1492 TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIH--NCTALGAGIVVTGSGAE 1569
Cdd:PRK12467 1951 VGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDgaNGKQLVAYVVPTDPGLV 2030
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1570 QFDDSTP---GALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKIAARLEAAARApqplDTSSTLTVVERLVAEVW 1646
Cdd:PRK12467 2031 DDDEAQValrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQ----AYVAPQSELEQRLAAIW 2106
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1647 SDVLGAPITGREDNFFAQGGDSLRATEAVARLTRRGVAGAEvGQLLSHQTLGQFSAACVLADPASEASESaadvgePVTp 1726
Cdd:PRK12467 2107 QDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTP-KDLFQHQTVQSLAAVAQEGDGTVSIDQG------PVT- 2178
|
1850
....*....|...
gi 2181016861 1727 GEgFPLTRLQQAY 1739
Cdd:PRK12467 2179 GD-LPLLPIQQMF 2190
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
718-1723 |
2.14e-121 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 433.43 E-value: 2.14e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 718 RVDAGRLAAALDALTRRHPMLRATFPDPGRCL--ITPEAVRLPLAVHDLTDAPVTTRDtHLAEIRRRLRTHR-FDIETGD 794
Cdd:PRK12467 83 ELDVSALRRAFDALVARHESLRTRFVQDEEGFrqVIDASLSLTIPLDDLANEQGRARE-SQIEAYINEEVARpFDLANGP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 795 TWTVELTRLP---HgcIVHFAVDLIIADVTSIGTMLRDLAASY------RGEKLPAPSATFAD----------------- 848
Cdd:PRK12467 162 LLRVRLLRLAddeH--VLVVTLHHIISDGWSMRVLVEELVQLYsaysqgREPSLPALPIQYADyaiwqrswleagererq 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 849 ------LIQSTSPPPQACADRlpEGPQLPRVQEAdisflRHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWA 922
Cdd:PRK12467 240 laywqeQLGGEHTVLELPTDR--PRPAVPSYRGA-----RLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 923 SQDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQkglRTALRAAPAPDL------LATQLRSGT 995
Cdd:PRK12467 313 GQSDIRIGVPNANRNrVETERLIGFFVNTQVLKAEVDPQASFLELLQQVK---RTALGAQAHQDLpfeqlvEALQPERSL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 996 GHSGIVPVVFTYAADSPLLSAEDANTLGAID----EVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCFPPGVVDDMFEAY 1071
Cdd:PRK12467 390 SHSPLFQVMFNHQNTATGGRDREGAQLPGLTveelSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHW 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1072 VTLLERLGGHDWSTPATPGL--SAHSRLARAHRNATTTPAPAGLLYDAFRENAATHPARLALRWrpddyrGERHgdviaq 1149
Cdd:PRK12467 470 RNLLEAIVAEPRRRLGELPLldAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVF------GEQV------ 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1150 drsqLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAgL 1228
Cdd:PRK12467 538 ----LSYAELNRQANRLAHVLIAAgVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVR-L 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1229 IRTDSDTQDAGVAVSDITAMIECAPTD----------PIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRN 1298
Cdd:PRK12467 613 LLTQSHLLAQLPVPAGLRSLCLDEPADllcgysghnpEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERL 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1299 RIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLiAAGDKAGSL 1378
Cdd:PRK12467 693 QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALL-QASRVALPR 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1379 PtLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQP 1458
Cdd:PRK12467 772 P-QRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVP 850
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1459 DYVAGELWIGGAGVALGYHNAPELTSDRFVHDPT---GSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEH 1535
Cdd:PRK12467 851 VGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEA 930
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1536 ALRGHPLVAAATVVPIHNCTA--LGAGIVVTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRG 1613
Cdd:PRK12467 931 RLLAQPGVREAVVLAQPGDAGlqLVAYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1614 KIaarleaaaraPQPLDTSSTLTVV------ERLVAEVWSDVLGAPITGREDNFFAQGGDSLRATEAVARLTRRGVAGAE 1687
Cdd:PRK12467 1011 AL----------PKPDASAVQATFVapqtelEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP 1080
|
1050 1060 1070
....*....|....*....|....*....|....*.
gi 2181016861 1688 VGQLLSHQTLGQFSAACVLADPASEASESAADVGEP 1723
Cdd:PRK12467 1081 LRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQP 1116
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1155-1548 |
1.62e-119 |
|
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: 385.08 E-value: 1.62e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1155 TYGELDELARS--VARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAmAGLIRTD 1232
Cdd:TIGR01733 1 TYRELDERANRlaRHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAG-ARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1233 SDTQDAGVAVSDITAMIE-----------CAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRID 1301
Cdd:TIGR01733 80 SALASRLAGLVLPVILLDplelaalddapAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1302 THDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAF-HWLSLTTEFGITVWNSVPGLMDMLLIAAgdkAGSLPT 1380
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAaLLAALIAEHPVTVLNLTPSLLALLAAAL---PPALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1381 LRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDPDWAS-IPYGYPLANQMFRVVDDNGDDQPD 1459
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1460 YVAGELWIGGAGVALGYHNAPELTSDRFVHDP----TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEH 1535
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVPDPfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396
|
410
....*....|...
gi 2181016861 1536 ALRGHPLVAAATV 1548
Cdd:TIGR01733 397 ALLRHPGVREAVV 409
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2531-2928 |
5.61e-115 |
|
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: 372.59 E-value: 5.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2531 FPLTVVQNAYRAGREGALILGGVAAHCYFEFELADFDRPRFDSAARQLVARHAGLRTTVSPAGTD---AASSGEVAVVH- 2606
Cdd:cd19535 2 FPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQqilPEVPWYGITVHd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2607 --TAPIEPVVRDHDDVRAAMRDQIIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETvDQL 2684
Cdd:cd19535 82 lrGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPG-EPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2685 PPLETSFAHYVWNHPELLPDAdeavlprLAASRDYWRARLPSLPPAPKL---ADMSllfEIEEPRFERATATIPAVDWSQ 2761
Cdd:cd19535 161 PPLELSFRDYLLAEQALRETA-------YERARAYWQERLPTLPPAPQLplaKDPE---EIKEPRFTRREHRLSAEQWQR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2762 VTRSCRAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDPDVVGIENVVGDFTSLVLLECRVDEPASIWESVRALQ 2841
Cdd:cd19535 231 LKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2842 RQLMTDLPHRGADAVWLQRELLRFHGNpTAALFPVVFTSGLGLVDASARAAVRFAEPVFAASQTPQTVLDFQVWESAGAL 2921
Cdd:cd19535 311 QQLWEDLDHSSYSGVVVVRRLLRRRGG-QPVLAPVVFTSNLGLPLLDEEVREVLGELVYMISQTPQVWLDHQVYEEDGGL 389
|
....*..
gi 2181016861 2922 KLSWDFV 2928
Cdd:cd19535 390 LLNWDAV 396
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
683-1082 |
2.38e-113 |
|
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: 367.97 E-value: 2.38e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 683 PWPTTPLQQAYWVGRGAEQPLGGVGCQTYFELVGARVDAGRLAAALDALTRRHPMLRATFPDPGRCLITPEAVRLPLAVH 762
Cdd:cd19535 1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 763 DLTDAPVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRLP-HGCIVHFAVDLIIADVTSIGTMLRDLAASYR--GEKL 839
Cdd:cd19535 81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPeGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 840 PAPSATFADLIQSTSPPPQACADR-----------LPEGPQLP-RVQEADIS---FLRHQHTLSALATKAIDDACHNHGV 904
Cdd:cd19535 161 PPLELSFRDYLLAEQALRETAYERaraywqerlptLPPAPQLPlAKDPEEIKeprFTRREHRLSAEQWQRLKERARQHGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 905 TRAAVLLAAYTLVLRRWASQDDFLVNVTTFGR---SPEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKGLRTAL--R 979
Cdd:cd19535 241 TPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRlplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLdhS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 980 AAPAPDLLATQLRSGTGHSGIVPVVFTYAADSPLLSAEDANTLGAIDEVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCF 1059
Cdd:cd19535 321 SYSGVVVVRRLLRRRGGQPVLAPVVFTSNLGLPLLDEEVREVLGELVYMISQTPQVWLDHQVYEEDGGLLLNWDAVDELF 400
|
410 420
....*....|....*....|...
gi 2181016861 1060 PPGVVDDMFEAYVTLLERLGGHD 1082
Cdd:cd19535 401 PEGMLDDMFDAYVRLLERLADDD 423
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1116-1612 |
4.85e-112 |
|
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: 366.99 E-value: 4.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1116 DAFRENAATHPARLALRWrpddyrgerhgdviaqDRSQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAV 1194
Cdd:cd17646 2 ALVAEQAARTPDAPAVVD----------------EGRTLTYRELDERANRLAHLLRARgVGPEDRVAVLLPRSADLVVAL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1195 LGVMMAGCTYLPVGVDQPAERLSRIcARSAMAGLIRTDSDTQDAG-----VAVSDITAMIECAPTDPIR-IDPHDAAYVI 1268
Cdd:cd17646 66 LAVLKAGAAYLPLDPGYPADRLAYM-LADAGPAVVLTTADLAARLpaggdVALLGDEALAAPPATPPLVpPRPDNLAYVI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1269 YTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSL 1348
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1349 TTEFGITVWNSVPGLMDMLLIAAGdkAGSLPTLRSVFLSGDWIPLDLPRRLrRAAPGVRLVAMGGATEAAIWSNEFVVDD 1428
Cdd:cd17646 225 IREHGVTTCHFVPSMLRVFLAEPA--AGSCASLRRVFCSGEALPPELAARF-LALPGAELHNLYGPTEAAIDVTHWPVRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1429 VDPDwASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYW 1506
Cdd:cd17646 302 PAET-PSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPfgPGSRMYRTGDLARWR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1507 RDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPiHNCTALGAGIVVTGSGAEQFDDSTPGALRAHLAVR 1586
Cdd:cd17646 381 PDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVA-RAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAER 459
|
490 500
....*....|....*....|....*.
gi 2181016861 1587 LPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17646 460 LPEYMVPAAFVVLDALPLTANGKLDR 485
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-1703 |
2.65e-110 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 397.41 E-value: 2.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 8 PPALHDGDRSVPAVFAEWVGRRPDAVAL----RTVAATGIDDWTyQRLWDHVREIrdvafsGLSAGIRIPMALPGGADYV 83
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIAEQAARAPEAIAVvfgdQHLSYAELDSRA-NRLAHRLRAR------GVGPEVRVAIAAERSFELV 2067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 84 AGMLAALAAGLIPVPVYLPSTREpqrflaRAQHILRDCEPSAVYTCGELvevLERDPILGALPiRTPASTADGLAPHPGG 163
Cdd:PRK12316 2068 VALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLLTQRHL---LERLPLPAGVA-RLPLDRDAEWADYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 164 TTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSI---LRQAAFAANVWNGDDDMHMVSwlplYHDMGIFWGVFMPLLNGG 240
Cdd:PRK12316 2138 APAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALvahCQAAGERYELSPADCELQFMS----FSFDGAHEQWFHPLLNGA 2213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 241 ctTLIpphdfVRNPRIWLetvsrfrgnwiggPDFAYRRCIE------AFDGTALQSLDLSC--------LRLATNGAEPV 306
Cdd:PRK12316 2214 --RVL-----IRDDELWD-------------PEQLYDEMERhgvtilDFPPVYLQQLAEHAerdgrppaVRVYCFGGEAV 2273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 307 RGTTLRdftakFRAAGLRDDVMAPQYGLAEAGLgvtgsqTVRVWveksfDADALERGIAVEVAQPNPADGRSralvscgd 386
Cdd:PRK12316 2274 PAASLR-----LAWEALRPVYLFNGYGPTEAVV------TPLLW-----KCRPQDPCGAAYVPIGRALGNRR-------- 2329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 387 gafgwdIQIVDPDRHMtLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGR 464
Cdd:PRK12316 2330 ------AYILDADLNL-LAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLyRTGDlARYRADGVVEYLGR 2402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 465 YRDLIIVGGRNHFPNDIEKTVEeAHCGVAPGGACAVQ-PDAPQANGewWLVLETGSPvEDLDDLSRILRRRILAHHETAP 543
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQ-AHPAVREAVVVAQDgASGKQLVA--YVVPDDAAE-DLLAELRAWLAARLPAYMVPAH 2478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 544 ervvWVPCRTLPTTTSGKIRRRETLNRltagqlevvhEVSPRAQAPDTPAAPDDppTELAQHLAAMLGVEpyELAPDADL 623
Cdd:PRK12316 2479 ----WVVLERLPLNPNGKLDRKALPKP----------DVSQLRQAYVAPQEGLE--QRLAAIWQAVLKVE--QVGLDDHF 2540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 624 TTLGLTSMMTAQIVEwSSSQSRRLDFA--DLYAEPTLRSWQ-RLFDAAPPVQTGTSSVAASGPWPTTPLQQAYWVGRGAE 700
Cdd:PRK12316 2541 FELGGHSLLATQVVS-RVRQDLGLEVPlrILFERPTLAAFAaSLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLE 2619
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 701 QPLGGVGCQTYFELVGaRVDAGRLAAALDALTRRHPMLRATFPDPG---RCLITPEAVRLPLAVHDLTDAPVTTRDTHLA 777
Cdd:PRK12316 2620 PESAAYHLPSALHLRG-VLDQAALEQAFDALVLRHETLRTRFVEVGeqtRQVILPNMSLRIVLEDCAGVADAAIRQRVAE 2698
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 778 EIRRRlrthrFDIETGDTWTVELTRLPHGCIVH-FAVDLIIADVTSIGTMLRDLAASYRGEK------LPAPSATFADLI 850
Cdd:PRK12316 2699 EIQRP-----FDLARGPLLRVRLLALDGQEHVLvITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYA 2773
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 851 QSTSPPPQACADRLP----------EGPQL------PRVQEADISFLRHQHTLSALATKAIDDACHNHGVTRAAVLLAAY 914
Cdd:PRK12316 2774 AWQRAWMDSGEGARQldywrerlggEQPVLelpldrPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASF 2853
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 915 TLVLRRWASQDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQkglRTALRAAPAPDL------L 987
Cdd:PRK12316 2854 QVLLHRYSGQSDIRVGVPIANRNrAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVK---EQALGAQAHQDLpfeqlvE 2930
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 988 ATQLRSGTGHSGIVPVVFTYAaDSPLLSAEDANTLGAIDEVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCFPPGVVDDM 1067
Cdd:PRK12316 2931 ALQPERSLSHSPLFQVMYNHQ-SGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERL 3009
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1068 FEAYVTLLER-LGGHDWSTPATPGLSAHSR-LARAHRNATTTPAPAGL-LYDAFRENAATHPARLALrwrpddYRGERHg 1144
Cdd:PRK12316 3010 ARHWQNLLRGmVENPQRSVDELAMLDAEERgQLLEAWNATAAEYPLERgVHRLFEEQVERTPDAVAL------AFGEQR- 3082
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1145 dviaqdrsqLTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARS 1223
Cdd:PRK12316 3083 ---------LSYAELNRRANRLAHRLIERGVGPDVlVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDS 3153
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1224 AMAGLIRTD--SDTQDAGVAVSDITAMIECAPTD--PIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNR 1299
Cdd:PRK12316 3154 GAQLLLSQShlRLPLAQGVQVLDLDRGDENYAEAnpAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG 3233
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1300 IDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLiaAGDKAGSLP 1379
Cdd:PRK12316 3234 LGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL--EEEDAHRCT 3311
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1380 TLRSVFLSGDWIPLDLprrLRRAAPGVRLVAMGGATEAAIWSNefVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPD 1459
Cdd:PRK12316 3312 SLKRIVCGGEALPADL---QQQVFAGLPLYNLYGPTEATITVT--HWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPV 3386
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1460 YVAGELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHAL 1537
Cdd:PRK12316 3387 GALGELYLGGEGLARGYHNRPGLTAERFVPDPfvPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL 3466
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1538 RGHPLVAAATVVPIhNCTALGAGIVVTGSGAEqfddsTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKIAA 1617
Cdd:PRK12316 3467 LEHPWVREAVVLAV-DGRQLVAYVVPEDEAGD-----LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1618 RLEAAARApqplDTSSTLTVVERLVAEVWSDVLGAPITGREDNFFAQGGDSLRATEAVARLTRRGVAGAEvGQLLSHQTL 1697
Cdd:PRK12316 3541 PDAALLQQ----DYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTP-KDLFQHQTI 3615
|
....*.
gi 2181016861 1698 GQFSAA 1703
Cdd:PRK12316 3616 QGLARV 3621
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
684-2961 |
3.34e-108 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 390.47 E-value: 3.34e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 684 WPTTPLQQAYWVGRGAEQPLGGVGCQTYFELVGarVDAGRLAAALDALTRRHPMLRATF---PDPGRCL-ITPEAVRLPL 759
Cdd:PRK12316 1557 YPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG--LDPDRFRAAWQATVDRHEILRSGFlwqDGLEQPLqVIHKQVELPF 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 760 AVHDLTDAPVTTRDthLAEIRRRLRTHRFDIETGDTWTVELTRLPHGCI-VHFAVDLIIADVTSIGTMLRDLAASYRGEK 838
Cdd:PRK12316 1635 AELDWRGREDLGQA--LDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHhLIYTNHHILMDGWSNAQLLGEVLQRYAGQP 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 839 LPAPSATFADLIQSTSPPPQACADRL-------PEGP----QLPRVQEADISFLRHQHTLSALATKAIDDACHNHGVTRA 907
Cdd:PRK12316 1713 VAAPGGRYRDYIAWLQRQDAAASEAFwkeqlaaLEEPtrlaQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLN 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 908 AVLLAAYTLVLRRWASQDDFLVNVTTFGRSPEVSDV---VGDFTETHLYRAQLDGQISFVDQAQVTQkGLRTALRAAPAP 984
Cdd:PRK12316 1793 TLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIeqqIGLFINTLPVIAAPRPDQSVADWLQEVQ-ALNLALREHEHT 1871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 985 DLLATQLRSGTGHSGIVP--VVF-TYAADSPLLSAEDANTlgAIDEVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCFPP 1061
Cdd:PRK12316 1872 PLYDIQRWAGQGGEALFDslLVFeNYPVAEALKQGAPAGL--VFGRVSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDA 1949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1062 GVVDDMFEAYVTLLERLGGH-DWSTPATPGLSAHSR-LARAHRNATTTPAPAGLL-YDAFRENAATHPARLALRWrpddy 1138
Cdd:PRK12316 1950 AAIERLDRHLLHLLEQMAEDaQAALGELALLDAGERqRILADWDRTPEAYPRGPGvHQRIAEQAARAPEAIAVVF----- 2024
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1139 rGERHgdviaqdrsqLTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLS 1217
Cdd:PRK12316 2025 -GDQH----------LSYAELDSRANRLAHRLRARGVGPEVrVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA 2093
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1218 RICARSAmAGLIRTDSDTQD-----AGVAVSDITAMIECA---PTDP-IRIDPHDAAYVIYTSGSTGEPKGVLVSHAAAL 1288
Cdd:PRK12316 2094 YMLEDSG-AALLLTQRHLLErlplpAGVARLPLDRDAEWAdypDTAPaVQLAGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1289 NTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTipeharRDAFHWLSLTT-----EFGITVWNSVPGL 1363
Cdd:PRK12316 2173 AHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI------RDDELWDPEQLydemeRHGVTILDFPPVY 2246
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1364 MdMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDP-DWASIPYGYPL 1442
Cdd:PRK12316 2247 L-QQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPcGAAYVPIGRAL 2325
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1443 ANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFLGRADS 1519
Cdd:PRK12316 2326 GNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPfsaSGERLYRTGDLARYRADGVVEYLGRIDH 2405
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1520 QVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTA-LGAGIVVTGSGAEQFddstPGALRAHLAVRLPQYMIPKVFVS 1598
Cdd:PRK12316 2406 QVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGkQLVAYVVPDDAAEDL----LAELRAWLAARLPAYMVPAHWVV 2481
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1599 CPELPLTANGKVDRGKIAARLEAAARAPQpldtSSTLTVVERLVAEVWSDVLGAPITGREDNFFAQGGDSLRATEAVARL 1678
Cdd:PRK12316 2482 LERLPLNPNGKLDRKALPKPDVSQLRQAY----VAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRV 2557
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1679 TRRGVAGAEVGQLLSHQTLGQFSAACvladpaSEASESAADVGEPVTPGEGFPLTRLQQAYTLGAAGLNGSTCAPTYFAV 1758
Cdd:PRK12316 2558 RQDLGLEVPLRILFERPTLAAFAASL------ESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSAL 2631
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1759 VLAAAPESAGIDlDRFARVVTRcvDEFAMLRCALDADTTQRVQVDAGPVPVHDLDIQDDPDLLLRRMAAA----PFDPHS 1834
Cdd:PRK12316 2632 HLRGVLDQAALE-QAFDALVLR--HETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEeiqrPFDLAR 2708
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1835 VPVIQCFAPSRSPRHVGLLIS--YLGLDARSLSTVVTTIIAEYQSQPRPRQVdPTAAVFARFASESAWGENDVDNS---- 1908
Cdd:PRK12316 2709 GPLLRVRLLALDGQEHVLVITqhHIVSDGWSMQVMVDELVQAYAGARRGEQP-TLPPLPLQYADYAAWQRAWMDSGegar 2787
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1909 ----------VAGPPLLPLHDQRRDPFERVTFARRSFTIEEQAAATLREHAAHLGVTPTALVFEAFAHALASIGAGQRFA 1978
Cdd:PRK12316 2788 qldywrerlgGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIR 2867
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1979 VTVPKSYRPdyAPADREVLGNF--TRLALCEVDYGAvrpGSAEAVAAAQRELWRAVSHDG----DITGGLAATRTAGGYP 2052
Cdd:PRK12316 2868 VGVPIANRN--RAETERLIGFFvnTQVLRAQVDAQL---AFRDLLGQVKEQALGAQAHQDlpfeQLVEALQPERSLSHSP 2942
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2053 ------VVFTSTLGLTHQDASGLTNVRTLTQTPGVWLDCQTEDEVAGIRMSWDIATNVVAAESISVAFSRFEEAVRrhaG 2126
Cdd:PRK12316 2943 lfqvmyNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLR---G 3019
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2127 QAEPPGTAVAPAVGGSPgPEWASAVIA---AALRHCRPEQVLPQYTMLVRRWE---ALRYVPSGYAASDVERAARRLA-G 2199
Cdd:PRK12316 3020 MVENPQRSVDELAMLDA-EERGQLLEAwnaTAAEYPLERGVHRLFEEQVERTPdavALAFGEQRLSYAELNRRANRLAhR 3098
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2200 IVTGAVSPQTLIG--------------------------DPQLTPE--ALLLRDDRMRMAL------------------- 2232
Cdd:PRK12316 3099 LIERGVGPDVLVGvaverslemvvgllailkaggayvplDPEYPEErlAYMLEDSGAQLLLsqshlrlplaqgvqvldld 3178
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2233 --DDLAGAIFGHARTLGRRLRVV-----------EVGSRTGLITERLTELVG-------------------VVVEEYLCL 2280
Cdd:PRK12316 3179 rgDENYAEANPAIRTMPENLAYViytsgstgkpkGVGIRHSALSNHLCWMQQayglgvgdrvlqfttfsfdVFVEELFWP 3258
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2281 EPNPTLAGIAAGRRFPAPTRHVD----------------------APDAASGVDVVIC-CGSLHQLPDAEAVLEA----- 2332
Cdd:PRK12316 3259 LMSGARVVLAGPEDWRDPALLVElinsegvdvlhaypsmlqafleEEDAHRCTSLKRIvCGGEALPADLQQQVFAglply 3338
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2333 ------ITVSDDGWLWMVENSEAT---------QATLISAAVLDP------------GLLASDSKTLRPADRWWRLIAD- 2384
Cdd:PRK12316 3339 nlygptEATITVTHWQCVEEGKDAvpigrpianRACYILDGSLEPvpvgalgelylgGEGLARGYHNRPGLTAERFVPDp 3418
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2385 --------------------------------------------------HGWRPTHMIQDGPGLTLIAHR--------- 2405
Cdd:PRK12316 3419 fvpgerlyrtgdlaryradgvieyigrvdhqvkirgfrielgeiearlleHPWVREAVVLAVDGRQLVAYVvpedeagdl 3498
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2406 ------------PDK---------PGMPTPPaeqrrDGRWSRPAVP---ASSLPTD--ATVVA---TLAEIWQRHLAIPT 2456
Cdd:PRK12316 3499 realkahlkaslPEYmvpahllflERMPLTP-----NGKLDRKALPrpdAALLQQDyvAPVNElerRLAAIWADVLKLEQ 3573
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2457 PGVDDDFFLLGGDSLVATRVYADLRAAGFgQLAFVDLFNHSTLGELAAHAgpRTGPEVSVAAESTRGGThdpnrfPLTVV 2536
Cdd:PRK12316 3574 VGLTDNFFELGGDSIISLQVVSRARQAGI-RFTPKDLFQHQTIQGLARVA--RVGGGVAVDQGPVSGET------LLLPI 3644
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2537 QNAYragregaLILGGVAAHCYFEFELADFDRP----RFDSAARQLVARHAGLRTTVSP-AGTDAASSGEVAVVHTAPIE 2611
Cdd:PRK12316 3645 QQQF-------FEEPVPERHHWNQSLLLKPREAldaaALEAALQALVEHHDALRLRFVEdAGGWTAEHLPVELGGALLWR 3717
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2612 PVVRDHDDVRAAMRD--QIIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLY----RGETVDqLP 2685
Cdd:PRK12316 3718 AELDDAEELERLGEEaqRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllQGEAPR-LP 3796
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2686 PLETSFAHY---VWNHPEllpdaDEAVLPRLAasrdYWRARL-------PSLPPAPKLadmsllfeieEPRFERATATIP 2755
Cdd:PRK12316 3797 AKTSSFKAWaerLQEHAR-----GEALKAELA----YWQEQLqgvsselPCDHPQGAL----------QNRHAASVQTRL 3857
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2756 AVDWSQ--VTRSCRAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDP--DVVGIENVVGDFTSLVLLecRVDEPA 2831
Cdd:PRK12316 3858 DRELTRrlLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDlfADIDLSRTVGWFTSLFPV--RLSPVE 3935
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2832 SIWESVRALQRQLMTdLPHRGadavwLQRELLRFHGNP----TAALFPV---VFTSgLGLVDASARAAVRFAEPV---FA 2901
Cdd:PRK12316 3936 DLGASIKAIKEQLRA-IPNKG-----IGFGLLRYLGDEesrrTLAGLPVpriTFNY-LGQFDGSFDEEMALFVPAgesAG 4008
|
2570 2580 2590 2600 2610 2620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 2902 ASQTPQTVLDFQVWESA----GALKLSWDFVSQAVSPATARTQLESLVDGITGVATRSRRIEHK 2961
Cdd:PRK12316 4009 AEQSPDAPLDNWLSLNGrvygGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAERH 4072
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
684-1719 |
5.99e-107 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 386.23 E-value: 5.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 684 WPTTPLQQAYWVGRGAEQPLGGVGCQTYFELVGarVDAGRLAAALDALTRRHPMLRATFPDPGRC----LITPEAVRLPL 759
Cdd:PRK12316 4103 YPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG--LDVERFRAAWQAALDRHDVLRSGFVWQGELgrplQVVHKQVSLPF 4180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 760 AVHDLTDAPvtTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRL-PHGCIVHFAVDLIIADVTSIGTMLRDLAASYRGEK 838
Cdd:PRK12316 4181 AELDWRGRA--DLQAALDALAAAERERGFDLQRAPLLRLVLVRTaEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRP 4258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 839 LPAPSATFADLIQSTSPPPQACADRLPEgPQLPRVQE----------ADI----SFLRHQHTLSALATKAIDDACHNHGV 904
Cdd:PRK12316 4259 PAQPGGRYRDYIAWLQRQDAAASEAFWR-EQLAALDEptrlaqaiarADLrsanGYGEHVRELDATATARLREFARTQRV 4337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 905 TRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRS---PEVSDVVGDFTETHLYRAQLDGQISFVDQ-AQVTQKGLrtALRA 980
Cdd:PRK12316 4338 TLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPaelPGIEGQIGLFINTLPVIATPRAQQSVVEWlQQVQRQNL--ALRE 4415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 981 APAPDLLATQLRSGTGHSGIVPVVFTYAADSPLLSAEDANTLG-AIDEVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCF 1059
Cdd:PRK12316 4416 HEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGlRFGEVTNHEQTNYPLTLAVGLGETLSLQFSYDRGHF 4495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1060 PPGVVDDMFEAYVTLLERLGGHDWSTPATPGL--SAHSRLARAHRNATTTPAPAG-LLYDAFRENAATHPARLALRWrpd 1136
Cdd:PRK12316 4496 DAATIERLARHLTNLLEAMAEDPQRRLGELQLleKAEQQRIVALWNRTDAGYPATrCVHQLVAERARMTPDAVAVVF--- 4572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1137 dyrgerhgdviaqDRSQLTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAER 1215
Cdd:PRK12316 4573 -------------DEEKLTYAELNRRANRLAHALIARGVGPEVlVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1216 LSRICARSAmAGLIRTDSDTQD-----AGVAVSDITAMIECA---PTDP-IRIDPHDAAYVIYTSGSTGEPKGVLVSHAA 1286
Cdd:PRK12316 4640 LAYMMEDSG-AALLLTQSHLLQrlpipDGLASLALDRDEDWEgfpAHDPaVRLHPDNLAYVIYTSGSTGRPKGVAVSHGS 4718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1287 ALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVtIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDM 1366
Cdd:PRK12316 4719 LVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVV-IRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQ 4797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1367 LLIAAgDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDPDWAS-IPYGYPLANQ 1445
Cdd:PRK12316 4798 LAEHA-ERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAyMPIGTPLGNR 4876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1446 MFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFLGRADSQVK 1522
Cdd:PRK12316 4877 SGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgaPGGRLYRTGDLARYRADGVIDYLGRVDHQVK 4956
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1523 IRGHRVECGEIEHALRGHPLVAAATVVPIHNctALGAGIV--VTGSGAEQFDDSTPGA-----LRAHLAVRLPQYMIPKV 1595
Cdd:PRK12316 4957 IRGFRIELGEIEARLREHPAVREAVVIAQEG--AVGKQLVgyVVPQDPALADADEAQAelrdeLKAALRERLPEYMVPAH 5034
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1596 FVSCPELPLTANGKVDRGKIaarleaaaraPQPlDTS-------STLTVVERLVAEVWSDVLGAPITGREDNFFAQGGDS 1668
Cdd:PRK12316 5035 LVFLARMPLTPNGKLDRKAL----------PQP-DASllqqayvAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHS 5103
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1669 LRATEAVARLTrrgvagAEVGQLLSHQTLGQFSAACVLADPASEASESAAD 1719
Cdd:PRK12316 5104 LLAIQVTSRIQ------LELGLELPLRELFQTPTLAAFVELAAAAGSGDDE 5148
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1153-1614 |
2.71e-105 |
|
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: 346.59 E-value: 2.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1153 QLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRIcARSAMAGLIRT 1231
Cdd:cd12116 12 SLSYAELDERANRLAARlRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI-LEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1232 DSDTQDAGVAVSDITAMIECAPT-DPIRI----DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRL 1306
Cdd:cd12116 91 DDALPDRLPAGLPVLLLALAAAAaAPAAPrtpvSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1307 LALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLrsvfL 1386
Cdd:cd12116 171 LAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTAL----C 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1387 SGDWIPLDLPRRLrrAAPGVRLVAMGGATEAAIWSnefVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELW 1466
Cdd:cd12116 247 GGEALPPDLAARL--LSRVGSLWNLYGPTETTIWS---TAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1467 IGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLV 1543
Cdd:cd12116 322 IGGDGVAQGYLGRPALTAERFVPDPfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGV 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1544 --AAATVVPIHNCTALGAgiVVTGSGAEQFDdstPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGK 1614
Cdd:cd12116 402 aqAAVVVREDGGDRRLVA--YVVLKAGAAPD---AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKA 469
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1122-1615 |
1.36e-104 |
|
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: 343.85 E-value: 1.36e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1122 AATHPARLALRWRPDDyrgerhgdviaqdrsqLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLGVMMA 1200
Cdd:cd05945 1 AAANPDRPAVVEGGRT----------------LTYRELKERADALAAAlASLGLDAGDPVVVYGHKSPDAIAAFLAALKA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1201 GCTYLPVGVDQPAERLSRICARSAMAGLIrtdsdtqdagvavsditamiecaptdpirIDPHDAAYVIYTSGSTGEPKGV 1280
Cdd:cd05945 65 GHAYVPLDASSPAERIREILDAAKPALLI-----------------------------ADGDDNAYIIFTSGSTGRPKGV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1281 LVSHAAaLNTIVDVNR-RNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNS 1359
Cdd:cd05945 116 QISHDN-LVSFTNWMLsDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1360 VPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEA--AIWSNEFVVDDVDpDWASIP 1437
Cdd:cd05945 195 TPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEAtvAVTYIEVTPEVLD-GYDRLP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1438 YGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDPtGSRWYRTGDMGCYWRDGTLQFLGRA 1517
Cdd:cd05945 274 IGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-GQRAYRTGDLVRLEADGLLFYRGRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1518 DSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHN---CTALgAGIVVTGSGAEQFDdstPGALRAHLAVRLPQYMIPK 1594
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKgekVTEL-IAFVVPKPGAEAGL---TKAIKAELAERLPPYMIPR 428
|
490 500
....*....|....*....|.
gi 2181016861 1595 VFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05945 429 RFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1116-1612 |
6.42e-104 |
|
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: 343.41 E-value: 6.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1116 DAFRENAATHPARLALRWRpddyrgerhgdviaqDRSqLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAV 1194
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYG---------------DRS-LTYAELNERANRLARRLRAAgVGPGDVVGVLAERSPELVVAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1195 LGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSDTQDAGVA----VSDITAMIECAPTDPIRIDPHDAAYVIYT 1270
Cdd:cd12117 65 LAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLevavVIDEALDAGPAGNPAVPVSPDDLAYVMYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1271 SGSTGEPKGVLVSHAAALNTIVDVNRRnRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTT 1350
Cdd:cd12117 145 SGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1351 EFGITVWNSVPGLMDMLliaAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVD 1430
Cdd:cd12117 224 EEGVTVLWLTAALFNQL---ADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1431 PDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYWRD 1508
Cdd:cd12117 301 EVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPfgPGERLYRTGDLARWLPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1509 GTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNC---TALGAGIVVTGSGaeqfddsTPGALRAHLAV 1585
Cdd:cd12117 381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAggdKRLVAYVVAEGAL-------DAAELRAFLRE 453
|
490 500
....*....|....*....|....*..
gi 2181016861 1586 RLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd12117 454 RLPAYMVPAAFVVLDELPLTANGKVDR 480
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1118-1612 |
6.09e-101 |
|
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: 335.08 E-value: 6.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1118 FRENAATHPARLALrwrpddyrgerhgdviAQDRSQLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLG 1196
Cdd:cd17651 1 FERQAARTPDAPAL----------------VAEGRRLTYAELDRRANRLAHRlRARGVGPGDLVALCARRSAELVVALLA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1197 VMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSDTQDAGVAVSDITAMIE-----CAPTDP-IRIDPHDAAYVIYT 1270
Cdd:cd17651 65 ILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQpgaaaGADAEPdPALDADDLAYVIYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1271 SGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTT 1350
Cdd:cd17651 145 SGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1351 EFGITVwNSVPGLMDMLLIAAGDKAGS-LPTLRSVFLSGDWIPLD-LPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDD 1428
Cdd:cd17651 225 EQRISR-VFLPTVALRALAEHGRPLGVrLAALRYLLTGGEQLVLTeDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1429 VDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYW 1506
Cdd:cd17651 304 PAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPfvPGARMYRTGDLARWL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1507 RDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTA---LGAGIVvtgsgAEQFDDSTPGALRAHL 1583
Cdd:cd17651 384 PDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGekrLVAYVV-----GDPEAPVDAAELRAAL 458
|
490 500
....*....|....*....|....*....
gi 2181016861 1584 AVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17651 459 ATHLPEYMVPSAFVLLDALPLTPNGKLDR 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
718-1739 |
7.14e-101 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 366.20 E-value: 7.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 718 RVDAGRLAAALDALTRRHPMLRATFPDPG--RCLITPEAVRLPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRFDIETGDT 795
Cdd:PRK12316 83 PLDRQALERAFASLVQRHETLRTVFPRGAddSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 796 WTVELTRLPHG------CIVHfavdlIIADVTSIGTMLRDLAASY------RGEKLPAPSATFAD--LIQSTSPPPQACA 861
Cdd:PRK12316 163 LRVRLLRLGEEehvlllTLHH-----IVSDGWSMNVLIEEFSRFYsayatgAEPGLPALPIQYADyaLWQRSWLEAGEQE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 862 DRLP--------EGPQL------PRVQEADISFLRHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQDDF 927
Cdd:PRK12316 238 RQLEywraqlgeEHPVLelptdhPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 928 LVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFvdqAQVTQKGLRTALRAAPAPDLL------ATQLRSGTGHSGI 1000
Cdd:PRK12316 318 RVGVPIANRNrAEVEGLIGFFVNTQVLRSVFDGRTRV---ATLLAGVKDTVLGAQAHQDLPferlveALKVERSLSHSPL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1001 VPVVFTY---AADSPLLSAEDANTLGAIdEVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLE- 1076
Cdd:PRK12316 395 FQVMYNHqplVADIEALDTVAGLEFGQL-EWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRg 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1077 RLGGHDWSTPATPGLSAHSRLARAH---RNATTTPAPAGLLYdAFRENAATHPARLALRWrpddyrGErhgdviaqdrSQ 1153
Cdd:PRK12316 474 MVENPQARVDELPMLDAEERGQLVEgwnATAAEYPLQRGVHR-LFEEQVERTPEAPALAF------GE----------ET 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1154 LTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAmAGLIRTD 1232
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVlVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSG-VQLLLSQ 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1233 SDTQ-----DAGV---AVSDITAMIECAPTDP--IRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDT 1302
Cdd:PRK12316 616 SHLGrklplAAGVqvlDLDRPAAWLEGYSEENpgTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGV 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1303 HDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKagSLPTLR 1382
Cdd:PRK12316 696 GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLR 773
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1383 SVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVddVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVA 1462
Cdd:PRK12316 774 RIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGGDSVPIGRPIANLACYILDANLEPVPVGVL 851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1463 GELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGH 1540
Cdd:PRK12316 852 GELYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 931
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1541 PLVAAAtVVPIHNCTALGAGIVVTGSGAeqfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKIaarle 1620
Cdd:PRK12316 932 PWVREA-AVLAVDGKQLVGYVVLESEGG-----DWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL----- 1000
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1621 aaaraPQPLDT------SSTLTVVERLVAEVWSDVLGAPITGREDNFFAQGGDSLRATEAVARLTRRGVAGAEvGQLLSH 1694
Cdd:PRK12316 1001 -----PAPEASvaqqgyVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSP-RDLFQH 1074
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 2181016861 1695 QTLGQfsaacvLADPASEASESAADVGePVTpGEgFPLTRLQQAY 1739
Cdd:PRK12316 1075 QTIRS------LALVAKAGQATAADQG-PAS-GE-VALAPVQRWF 1110
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
684-1730 |
2.00e-99 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 361.02 E-value: 2.00e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 684 WPTTPLQQAYWVGRGAEQPLGGVGCQTYFELVGarVDAGRLAAALDALTRRHPMLRATFPDPGRcLITP-----EAVRLP 758
Cdd:PRK12467 2647 YPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG--LDVERFRTAWQAVIDRHEILRSGFLWDGE-LEEPlqvvyKQARLP 2723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 759 LAVHDLTDAPVTTRDthLAEIRRRLRTHRFDIETGDTWTVELTRLPHG-CIVHFAVDLIIADVTSIGTMLRDLAASYRGE 837
Cdd:PRK12467 2724 FSRLDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDrHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQ 2801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 838 KLPAPSATFADLIQ------------------STSPPPQACADRLPEGPQLPRVQEADisflrHQHTLSALATKAIDDAC 899
Cdd:PRK12467 2802 PPPAREGRYRDYIAwlqaqdaeaseafwkeqlAALEEPTRLARALYPAPAEAVAGHGA-----HYLHLDATQTRQLIEFA 2876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 900 HNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRSPE---VSDVVGDFTETHLYRAQLDGQISFVDQAQVTQkGLRT 976
Cdd:PRK12467 2877 RRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQlrgAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQ-AQNL 2955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 977 ALRAAPAPDLLATQLRSGTGHSGIVP--VVF-TYAADSPLlsAEDANTLGAIDEVVSMT----PQVLidhqACRLGDDVV 1049
Cdd:PRK12467 2956 ALREFEHTPLADIQRWAGQGGEALFDsiLVFeNYPISEAL--KQGAPSGLRFGAVSSREqtnyPLTL----AVGLGDTLE 3029
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1050 LSWDYRAGCFPPGVVDDMFEAYVTLLERLGGHDWSTPAT-PGLSAHSRLARAH-RNATTTPAPAG-LLYDAFRENAATHP 1126
Cdd:PRK12467 3030 LEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGElPTLAAHERRQVLHaWNATAAAYPSErLVHQLIEAQVARTP 3109
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1127 ARLALrwrpddyrgerhgdvIAQDRsQLTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMAGCTYL 1205
Cdd:PRK12467 3110 EAPAL---------------VFGDQ-QLSYAELNRRANRLAHRLIAIGVGPDVlVGVAVERSVEMIVALLAVLKAGGAYV 3173
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1206 PVGVDQPAERLSRICARSAMAGLIRTDSDTQDAGVAVSDITAMIE------CAPTDP-IRIDPHDAAYVIYTSGSTGEPK 1278
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDrldlngYSENNPsTRVMGENLAYVIYTSGSTGKPK 3253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1279 GVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEfGITVWN 1358
Cdd:PRK12467 3254 GVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAH-RISIAC 3332
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1359 SVPGLMDMLLIAAGdkAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVD-DVDPDWASIP 1437
Cdd:PRK12467 3333 FPPAYLQQFAEDAG--GADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGgDAVCEAPYAP 3410
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1438 YGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFL 1514
Cdd:PRK12467 3411 IGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPfsgSGGRLYRTGDLARYRADGVIEYL 3490
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1515 GRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHncTALG---AGIVVTGSGAEQFDDstpgALRAHLAVRLPQYM 1591
Cdd:PRK12467 3491 GRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD--GAGGkqlVAYVVPADPQGDWRE----TLRDHLAASLPDYM 3564
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1592 IPKVFVSCPELPLTANGKVDRG---KIAARLEAAARAPQpldtsstlTVVERLVAEVWSDVLGAPITGREDNFFAQGGDS 1668
Cdd:PRK12467 3565 VPAQLLVLAAMPLGPNGKVDRKalpDPDAKGSREYVAPR--------SEVEQQLAAIWADVLGVEQVGVTDNFFELGGDS 3636
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1669 LRATEAVARLtrRGVAGAEVG--QLLSHQTLGQFSAAC----VLADPASEASESAADVGEPVTPGEGF 1730
Cdd:PRK12467 3637 LLALQVLSRI--RQSLGLKLSlrDLMSAPTIAELAGYSplgdVPVNLLLDLNRLETGFPALFCRHEGL 3702
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1150-1612 |
5.57e-98 |
|
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: 324.65 E-value: 5.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1150 DRSQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICArsamagl 1228
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEgVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1229 irtdsdtqDAGVAVsditamiecaptdpIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLA 1308
Cdd:cd17643 82 --------DSGPSL--------------LLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1309 LSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSG 1388
Cdd:cd17643 140 FHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1389 DWIPLDLPRRL--RRAAPGVRLVAMGGATEAAIWSNEFVVDDVD-PDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGEL 1465
Cdd:cd17643 220 EALEAAMLRPWagRFGLDRPQLVNMYGITETTVHVTFRPLDAADlPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGEL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1466 WIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPL 1542
Cdd:cd17643 300 YVSGAGVARGYLGRPELTAERFVANPfggPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPS 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1543 VAAATVVPIHNCT---ALgAGIVVTGSGAEQfddsTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17643 380 VRDAAVIVREDEPgdtRL-VAYVVADDGAAA----DIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1089-1732 |
7.34e-96 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 341.64 E-value: 7.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1089 PGLSAHSRLARAHRNATTTPAPAGLLYDAFRENAATHParlalrwrpddyrgerHGDVIAQDRSQLTYGELDELARSVAR 1168
Cdd:PRK10252 435 DILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTP----------------DAPALADARYQFSYREMREQVVALAN 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1169 A-VAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICArSAMAGLIRTDSDTQDAGVAVSDITA 1247
Cdd:PRK10252 499 LlRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE-DARPSLLITTADQLPRFADVPDLTS 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1248 MIECAP-----TDPIRID-PHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDT 1321
Cdd:PRK10252 578 LCYNAPlapqgAAPLQLSqPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEF 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1322 FGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAG--DKAGSLPTLRSVFLSGDWIPLDLPRRL 1399
Cdd:PRK10252 658 FWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTpeGARQSCASLRQVFCSGEALPADLCREW 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1400 RRAApGVRLVAMGGATEAAI---WSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGY 1476
Cdd:PRK10252 738 QQLT-GAPLHNLYGPTEAAVdvsWYPAFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGY 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1477 HNAPELTSDRFVHDP--TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI--- 1551
Cdd:PRK10252 817 LGRPDLTASRFIADPfaPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvin 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1552 -HNCTALGA----GIVVTGSGAEQfdDStpGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKIaarleaaaraP 1626
Cdd:PRK10252 897 qAAATGGDArqlvGYLVSQSGLPL--DT--SALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL----------P 962
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1627 QPLDTSST-----LTVVERLVAEVWSDVLGAPITGREDNFFAQGGDSLRATEAVARLTRRGVAGAEVGQLLSHQTLGQFS 1701
Cdd:PRK10252 963 LPELKAQVpgrapKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLA 1042
|
650 660 670
....*....|....*....|....*....|.
gi 2181016861 1702 AAcvLADPASEASESAADVGEPVTPGEGFPL 1732
Cdd:PRK10252 1043 TL--LDAEEDESRRLGFGTILPLREGDGPTL 1071
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1114-1615 |
2.63e-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: 315.25 E-value: 2.63e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAATHPARLAlrwrpddyrgerhgdVIAQDRSqLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIV 1192
Cdd:cd05918 1 VHDLIEERARSQPDAPA---------------VCAWDGS-LTYAELDRLSSRLAHHlRSLGVGPGVFVPLCFEKSKWAVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1193 AVLGVMMAGCTYLPVGVDQPAERLSRICARSamaglirtdsdtqDAGVAVSDitamiecaptdpiriDPHDAAYVIYTSG 1272
Cdd:cd05918 65 AMLAVLKAGGAFVPLDPSHPLQRLQEILQDT-------------GAKVVLTS---------------SPSDAAYVIFTSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1273 STGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDafhwlSLT--- 1349
Cdd:cd05918 117 STGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN-----DLAgfi 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1350 TEFGITVWNSVPGLMDMLliaagdKAGSLPTLRSVFLSGDwiPLDlPRRLRRAAPGVRLVAMGGATEAAIWSNEF-VVDD 1428
Cdd:cd05918 192 NRLRVTWAFLTPSVARLL------DPEDVPSLRTLVLGGE--ALT-QSDVDTWADRVRLINAYGPAECTIAATVSpVVPS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1429 VDPdwASIpyGYPLANQMFrVVDDNGDDQPdyVA----GELWIGGAGVALGYHNAPELTSDRFVHDP---------TGSR 1495
Cdd:cd05918 263 TDP--RNI--GRPLGATCW-VVDPDNHDRL--VPigavGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegsgRGRR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1496 WYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGH-PLVAAATVVPIHNCTALGAGIVV---------TG 1565
Cdd:cd05918 336 LYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPQLVafvvldgssSG 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1566 SGAEQFDDSTPG--------ALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05918 416 SGDGDSLFLEPSdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1114-1615 |
6.19e-92 |
|
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: 307.32 E-value: 6.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAATHPARLAlrwrpddyrgerhgdVIAQDRSqLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIV 1192
Cdd:cd12115 1 LHDLVEAQAARTPDAIA---------------LVCGDES-LTYAELNRRANRLAARLRAAgVGPESRVGVCLERTPDLVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1193 AVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIrtdsdtqdagvavsditamiecaptdpirIDPHDAAYVIYTSG 1272
Cdd:cd12115 65 ALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVL-----------------------------TDPDDLAYVIYTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1273 STGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIpeharRDAFHWLSLTTEF 1352
Cdd:cd12115 116 STGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1353 GITVWNSVPGLMDMLLiaagdKAGSLPT-LRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDP 1431
Cdd:cd12115 191 EVTLINTVPSAAAELL-----RHDALPAsVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGAS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1432 DWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDPT--GSRWYRTGDMGCYWRDG 1509
Cdd:cd12115 266 GEVSI--GRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpGARLYRTGDLVRWRPDG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1510 TLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTA---LGAGIVVTGSGAeqfddSTPGALRAHLAVR 1586
Cdd:cd12115 344 LLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGerrLVAYIVAEPGAA-----GLVEDLRRHLGTR 418
|
490 500
....*....|....*....|....*....
gi 2181016861 1587 LPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd12115 419 LPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1146-1612 |
1.23e-91 |
|
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: 306.10 E-value: 1.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1146 VIAQDRsQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSA 1224
Cdd:cd17652 6 VVFGDE-TLTYAELNARANRLARLLAARgVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1225 MAGLIRTdsdtqdagvavsditamiecaptdpiridPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHD 1304
Cdd:cd17652 85 PALLLTT-----------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1305 RLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLliaagdKAGSLPTLRSV 1384
Cdd:cd17652 136 RVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL------PPDDLPDLRTL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1385 FLSGDWIPLDLprrLRRAAPGVRLVAMGGATEAAIWSnefVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGE 1464
Cdd:cd17652 210 VVAGEACPAEL---VDRWAPGRRMINAYGPTETTVCA---TMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1465 LWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHP 1541
Cdd:cd17652 284 LYIAGAGLARGYLNRPGLTAERFVADPfgaPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHP 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1542 LVAAATVVpIHNCTALGAGIV--VTGSGAEQfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17652 364 GVAEAVVV-VRDDRPGDKRLVayVVPAPGAA---PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1118-1615 |
4.72e-89 |
|
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: 300.40 E-value: 4.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1118 FRENAATHPARLAlrwrpddyrgerhgdVIAQDRsQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLG 1196
Cdd:cd17655 3 FEEQAEKTPDHTA---------------VVFEDQ-TLTYRELNERANQLARTLREKgVGPDTIVGIMAERSLEMIVGILG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1197 VMMAGCTYLPVGVDQPAERLSRIcARSAMAGLIRTDSDTQ----DAG--VAVSDITAMIECAPTDPIRIDPHDAAYVIYT 1270
Cdd:cd17655 67 ILKAGGAYLPIDPDYPEERIQYI-LEDSGADILLTQSHLQppiaFIGliDLLDEDTIYHEESENLEPVSKSDDLAYVIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1271 SGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTT 1350
Cdd:cd17655 146 SGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1351 EFGITVWNSVPGLMDMlLIAAGDKAGslPTLRSVFLSGDWIPLDLPRRL-RRAAPGVRLVAMGGATEAAIWSNEFVVDDV 1429
Cdd:cd17655 226 QNRITIIDLTPAHLKL-LDAADDSEG--LSLKHLIVGGEALSTELAKKIiELFGTNPTITNAYGPTETTVDASIYQYEPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1430 DPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYWR 1507
Cdd:cd17655 303 TDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMYRTGDLARWLP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1508 DGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI---HNCTALGAGIVvtgsgaeQFDDSTPGALRAHLA 1584
Cdd:cd17655 383 DGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARkdeQGQNYLCAYIV-------SEKELPVAQLREFLA 455
|
490 500 510
....*....|....*....|....*....|.
gi 2181016861 1585 VRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd17655 456 RELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1147-1612 |
4.07e-87 |
|
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: 293.22 E-value: 4.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1147 IAQDRSQLTYGELDELA-RSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSricarsam 1225
Cdd:cd17650 6 VSDATRQLTYRELNERAnQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQ-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1226 aglirtdsdtqdagvavsditAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHD- 1304
Cdd:cd17650 78 ---------------------YMLEDSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPv 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1305 RLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSV 1384
Cdd:cd17650 137 RLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1385 FLSGDWIPLDLPRRL-RRAAPGVRLVAMGGATEAAIWSNEFVVDDVD-PDWASIPYGYPLANQMFRVVDDNGDDQPDYVA 1462
Cdd:cd17650 217 IVGSDGCKAQDFKTLaARFGQGMRIINSYGVTEATIDSTYYEEGRDPlGDSANVPIGRPLPNTAMYVLDERLQPQPVGVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1463 GELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGH 1540
Cdd:cd17650 297 GELYIGGAGVARGYLNRPELTAERFVENPfaPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARH 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 1541 PLVAAATVVPIHNC---TALGAGIVvtgsGAEQFDDStpgALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17650 377 PAIDEAVVAVREDKggeARLCAYVV----AAATLNTA---ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1147-1612 |
7.20e-87 |
|
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: 292.74 E-value: 7.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1147 IAQDRSQLTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRIcarsam 1225
Cdd:cd17649 6 LVFGDQSLSYAELDARANRLAHRLRALGVGPEVrVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1226 aglirtdsdTQDAGVAVSditamiecaptdpIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDR 1305
Cdd:cd17649 80 ---------LEDSGAGLL-------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1306 LLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPG-LMDMLLIAAGDKAGSLPTLRSV 1384
Cdd:cd17649 138 ELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAyLQQLAEEADRTGDGRPPSLRLY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1385 FLSGDWIPLDLprrLRRAAP-GVRLVAMGGATEAAIWSNEFVVD-DVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVA 1462
Cdd:cd17649 218 IFGGEALSPEL---LRRWLKaPVRLFNAYGPTEATVTPLVWKCEaGAARAGASMPIGRPLGGRSAYILDADLNPVPVGVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1463 GELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRG 1539
Cdd:cd17649 295 GELYIGGEGLARGYLGRPELTAERFVPDPfgaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 1540 HPLVAAATVV--PIHNCTALgAGIVVTGSGAEQFDDstPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17649 375 HPGVREAAVValDGAGGKQL-VAYVVLRAAAAQPEL--RAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1118-1524 |
7.16e-85 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 285.75 E-value: 7.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1118 FRENAATHPARLALrwrpDDYRGERhgdviaqdrsqLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLG 1196
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRR-----------LTYRELDERANRLAAGlRALGVGKGDRVAILLPNSPEWVVAFLA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1197 VMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSDTQDAGVAVSDITAMIEC------------------------A 1252
Cdd:pfam00501 66 CLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLvlvldrdpvlkeeplpeeakpadvP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1253 PTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRN----RIDTHDRLLALSALDFDLSV-YDTFGALGC 1327
Cdd:pfam00501 146 PPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1328 GAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVr 1407
Cdd:pfam00501 226 GATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 LVAMGGATEAAIWSneFVVDDVDPDWASIP-YGYPLANQMFRVVDDN-GDDQPDYVAGELWIGGAGVALGYHNAPELTSD 1485
Cdd:pfam00501 305 LVNGYGLTETTGVV--TTPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAE 382
|
410 420 430
....*....|....*....|....*....|....*....
gi 2181016861 1486 RFVHDptgsRWYRTGDMGCYWRDGTLQFLGRADSQVKIR 1524
Cdd:pfam00501 383 AFDED----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
16-566 |
1.23e-84 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 290.69 E-value: 1.23e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 16 RSVPAVFAEWVGRRPDAVALrtvaaTGID---DWT-----------YQRLWDHVREIRDVAfsglSAGIRIPMALPGGAD 81
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAF-----TFIDyeqDPAgvaetltwsqlYRRTLNVAEELRRHG----STGDRAVILAPQGLE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 82 YVAGMLAALAAGLIPVPvyLPstrEPQRFLA--RAQHILRDCEPSAVYTC----GELVEVLERDPILGALPIrtpaSTAD 155
Cdd:PRK05850 72 YIVAFLGALQAGLIAVP--LS---VPQGGAHdeRVSAVLRDTSPSVVLTTsavvDDVTEYVAPQPGQSAPPV----IEVD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 156 GLA-PHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSI---LRQ---AAFAANVWNGDDDMHMVSWLPLYHDMGI 228
Cdd:PRK05850 143 LLDlDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVianFEQlmsDYFGDTGGVPPPDTTVVSWLPFYHDMGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 229 FWGVFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAY----RRCIEAfDgtaLQSLDLSCLRLATNGAE 304
Cdd:PRK05850 223 VLGVCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFelavRKTSDD-D---MAGLDLGGVLGIISGSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 305 PVRGTTLRDFTAKFRAAGLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDADALERGiaveVAQPNPADGRSrALVSC 384
Cdd:PRK05850 299 RVHPATLKRFADRFAPFNLRETAIRPSYGLAEATVYVATREPGQPPESVRFDYEKLSAG----HAKRCETGGGT-PLVSY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 385 GDGAfGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTAD---GL--GPYLRTGDAGFRYQGEL 459
Cdd:PRK05850 374 GSPR-SPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpspGTpeGPWLRTGDLGFISEGEL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 460 YVCGRYRDLIIVGGRNHFPNDIEKTVEEahcgVAPGGACAVQ-PDapqaNGEWWLVL-----ETGSPVEDLDDLSRILRR 533
Cdd:PRK05850 453 FIVGRIKDLLIVDGRNHYPDDIEATIQE----ITGGRVAAISvPD----DGTEKLVAiielkKRGDSDEEAMDRLRTVKR 524
|
570 580 590
....*....|....*....|....*....|....*..
gi 2181016861 534 RILA----HHETAPERVVWVPCRTLPTTTSGKIRRRE 566
Cdd:PRK05850 525 EVTSaiskSHGLSVADLVLVAPGSIPITTSGKIRRAA 561
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
18-577 |
1.64e-83 |
|
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: 283.24 E-value: 1.64e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 18 VPAVFAEWVGRRPDAVALRTVAATgiddWTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIP 96
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR----LTYAELDARARRLaAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 97 VPVYLPSTREpqrflaRAQHILRDCEPSAVYTcgelvevlerdpilgalpirtpastadglaphpggttadadhgehvAF 176
Cdd:COG0318 77 VPLNPRLTAE------ELAYILEDSGARALVT----------------------------------------------AL 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDfvrnPRI 256
Cdd:COG0318 105 ILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFD----PER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 257 WLETVSRFRGNWIGGPDFAYRRCIEAFDgtaLQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAPQYGLAE 336
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPE---FARYDLSSLRLVVSGGAPLPPELLERFEERF------GVRIVEGYGLTE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 337 AGLGVTGsqtvrvwveksfdadalergiavevaqpNPADGRSRALVSCGDGAFGWDIQIVDPDrHMTLTDGEVGEIWVGG 416
Cdd:COG0318 252 TSPVVTV----------------------------NPEDPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 417 PGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFRY-QGELYVCGRYRDLIIVGGRNHFPNDIEKTVeEAHCGVAPG 495
Cdd:COG0318 303 PNVMKGYWNDPEATAEAF----RDG---WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVL-AAHPGVAEA 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 496 GACAVqPDApqangEW------WLVLETGSPVeDLDDLSRILRRRiLAHHEtAPERVVWVPcrTLPTTTSGKIRRRETLN 569
Cdd:COG0318 375 AVVGV-PDE-----KWgervvaFVVLRPGAEL-DAEELRAFLRER-LARYK-VPRRVEFVD--ELPRTASGKIDRRALRE 443
|
....*...
gi 2181016861 570 RLTAGQLE 577
Cdd:COG0318 444 RYAAGALE 451
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1118-1612 |
5.95e-81 |
|
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: 276.24 E-value: 5.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1118 FRENAATHPARLALRWrpddyrgerhgdviaqDRSQLTYGELDELARSVAR-AVAARHAAGSVIGIQLPKGPSQIVAVLG 1196
Cdd:cd17644 6 FEEQVERTPDAVAVVF----------------EDQQLTYEELNTKANQLAHyLQSLGVKSESLVGICVERSLEMIIGLLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1197 VMMAGCTYLPVGVDQPAERLSRIcarsamaglirtdsdTQDAGVAVsditamiecaptdpIRIDPHDAAYVIYTSGSTGE 1276
Cdd:cd17644 70 ILKAGGAYVPLDPNYPQERLTYI---------------LEDAQISV--------------LLTQPENLAYVIYTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1277 PKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITV 1356
Cdd:cd17644 121 PKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1357 WNSVPGLMDmLLIAAG--DKAGSLPTLRSVFLSGDWIPLDLPRRLRRA-APGVRLVAMGGATEAAIWSNEF-VVDDVDPD 1432
Cdd:cd17644 201 LSLPPAYWH-LLVLELllSTIDLPSSLRLVIVGGEAVQPELVRQWQKNvGNFIQLINVYGPTEATIAATVCrLTQLTERN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1433 WASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP----TGSRWYRTGDMGCYWRD 1508
Cdd:cd17644 280 ITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPfnssESERLYKTGDLARYLPD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1509 GTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTA---LGAGIVvtgsgAEQFDDSTPGALRAHLAV 1585
Cdd:cd17644 360 GNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGnkrLVAYIV-----PHYEESPSTVELRQFLKA 434
|
490 500
....*....|....*....|....*..
gi 2181016861 1586 RLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17644 435 KLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1114-1615 |
5.99e-81 |
|
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: 275.54 E-value: 5.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAATHPARLALRWrpddyrgerhgdviaqDRSQLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIV 1192
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF----------------GGRRLTYAELDARARRLAAAlRALGVGPGDRVALLLPNSPEFVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1193 AVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIrtdsdtqdagvavsditamiecaptdpiridphdAAYVIYTSG 1272
Cdd:COG0318 65 AFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV----------------------------------TALILYTSG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1273 STGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLS-VYDTFGALGCGAQLVTIPehaRRDAFHWLSLTTE 1351
Cdd:COG0318 111 TTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLP---RFDPERVLELIER 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1352 FGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGGATEAAIWSNEFVVDDVDP 1431
Cdd:COG0318 188 ERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGER 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1432 DWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHdptgsRWYRTGDMGCYWRDGTL 1511
Cdd:COG0318 267 RPGSV--GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-----GWLRTGDLGRLDEDGYL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1512 QFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCT---ALGAgIVVTGSGAEqfddSTPGALRAHLAVRLP 1588
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKwgeRVVA-FVVLRPGAE----LDAEELRAFLRERLA 414
|
490 500
....*....|....*....|....*..
gi 2181016861 1589 QYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-1726 |
1.43e-80 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 299.01 E-value: 1.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 112 ARAQHILRDCEPSAVYTCGELVEVLERDPILGALPIRTpaSTADGLAPHPGGTTAdadHGEHVAFLQYSSGSTGKPKGVV 191
Cdd:PRK05691 1218 ERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDS--LHLDSWPSQAPGLHL---HGDNLAYVIYTSGSTGQPKGVG 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 192 NTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGgCTTLIPPHDFVRNPRIWLETVSRFRGNWIGG 271
Cdd:PRK05691 1293 NTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSV-WECFWPLITG-CRLVLAGPGEHRDPQRIAELVQQYGVTTLHF 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 272 PDFAYRRCIEAFDGTALQSLdlsclRLATNGAEPVrgttlrdftakfrAAGLRDDVMA--PQ------YGLAEAGLGVTG 343
Cdd:PRK05691 1371 VPPLLQLFIDEPLAAACTSL-----RRLFSGGEAL-------------PAELRNRVLQrlPQvqlhnrYGPTETAINVTH 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 344 SQTvrvwveksfDADALERgiavevaqpNPAdGRSRALVSCgdgafgwdiQIVDPDRHMtLTDGEVGEIWVGGPGLPDGY 423
Cdd:PRK05691 1433 WQC---------QAEDGER---------SPI-GRPLGNVLC---------RVLDAELNL-LPPGVAGELCIGGAGLARGY 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 424 WRQPEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEktveeAHCGVAPGGACAVQ 501
Cdd:PRK05691 1484 LGRPALTAERFVPDPLGEDGARLyRTGDrARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ-----ARLLAQPGVAQAAV 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 502 PDAPQANGEWWLVLETGSPVEDlDDLSRILRrrilAHHETAPERVV---WVPCRTLPTTTSGKIRRREtlnrLTAGQLEV 578
Cdd:PRK05691 1559 LVREGAAGAQLVGYYTGEAGQE-AEAERLKA----ALAAELPEYMVpaqLIRLDQMPLGPSGKLDRRA----LPEPVWQQ 1629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 579 VHEVSPRaqapdtpaapddppTELAQHLAAM----LGVEPYELapDADLTTLGLTSMMTAQIVewsssqSRRLDFADLya 654
Cdd:PRK05691 1630 REHVEPR--------------TELQQQIAAIwrevLGLPRVGL--RDDFFALGGHSLLATQIV------SRTRQACDV-- 1685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 655 EPTLRSwqrLFDA-----------------APPVQTGTSSVAASGPWPTTPLQQAYWVGRGAE--QPLGGVGCQTYFELV 715
Cdd:PRK05691 1686 ELPLRA---LFEAselgafaeqvariqaagERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEpdSPAYNVGGMARLSGV 1762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 716 garVDAGRLAAALDALTRRHPMLRATFPD----PGRCLITPEAVRLplAVHDLTDAPVTTRDTHLAEIRRRLRTHRFDIE 791
Cdd:PRK05691 1763 ---LDVDRFEAALQALILRHETLRTTFPSvdgvPVQQVAEDSGLRM--DWQDFSALPADARQQRLQQLADSEAHQPFDLE 1837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 792 TGDTWTVELTR---LPHgcivHFAVDL--IIADVTSIGTMLRDLAASYRG--EKLPAPSATFA----------------- 847
Cdd:PRK05691 1838 RGPLLRACLVKaaeREH----YFVLTLhhIVTEGWAMDIFARELGALYEAflDDRESPLEPLPvqyldysvwqrqwlesg 1913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 848 ----------DLIQSTSPPPQACADRlpegPQlPRVQEadisflrHQHTL------SALATK--AIDDAchnHGVTRAAV 909
Cdd:PRK05691 1914 erqrqldywkAQLGNEHPLLELPADR----PR-PPVQS-------HRGELyrfdlsPELAARvrAFNAQ---RGLTLFMT 1978
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 910 LLAAYTLVLRRWASQDDFLVNVTTFGR-SPEVSDVVGDFTETHLYRAQLDGQISFvdqAQVTQKGLRTALRAAPAPDLLA 988
Cdd:PRK05691 1979 MTATLAALLYRYSGQRDLRIGAPVANRiRPESEGLIGAFLNTQVLRCQLDGQMSV---SELLEQVRQTVIEGQSHQDLPF 2055
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 989 TQL-------RSgtghsgivpvvftyAADSPLLSA-------EDANTlgaiDEVVSMTPQVLI-DHQACRLGDDV-VLSW 1052
Cdd:PRK05691 2056 DHLvealqppRS--------------AAYNPLFQVmcnvqrwEFQQS----RQLAGMTVEYLVnDARATKFDLNLeVTDL 2117
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1053 DYRAGC--------FPPGVVDDMFEAYVTLLERLGGHDWSTPATPGLSAHSRLARAHRNATTTPAPAGL---LYDAFREN 1121
Cdd:PRK05691 2118 DGRLGCcltysrdlFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLdqtLHGLFAAQ 2197
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1122 AATHPARLALrwrpdDYRGErhgdviaqdrsQLTYGELDELARSVARAVAARHAAGSV-IGIQLPKGPSQIVAVLGVMMA 1200
Cdd:PRK05691 2198 AARTPQAPAL-----TFAGQ-----------TLSYAELDARANRLARALRERGVGPQVrVGLALERSLEMVVGLLAILKA 2261
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1201 GCTYLPVGVDQPAERLSRICARSAMaGLIRTDSDTQDA------GVA---VSDITAMIECAPTDPI-RID-PHDAAYVIY 1269
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGI-GLLLSDRALFEAlgelpaGVArwcLEDDAAALAAYSDAPLpFLSlPQHQAYLIY 2340
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1270 TSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVtIPEHARRDAFHWLSLT 1349
Cdd:PRK05691 2341 TSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVV-LRAQGQWGAEEICQLI 2419
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1350 TEFGITVWNSVPGLMDMLLIAAGDKAGSLPtLRSVFLSGDWIPLDLPRRLRRA-APGVRLVAMGGATEAAIWSNEFVVDD 1428
Cdd:PRK05691 2420 REQQVSILGFTPSYGSQLAQWLAGQGEQLP-VRMCITGGEALTGEHLQRIRQAfAPQLFFNAYGPTETVVMPLACLAPEQ 2498
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1429 VDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRWYRTGDMGCY 1505
Cdd:PRK05691 2499 LEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPfaaDGGRLYRTGDLVRL 2578
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1506 WRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTALG-AGIVVT--GSGAEQFDDSTPGALRAH 1582
Cdd:PRK05691 2579 RADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQlAGYLVSavAGQDDEAQAALREALKAH 2658
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1583 LAVRLPQYMIPKVFVSCPELPLTANGKVDRGKIaarleaaaraPQP---LDTSSTL---TVVERLVAEVWSDVLGAPITG 1656
Cdd:PRK05691 2659 LKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL----------PAPdpeLNRQAYQaprSELEQQLAQIWREVLNVERVG 2728
|
1690 1700 1710 1720 1730 1740 1750
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1657 REDNFFAQGGDSLRATEAVARLTRRGVAGAEvGQLLSHQTLgQFSAACVLADPASEASESAADVGEPVTP 1726
Cdd:PRK05691 2729 LGDNFFELGGDSILSIQVVSRARQLGIHFSP-RDLFQHQTV-QTLAAVATHSEAAQAEQGPLQGASGLTP 2796
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1116-1615 |
1.17e-76 |
|
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: 262.63 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1116 DAFRENAATHPARLALrwrpddyrgERHGDviaqdrsQLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAV 1194
Cdd:cd17653 1 DAFERIAAAHPDAVAV---------ESLGG-------SLTYGELDAASNALANRlLQLGVVPGDVVPLLSDRSLEMLVAI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1195 LGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSdtqdagvavsditamiecaptdpiridPHDAAYVIYTSGST 1274
Cdd:cd17653 65 LAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS---------------------------PDDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1275 GEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTipehaRRDAFHWLSLTTEfgI 1354
Cdd:cd17653 118 GIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL-----ADPSDPFAHVART--V 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1355 TVWNSVPGLMDMLliaagdKAGSLPTLRSVFLSGDWIPLDLprrLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDPdwa 1434
Cdd:cd17653 191 DALMSTPSILSTL------SPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTMTELLPGQP--- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1435 sIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDPT--GSRWYRTGDMGCYWRDGTLQ 1512
Cdd:cd17653 259 -VTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpGSRMYRTGDYGRWTEDGGLE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1513 FLGRADSQVKIRGHRVECGEIEH-ALRGHPLVAAATVVpIHNCTALGagiVVTGSGAeqfDDStpgALRAHLAVRLPQYM 1591
Cdd:cd17653 338 FLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI-VVNGRLVA---FVTPETV---DVD---GLRSELAKHLPSYA 407
|
490 500
....*....|....*....|....
gi 2181016861 1592 IPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd17653 408 VPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
95-577 |
2.68e-76 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 266.49 E-value: 2.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 95 IPVPVYLPST---REPqrFLARAQHILRDCEPSAVYTCGELVEVLERdpILGALPIRTPASTADGLAPHPGGTTADADHG 171
Cdd:PRK09192 100 VPVPLPLPMGfggRES--YIAQLRGMLASAQPAAIITPDELLPWVNE--ATHGNPLLHVLSHAWFKALPEADVALPRPTP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAA----NVWNGDddmHMVSWLPLYHDMGIFwGVFM-PLLNGGCTTLIP 246
Cdd:PRK09192 176 DDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShdglKVRPGD---RCVSWLPFYHDMGLV-GFLLtPVATQLSVDYLP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 247 PHDFVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLRDD 326
Cdd:PRK09192 252 TRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 327 VMAPQYGLAEAGLGVT------GSQTVRVwveksfDADALER-GIAVEvaqPNPADGRSRALVSCGDGAFGWDIQIVDPD 399
Cdd:PRK09192 332 AFMPSYGLAEATLAVSfsplgsGIVVEEV------DRDRLEYqGKAVA---PGAETRRVRTFVNCGKALPGHEIEIRNEA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 400 RHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTfgarTADGlgpYLRTGDAGFRYQGELYVCGRYRDLIIVGGRNHFPN 479
Cdd:PRK09192 403 GM-PLPERVVGHICVRGPSLMSGYFRDEESQDVL----AADG---WLDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 480 DIEKTVeEAHCGVAPGGACAVQpdAPQANGEWWLVL---ETGSPvEDLDDLSRILRRRILAHHETaPERVVWVPCRTLPT 556
Cdd:PRK09192 475 DIEWIA-EQEPELRSGDAAAFS--IAQENGEKIVLLvqcRISDE-ERRGQLIHALAALVRSEFGV-EAAVELVPPHSLPR 549
|
490 500
....*....|....*....|.
gi 2181016861 557 TTSGKIRRRETLNRLTAGQLE 577
Cdd:PRK09192 550 TSSGKLSRAKAKKRYLSGAFA 570
|
|
| FadD32_Coryne |
NF040633 |
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ... |
95-565 |
5.70e-76 |
|
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.
Pssm-ID: 468603 [Multi-domain] Cd Length: 613 Bit Score: 266.52 E-value: 5.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 95 IPVPVYLPStrEPqrflARAQH---ILRDCEPSAVYTCGELVEVL----------ERDPIL--GALP------IRTPAST 153
Cdd:NF040633 112 VPVPLYDPN--EP----GHADHlraVLADSGPTVVLTNKTSAPAVrahfadlpaaERPRILsvDSLPdslaesWVNPMAT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 154 ADGLAPHPGGTTADADHgehVAFLQYSSGSTGKPKGVVNTHQSILR---QAAFAANVwngDDDMHMVSWLPLYHDMGIFW 230
Cdd:NF040633 186 IEGQPLLAPAGTDPSDD---TAFLQYTSGSTRTPAGVVLTNRSIVTnvlQIFTAAQL---KTPLRLVSWLPLHHDMGIIL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 231 GVFMPLLnGGCTTLIPPHDFVRNPRIWLETVSRFRGN---WIGGPDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVR 307
Cdd:NF040633 260 AAFVTIL-GLEFELMSPRDFIQQPKRWVDQLSRREDDvnvYTVVPNFALELAARYANPEEGEDLDLSAVDGIIIGSEPVT 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 308 GTTLRDFTAKFRAAGLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDADALERGIAVEVAqpnPADGRSRALVSCGDG 387
Cdd:NF040633 339 EKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYFDREALAEGRAVEVA---EDSENAVPFASNGQV 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 388 AFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTF----GARTADGLGP-------YLRTGDAGFRYQ 456
Cdd:NF040633 416 VRPQVLAIVDPETGQELPDGTVGEIWVHGDNMAAGYLDREEETAETFrntlGERLAENSRAegapednWMATGDLGVIVD 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 457 GELYVCGRYRDLIIVGGRNHFPNDIEKTVEEAHCGVAPG--GACAVQPDapqaNGEWWLVL----ETGSPVEDLDDLSRI 530
Cdd:NF040633 496 GELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDsvAAFAVPGD----DVEKLVILaerdDEADESGDAEAIEAI 571
|
490 500 510
....*....|....*....|....*....|....*
gi 2181016861 531 lRRRILAHHETAPERVVWVPCRTLPTTTSGKIRRR 565
Cdd:NF040633 572 -RAAVTSAHGVVPADIRIVAPGEIARSSSGKIARR 605
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
69-596 |
3.02e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 253.11 E-value: 3.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 69 GIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPStrEPQRfLARAQHILRDCEPSAVYTCGELVEVLeRDPILGALPIR 148
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPA--EPGH-VGRLHAVLDDCTPSAILTTTDSAEGV-RKFFRARPAKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 149 TPASTADGLAPHPGGTT---ADADHgEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHD 225
Cdd:PRK07769 155 RPRVIAVDAVPDEVGATwvpPEANE-DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 226 MGIFwGVFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNWIG----GPDFAYRRC-IEAFDGTALQSLDLSCLRLAT 300
Cdd:PRK07769 234 MGLI-TVLLPALLGHYITFMSPAAFVRRPGRWIRELARKPGGTGGtfsaAPNFAFEHAaARGLPKDGEPPLDLSNVKGLL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 301 NGAEPVRGTTLRDFTAKFRAAGLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDADALERGIAVEVAQPNPadgRSRA 380
Cdd:PRK07769 313 NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPTVIYVDRDELNAGRFVEVPADAP---NAVA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 381 LVSCGD-GAFGWDIqIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTF----GART----ADGLGP---YLRT 448
Cdd:PRK07769 390 QVSAGKvGVSEWAV-IVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilKSRLseshAEGAPDdalWVRT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 449 GDAGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEAHCGVAPGGACAVQ------PDAPQANGEWWLVLETGSPVE 522
Cdd:PRK07769 469 GDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSvpanqlPQVVFDDSHAGLKFDPEDTSE 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 523 DL------------DDLSRI---LRRRILAHHETAPERVVWVPCRTLPTTTSGKIRRRETLNRLTAGQLEVvhevspRAQ 587
Cdd:PRK07769 549 QLvivaerapgahkLDPQPIaddIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRS------GYG 622
|
....*....
gi 2181016861 588 APDTPAAPD 596
Cdd:PRK07769 623 QPAFPDASD 631
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
31-565 |
5.39e-71 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 251.97 E-value: 5.39e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 31 DAVALRTVAATGIDDW-----TYQRLWDHVREIRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPstr 105
Cdd:PRK12476 49 DTVAYRYLDHSHSAAGcavelTWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAP--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 106 EPQRFLARAQHILRDCEPSAVYTCGELVEVLERdpILGALPIRT----------PASTADGLAPHPGGTTAdadhgehVA 175
Cdd:PRK12476 126 ELPGHAERLDTALRDAEPTVVLTTTAAAEAVEG--FLRNLPRLRrprviaidaiPDSAGESFVPVELDTDD-------VS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 176 FLQYSSGSTGKPKGVVNTHQSI---LRQAAFAANVWngDDDMHMVSWLPLYHDMGIFWGVFmPLLNGGCTTLIPPHDFVR 252
Cdd:PRK12476 197 HLQYTSGSTRPPVGVEITHRAVgtnLVQMILSIDLL--DRNTHGVSWLPLYHDMGLSMIGF-PAVYGGHSTLMSPTAFVR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 NPRIWLETVS---RFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLRLaTNGAEPVRGTTLRDFTAKFRAAGLRDDVMA 329
Cdd:PRK12476 274 RPQRWIKALSegsRTGRVVTAAPNFAYEWAAQRGLPAEGDDIDLSNVVL-IIGSEPVSIDAVTTFNKAFAPYGLPRTAFK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 330 PQYGLAEAGLGVTgsqTVRVWVEKS---FDADALERGIAVEVAqpnPADGRSRALVSCGDGAFGWDIQIVDPDRHMTLTD 406
Cdd:PRK12476 353 PSYGIAEATLFVA---TIAPDAEPSvvyLDREQLGAGRAVRVA---ADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 407 GEVGEIWVGGPGLPDGYWRQPEQTATTFGART---------ADGL---GPYLRTGDAGFRYQGELYVCGRYRDLIIVGGR 474
Cdd:PRK12476 427 GEVGEIWLHGDNIGRGYWGRPEETERTFGAKLqsrlaegshADGAaddGTWLRTGDLGVYLDGELYITGRIADLIVIDGR 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 475 NHFPNDIEKTVEEAHCGVAPGGACAVQPDApQANGEWWLVLE--TGSPVEDLDDLSRILRRRILAHHETAPERVVWVPCR 552
Cdd:PRK12476 507 NHYPQDIEATVAEASPMVRRGYVTAFTVPA-EDNERLVIVAEraAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAG 585
|
570
....*....|...
gi 2181016861 553 TLPTTTSGKIRRR 565
Cdd:PRK12476 586 AIPRTTSGKLARR 598
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1141-1612 |
6.44e-71 |
|
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: 246.31 E-value: 6.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1141 ERHGDVIA-QDRSQ-LTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLS 1217
Cdd:cd17645 9 ERTPDHVAvVDRGQsLTYKQLNEKANQLARHLRGKgVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1218 RICARSAMAGLIRtdsdtqdagvavsditamiecaptdpiriDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRR 1297
Cdd:cd17645 89 YMLADSSAKILLT-----------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1298 NRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLiaagdkAGS 1377
Cdd:cd17645 140 FGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFM------QLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1378 LPTLRSVFLSGDwipldlprRLRRAA-PGVRLVAMGGATEAAIWSNEFvvdDVDPDWASIPYGYPLANQMFRVVDDNGDD 1456
Cdd:cd17645 214 NQSLRVLLTGGD--------KLKKIErKGYKLVNNYGPTENTVVATSF---EIDKPYANIPIGKPIDNTRVYILDEALQL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1457 QPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP--TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIE 1534
Cdd:cd17645 283 QPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPfvPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1535 HALRGHPLVAAATVVPIHNC---TALGAGIVVTgsgaeqfDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd17645 363 PFLMNHPLIELAAVLAKEDAdgrKYLVAYVTAP-------EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
|
.
gi 2181016861 1612 R 1612
Cdd:cd17645 436 R 436
|
|
| FAAL_FadD32 |
NF038339 |
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ... |
69-565 |
1.81e-70 |
|
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.
Pssm-ID: 468483 [Multi-domain] Cd Length: 625 Bit Score: 250.79 E-value: 1.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 69 GIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPStrEPQRfLARAQHILRDCEPSAVYT---CGELVEVLERDpilgaL 145
Cdd:NF038339 76 GDRVAILAPQGLDYVVSFFAAIYAGNIAVPLFDPD--EPGH-TDRLHAVLGDCKPSAILTatsSAEGVRKFFRS-----L 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 146 PIRT-PASTA-DGLAPHPGGTTADADHGEH-VAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPL 222
Cdd:NF038339 148 PAKErPRVIAvDAVPDSVGSTWVRPDADLDdIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDENSRGVTWLPL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 223 YHDMGIFwGVFMPLLNGGCTTLIPPHDFVRNPRIW---LETVSRFRGNWIGGPDFAYRRCieAFDG--TALQSLDLSCLR 297
Cdd:NF038339 228 FHDMGLL-TVILPALGGKYITIMSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFAFEHA--AARGlpKEGEPLDLSNVI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 298 LATNGAEPVRGTTLRDFTAKFRAAGLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDADALERGIAVEVAQPNPAdgr 377
Cdd:NF038339 305 GLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVSSTPREDEAKVIYVDREELNAGRIVEVDPDAPN--- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 378 SRALVSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGP------------Y 445
Cdd:NF038339 382 AVAQVSCGYVARSQWAVIVDPETGTELPDGQVGEIWLHGNNIGTGYWGRPEETEETFHNKLKSRLEEgshaegapedanW 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 446 LRTGDAGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEAHCGVAPGGACAVQPDAPQANGEwwlVLETGSP--VED 523
Cdd:NF038339 462 MRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSVPANQLPAE---VFENSHSglKYD 538
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 524 LDDLSRIL----------------------RRRILAHHETAPERVVWVPCRTLPTTTSGKIRRR 565
Cdd:NF038339 539 ADDSSEQLvivaerapgagkadpqpiadavRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARR 602
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
133-572 |
8.54e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 243.36 E-value: 8.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 133 VEVLERDPILGALPIRTPASTADGlaphpggttadadhgehVAFLQYSSGSTGKPKGVVNTHQSILRQAA--FAANVWNG 210
Cdd:PRK07768 130 IRVLTVADLLAADPIDPVETGEDD-----------------LALMQLTSGSTGSPKAVQITHGNLYANAEamFVAAEFDV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 211 DDDMhMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAY----RRCIEAFDGT 286
Cdd:PRK07768 193 ETDV-MVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYallaRRLRRQAKPG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 287 AlqsLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDADALE-RGIA 365
Cdd:PRK07768 272 A---FDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEATLAVSFSPCGAGLVVDEVDADLLAaLRRA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 366 VEVAQPNpadgrSRALVSCGDGAFGWDIQIVDPDRHMtLTDGEVGEIWVGGPGLPDGYwrqpeqtattfgaRTADGLGP- 444
Cdd:PRK07768 349 VPATKGN-----TRRLATLGPPLPGLEVRVVDEDGQV-LPPRGVGVIELRGESVTPGY-------------LTMDGFIPa 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 445 -----YLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEAHcGVAPGGACAVQPDAPQANGEWWLVLET- 517
Cdd:PRK07768 410 qdadgWLDTGDLGyLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVE-GVRPGNAVAVRLDAGHSREGFAVAVESn 488
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 518 -GSPVEDLDDLSRILRRRILAHHETAPERVVWVPCRTLPTTTSGKIRRRETLNRLT 572
Cdd:PRK07768 489 aFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAELVT 544
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1120-1615 |
1.08e-68 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 241.72 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1120 ENAATHPARLALrwrpdDYRGERHgdviaqdrsqlTYGELDELARSVARAvaarhaagsVIGIQLPKG----------PS 1189
Cdd:PRK04813 10 EFAQTQPDFPAY-----DYLGEKL-----------TYGQLKEDSDALAAF---------IDSLKLPDKspiivfghmsPE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1190 QIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSDTQDAG----VAVSDITAMIEcAPTDPIRIDP---H 1262
Cdd:PRK04813 65 MLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILgipvITLDELKDIFA-TGNPYDFDHAvkgD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAaLNTIVD-VNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPeHARRD 1341
Cdd:PRK04813 144 DNYYIIFTSGTTGKPKGVQISHDN-LVSFTNwMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALP-KDMTA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1342 AFHWLSLT-TEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEA--A 1418
Cdd:PRK04813 222 NFKQLFETlPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEAtvA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1419 IWSNEfVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDpTGSRWYR 1498
Cdd:PRK04813 302 VTSIE-ITDEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-DGQPAYH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1499 TGDMGcYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI---HNCTALGAGIVVTgsgAEQFDDS- 1574
Cdd:PRK04813 380 TGDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkdHKVQYLIAYVVPK---EEDFEREf 455
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2181016861 1575 --TPgALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:PRK04813 456 elTK-AIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FAAL_FadD21 |
NF038337 |
fatty-acid--AMP ligase FAAL21/FadD21; |
15-575 |
5.53e-67 |
|
fatty-acid--AMP ligase FAAL21/FadD21;
Pssm-ID: 439631 [Multi-domain] Cd Length: 579 Bit Score: 239.39 E-value: 5.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 15 DRSVPAVFAEWVGRRPDAVALRTVAATgiDDWT-----------YQRLWDHVREIRDVAFSGLSAGIRIPMALPggadYV 83
Cdd:NF038337 3 NSSVVSLLRERAGLQPDDVAFRYTDYE--QDWAgvtetltwaqlYRRTLNVAHEVRRHGTTGDRAVILAPQGLP----YI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 84 AGMLAALAAGLIPVPVYLPstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLE---RDPILGALP--IRTPASTADGLA 158
Cdd:NF038337 77 VAFLGAMQAGLIAVPLSVP---QPGSHDERVSAVLADTSPSVVLTTSAAAAAVAeylHRPDTGAVPavIEIDSLDLDGPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 159 PhPGGTTADAdhgEHVAFLQYSSGSTGKPKGVVNTHQSI---LRQ--AAFAANVwNG--DDDMHMVSWLPLYHDMGIFWG 231
Cdd:NF038337 154 S-PSIRISDA---PSIAYLQYTSGSTRLPAGVMVSHRNLqvnFQQlmAAYFPDT-NGvaPRDTTIVSWLPFYHDMGLVLG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 232 VFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTL 311
Cdd:NF038337 229 VIAPILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTTDADLAGLDLGNVIGIVSGAERIHPATL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 312 RDFTAKFRAAGLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDADALERGiaveVAQPNPADGRSrALVSCGDGAfGW 391
Cdd:NF038337 309 DRFCKRFAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEPEKLSEG----SAQRCEARTGS-PLLSYGTPT-SP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 392 DIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGL-----GPYLRTGDAGFRYQGELYVCGRYR 466
Cdd:NF038337 383 TVRIVDPDTCIECPAGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLANPSpgtpeGPWLRTGDLGFISEDEMFIVGRMK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 467 DLIIVGGRNHFPNDIEKTVEEAHCG-VApggACAVQPDAPQANGEWWLVLETGSPVEDLDDLSRILRRRILA----HHET 541
Cdd:NF038337 463 DLLIVYGRNHYPEDIESTVQEITGGrVA---AISVPVDETEKLVTIIELKKRGDSDEEAMRKLDAVKNNVTAaisrSHGL 539
|
570 580 590
....*....|....*....|....*....|....
gi 2181016861 542 APERVVWVPCRTLPTTTSGKIRRRETLNRLTAGQ 575
Cdd:NF038337 540 NVADLVLVPPGSIPTTTSGKIRRAACVEQYRRQQ 573
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1263-1611 |
9.20e-66 |
|
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: 227.55 E-value: 9.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPehaRRDA 1342
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1343 FHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRrAAPGVRLVAMGGATEAAIWSN 1422
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFE-EAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1423 EFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFvhdptGSRWYRTGDM 1502
Cdd:cd04433 157 TGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-----EDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1503 GCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI--HNCTALGAGIVVTGSGAEQfddsTPGALR 1580
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpdPEWGERVVAVVVLRPGADL----DAEELR 305
|
330 340 350
....*....|....*....|....*....|.
gi 2181016861 1581 AHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
172-575 |
1.70e-64 |
|
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: 229.68 E-value: 1.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDFV 251
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 252 RNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLRDDVMAPQ 331
Cdd:cd05908 186 RRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 332 YGLAEAGLGVTGSQTVRVWVEKSFDADALERGI-AVEVAQPNPadgRSRALVSCGDGAFGWDIQIVDPDRHMtLTDGEVG 410
Cdd:cd05908 266 YGLAEASVGASLPKAQSPFKTITLGRRHVTHGEpEPEVDKKDS---ECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 411 EIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEAHc 490
Cdd:cd05908 342 HIQIRGKNVTPGYYNNPEATAKVF---TDDG---WLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELE- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 491 GVAPG--GACAVQpDAPQANGEWWLVLETGSPVEDLDDLSRILRRRIlahhetaPERVVW-----VPCRTLPTTTSGKIR 563
Cdd:cd05908 415 GVELGrvVACGVN-NSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHL-------NKRGGWqinevLPIRRIPKTTSGKVK 486
|
410
....*....|..
gi 2181016861 564 RRETLNRLTAGQ 575
Cdd:cd05908 487 RYELAQRYQSGE 498
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1146-1611 |
4.10e-64 |
|
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: 226.90 E-value: 4.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1146 VIAQDRSqLTYGELDELARSVARAVAARHAAGS--VIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICars 1223
Cdd:cd17648 6 VVYGDKR-LTYRELNERANRLAHYLLSVAEIRPddLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1224 amaglirtdSDTQDAGVavsdITamiecaptdpiriDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTH 1303
Cdd:cd17648 82 ---------EDTGARVV----IT-------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1304 D--RLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLliaagdKAGSLPTL 1381
Cdd:cd17648 136 GdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY------DLARLPHL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1382 RSVFLSGDWIPLDLPRRLRRAAPGvRLVAMGGATEAAIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYV 1461
Cdd:cd17648 210 KRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQRFDKSL--GRPVRNTKCYVLNDAMKRVPVGA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1462 AGELWIGGAGVALGYHNAPELTSDRFVHDP----------TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECG 1531
Cdd:cd17648 287 VGELYLGGDGVARGYLNRPELTAERFLPNPfqteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1532 EIEHALRGHPLVAAATVVPIHNCTALGAGIV--VTG---SGAEQFDDStpgALRAHLAVRLPQYMIPKVFVSCPELPLTA 1606
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSRIQkyLVGyylPEPGHVPES---DLLSFLRAKLPRYMVPARLVRLEGIPVTI 443
|
....*
gi 2181016861 1607 NGKVD 1611
Cdd:cd17648 444 NGKLD 448
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1178-1615 |
8.08e-64 |
|
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: 226.97 E-value: 8.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1178 SVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSDT---QDAGVAVSDITAMIECAPT 1254
Cdd:cd17656 39 SIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQRHLKsklSFNKSTILLEDPSISQEDT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1255 DPIRI--DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLV 1332
Cdd:cd17656 119 SNIDYinNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1333 TIPEHARRDAFHWLSLTTEFGITVWnSVPGLMDMLLIAAGDKAGSLPT-LRSVFLSGDWIPLDLPRRLRRAAPGVRLVAM 1411
Cdd:cd17656 199 IIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSEREFINRFPTcVKHIITAGEQLVITNEFKEMLHEHNVHLHNH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1412 GGATEAAIWSNeFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP 1491
Cdd:cd17656 278 YGPSETHVVTT-YTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1492 --TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAAtVVPIHNCTALGAGIVVTGSGAE 1569
Cdd:cd17656 357 fdPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEA-VVLDKADDKGEKYLCAYFVMEQ 435
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2181016861 1570 QFDDSTpgaLRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd17656 436 ELNISQ---LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1122-1615 |
1.82e-63 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 226.56 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1122 AATHPARLALRwrpddYRGERHgdviaqdrsqlTYGEL-DELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMA 1200
Cdd:TIGR01734 10 AETYPQTIAYR-----YQGQEL-----------TYQQLkEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1201 GCTYLPVGVDQPAERLSRICARSAMAGLIRTDS---DTQDAGVAVSDITAMIEcAPTDPIRIDP----HDAAYVIYTSGS 1273
Cdd:TIGR01734 74 GHAYIPVDTSIPSERIEMIIEAAGPELVIHTAElsiDAVGTQIITLSALEQAE-TSGGPVSFDHavkgDDNYYIIYTSGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1274 TGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFG 1353
Cdd:TIGR01734 153 TGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1354 ITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEA--AIWSNEfVVDDVDP 1431
Cdd:TIGR01734 233 LNVWVSTPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEAtvAVTSVK-ITQEILD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1432 DWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDpTGSRWYRTGDMGCYwRDGTL 1511
Cdd:TIGR01734 312 QYPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH-EGQPAYRTGDAGTI-TDGQL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1512 QFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI----HNCTALGAGIVVTgsgAEQFDDS--TPGALRAHLAV 1585
Cdd:TIGR01734 390 FYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKynkdHKVEYLIAAIVPE---TEDFEKEfqLTKAIKKELKK 466
|
490 500 510
....*....|....*....|....*....|
gi 2181016861 1586 RLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:TIGR01734 467 SLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
173-563 |
8.64e-62 |
|
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: 216.00 E-value: 8.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 173 HVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWgVFMPLLNGGCTTLIPPHDfvr 252
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFG-LLGALLAGGTVVLLPKFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 nPRIWLETVSRFRGNWIGGPDFAYRRCIEAfdgTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAPQY 332
Cdd:cd04433 77 -PEAALELIEREKVTILLGVPTLLARLLKA---PESAGYDLSSLRALVSGGAPLPPELLERFEEAP------GIKLVNGY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 333 GLAEAGLGVTGsqtvrvwveksfdadalergiavevaqpNPADGRSRALVSCGDGAFGWDIQIVDPDRHmTLTDGEVGEI 412
Cdd:cd04433 147 GLTETGGTVAT----------------------------GPPDDDARKPGSVGRPVPGVEVRIVDPDGG-ELPPGEIGEL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 413 WVGGPGLPDGYWRQPEQTAttfgARTADGlgpYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCG 491
Cdd:cd04433 198 VVRGPSVMKGYWNNPEATA----AVDEDG---WYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLG-HPG 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 492 VAPGGACAVqPDapQANGEW---WLVLETGSPVeDLDDLSRILRRRILAHHEtaPERVVWVPcrTLPTTTSGKIR 563
Cdd:cd04433 270 VAEAAVVGV-PD--PEWGERvvaVVVLRPGADL-DAEELRAHVRERLAPYKV--PRRVVFVD--ALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
22-472 |
6.27e-55 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 199.08 E-value: 6.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 22 FAEWVGRRPDAVALRTVAATgidDWTYQRLWDHVREIrdvAfSGL-SAGI----RIPMALPGGADYVAGMLAALAAGLIP 96
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR---RLTYRELDERANRL---A-AGLrALGVgkgdRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 97 VPVYLPSTREpqrflaRAQHILRDCEPSAVYTCGELVeVLERDPILGALP-------------IRTPASTADGLAPHPGG 163
Cdd:pfam00501 74 VPLNPRLPAE------ELAYILEDSGAKVLITDDALK-LEELLEALGKLEvvklvlvldrdpvLKEEPLPEEAKPADVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 164 TTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMH----MVSWLPLYHDMGIFWGVFMPLLNG 239
Cdd:pfam00501 147 PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpddrVLSTLPLFHDFGLSLGLLGPLLAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 240 GCTTLIPPHDFvRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFdgtALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFR 319
Cdd:pfam00501 227 ATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAG---APKRALLSSLRLVLSGGAPLPPELARRFRELFG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 320 AAglrddvMAPQYGLAEAGLGVTgsqtvrvwveksfdadalergiavevaQPNPADGRSRALVSCGDGAFGWDIQIVDPD 399
Cdd:pfam00501 303 GA------LVNGYGLTETTGVVT---------------------------TPLPLDEDLRSLGSVGRPLPGTEVKIVDDE 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 400 RHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFRYQ-GELYVCGRYRDLIIVG 472
Cdd:pfam00501 350 TGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF---DEDG---WYRTGDLGRRDEdGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
46-574 |
1.34e-54 |
|
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: 201.74 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 46 WTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPST-REPQRFLARAQHILRDCEP 123
Cdd:cd05906 40 QSYQDLLEDARRLaAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 124 SAVYTCGELV-EVLERDPILGALPIRTPASTA--DGLAPHPGgTTADADHgehVAFLQYSSGSTGKPKGVVNTHQSILrq 200
Cdd:cd05906 120 PVVLTDAELVaEFAGLETLSGLPGIRVLSIEEllDTAADHDL-PQSRPDD---LALLMLTSGSTGFPKAVPLTHRNIL-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 201 AAFAANVWN---GDDDMHMvSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYR 277
Cdd:cd05906 194 ARSAGKIQHnglTPQDVFL-NWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 278 RCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLRDDVMAPQYGLAEAGLGVTgsqtvrvwveksfda 357
Cdd:cd05906 273 LLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGVI--------------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 358 dalergiaveVAQPNPADGRSRAL--VSCGDGAFGWDIQIVDPDRHMtLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFg 435
Cdd:cd05906 338 ----------YSRSFPTYDHSQALefVSLGRPIPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGYYNNPEANAEAF- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 436 arTADGlgpYLRTGDAGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEAHcGVAPGGACAVQPDAPQANGEWWLVl 515
Cdd:cd05906 406 --TEDG---WFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVP-GVEPSFTAAFAVRDPGAETEELAI- 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 516 eTGSPVEDLDD-LSRILR--RRILAHHET-APERVVWVPCRTLPTTTSGKIRRRETLNRLTAG 574
Cdd:cd05906 479 -FFVPEYDLQDaLSETLRaiRSVVSREVGvSPAYLIPLPKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1194-1681 |
1.09e-53 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 210.41 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1194 VLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSDTQDA-------------GVAVSDITAMIECAPTDP-IRI 1259
Cdd:PRK05691 3787 IVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQAralldelgcanrpRLLVWEEVQAGEVASHNPgIYS 3866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHAR 1339
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIA 3946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1340 RDAFHWLSLTTEFGITVWNSVPGLMDMLLiaAGDKAgSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAI 1419
Cdd:PRK05691 3947 HDPQGLLAHVQAQGITVLESVPSLIQGML--AEDRQ-ALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSD 4023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1420 WSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDP---TGSRW 1496
Cdd:PRK05691 4024 DVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPfgaPGERL 4103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1497 YRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLV--AAATVVPIHNCTALgAGIVVTGSGAEqfdds 1574
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVreAAVAVQEGVNGKHL-VGYLVPHQTVL----- 4177
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1575 TPGAL----RAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKIAARLEAAArapQPLDTSSTLTVVERLVAEVWSDVL 1650
Cdd:PRK05691 4178 AQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQL---QSQAYLAPRNELEQTLATIWADVL 4254
|
490 500 510
....*....|....*....|....*....|.
gi 2181016861 1651 GAPITGREDNFFAQGGDSLRATEAVARLTRR 1681
Cdd:PRK05691 4255 KVERVGVHDNFFELGGHSLLATQIASRVQKA 4285
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
18-566 |
2.19e-47 |
|
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: 178.53 E-value: 2.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 18 VPAVFAEWVGRRPDAVALRTVAATgiddWTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIP 96
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK----LTYRELDALAEAFaAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 97 VPVylpstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLERDPILGALPIRTPastadglaphpggttadadhgEHVAF 176
Cdd:cd05936 77 VPL------NPLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALTP---------------------EDVAV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSIL---RQAAFAANVWNGDDDMHMVSwLPLYHDMGIFWGVFMPLLNGGCTTLIPphdfvrN 253
Cdd:cd05936 130 LQYTSGTTGVPKGAMLTHRNLVanaLQIKAWLEDLLEGDDVVLAA-LPLFHVFGLTVALLLPLALGATIVLIP------R 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 254 PRI--WLETVSRFRGNWIGGPDFAYRRCIEAFDGTAlqsLDLSCLRLATNGAEPVRGTTLRDFTAKFRAA---Glrddvm 328
Cdd:cd05936 203 FRPigVLKEIRKHRVTIFPGVPTMYIALLNAPEFKK---RDFSSLRLCISGGAPLPVEVAERFEELTGVPiveG------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 apqYGLAEAGLGVTGsqtvrvwveksfdadalergiavevaqpNPADGRSRAlVSCGDGAFGWDIQIVDPDRHmTLTDGE 408
Cdd:cd05936 274 ---YGLTETSPVVAV----------------------------NPLDGPRKP-GSIGIPLPGTEVKIVDDDGE-ELPPGE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 409 VGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEE 487
Cdd:cd05936 321 VGELWVRGPQVMKGYWNRPEETAEAF----VDG---WLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYE 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 488 aHCGVApggACAV--QPD-----APQAngewWLVLETGSPVeDLDDLSRILRRRiLAHHEtAPERVVWVPcrTLPTTTSG 560
Cdd:cd05936 394 -HPAVA---EAAVvgVPDpysgeAVKA----FVVLKEGASL-TEEEIIAFCREQ-LAGYK-VPRQVEFRD--ELPKSAVG 460
|
....*.
gi 2181016861 561 KIRRRE 566
Cdd:cd05936 461 KILRRE 466
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1182-1615 |
1.34e-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.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 166.85 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1182 IQLPKGPSQIVAVLGVMMAGCTYLPVGVD--------------QPAERLSRICARSAMAGLIRTDSDTQDAGVAVSDITA 1247
Cdd:cd05922 23 LILPNRFTYIELSFAVAYAGGRLGLVFVPlnptlkesvlrylvADAGGRIVLADAGAADRLRDALPASPDPGTVLDADGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1248 MIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGC 1327
Cdd:cd05922 103 RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1328 GAQLVTIPEHARRDAFhWLSLtTEFGITVWNSVPGLMDMLLIAAGDKAGsLPTLRSVFLSGDWIPLDLPRRLRRAAPGVR 1407
Cdd:cd05922 183 GATLVLTNDGVLDDAF-WEDL-REHGATGLAGVPSTYAMLTRLGFDPAK-LPSLRYLTQAGGRLPQETIARLRELLPGAQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 LVAMGGATEAAIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPEltsdrf 1487
Cdd:cd05922 260 VYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPP------ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1488 vHDPTGSRW---YRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPL--VAAATVVPihncTALGAGIV 1562
Cdd:cd05922 332 -YRRKEGRGggvLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLiiEAAAVGLP----DPLGEKLA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1563 VTGSGAEQFDDStpgALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05922 407 LFVTAPDKIDPK---DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1180-1611 |
7.67e-43 |
|
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: 164.57 E-value: 7.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1180 IGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDSDTQDAGVAVSDITAMiecaptdPIRI 1259
Cdd:cd17654 44 IGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKELDNAPLSFTPEHRHF-------NIRT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DpHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPeHAR 1339
Cdd:cd17654 117 D-ECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVP-TSV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1340 RDAFHWL--SLTTEFGITVWNSVPGLMDMLLIAAGDKA--GSLPTLRSVFLSGDWIP-LDLPRRLRRAAPGVRLVAMGGA 1414
Cdd:cd17654 195 KVLPSKLadILFKRHRITVLQATPTLFRRFGSQSIKSTvlSATSSLRVLALGGEPFPsLVILSSWRGKGNRTRIFNIYGI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1415 TEAAIWSNEFVVDDVDpdwASIPYGYPLANQMFRVVDDNGDDQpdyvAGELWIGG-AGVAL--GYHNAPEltsdrfvhdp 1491
Cdd:cd17654 275 TEVSCWALAYKVPEED---SPVQLGSPLLGTVIEVRDQNGSEG----TGQVFLGGlNRVCIldDEVTVPK---------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1492 tgSRWYRTGDMgCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHpLVAAATVVPIHNCTALGAGIVVTGSGAEQF 1571
Cdd:cd17654 338 --GTMRATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC-LGVESCAVTLSDQQRLIAFIVGESSSSRIH 413
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2181016861 1572 DDstpgaLRAHLavrLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd17654 414 KE-----LQLTL---LSSHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1177-1612 |
8.93e-43 |
|
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: 166.11 E-value: 8.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMA-----------------------GLIRTDS 1233
Cdd:TIGR03098 50 GERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRllvtsserldllhpalpgchdlrTLIIVGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1234 DTQD----AGVAVSDITAMIECAPTDPI--RIDPhDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLL 1307
Cdd:TIGR03098 130 PAHAseghPGEEPASWPKLLALGDADPPhpVIDS-DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1308 ALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAfhwLSLTTEFGITVWNSVPGLMDMLliAAGD-KAGSLPTLRSVFL 1386
Cdd:TIGR03098 209 AVLPLSFDYGFNQLTTAFYVGATVVLHDYLLPRDV---LKALEKHGITGLAAVPPLWAQL--AQLDwPESAAPSLRYLTN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1387 SGDWIPLDLPRRLRRAAPGVRLVAMGGATEaAIWSNEFVVDDVDPDWASIPYGYPLANQMfrVVDDNGDDQPDYVAGELW 1466
Cdd:TIGR03098 284 SGGAMPRATLSRLRSFLPNARLFLMYGLTE-AFRSTYLPPEEVDRRPDSIGKAIPNAEVL--VLREDGSECAPGEEGELV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1467 IGGAGVALGYHNAPELTSDRF---------VHDPTGSRWyrTGDMGcyWRD--GTLQFLGRADSQVKIRGHRVECGEIEH 1535
Cdd:TIGR03098 361 HRGALVAMGYWNDPEKTAERFrplppfpgeLHLPELAVW--SGDTV--RRDeeGFLYFVGRRDEMIKTSGYRVSPTEVEE 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 1536 ALRGHPLVAAATVVPIHNCTaLGAGI--VVTGSGAEQFDdstPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:TIGR03098 437 VAYATGLVAEAVAFGVPDPT-LGQAIvlVVTPPGGEELD---RAALLAECRARLPNYMVPALIHVRQALPRNANGKIDR 511
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1146-1615 |
1.52e-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: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1146 VIAQDRSqLTYGELDE-LARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGctylpvgvdqpaerlsricarsA 1224
Cdd:cd05919 4 FYAADRS-VTYGQLHDgANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARG----------------------A 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1225 MAGLIRTDSDTQDAGVAVSDitamieCAPTDPIRiDPHDAAYVIYTSGSTGEPKGVLVSHAAALnTIVDVNRRN--RIDT 1302
Cdd:cd05919 61 IAVVINPLLHPDDYAYIARD------CEARLVVT-SADDIAYLLYSSGTTGPPKGVMHAHRDPL-LFADAMAREalGLTP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1303 HDRLLALSALDFDLSVYDT-FGALGCGAQLVTIPehARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTL 1381
Cdd:cd05919 133 GDRVFSSAKMFFGYGLGNSlWFPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1382 RSVFLSGDWIPLDLPRRLRrAAPGVRLVAMGGATEAAiwsNEFVVDDVDpDWASIPYGYPLANQMFRVVDDNGDDQPDYV 1461
Cdd:cd05919 211 RLCVSAGEALPRGLGERWM-EHFGGPILDGIGATEVG---HIFLSNRPG-AWRLGSTGRPVPGYEIRLVDEEGHTIPPGE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1462 AGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHP 1541
Cdd:cd05919 286 EGDLLVRGPSAAVGYWNNPEKSRATFNGG-----WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHP 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1542 LVAAATVVPI---HNCTALGAGIVVTGSGAEQfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05919 361 AVAEAAVVAVpesTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
896-1703 |
1.52e-41 |
|
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: 169.48 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 896 DDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVttfgRSPEVsdvvgdfTETHLYRAQLDGQISFVDQAQVTQKGLR 975
Cdd:TIGR03443 38 AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT----SSNKS-------GRPFVLRLNITPELSFLQLYAKVSEEEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 976 TALRAAPAP-DLLATQLRSGTGhSGIVPVVFTYAA-DSPLLSAEDANTLGAIDEVVSMTPQvlidhqacrlGDDVVLSWD 1053
Cdd:TIGR03443 107 EGASDIGVPfDELSEHIQAAKK-LERTPPLFRLAFqDAPDNQQTTYSTGSTTDLTVFLTPS----------SPELELSIY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1054 YRAGCFPpgvvDDMFEAYVTLLERLGGHDWSTPATPgLSAHSRLARAHRNATttPAPA---------GLLYDAFRENAAT 1124
Cdd:TIGR03443 176 YNSLLFS----SDRITIVADQLAQLLSAASSNPDEP-IGKVSLITPSQKSLL--PDPTkdldwsgfrGAIHDIFADNAEK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1125 HPARLALRWRPDDYRGERhgdviaQDRSqLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCT 1203
Cdd:TIGR03443 249 HPDRTCVVETPSFLDPSS------KTRS-FTYKQINEASNILAHYLLKTgIKRGDVVMIYAYRGVDLVVAVMGVLKAGAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1204 -------YLP------VGVDQP--------AERLSRICA---------RSAMAGLIRTDSDTQDAGV---AVSDITAMIE 1250
Cdd:TIGR03443 322 fsvidpaYPParqtiyLSVAKPraliviekAGTLDQLVRdyidkelelRTEIPALALQDDGSLVGGSlegGETDVLAPYQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1251 CAPTDP--IRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCG 1328
Cdd:TIGR03443 402 ALKDTPtgVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1329 AQLVtIPehARRDA------FHWLSlttEFGITVWNSVPGlMDMLLIAAGDKAgsLPTLRSVFLSGDWIPLDLPRRLRRA 1402
Cdd:TIGR03443 482 AQLL-VP--TADDIgtpgrlAEWMA---KYGATVTHLTPA-MGQLLSAQATTP--IPSLHHAFFVGDILTKRDCLRLQTL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1403 APGVRLVAMGGATEAAIWSNEFVVDDV--DPDWAS-----IPYGYPLANQMFRVVDDNGDDQPDYVA--GELWIGGAGVA 1473
Cdd:TIGR03443 553 AENVCIVNMYGTTETQRAVSYFEIPSRssDSTFLKnlkdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLA 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1474 LGYHNAPELTSDRFVH------------DPTGSRW------------YRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVE 1529
Cdd:TIGR03443 633 EGYLGLPELNAEKFVNnwfvdpshwidlDKENNKPerefwlgprdrlYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIE 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1530 CGEIEHALRGHPLVA----------------AATVVPIHNCTALGAgiVVTGSGAEQFDDSTPGAL----------RAHL 1583
Cdd:TIGR03443 713 LGEIDTHLSQHPLVRenvtlvrrdkdeeptlVSYIVPQDKSDELEE--FKSEVDDEESSDPVVKGLikyrklikdiREYL 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1584 AVRLPQYMIPKVFVSCPELPLTANGKVDRGKIAARLEAAARAPQPLDTSS----TLTVVERLVAEVWSDVL-GAPIT-GR 1657
Cdd:TIGR03443 791 KKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASaadeEFTETEREIRDLWLELLpNRPATiSP 870
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 2181016861 1658 EDNFFAQGGDSLRATEAVARLTRRGVAGAEVGQLLSHQTLGQFSAA 1703
Cdd:TIGR03443 871 DDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKE 916
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
47-576 |
8.33e-41 |
|
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: 161.36 E-value: 8.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 47 TYQRLWDHVREIRDVAF--SGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPV-----------YLPSTREPQRFLAR 113
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQkkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIeppdisqqlgfLLGTCKVRVALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 114 AQHILRDCEPSAVYTCGELVEVLERDPILGA--LPIRTPASTADgLAPHPGgtTADADhgehVAFLQYSSGSTGKPKGVV 191
Cdd:cd05905 96 ACLKGLPKKLLKSKTAAEIAKKKGWPKILDFvkIPKSKRSKLKK-WGPHPP--TRDGD----TAYIEYSFSSDGSLSGVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 192 NTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNwigg 271
Cdd:cd05905 169 VSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVR---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 272 PDFA-YRRCIEAFDGTALQ-------SLDLSCLRLATNGAE-PVRGTTLRDFTAKFRAAGLRDDVMAPQYG----LAEAG 338
Cdd:cd05905 245 DAYVkLRTLHWCLKDLSSTlaslknrDVNLSSLRMCMVPCEnRPRISSCDSFLKLFQTLGLSPRAVSTEFGtrvnPFICW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 339 LGVTGSQTVRVWVEKSfdadALERGIavevaqPNPAD---GRSRALVSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVG 415
Cdd:cd05905 325 QGTSGPEPSRVYLDMR----ALRHGV------VRLDErdkPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 416 GPGLPDGYWRQPEQTATTFGARTADGLG------PYLRTGDAGFRYQGE-----------LYVCGRYRDLIIVGGRNHFP 478
Cdd:cd05905 395 SPANASGYFLLDGETNDTFKVFPSTRLStgitnnSYARTGLLGFLRPTKctdlnveehdlLFVVGSIDETLEVRGLRHHP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 479 NDIEKTVEEAHCGVapgGACAVQpdapQANGEWWLVLE--TGSPVEDLDDLSRILrRRILAHHETAPERVVWVPCRTLPT 556
Cdd:cd05905 475 SDIEATVMRVHPYR---GRCAVF----SITGLVVVVAEqpPGSEEEALDLVPLVL-NAILEEHQVIVDCVALVPPGSLPK 546
|
570 580
....*....|....*....|
gi 2181016861 557 TTSGKIRRRETLNRLTAGQL 576
Cdd:cd05905 547 NPLGEKQRMEIRQAFLAGKL 566
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1114-1612 |
4.74e-40 |
|
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: 156.95 E-value: 4.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAATHPARLALRWrpddyrgerhgdviaQDRSqLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIV 1192
Cdd:cd05936 1 LADLLEEAARRFPDKTALIF---------------MGRK-LTYRELDALAEAFAAGLQNLgVQPGDRVALMLPNCPQFPI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1193 AVLGVMMAGCTYLPVGVDQPAERLsricarsamaGLIRTDSDTQDAGVAVSDITAMIECAPTD-PIRIDPHDAAYVIYTS 1271
Cdd:cd05936 65 AYFGALKAGAVVVPLNPLYTPREL----------EHILNDSGAKALIVAVSFTDLLAAGAPLGeRVALTPEDVAVLQYTS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1272 GSTGEPKGVLVSHAAALNTIVDVNRR--NRIDTHDRLLALsaldfdLSVYDTFG-------ALGCGAQLVTIPehaRRDA 1342
Cdd:cd05936 135 GTTGVPKGAMLTHRNLVANALQIKAWleDLLEGDDVVLAA------LPLFHVFGltvalllPLALGATIVLIP---RFRP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1343 FHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGGATEAA--IW 1420
Cdd:cd05936 206 IGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSpvVA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1421 SNEFVvddvDPDWA-SIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRT 1499
Cdd:cd05936 285 VNPLD----GPRKPgSI--GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG-----WLRT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1500 GDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTAlGAGI---VVTGSGAeqfdDSTP 1576
Cdd:cd05936 354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYS-GEAVkafVVLKEGA----SLTE 428
|
490 500 510
....*....|....*....|....*....|....*.
gi 2181016861 1577 GALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05936 429 EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILR 464
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1146-1615 |
1.23e-39 |
|
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: 156.32 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1146 VIAQDRSQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARS- 1223
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALgIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1224 AMAGLIRTDSDTQDAGVAVSDITAMIECAPTDPIRI------------------------DPHDAAYVIYTSGSTGEPKG 1279
Cdd:cd05926 87 SKLVLTPKGELGPASRAASKLGLAILELALDVGVLIrapsaeslsnlladkknaksegvpLPDDLALILHTSGTTGRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1280 VLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdFDL-----SVYDTFGALGCgaqlVTIPehARRDAFHWLSLTTEFGI 1354
Cdd:cd05926 167 VPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVhglvaSLLSTLAAGGS----VVLP--PRFSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1355 TVWNSVPGLMDMLLIAAGDKAGS-LPTLRSVFLSGDWIPLDLPRRLRR--AAPGVRLVAMggaTEAA--IWSNEFVVDDV 1429
Cdd:cd05926 240 TWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEAtfGAPVLEAYGM---TEAAhqMTSNPLPPGPR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1430 DPDWASIPYGyplanQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDPtgsrWYRTGDMGCYWRDG 1509
Cdd:cd05926 317 KPGSVGKPVG-----VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG----WFRTGDLGYLDADG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1510 TLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCT---ALGAGIVVTGSGAeqfddSTPGALRAHLAVR 1586
Cdd:cd05926 388 YLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKygeEVAAAVVLREGAS-----VTEEELRAFCRKH 462
|
490 500
....*....|....*....|....*....
gi 2181016861 1587 LPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05926 463 LAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1118-1612 |
1.83e-39 |
|
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: 154.31 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1118 FRENAATHPARLALRWRpddyrgerhgdviaqDRSqLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLG 1196
Cdd:cd17631 1 LRRRARRHPDRTALVFG---------------GRS-LTYAELDERVNRLAHAlRALGVAKGDRVAVLSKNSPEFLELLFA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1197 VMMAGCTYLPVGVDQPAERLSRICARSamaglirtdsdtqDAGVAVSDItamiecaptdpiridphdaAYVIYTSGSTGE 1276
Cdd:cd17631 65 AARLGAVFVPLNFRLTPPEVAYILADS-------------GAKVLFDDL-------------------ALLMYTSGTTGR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1277 PKGVLVSH----AAALNTIVDVNrrnrIDTHDRLLALSALdF---DLSVYdTFGALGCGAQLVTIPEHarrDAFHWLSLT 1349
Cdd:cd17631 113 PKGAMLTHrnllWNAVNALAALD----LGPDDVLLVVAPL-FhigGLGVF-TLPTLLRGGTVVILRKF---DPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1350 TEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAapGVRLVAMGGATEAAiwSNEFVV--D 1427
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETS--PGVTFLspE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1428 DVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWR 1507
Cdd:cd17631 260 DHRRKLGSA--GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-----WFHTGDLGRLDE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1508 DGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCT--ALGAGIVVTGSGAEQfddsTPGALRAHLAV 1585
Cdd:cd17631 333 DGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwgEAVVAVVVPRPGAEL----DEDELIAHCRE 408
|
490 500
....*....|....*....|....*..
gi 2181016861 1586 RLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17631 409 RLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
168-574 |
7.85e-39 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 154.54 E-value: 7.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 168 ADHGEhVAFLQYSSGSTGKPKgvvnthQSILRQAAFAANV--------WNGDDDMHMvSWLPLYHDMGIFWgVFMPLLNG 239
Cdd:PRK05851 149 PDSGG-PAVLQGTAGSTGTPR------TAILSPGAVLSNLrglnarvgLDAATDVGC-SWLPLYHDMGLAF-LLTAALAG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 240 GCTTLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYRrCIEAFdGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFR 319
Cdd:PRK05851 220 APLWLAPTTAFSASPFRWLSWLSDSRATLTAAPNFAYN-LIGKY-ARRVSDVDLGALRVALNGGEPVDCDGFERFATAMA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 320 AAGLRDDVMAPQYGLAEAGLGVTGSqtvrvwveksfdadalERGIAVEVAQPNPADGRS-RALVSCGDGAFGWDIQIVDP 398
Cdd:PRK05851 298 PFGFDAGAAAPSYGLAESTCAVTVP----------------VPGIGLRVDEVTTDDGSGaRRHAVLGNPIPGMEVRISPG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 399 DRHMTLTDGEVGEIWVGGPGLPDGYwrqpeqtattFGARTADGlGPYLRTGDAGFRYQGELYVCGRYRDLIIVGGRNHFP 478
Cdd:PRK05851 362 DGAAGVAGREIGEIEIRGASMMSGY----------LGQAPIDP-DDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFP 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 479 NDIEKTVEEAHcGVAPGGACAVQPDAPQANGEWWLVLETGSPveDLDDLSRILRRRILAHHETAPERVVWVPCRTLPTTT 558
Cdd:PRK05851 431 TEIERVAAQVR-GVREGAVVAVGTGEGSARPGLVIAAEFRGP--DEAGARSEVVQRVASECGVVPSDVVFVAPGSLPRTS 507
|
410
....*....|....*.
gi 2181016861 559 SGKIRRRETLNRLTAG 574
Cdd:PRK05851 508 SGKLRRLAVKRSLEAA 523
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1115-1615 |
9.03e-39 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 154.88 E-value: 9.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1115 YDAFRENAATHPARLALRWRPDDyrgerhgdviaQDRSQLTYGELDE-------------LARsvaravaarhaaGSVIG 1181
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGED-----------GEERTLTYAELRRevnrfanalralgVKK------------GDRVA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1182 IQLPKGPSQIVAVLGVMMAGCTYLPV----GVDQPAERLSR------ICA-----------RSAMAGLIRTDSDT----- 1235
Cdd:COG0365 69 IYLPNIPEAVIAMLACARIGAVHSPVfpgfGAEALADRIEDaeakvlITAdgglrggkvidLKEKVDEALEELPSlehvi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1236 --QDAGVAVS-----DITAMIECAPT--DPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALnTIVDVNRRNRIDTH--D 1304
Cdd:COG0365 149 vvGRTGADVPmegdlDWDELLAAASAefEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYL-VHAATTAKYVLDLKpgD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1305 RLLALSALDF--DLSvYDTFGALGCGAQLVTIPEHAR-RDAFHWLSLTTEFGITVWNSVPGLMDMLlIAAGD---KAGSL 1378
Cdd:COG0365 228 VFWCTADIGWatGHS-YIVYGPLLNGATVVLYEGRPDfPDPGRLWELIEKYGVTVFFTAPTAIRAL-MKAGDeplKKYDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1379 PTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGGATEA-AIWSNEFVVDDVDPDWASIPY-GYPLanqmfRVVDDNGDD 1456
Cdd:COG0365 306 SSLRLLGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTETgGIFISNLPGLPVKPGSMGKPVpGYDV-----AVVDEDGNP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1457 QPDYVAGELWIGGA--GVALGYHNAPELTSDRFVHDPTGsrWYRTGDMgcYWRD--GTLQFLGRADSQVKIRGHRVECGE 1532
Cdd:COG0365 380 VPPGEEGELVIKGPwpGMFRGYWNDPERYRETYFGRFPG--WYRTGDG--ARRDedGYFWILGRSDDVINVSGHRIGTAE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1533 IEHALRGHPLVAAATVVPIHNCTAlGAGI---VVTGSGAEqFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGK 1609
Cdd:COG0365 456 IESALVSHPAVAEAAVVGVPDEIR-GQVVkafVVLKPGVE-PSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGK 533
|
....*.
gi 2181016861 1610 VDRGKI 1615
Cdd:COG0365 534 IMRRLL 539
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1177-1615 |
3.54e-38 |
|
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: 152.29 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIrtdsDTQDAGVAVSditamiecaptdp 1256
Cdd:cd17647 45 GDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI----VIRAAGVVVG------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1257 iridPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVtIPe 1336
Cdd:cd17647 108 ----PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL-VP- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1337 hARRDA------FHWLSlttEFGITVWNSVPGlMDMLLIAagDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVA 1410
Cdd:cd17647 182 -TQDDIgtpgrlAEWMA---KYGATVTHLTPA-MGQLLTA--QATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1411 MGGATEAAIWSNEFVVD--DVDPDW-----ASIPYGYPLANQMFRVVDDNGDDQPDYVA--GELWIGGAGVALGYHNAPE 1481
Cdd:cd17647 255 MYGTTETQRAVSYFEVPsrSSDPTFlknlkDVMPAGRGMLNVQLLVVNRNDRTQICGIGevGEIYVRAGGLAEGYRGLPE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1482 LTSDRFVH------------DPTGS------------RWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHAL 1537
Cdd:cd17647 335 LNKEKFVNnwfvepdhwnylDKDNNepwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1538 RGHPLVAA-ATVV--PIHNCTALGAGIVVTGSGAEQFDDSTPGA----------------------LRAHLAVRLPQYMI 1592
Cdd:cd17647 415 SQHPLVREnITLVrrDKDEEPTLVSYIVPRFDKPDDESFAQEDVpkevstdpivkgligyrklikdIREFLKKRLASYAI 494
|
490 500
....*....|....*....|...
gi 2181016861 1593 PKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd17647 495 PSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1730-2099 |
3.99e-38 |
|
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: 149.95 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1730 FPLTRLQQAYTLGAAG---LNGSTCaPTYFAVvlaaapESAGIDLDRFARVVTRCVDEFAMLRCALDADTTQRV--QVDA 1804
Cdd:cd19535 2 FPLTDVQYAYWIGRQDdqeLGGVGC-HAYLEF------DGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQIlpEVPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1805 GPVPVHDLDIQDDPDL---LLR---RMAAAPFDPHSVPVIQCFApSRSPRHVGLL---ISYLGLDARSLSTVVTTIIAEY 1875
Cdd:cd19535 75 YGITVHDLRGLSEEEAeaaLEElreRLSHRVLDVERGPLFDIRL-SLLPEGRTRLhlsIDLLVADALSLQILLRELAALY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1876 QSQPRPRqvdPTAAV-FARF-ASESAWGENDVDNSVA----------GPPLLPLhdqRRDP--FERVTFARRSFTIEEQA 1941
Cdd:cd19535 154 EDPGEPL---PPLELsFRDYlLAEQALRETAYERARAywqerlptlpPAPQLPL---AKDPeeIKEPRFTRREHRLSAEQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1942 AATLREHAAHLGVTPTALVFEAFAHALASIGAGQRFAVTVPKSYRPDYAPADREVLGNFTRLALCEVDYGAvrPGS-AEA 2020
Cdd:cd19535 228 WQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSE--GQSfLER 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2021 VAAAQRELWRAVSHdGDITGG-----LAATRTAGGY--PVVFTSTLGLT----HQDASGLTNVRTLTQTPGVWLDCQTED 2089
Cdd:cd19535 306 ARRLQQQLWEDLDH-SSYSGVvvvrrLLRRRGGQPVlaPVVFTSNLGLPlldeEVREVLGELVYMISQTPQVWLDHQVYE 384
|
410
....*....|
gi 2181016861 2090 EVAGIRMSWD 2099
Cdd:cd19535 385 EDGGLLLNWD 394
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1177-1614 |
1.30e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 148.59 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIrtdsdtqdagvavsditamiecapTDP 1256
Cdd:cd05934 28 GDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV------------------------VDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1257 iridphdaAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLA-LSALDFDLSVYDTFGALGCGAQLVTIP 1335
Cdd:cd05934 84 --------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTvLPLFHINAQAVSVLAALSVGATLVLLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1336 E-HARRdafhWLSLTTEFGITVWNSVPGLMDMLL---IAAGDKAGslpTLRSVFLSGdwIPLDLPRRLRRAApGVRLVAM 1411
Cdd:cd05934 156 RfSASR----FWSDVRRYGATVTNYLGAMLSYLLaqpPSPDDRAH---RLRAAYGAP--NPPELHEEFEERF-GVRLLEG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1412 GGATEAAIwsneFVVDDVDPD--WASIPYGYPLANqmFRVVDDNGDDQPDYVAGELWI---GGAGVALGYHNAPELTSDR 1486
Cdd:cd05934 226 YGMTETIV----GVIGPRDEPrrPGSIGRPAPGYE--VRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1487 FVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNctALG-----AGI 1561
Cdd:cd05934 300 MRNG-----WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPD--EVGedevkAVV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1562 VVTGSGAeqfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGK 1614
Cdd:cd05934 373 VLRPGET-----LDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
25-566 |
1.79e-37 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 151.03 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 25 WVGRRPDAVALRTVAATGID-DWTYQRLWDHVReirdvAFSG--LSAGIR-----------IPMALPG-------GAdyv 83
Cdd:COG0365 18 HAEGRGDKVALIWEGEDGEErTLTYAELRREVN-----RFANalRALGVKkgdrvaiylpnIPEAVIAmlacariGA--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 84 agmlaalaaglIPVPVYlpstrepQRFLARA-QHILRDCEPSAVYTC------GELVEVLER-DPILGALPI-------- 147
Cdd:COG0365 90 -----------VHSPVF-------PGFGAEAlADRIEDAEAKVLITAdgglrgGKVIDLKEKvDEALEELPSlehvivvg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 148 RTPASTA-------DGLAPHPGGTTADAD-HGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAA-FAANVWN-GDDDMHM- 216
Cdd:COG0365 152 RTGADVPmegdldwDELLAAASAEFEPEPtDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAtTAKYVLDlKPGDVFWc 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 217 ---VSWLplyhdMGIFWGVFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAfDGTALQSLDL 293
Cdd:COG0365 232 tadIGWA-----TGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKA-GDEPLKKYDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 294 SCLRLATNGAEPVRGTTLRDFTAKFRAAgLRDdvmapQYGLAEAGLGVTGSqtvrvwveksFDADALERGiavevaqpnp 373
Cdd:COG0365 306 SSLRLLGSAGEPLNPEVWEWWYEAVGVP-IVD-----GWGQTETGGIFISN----------LPGLPVKPG---------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 374 adgrsralvSCGDGAFGWDIQIVDPDRHmTLTDGEVGEIWVGG--PGLPDGYWRQPEQTATTFGARTADglgpYLRTGDA 451
Cdd:COG0365 360 ---------SMGKPVPGYDVAVVDEDGN-PVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFGRFPG----WYRTGDG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 452 GFRYQ-GELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVApggACAV--QPDApqANGEW---WLVLETG-SPVEDL 524
Cdd:COG0365 426 ARRDEdGYFWILGRSDDVINVSGHRIGTAEIESALVS-HPAVA---EAAVvgVPDE--IRGQVvkaFVVLKPGvEPSDEL 499
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2181016861 525 -DDLSRILRRRILAHHetAPERVVWVPcrTLPTTTSGKIRRRE 566
Cdd:COG0365 500 aKELQAHVREELGPYA--YPREIEFVD--ELPKTRSGKIMRRL 538
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
26-564 |
1.41e-36 |
|
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: 145.83 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 26 VGRRPDAVALRTVAATgiddWTYQRLWDHVREIRDV-AFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPST 104
Cdd:cd17631 5 ARRHPDRTALVFGGRS----LTYAELDERVNRLAHAlRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 105 REPQRFlaraqhILRDCEPSavytcgelveVLERDPilgalpirtpastadglaphpggttadadhgehvAFLQYSSGST 184
Cdd:cd17631 81 PPEVAY------ILADSGAK----------VLFDDL----------------------------------ALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 185 GKPKGVVNTHQSILrqAAFAANVWNGDDDMHMVSW--LPLYHDMGIFWGVFMPLLNGGctTLIPPHDFvrNPRIWLETVS 262
Cdd:cd17631 111 GRPKGAMLTHRNLL--WNAVNALAALDLGPDDVLLvvAPLFHIGGLGVFTLPTLLRGG--TVVILRKF--DPETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 263 RFRGNWIGGPDFAYRRCI--EAFDGTalqslDLSCLRLATNGAEPVRGTTLRDFTAkfraaglRDDVMAPQYGLAEAGLG 340
Cdd:cd17631 185 RHRVTSFFLVPTMIQALLqhPRFATT-----DLSSLRAVIYGGAPMPERLLRALQA-------RGVKFVQGYGMTETSPG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 341 VTGsqtvrvwveksfdadalergiavevaqpNPADGRSRALVSCGDGAFGWDIQIVDPDRHmTLTDGEVGEIWVGGPGLP 420
Cdd:cd17631 253 VTF----------------------------LSPEDHRRKLGSAGRPVFFVEVRIVDPDGR-EVPPGEVGEIVVRGPHVM 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 421 DGYWRQPEQTATTFgartADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVApggACA 499
Cdd:cd17631 304 AGYWNRPEATAAAF----RDG---WFHTGDLGrLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYE-HPAVA---EVA 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 500 V--QPD-----APQAngewWLVLETGSPVeDLDDLSRILRRRILAHHetAPERVVWVPcrTLPTTTSGKIRR 564
Cdd:cd17631 373 VigVPDekwgeAVVA----VVVPRPGAEL-DEDELIAHCRERLARYK--IPKSVEFVD--ALPRNATGKILK 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
175-566 |
3.44e-36 |
|
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: 144.74 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHD-FVRN 253
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDpKEVA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 254 PRIWLETVSRFrgnwIGGPDFaYRRCIEAFDGTALQSLDLSC-----LRLATNGAEPVRGTTLRDFTAKFraaGLRddvM 328
Cdd:cd05941 172 ISRLMPSITVF----MGVPTI-YTRLLQYYEAHFTDPQFARAaaaerLRLMVSGSAALPVPTLEEWEAIT---GHT---L 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 APQYGLAEAGlgvtgsqtvrvwveksfdadalergiaveVAQPNPADGRSRAlvscgdGAFGW-----DIQIVDPDRHMT 403
Cdd:cd05941 241 LERYGMTEIG-----------------------------MALSNPLDGERRP------GTVGMplpgvQARIVDEETGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 404 LTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFR-YQGELYVCGRYRDLII-VGGRNHFPNDI 481
Cdd:cd05941 286 LPRGEVGEIQVRGPSVFKEYWNKPEATKEEF---TDDG---WFKTGDLGVVdEDGYYWILGRSSVDIIkSGGYKVSALEI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 482 EKTVeEAHCGVApggACAV--QPDAPQanGE---WWLVLETGSPVEDLDDLSRILRRRiLAHHETaPERVVWVPcrTLPT 556
Cdd:cd05941 360 ERVL-LAHPGVS---ECAVigVPDPDW--GErvvAVVVLRAGAAALSLEELKEWAKQR-LAPYKR-PRRLILVD--ELPR 429
|
410
....*....|
gi 2181016861 557 TTSGKIRRRE 566
Cdd:cd05941 430 NAMGKVNKKE 439
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2508-2954 |
4.13e-36 |
|
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: 151.55 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2508 PRTGPEVSVAAESTRGGTHDPNRFPLTVVQNAYRAGREGALILGGVAAHCYFEFELADFDRPRFDSAARQLVARHAGLRT 2587
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2588 TVSPAGTDAASSGEVAVVHTAPIEPVVRDHDDVRAAMRDQ-IIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMM 2666
Cdd:COG1020 81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALaPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2667 IALSELDHLYRGETVDQ---LPPLETSFAHYVWNHPELLPDAdeavlpRLAASRDYWRARLPSLPPAPKLADMSLLFEIE 2743
Cdd:COG1020 161 LLLAELLRLYLAAYAGAplpLPPLPIQYADYALWQREWLQGE------ELARQLAYWRQQLAGLPPLLELPTDRPRPAVQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2744 EPRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDPDvvGIENVVGDFTSLVLL 2823
Cdd:COG1020 235 SYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2824 ECRVDEPASIWESVRALQRQLMTDLPHRGADAVWLQRELLRFHGNPTAALFPVVFTSGLGLVDASARAAVRFaEPVFAAS 2903
Cdd:COG1020 313 RVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTL-EPLELDS 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 2904 QTPQTVLDFQVWESAGALKLSWDFVSQAVSPATARTQLESLVDGITGVATR 2954
Cdd:COG1020 392 GTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1177-1610 |
2.50e-35 |
|
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: 143.12 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSR----------ICA-------RSAMAGLIRTDS----DT 1235
Cdd:cd05911 35 GDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHqlkiskpkviFTDpdglekvKEAAKELGPKDKiivlDD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1236 QDAGVA----VSDITAMIECAPTDPIRIDPHDA-AYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDT--HDRLLA 1308
Cdd:cd05911 115 KPDGVLsiedLLSPTLGEEDEDLPPPLKDGKDDtAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDgsNDVILG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1309 LSALDFdlsVYDTFGALGC---GAQLVTIPehaRRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVF 1385
Cdd:cd05911 195 FLPLYH---IYGLFTTLASllnGATVIIMP---KFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1386 LSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAiwsnefVVDDVDPDWASIP--YGYPLANQMFRVVDDNGDDQ--PDYV 1461
Cdd:cd05911 269 SGGAPLSKELQELLAKRFPNATIKQGYGMTETG------GILTVNPDGDDKPgsVGRLLPNVEAKIVDDDGKDSlgPNEP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1462 aGELWIGGAGVALGYHNAPELTSDRFVHDptgsRWYRTGDMGcYWR-DGTLQFLGRADSQVKIRGHRVECGEIEHALRGH 1540
Cdd:cd05911 343 -GEICVRGPQVMKGYYNNPEATKETFDED----GWLHTGDIG-YFDeDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEH 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1541 PLVAAATV--VPIHNCTALGAGIVVTGSGAEQFDDstpgALRAHLAVRLPQYmipK------VFVscPELPLTANGKV 1610
Cdd:cd05911 417 PGVADAAVigIPDEVSGELPRAYVVRKPGEKLTEK----EVKDYVAKKVASY---KqlrggvVFV--DEIPKSASGKI 485
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
683-1078 |
6.73e-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: 140.62 E-value: 6.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 683 PWPTTPLQQAYWVGRGAEQPLGGVGCQTYFELVGArVDAGRLAAALDALTRRHPMLRATFP-DPGRC--LITPEAVRLPL 759
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGS-LDLARLKQALDAVMERHDVLRTRFCeEAGRYeqVVLDKTVRFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 760 AVHDLTDapVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRL---PHGCIVhfAVDLIIADVTSIGTMLRDLAASYRG 836
Cdd:cd19066 80 EIIDLRN--LADPEARLLELIDQIQQTIYDLERGPLVRVALFRLadeRDVLVV--AIHHIIVDGGSFQILFEDISSVYDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 837 -----EKLPAPSATFADLI-----QSTSPPPQACAD-------RLPEGPQLP----RVQEADISFLRHQHTLSALATKAI 895
Cdd:cd19066 156 aerqkPTLPPPVGSYADYAawlekQLESEAAQADLAywtsylhGLPPPLPLPkakrPSQVASYEVLTLEFFLRSEETKRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 896 DDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGR-SPEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKGL 974
Cdd:cd19066 236 REVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRpDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 975 RTALRAA--PAPDLL-ATQLRSGTGHSGIVPVVFTYAADSPLLSAEDANTLGAIDEVVSMTPQVLIDHQAC-RLGDDVVL 1050
Cdd:cd19066 316 REAIEHQrvPFIELVrHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASeDPDGDLLL 395
|
410 420
....*....|....*....|....*...
gi 2181016861 1051 SWDYRAGCFPPGVVDDMFEAYVTLLERL 1078
Cdd:cd19066 396 RLEYSRGVYDERTIDRFAERYMTALRQL 423
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1113-1612 |
1.93e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 141.09 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1113 LLYDAFRENAATHPARLALRWrpddyrgerhgdviaqDRSQLTYGELDE--------LARsvaravaarhaagsvIGIQl 1184
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYF----------------DGRRTTYAELDErvnrlanaLRA---------------LGVK- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1185 pkgPSQIVAV------------LGVMMAGCTYLPVGVDQPAERLSRIC---------ARSAMAGLIR------------- 1230
Cdd:PRK06187 55 ---KGDRVAVfdwnsheyleayFAVPKIGAVLHPINIRLKPEEIAYILndaedrvvlVDSEFVPLLAailpqlptvrtvi 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1231 --TDSDTQDAGVAVSDITAMIECAPTDP--IRIDPHDAAYVIYTSGSTGEPKGVLVSHA-AALNTIVdVNRRNRIDTHDR 1305
Cdd:PRK06187 132 veGDGPAAPLAPEVGEYEELLAAASDTFdfPDIDENDAAAMLYTSGTTGHPKGVVLSHRnLFLHSLA-VCAWLKLSRDDV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1306 LLALsaldfdLSVYDTFG------ALGCGAQLVtIPehARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLP 1379
Cdd:PRK06187 211 YLVI------VPMFHVHAwglpylALMAGAKQV-IP--RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1380 TLRSVFLSGDWIPLDLprrLRRAA--PGVRLVAMGGATEAaiwSNEFVV---DDVDPDWASIPY--GYPLANQMFRVVDD 1452
Cdd:PRK06187 282 SLRLVIYGGAALPPAL---LREFKekFGIDLVQGYGMTET---SPVVSVlppEDQLPGQWTKRRsaGRPLPGVEARIVDD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1453 NGDDQP--DYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVEC 1530
Cdd:PRK06187 356 DGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG-----WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1531 GEIEHALRGHPLVAAATVVpihnctalgaGI------------VVTGSGAEqfddSTPGALRAHLAVRLPQYMIPK--VF 1596
Cdd:PRK06187 431 RELEDALYGHPAVAEVAVI----------GVpdekwgerpvavVVLKPGAT----LDAKELRAFLRGRLAKFKLPKriAF 496
|
570
....*....|....*.
gi 2181016861 1597 VscPELPLTANGKVDR 1612
Cdd:PRK06187 497 V--DELPRTSVGKILK 510
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
12-575 |
7.24e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 139.55 E-value: 7.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 12 HDGDRSVPAVFAEWVGRRPDAVALRTvaatGIDDWTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAAL 90
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHPDKEAVYF----DGRRTTYAELDERVNRLaNALRALGVKKGDRVAVFDWNSHEYLEAYFAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 91 AAGLIPVPVylpSTREPQRFLAraqHILRDCEPSAVYTCGELVEVLErdPILGALP-IRTPASTADGLAPHPGGTTAD-- 167
Cdd:PRK06187 78 KIGAVLHPI---NIRLKPEEIA---YILNDAEDRVVLVDSEFVPLLA--AILPQLPtVRTVIVEGDGPAAPLAPEVGEye 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 168 ------------ADHGEHVAFLQ-YSSGSTGKPKGVVNTHQSILRQAAfAANVWNG--DDDMHMVSwLPLYHDMGifWGV 232
Cdd:PRK06187 150 ellaaasdtfdfPDIDENDAAAMlYTSGTTGHPKGVVLSHRNLFLHSL-AVCAWLKlsRDDVYLVI-VPMFHVHA--WGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 233 -FMPLLNGGctTLIPPHDFvrNPRIWLETVSRFRgnwiggPDFAYrrCIEafdgTALQSL---------DLSCLRLATNG 302
Cdd:PRK06187 226 pYLALMAGA--KQVIPRRF--DPENLLDLIETER------VTFFF--AVP----TIWQMLlkaprayfvDFSSLRLVIYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 303 AEPVRGTTLRDFTAKFRAaglrdDVMApQYGLAEAGlgvtgsqtvrvwveksfdadalerGIAVeVAQPNPAD-GRSRAL 381
Cdd:PRK06187 290 GAALPPALLREFKEKFGI-----DLVQ-GYGMTETS------------------------PVVS-VLPPEDQLpGQWTKR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 382 VSCGDGAFGWDIQIVDPD-RHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFR-YQGEL 459
Cdd:PRK06187 339 RSAGRPLPGVEARIVDDDgDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETI----DGG---WLHTGDVGYIdEDGYL 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 460 YVCGRYRDLIIVGGRNHFPNDIEKTVeEAHCGVApggACAV--QPDapqangEWW-------LVLETGSPVeDLDDLSRI 530
Cdd:PRK06187 412 YITDRIKDVIISGGENIYPRELEDAL-YGHPAVA---EVAVigVPD------EKWgerpvavVVLKPGATL-DAKELRAF 480
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2181016861 531 LRRRIlAHHETaPERVVWVPcrTLPTTTSGKIRRRETLNRLTAGQ 575
Cdd:PRK06187 481 LRGRL-AKFKL-PKRIAFVD--ELPRTSVGKILKRVLREQYAEGK 521
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1177-1615 |
4.51e-33 |
|
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: 135.16 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLP----VGVDQPAERLSRicarsAMAGLIRTDSDtqdagvavsditamieca 1252
Cdd:cd05972 25 GDRVAVLLPRVPELWAVILAVIKLGAVYVPlttlLGPKDIEYRLEA-----AGAKAIVTDAE------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1253 ptdpiridphDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTF-GALGCGAQL 1331
Cdd:cd05972 82 ----------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFfGPWLLGATV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1332 VTIpEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLlIAAGDKAGSLPTLRSVFLSGDwiPLdLPRRLR--RAAPGVRLV 1409
Cdd:cd05972 152 FVY-EGPRFDAERILELLERYGVTSFCGPPTAYRML-IKQDLSSYKFSHLRLVVSAGE--PL-NPEVIEwwRAATGLPIR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1410 AMGGATEAAIWSNEFVVDDVDPdwASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWI--GGAGVALGYHNAPELTSDRF 1487
Cdd:cd05972 227 DGYGQTETGLTVGNFPDMPVKP--GSM--GRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1488 VHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCT--ALGAGIVVTG 1565
Cdd:cd05972 303 RGD-----YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVrgEVVKAFVVLT 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 1566 SGAEQfDDSTPGALRAHLAVRLPQYMIPKV--FVscPELPLTANGKVDRGKI 1615
Cdd:cd05972 378 SGYEP-SEELAEELQGHVKKVLAPYKYPREieFV--EELPKTISGKIRRVEL 426
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
115-562 |
1.81e-32 |
|
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: 134.65 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 115 QHILRDCEPSAVYTCGELVEV-------LERDP--ILGALPIRTPASTADGLAPHPGGTTAD-----ADHGEHVAFLQYS 180
Cdd:cd05911 75 AHQLKISKPKVIFTDPDGLEKvkeaakeLGPKDkiIVLDDKPDGVLSIEDLLSPTLGEEDEDlppplKDGKDDTAAILYS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 181 SGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMV--SWLPLYHDMGIFWGVFMPLLngGCTTLIPPHDFVRNpriWL 258
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVilGFLPLYHIYGLFTTLASLLN--GATVIIMPKFDSEL---FL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 259 ETVSRFRGNWIGgpdFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVrgttLRDFTAKFRAAGLRDDVMapQ-YGLAEA 337
Cdd:cd05911 230 DLIEKYKITFLY---LVPPIAAALAKSPLLDKYDLSSLRVILSGGAPL----SKELQELLAKRFPNATIK--QgYGMTET 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 338 GLGVTGSQTVRVWVEksfdadalergiavevaqpnpadgrsralvSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGP 417
Cdd:cd05911 301 GGILTVNPDGDDKPG------------------------------SVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 418 GLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVAPgg 496
Cdd:cd05911 351 QVMKGYYNNPEATKETF---DEDG---WLHTGDIGyFDEDGYLYIVDRKKELIKYKGFQVAPAELE-AVLLEHPGVAD-- 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 497 AC------AVQPDAPQAngewwLVLETGSPVEDLDDLSRILRRRiLAHHETAPERVVWVPcrTLPTTTSGKI 562
Cdd:cd05911 422 AAvigipdEVSGELPRA-----YVVRKPGEKLTEKEVKDYVAKK-VASYKQLRGGVVFVD--EIPKSASGKI 485
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
106-580 |
2.58e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 134.73 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 106 EPQRFLARAQHILRDCePSavytcgeLVEVLERDPILGALPIRTPASTADGLAPHPGGTTADadhgehVAFLQYSSGSTG 185
Cdd:PRK06188 116 DPAPFVERALALLARV-PS-------LKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPPD------IAGLAYTGGTTG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 186 KPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFwgvFMP-LLNGGCTTLIPPHDfvrnPRIWLETVSRF 264
Cdd:PRK06188 182 KPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF---FLPtLLRGGTVIVLAKFD----PAEVLRAIEEQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 265 RGNW-IGGPDFAYRrcieAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAPQYGLAEAGlgvtg 343
Cdd:PRK06188 255 RITAtFLVPTMIYA----LLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERF------GPIFAQYYGQTEAP----- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 344 sQTVRVWVEKSFDADALERgiavevaqpnpadgrsraLVSCGDGAFGWDIQIVDPDRHMTLTdGEVGEIWVGGPGLPDGY 423
Cdd:PRK06188 320 -MVITYLRKRDHDPDDPKR------------------LTSCGRPTPGLRVALLDEDGREVAQ-GEVGEICVRGPLVMDGY 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 424 WRQPEQTATTFgartADGlgpYLRTGDAGFRYQ-GELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVApggACAV-- 500
Cdd:PRK06188 380 WNRPEETAEAF----RDG---WLHTGDVAREDEdGFYYIVDRKKDMIVTGGFNVFPREVEDVLAE-HPAVA---QVAVig 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 501 QPDapqangEWW-------LVLETGSPVeDLDDLSRILRRRILAHHetAPERVVWVpcRTLPTTTSGKIRRRETLNRLTA 573
Cdd:PRK06188 449 VPD------EKWgeavtavVVLRPGAAV-DAAELQAHVKERKGSVH--APKQVDFV--DSLPLTALGKPDKKALRARYWE 517
|
....*..
gi 2181016861 574 GQLEVVH 580
Cdd:PRK06188 518 GRGRAVG 524
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
112-464 |
5.26e-32 |
|
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: 131.62 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 112 ARAQHILRDCEPSAVYTCGELVEVLERDPILGALPIRTPASTADGLAPhpGGTTADADHGEHVAFLQYSSGSTGKPKGVV 191
Cdd:TIGR01733 62 ERLAFILEDAGARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPA--PPPPDAPSGPDDLAYVIYTSGSTGRPKGVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 192 NTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGGCTTLIPPHDFVRNPRIWLETVSRFRGNWIGG 271
Cdd:TIGR01733 140 VTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASV-EEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 272 PDFAYRRCIEAfdgtalQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLrddvmAPQYGLAEAGLGVTGsqtvrvwv 351
Cdd:TIGR01733 219 TPSLLALLAAA------LPPALASLRLVILGGEALTPALVDRWRARGPGARL-----INLYGPTETTVWSTA-------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 352 eKSFDADALERGIAVEVAQPNPadgrsralvscgdgafGWDIQIVDPDRhMTLTDGEVGEIWVGGPGLPDGYWRQPEQTA 431
Cdd:TIGR01733 280 -TLVDPDDAPRESPVPIGRPLA----------------NTRLYVLDDDL-RPVPVGVVGELYIGGPGVARGYLNRPELTA 341
|
330 340 350
....*....|....*....|....*....|....*...
gi 2181016861 432 TTFGA---RTADGLGPYlRTGDAGfRYQ--GELYVCGR 464
Cdd:TIGR01733 342 ERFVPdpfAGGDGARLY-RTGDLV-RYLpdGNLEFLGR 377
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1146-1612 |
1.23e-31 |
|
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: 131.26 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1146 VIAQDRSqLTYGEL--DELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRIcars 1223
Cdd:cd05941 5 IVDDGDS-ITYADLvaRAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1224 amagliRTDSDTQdagvavsditamiecaptdpIRIDPhdaAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTH 1303
Cdd:cd05941 80 ------ITDSEPS--------------------LVLDP---ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1304 DRLLALsaldfdLSVYDTFG-------ALGCGAQLVTIPEHarrDAFHWLSLTTEFGITVWNSVPG----LMD----MLL 1368
Cdd:cd05941 131 DVLLHV------LPLHHVHGlvnallcPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTiytrLLQyyeaHFT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1369 IAAGDKAGSLPTLRsVFLSGDwIPLDLPRRLR-RAAPGVRLVAMGGATEAAIWsnefvvddvdpdwASIPY--------- 1438
Cdd:cd05941 202 DPQFARAAAAERLR-LMVSGS-AALPVPTLEEwEAITGHTLLERYGMTEIGMA-------------LSNPLdgerrpgtv 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1439 GYPLANQMFRVVDDNGDDQPDYVA-GELWIGGAGVALGYHNAPELTSDRFVHDptgsRWYRTGDMGCYWRDGTLQFLGR- 1516
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEvGEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGVVDEDGYYWILGRs 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1517 ADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTaLG---AGIVVTGSGAEQFDdstPGALRAHLAVRLPQYMIP 1593
Cdd:cd05941 343 SVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPD-WGervVAVVVLRAGAAALS---LEELKEWAKQRLAPYKRP 418
|
490
....*....|....*....
gi 2181016861 1594 KVFVSCPELPLTANGKVDR 1612
Cdd:cd05941 419 RRLILVDELPRNAMGKVNK 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
16-566 |
3.70e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 131.18 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 16 RSVPAVFAEWVGRRPDAVALrtvaATGIDDWTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGL 94
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAY----VFGDQRLTYAELNARVRRAaAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 95 IPVPV---YLPStrepqrflaRAQHILRDCEPSAVYTCGELVEVLErdPILGALP-----IRTPASTADG---------- 156
Cdd:PRK07656 81 VVVPLntrYTAD---------EAAYILARGDAKALFVLGLFLGVDY--SATTRLPalehvVICETEEDDPhtekmktftd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 157 -LAPHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRqaafAANVW------NGDDDMHMVswLPLYHDMGIF 229
Cdd:PRK07656 150 fLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLS----NAADWaeylglTEGDRYLAA--NPFFHVFGYK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 230 WGVFMPLLNGGctTLIPPHDFvrNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTAlqsLDLSCLRLATNGAE--PVR 307
Cdd:PRK07656 224 AGVNAPLMRGA--TILPLPVF--DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA---EDLSSLRLAVTGAAsmPVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 308 gtTLRDFTAKFRAaglrdDVMAPQYGLAEAGlGVTgsqtvrvwvekSFdadalergiavevaqpNPADgRSRALV--SCG 385
Cdd:PRK07656 297 --LLERFESELGV-----DIVLTGYGLSEAS-GVT-----------TF----------------NRLD-DDRKTVagTIG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 386 DGAFGWDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFRYQ-GELYVCGR 464
Cdd:PRK07656 341 TAIAGVENKIVNELGE-EVPVGEVGELLVRGPNVMKGYYDDPEATAAAI---DADG---WLHTGDLGRLDEeGYLYIVDR 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 465 YRDLIIVGGRNHFPNDIEKtVEEAHCGVAPGGACAVqPDAPQAN-GEWWLVLETGSPV--EDLDDLSrilrRRILAHHET 541
Cdd:PRK07656 414 KKDMFIVGGFNVYPAEVEE-VLYEHPAVAEAAVIGV-PDERLGEvGKAYVVLKPGAELteEELIAYC----REHLAKYKV 487
|
570 580
....*....|....*....|....*
gi 2181016861 542 aPERVVWVPcrTLPTTTSGKIRRRE 566
Cdd:PRK07656 488 -PRSIEFLD--ELPKNATGKVLKRA 509
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1146-1615 |
1.01e-30 |
|
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: 129.80 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1146 VIAQDRSQLTYGEL-DELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERL-------- 1216
Cdd:cd05959 22 AFIDDAGSLTYAELeAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYayyledsr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1217 -------SRICARSAMAG---------LIRTDSDTQDAGvaVSDITAMIECAPTD--PIRIDPHDAAYVIYTSGSTGEPK 1278
Cdd:cd05959 102 arvvvvsGELAPVLAAALtksehtlvvLIVSGGAGPEAG--ALLLAELVAAEAEQlkPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1279 GVLVSHA---AALNTIVdvnrRN--RIDTHDRLLALSALDF--DLSVYDTFgALGCGAQLVTIPEHARRDAFhwLSLTTE 1351
Cdd:cd05959 180 GVVHLHAdiyWTAELYA----RNvlGIREDDVCFSAAKLFFayGLGNSLTF-PLSVGATTVLMPERPTPAAV--FKRIRR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1352 FGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLrRAAPGVRLVAMGGATEAA-IW-SNefVVDDV 1429
Cdd:cd05959 253 YRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERW-KARFGLDILDGIGSTEMLhIFlSN--RPGRV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1430 DPDWASIPY-GYPLanqmfRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVhdptGSrWYRTGDMGCYWRD 1508
Cdd:cd05959 330 RYGTTGKPVpGYEV-----ELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GE-WTRTGDKYVRDDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1509 GTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI---HNCTALGAgIVVTGSGAEQFDDSTPGaLRAHLAV 1585
Cdd:cd05959 400 GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVedeDGLTKPKA-FVVLRPGYEDSEALEEE-LKEFVKD 477
|
490 500 510
....*....|....*....|....*....|
gi 2181016861 1586 RLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05959 478 RLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2531-2952 |
3.96e-30 |
|
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: 126.37 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2531 FPLTVVQNAYRAGREGALilGGVAAHCYFEFEL-ADFDRPRFDSAARQLVARHAGLRTtVSPAGTDAAS---SGEVAVVH 2606
Cdd:cd19066 2 IPLSPMQRGMWFLKKLAT--DPSAFNVAIEMFLtGSLDLARLKQALDAVMERHDVLRT-RFCEEAGRYEqvvLDKTVRFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2607 TAPIEpvVRDHDDVRA-------AMRDQIIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGE 2679
Cdd:cd19066 79 IEIID--LRNLADPEArllelidQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2680 TVDQ--LPPLETSFAHYVWNHPELLPDADeavlprLAASRDYWRARLPSLPPAPKLADMSLLFEIEEPRFERATATIPAV 2757
Cdd:cd19066 157 ERQKptLPPPVGSYADYAAWLEKQLESEA------AQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2758 DWSQVTRSCRAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDPDvvGIENVVGDFTSLVLLECRVDEPASIWESV 2837
Cdd:cd19066 231 ETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2838 RALQRQLMTDLPHRGADAVWLQRELLRFHGNPTAALFPVVFTSGLGLVDASARAAVRFAEPVFAASQTPQTVLDFQVWE- 2916
Cdd:cd19066 309 KRTKEQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEd 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 2181016861 2917 SAGALKLSWDFVSQAVSPATARTQLESLVDGITGVA 2952
Cdd:cd19066 389 PDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLI 424
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1154-1615 |
1.74e-29 |
|
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: 124.80 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1154 LTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTD 1232
Cdd:cd05903 2 LTYSELDTRADRLAAGlAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1233 SDTQdagvavSDITAMiecaptdpiridPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSAL 1312
Cdd:cd05903 82 RFRQ------FDPAAM------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1313 -DFDLSVYDTFGALGCGAQLVTIpehARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWI 1391
Cdd:cd05903 144 aHQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1392 PLDLPRRLrRAAPGVRLVAMGGATEAAiwSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAG 1471
Cdd:cd05903 221 PRSLARRA-AELLGAKVCSAYGSTECP--GAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1472 VALGYHNAPELTSDRFvhdPTGsrWYRTGDMGCYWRDGTLQFLGRAdSQVKIR-GHRVECGEIEHALRGHPLVAAATVVP 1550
Cdd:cd05903 298 VFLGYLDRPDLTADAA---PEG--WFRTGDLARLDEDGYLRITGRS-KDIIIRgGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1551 IHNcTALG---AGIVVTGSGAE-QFDDstpgaLRAHL-AVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05903 372 LPD-ERLGeraCAVVVTKSGALlTFDE-----LVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1177-1612 |
2.04e-29 |
|
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: 124.47 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPV----GVDQPAERLSRicarsamaglirtdsdtqdagvavSDITAMIECA 1252
Cdd:cd05971 31 GDRVGVFLSQGPECAIAHIAILRSGAIAVPLfalfGPEALEYRLSN------------------------SGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1253 PTDPiridphdaAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNrrnridthdrlLALSALDFDLSVYDT------FGALG 1326
Cdd:cd05971 87 SDDP--------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQ-----------FPFNLFPRDGDLYWTpadwawIGGLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1327 CG---AQLVTIPEHARR----DAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRL 1399
Cdd:cd05971 148 DVllpSLYFGVPVLAHRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1400 RRAApGVRLVAMGGATEA-AIWSNEFVVDDVDPdwASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWI--GGAGVALGY 1476
Cdd:cd05971 228 REQF-GVEVNEFYGQTECnLVIGNCSALFPIKP--GSM--GKPIPGHRVAIVDDNGTPLPPGEVGEIAVelPDPVAFLGY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1477 HNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV----PIH 1552
Cdd:cd05971 303 WNNPSATEKKMAGD-----WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVgipdPIR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1553 NcTALGAGIVVTGSgaEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05971 378 G-EIVKAFVVLNPG--ETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRR 434
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
169-566 |
3.97e-29 |
|
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: 123.79 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 169 DHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGGCTTLIPPH 248
Cdd:cd05930 90 TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSV-WEIFGALLAGATLVVLPEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 249 DfVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAfdgtaLQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLRDDvm 328
Cdd:cd05930 169 V-RKDPEALADLLAEEGITVLHLTPSLLRLLLQE-----LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNL-- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 apqYGLAEAGLGVTgsqtvrvwveksfdadalergiavevAQPNPADGRSRALVSCGDGAFGWDIQIVDPDRHmTLTDGE 408
Cdd:cd05930 241 ---YGPTEATVDAT--------------------------YYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLR-PVPPGV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 409 VGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYLRTGDAG-FRYQGELYVCGRYRDLIIVGGrnhF---PNDIEKT 484
Cdd:cd05930 291 PGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVrWLPDGNLEFLGRIDDQVKIRG---YrieLGEIEAA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 485 VeEAHCGVApggACAVQPDAPQANGEW---WLVLETGSPVeDLDDLSRILRRRiLAHHeTAPERVVWVPcrTLPTTTSGK 561
Cdd:cd05930 368 L-LAHPGVR---EAAVVAREDGDGEKRlvaYVVPDEGGEL-DEEELRAHLAER-LPDY-MVPSAFVVLD--ALPLTPNGK 438
|
....*
gi 2181016861 562 IRRRE 566
Cdd:cd05930 439 VDRKA 443
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1114-1612 |
5.15e-29 |
|
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: 124.87 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAATHPARLAlrwrpddyrgerhgdVIAQDRsQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIV 1192
Cdd:COG1021 27 LGDLLRRRAERHPDRIA---------------VVDGER-RLSYAELDRRADRLAAGLLALgLRPGDRVVVQLPNVAEFVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1193 AVLGVMMAGCtyLPVGVdQPAER---LSRICARSAMAGLIRTDSD------------------------TQDAGVAVSdI 1245
Cdd:COG1021 91 VFFALFRAGA--IPVFA-LPAHRraeISHFAEQSEAVAYIIPDRHrgfdyralarelqaevpslrhvlvVGDAGEFTS-L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1246 TAMIEC-APTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLAlsAL----DFDLSVYD 1320
Cdd:COG1021 167 DALLAApADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLA--ALpaahNFPLSSPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1321 TFGALGCGAQLVTIPEHARRDAFhwlSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLR 1400
Cdd:COG1021 245 VLGVLYAGGTVVLAPDPSPDTAF---PLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1401 RAApGVRLVAMGGATEAAIwsNEFVVDDvdPDWASIPY-GYPL--ANQmFRVVDDNGDDQPDYVAGELWIGGAGVALGYH 1477
Cdd:COG1021 322 PAL-GCTLQQVFGMAEGLV--NYTRLDD--PEEVILTTqGRPIspDDE-VRIVDEDGNPVPPGEVGELLTRGPYTIRGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1478 NAPELTSDRFvhDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVkIR-GHRVECGEIEHALRGHPLVAAATVVPIHNcTA 1556
Cdd:COG1021 396 RAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPD-EY 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1557 LG----AGIVVTGsgaeqfDDSTPGALRAHLAVR-LPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:COG1021 470 LGerscAFVVPRG------EPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDK 524
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1177-1615 |
6.29e-29 |
|
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: 122.94 E-value: 6.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRTDS----DTQdaGVAVSDITAMIECA 1252
Cdd:TIGR01923 24 GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLleekDFQ--ADSLDRIEAAGRYE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1253 PTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDR-LLALSAldFDLSVYDT-FGALGCGAQ 1330
Cdd:TIGR01923 102 TSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNwLLSLPL--YHISGLSIlFRWLIEGAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1331 LVTipeHARRDAFhwLSLTTEFGITVWNSVPGLMDMLLiaagDKAGSLPTLRSVFLSGDWIPLDLprrLRRAAP-GVRLV 1409
Cdd:TIGR01923 180 LRI---VDKFNQL--LEMIANERVTHISLVPTQLNRLL----DEGGHNENLRKILLGGSAIPAPL---IEEAQQyGLPIY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1410 AMGGATEAAiwsNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQpdyvaGELWIGGAGVALGYHNAPELTSDRFVH 1489
Cdd:TIGR01923 248 LSYGMTETC---SQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIMVKGANLMKGYLYQGELTPAFEQQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1490 DptgsrWYRTGDMGcYWR-DGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTaLGAGIVVTGSGA 1568
Cdd:TIGR01923 320 G-----WFNTGDIG-ELDgEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAE-WGQVPVAYIVSE 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2181016861 1569 EQFDDSTpgaLRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:TIGR01923 393 SDISQAK---LIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1265-1612 |
1.03e-28 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 119.74 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1265 AYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVtipEHARRDAFh 1344
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELV---LLERNQAL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1345 wLSLTTEFGITVWNSVPGLMDMLLiAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLrrAAPGVRLVAMGGATEAAIwsnef 1424
Cdd:cd17630 79 -AEDLAPPGVTHVSLVPTQLQRLL-DSGQGPAALKSLRAVLLGGAPIPPELLERA--ADRGIPLYTTYGMTETAS----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1425 VVDDVDPDWASIPY-GYPLANQMFRVVDDngddqpdyvaGELWIGGAGVALGYHNAPEltsdrfVHDPTGSRWYRTGDMG 1503
Cdd:cd17630 150 QVATKRPDGFGRGGvGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQL------VPEFNEDGWFTTKDLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1504 CYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTaLGAGIVVTGSGAeqfDDSTPGALRAHL 1583
Cdd:cd17630 214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEE-LGQRPVAVIVGR---GPADPAELRAWL 289
|
330 340
....*....|....*....|....*....
gi 2181016861 1584 AVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDR 318
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1190-1613 |
1.26e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 122.99 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1190 QIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAgLIRTDSDTQDAG---VAVSDITAMIECA-PTDPIRIDPHDAA 1265
Cdd:PRK09088 60 LVALHFACARVGAIYVPLNWRLSASELDALLQDAEPR-LLLGDDAVAAGRtdvEDLAAFIASADALePADTPSIPPERVS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1266 YVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLAlsaldfDLSVYDTFG-------ALGCGAQLVTIPEHA 1338
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLC------DAPMFHIIGlitsvrpVLAVGGSILVSNGFE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1339 RRDAFHWLSlTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGdwIPLDLPRRLRRAAPGVRLVAMGGATEAA 1418
Cdd:PRK09088 213 PKRTLGRLG-DPALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGG--APHAAEDILGWLDDGIPMVDGFGMSEAG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1419 iwsnefVVDDVDPDWASI-----PYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFvhdpTG 1493
Cdd:PRK09088 290 ------TVFGMSVDCDVIrakagAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF----TG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1494 SRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCT--ALGAGIVVTGSGaeqf 1571
Cdd:PRK09088 360 DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwgEVGYLAIVPADG---- 435
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2181016861 1572 DDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRG 1613
Cdd:PRK09088 436 APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKA 477
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1140-1610 |
1.30e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 123.48 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1140 GERHGDVIA--QDRSQLTYGELD-ELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERL 1216
Cdd:PRK07656 15 ARRFGDKEAyvFGDQRLTYAELNaRVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1217 SRICARSAMAGLIRTD----SDTQdAGVAVSDITAMIECAPTDPIR-----------------------IDPHDAAYVIY 1269
Cdd:PRK07656 95 AYILARGDAKALFVLGlflgVDYS-ATTRLPALEHVVICETEEDDPhtekmktftdflaagdpaerapeVDPDDVADILF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1270 TSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLAlsALDFdlsvYDTFG-ALGCGAQLV---TIPEHARRDAFHW 1345
Cdd:PRK07656 174 TSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA--ANPF----FHVFGyKAGVNAPLMrgaTILPLPVFDPDEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1346 LSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMG-GATEAAiwsnEF 1424
Cdd:PRK07656 248 FRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESEL-GVDIVLTGyGLSEAS----GV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1425 VV-----DDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDrfVHDPTGsrWYRT 1499
Cdd:PRK07656 323 TTfnrldDDRKTVAGTI--GTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA--AIDADG--WLHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1500 GDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VPIHNCTALGAGIVVTGSGAEqfddSTPG 1577
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVigVPDERLGEVGKAYVVLKPGAE----LTEE 472
|
490 500 510
....*....|....*....|....*....|...
gi 2181016861 1578 ALRAHLAVRLPQYMIPKVFVSCPELPLTANGKV 1610
Cdd:PRK07656 473 ELIAYCREHLAKYKVPRSIEFLDELPKNATGKV 505
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
30-565 |
1.68e-28 |
|
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: 122.81 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 30 PDAVALrtVAATGIDDWTYQRLWDHVRE-IRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPSTR-EP 107
Cdd:cd05926 1 PDAPAL--VVPGSTPALTYADLAELVDDlARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKaEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 108 QRFLARAQH---ILRDCE-----PSAVYTCGELVEVLERDPIL------GALPIRTPASTADGLAPHPggttadadHGEH 173
Cdd:cd05926 79 EFYLADLGSklvLTPKGElgpasRAASKLGLAILELALDVGVLirapsaESLSNLLADKKNAKSEGVP--------LPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDMHMVSwLPLYHDMGIFWGVFMPLLNGGCTTLIP---PHD 249
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKlTPDDRTLVV-MPLFHVHGLVASLLSTLAAGGSVVLPPrfsAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 FvrnpriWLEtVSRFRGNWIGG-PdfayrrcieafdgTALQSL----------DLSCLRLATNGAEPVRGTTLRDFTAKF 318
Cdd:cd05926 230 F------WPD-VRDYNATWYTAvP-------------TIHQILlnrpepnpesPPPKLRFIRSCSASLPPAVLEALEATF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 319 RAAGLRddvmapQYGLAEAGLGVTGsqtvrvwveksfdadalergiavevaqpNPADGRSRALVSCGDGaFGWDIQIVDP 398
Cdd:cd05926 290 GAPVLE------AYGMTEAAHQMTS----------------------------NPLPPGPRKPGSVGKP-VGVEVRILDE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 399 DRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFRYQ-GELYVCGRYRDLIIVGGRNHF 477
Cdd:cd05926 335 DGE-ILPPGVVGEICLRGPNVTRGYLNNPEANAEAA---FKDG---WFRTGDLGYLDAdGYLFLTGRIKELINRGGEKIS 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 478 PNDIEKtVEEAHCGVAPGGACAVqPDapQANGE---WWLVLETGSPVeDLDDLSRILRRRiLAHHETaPERVVWVpcRTL 554
Cdd:cd05926 408 PLEVDG-VLLSHPAVLEAVAFGV-PD--EKYGEevaAAVVLREGASV-TEEELRAFCRKH-LAAFKV-PKKVYFV--DEL 478
|
570
....*....|.
gi 2181016861 555 PTTTSGKIRRR 565
Cdd:cd05926 479 PKTATGKIQRR 489
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
685-1081 |
3.96e-28 |
|
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: 120.90 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 685 PTTPLQQAYWVgrgAEQPL-GGVGC--QTYFELVGArVDAGRLAAALDALTRRHPMLRATFP-----DPGRCLItpEAVR 756
Cdd:pfam00668 6 PLSPAQKRMWF---LEKLEpHSSAYnmPAVLKLTGE-LDPERLEKALQELINRHDALRTVFIrqengEPVQVIL--EERP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 757 LPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRL-PHGCIVHFAVDLIIADVTSIGTMLRDLAASY- 834
Cdd:pfam00668 80 FELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIaENRHHLLLSMHHIIVDGVSLGILLRDLADLYq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 835 ---RGEKLPAPSAT-FADLIQSTSPPPQA------------CADRLPEGPQLPRV--QEADISFLRHQHT--LSALATKA 894
Cdd:pfam00668 160 qllKGEPLPLPPKTpYKDYAEWLQQYLQSedyqkdaaywleQLEGELPVLQLPKDyaRPADRSFKGDRLSftLDEDTEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 895 IDDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGR-SPEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKG 973
Cdd:pfam00668 240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRpSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 974 LRTALRAA--PAPDLLA-TQLRSGTGHSGIVPVVFTYAADSPLLSAEDANTLGAIDEVVSMTPQVL----IDHQACRLGD 1046
Cdd:pfam00668 320 LLSAEPHQgyPFGDLVNdLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEEFQLSELDLSVSSVIEEEakydLSLTASERGG 399
|
410 420 430
....*....|....*....|....*....|....*
gi 2181016861 1047 DVVLSWDYRAGCFPPGVVDDMFEAYVTLLERLGGH 1081
Cdd:pfam00668 400 GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAH 434
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-566 |
4.34e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 118.53 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVfMPLLNGGCTTLIPPHDFvrNPRI 256
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGV-LACLTHGATMVFPSPSF--DPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 257 WLETVSRFRGNWIGG-----------PDFAyrrcieafdgtalqSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaGLRD 325
Cdd:cd05917 84 VLEAIEKEKCTALHGvptmfiaelehPDFD--------------KFDLSSLRTGIMAGAPCPPELMKRVIEVM---NMKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 326 DVMApqYGLAEAGLGVTGSQTVrvwveksfdaDALERGIAVeVAQPNPADgrsralvscgdgafgwDIQIVDPDRHMTLT 405
Cdd:cd05917 147 VTIA--YGMTETSPVSTQTRTD----------DSIEKRVNT-VGRIMPHT----------------EAKIVDPEGGIVPP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 406 DGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIE-- 482
Cdd:cd05917 198 VGVPGELCIRGYSVMKGYWNDPEKTAEAI---DGDG---WLHTGDlAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEef 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 483 ----KTVEEAHC-GVapggacavqPDAPQanGE---WWLVLETGSPVEDlDDLSRILRRRIlAHHEtAPERVVWVpcRTL 554
Cdd:cd05917 272 lhthPKVSDVQVvGV---------PDERY--GEevcAWIRLKEGAELTE-EDIKAYCKGKI-AHYK-VPRYVFFV--DEF 335
|
410
....*....|..
gi 2181016861 555 PTTTSGKIRRRE 566
Cdd:cd05917 336 PLTVSGKIQKFK 347
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1258-1611 |
1.58e-27 |
|
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: 120.04 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1258 RIDPHDAAYVIYTSGSTGEPKGVLVSH-AAALNTivdvnrrnridthdrLLALSALDFDLSVYDT--------------- 1321
Cdd:cd12119 159 DFDENTAAAICYTSGTTGNPKGVVYSHrSLVLHA---------------MAALLTDGLGLSESDVvlpvvpmfhvnawgl 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1322 -FGALGCGAQLVtIPEhARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLR 1400
Cdd:cd12119 224 pYAAAMVGAKLV-LPG-PYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1401 RAapGVRLVAMGGATE------AAIWSNEFVVDDVDPDWA-SIPYGYPLANQMFRVVDDNGDDQP-DYVA-GELWIGGAG 1471
Cdd:cd12119 302 ER--GVRVIHAWGMTEtsplgtVARPPSEHSNLSEDEQLAlRAKQGRPVPGVELRIVDDDGRELPwDGKAvGELQVRGPW 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1472 VALGYHNAPElTSDRFVHDptGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV-- 1549
Cdd:cd12119 380 VTKSYYKNDE-ESEALTED--G--WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIgv 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1550 --------PIhnctalgaGIVVTGSGAeqfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd12119 455 phpkwgerPL--------AVVVLKEGA----TVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKID 512
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
2555-2953 |
1.66e-27 |
|
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: 117.79 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2555 AHCYFEFElADFDRPRFDSAARQLVARHAGLRTTVSPagtdaaSSGE---VAVVHTAPIEPV--VRDHDDVRAAMRDQI- 2628
Cdd:cd19542 24 NHFVFDLD-SSVDVERLRNAWRQLVQRHDILRTVFVE------SSAEgtfLQVVLKSLDPPIeeVETDEDSLDALTRDLl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2629 --IDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQLPPLETsFAHYVWNHPellpdad 2706
Cdd:cd19542 97 ddPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSD-YISYLQSQS------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2707 eavlprLAASRDYWRARLPSLPPApklADMSLLFEIEEPRFERATATIPAVdwsqVTRSCRAEGVTVASFLLANYARVLS 2786
Cdd:cd19542 169 ------QEESLQYWRKYLQGASPC---AFPSLSPKRPAERSLSSTRRSLAK----LEAFCASLGVTLASLFQAAWALVLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2787 RWSGTDHFCINVTLFDRDPDVVGIENVVGDFTSLVLLECRVDEPASIWESVRALQRQLMTDLPHRGADAVWLQRELLRfh 2866
Cdd:cd19542 236 RYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGL-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2867 gNPTAALFPVVFT-SGLGLVDASARAAVRFAEPVFAASQTPQTVLdFQVWESAGALKLSWDFVSQAVSPATARTQLESLV 2945
Cdd:cd19542 314 -WPSGTLFNTLVSyQNFEASPESELSGSSVFELSAAEDPTEYPVA-VEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFD 391
|
....*...
gi 2181016861 2946 DGITGVAT 2953
Cdd:cd19542 392 DILEALLA 399
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
45-566 |
2.63e-27 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 118.47 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 45 DWTYQRLWDHVREIRDV-AFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPSTREpqrflaRAQHILRDCEP 123
Cdd:cd05907 5 PITWAEFAEEVRALAKGlIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAE------QIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 124 SAVYTcgelvevlerdpilgalpirtpastadglaphpggttadaDHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAF 203
Cdd:cd05907 79 KALFV----------------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 204 AANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCT-------TLIP------PHDFVRNPRIWlETVSrfrgnwig 270
Cdd:cd05907 119 LAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIyfassaeTLLDdlsevrPTVFLAVPRVW-EKVY-------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 271 gpDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRgttlRDFTAKFRAAGLrddVMAPQYGLAEAGLGVTGSqtvrvw 350
Cdd:cd05907 190 --AAIKVKAVPGLKRKLFDLAVGGRLRFAASGGAPLP----AELLHFFRALGI---PVYEGYGLTETSAVVTLN------ 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 351 veksfdadalergiavevaqpNPADGRSRALVSCGDGAfgwDIQIvdpdrhmtltdGEVGEIWVGGPGLPDGYWRQPEQT 430
Cdd:cd05907 255 ---------------------PPGDNRIGTVGKPLPGV---EVRI-----------ADDGEILVRGPNVMLGYYKNPEAT 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 431 ATTFgarTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIV-GGRNHFPNDIEKTVEE----AHCGV----APGGACAV 500
Cdd:cd05907 300 AEAL---DADG---WLHTGDLGeIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKAspliSQAVVigdgRPFLVALI 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 501 QPDAPQANGEWWLVLETGSPVEDL---DDLSRILRRRI------LAHHETApeRVVWVpcrtLPT---------TTSGKI 562
Cdd:cd05907 374 VPDPEALEAWAEEHGIAYTDVAELaanPAVRAEIEAAVeaanarLSRYEQI--KKFLL----LPEpftiengelTPTLKL 447
|
....
gi 2181016861 563 RRRE 566
Cdd:cd05907 448 KRPV 451
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1177-1612 |
2.72e-27 |
|
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: 117.99 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVgvdqpaerlsricaRSA-MAGLIRTDSDTQDAGVAVSditamiecAPTD 1255
Cdd:cd05969 25 GDRVFVLSPRSPELYFSMLGIGKIGAVICPL--------------FSAfGPEAIRDRLENSEAKVLIT--------TEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1256 PIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVdvNRRNRIDTHDRLLALSALD---FDLSVYDTFGALGCGAQLV 1332
Cdd:cd05969 83 YERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYF--TGKYVLDLHPDDIYWCTADpgwVTGTVYGIWAPWLNGVTNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1333 TipEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGS--LPTLRSVFLSGDwiPLDlPRRLR--RAAPGVRL 1408
Cdd:cd05969 161 V--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKydLSSLRFIHSVGE--PLN-PEAIRwgMEVFGVPI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1409 VAMGGATE-AAIWSNEFVVDDVDPdwASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWI--GGAGVALGYHNAPELTSD 1485
Cdd:cd05969 236 HDTWWQTEtGSIMIANYPCMPIKP--GSM--GKPLPGVKAAVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1486 RFvhdPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV----PIhnctaLGAGI 1561
Cdd:cd05969 312 SF---IDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIgkpdPL-----RGEII 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1562 VVTGSGAEQFD--DSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05969 382 KAFISLKEGFEpsDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
36-564 |
3.04e-27 |
|
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: 119.01 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 36 RTVAATGIDDWTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPSTREPQRFlara 114
Cdd:cd05959 20 KTAFIDDAGSLTYAELEAEARRVaGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 115 qhILRDCEPSAVYTCGELVEVLE-----RDPIL-------GALPIRTPASTADGLAPHPGGTTADADHGEHVAFLQYSSG 182
Cdd:cd05959 96 --YLEDSRARVVVVSGELAPVLAaaltkSEHTLvvlivsgGAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 183 STGKPKGVVNTHQSILRQA-AFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIP--PhdfvrNPRIWLE 259
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPerP-----TPAAVFK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 260 TVSRFRGNWIGGPDFAYRRCIEAFDgtaLQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaGLrdDVMapqyglaeAGL 339
Cdd:cd05959 249 RIRRYRPTVFFGVPTLYAAMLAAPN---LPSRDLSSLRLCVSAGEALPAEVGERWKARF---GL--DIL--------DGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 340 GVTgsQTVRVWVekSFDADALERGIAvevAQPNPadgrsralvscgdgafGWDIQIVDPDRHMTlTDGEVGEIWVGGPGL 419
Cdd:cd05959 313 GST--EMLHIFL--SNRPGRVRYGTT---GKPVP----------------GYEVELRDEDGGDV-ADGEPGELYVRGPSS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 420 PDGYWRQPEQTATTFgartadgLGPYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVApggAC 498
Cdd:cd05959 369 ATMYWNNRDKTRDTF-------QGEWTRTGDKYVRdDDGFYTYAGRADDMLKVSGIWVSPFEVE-SALVQHPAVL---EA 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 499 AVQP-------DAPQAngewWLVLETG--SPVEDLDDLSRILRRRILAHHetAPERVVWVPcrTLPTTTSGKIRR 564
Cdd:cd05959 438 AVVGvededglTKPKA----FVVLRPGyeDSEALEEELKEFVKDRLAPYK--YPRWIVFVD--ELPKTATGKIQR 504
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-982 |
3.74e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 122.76 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 9 PALHDGDRSVPAVFAEWVGRRPDAVALrtvaATGIDDWTY-------QRLWDHVREirdvafSGLSAGIRIPMALPGGAD 81
Cdd:PRK12316 504 AAEYPLQRGVHRLFEEQVERTPEAPAL----AFGEETLDYaelnrraNRLAHALIE------RGVGPDVLVGVAMERSIE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 82 YVAGMLAALAAGLIPVPVylpstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLERDPILGALPIRTPASTADGLAPHP 161
Cdd:PRK12316 574 MVVALLAILKAGGAYVPL------DPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEEN 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 162 GGTTAdadHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGGC 241
Cdd:PRK12316 648 PGTEL---NPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGAR 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 TTLIPPHDFvRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLrlatnGAEPVRGTTLRDFTAKFRAA 321
Cdd:PRK12316 724 LVVAAPGDH-RDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVC-----SGEALPADAQEQVFAKLPQA 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 322 GLRDdvmapQYGLAEAGLGVTGSQTVRvwveksfdadalERGIAVEVAQPnPADGRSRALvscgDGAFGwdiqivdpdrh 401
Cdd:PRK12316 798 GLYN-----LYGPTEAAIDVTHWTCVE------------EGGDSVPIGRP-IANLACYIL----DANLE----------- 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 402 mTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTF-GARTADGLGPYlRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPN 479
Cdd:PRK12316 845 -PVPVGVLGELYLAGRGLARGYHGRPGLTAERFvPSPFVAGERMY-RTGDlARYRADGVIEYAGRIDHQVKLRGLRIELG 922
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 480 DIEKTVEEaHCGVAPGGACAVqpDAPQANGewWLVLETGSpvedlDDLSRILRRRILAHhetAPERVV---WVPCRTLPT 556
Cdd:PRK12316 923 EIEARLLE-HPWVREAAVLAV--DGKQLVG--YVVLESEG-----GDWREALKAHLAAS---LPEYMVpaqWLALERLPL 989
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 557 TTSGKIRRRETlnrltagqlevvhevsPRAQAPDTPAAPDDPPTELAQHLAA----MLGVEPYELapDADLTTLGLTSMM 632
Cdd:PRK12316 990 TPNGKLDRKAL----------------PAPEASVAQQGYVAPRNALERTLAAiwqdVLGVERVGL--DDNFFELGGDSIV 1051
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 633 TAQIVEWSSSQSRRLDFADLYAEPTLRSWQRLFDAAPpvQTGTSSVAASGPWPTTPLQQAYWvgrgaEQPLGGVGCQTYF 712
Cdd:PRK12316 1052 SIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQ--ATAADQGPASGEVALAPVQRWFF-----EQAIPQRQHWNQS 1124
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 713 ELVGAR--VDAGRLAAALDALTRRHPMLRATFPDPG---RCLITPEAVRLPLAVHDLTDApvTTRDTHLAEIRRRLrthr 787
Cdd:PRK12316 1125 LLLQARqpLDPDRLGRALERLVAHHDALRLRFREEDggwQQAYAAPQAGEVLWQRQAASE--EELLALCEEAQRSL---- 1198
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 788 fDIETGDTWTVELTRLPHG------CIVHFAVDLIiadvtSIGTMLRDLAASYRG--EKLPAPSATFADLIQSTSPPPQA 859
Cdd:PRK12316 1199 -DLEQGPLLRALLVDMADGsqrlllVIHHLVVDGV-----SWRILLEDLQRAYADldADLPARTSSYQAWARRLHEHAGA 1272
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 860 CADRLP-------EGPQ-LPRVQEADISFLRHQH----TLSALAT-KAIDDACHNHGVTRAAVLLAAYTLVLRRWASQDD 926
Cdd:PRK12316 1273 RAEELDywqaqleDAPHeLPCENPDGALENRHERklelRLDAERTrQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQAS 1352
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 927 FLVNVTTFGRSP-----EVSDVVGDFTETHLYRAQLDGQISfvdqaqVTQKGLRTALRAAP 982
Cdd:PRK12316 1353 VLVQLEGHGREDlfediDLSRTVGWFTSLFPVRLTPAADLG------ESIKAIKEQLRAVP 1407
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1120-1613 |
5.11e-27 |
|
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: 118.88 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1120 ENAATHPARLALRWRPDDYRGERHgdviaqdrsqLTYGELDELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMM 1199
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREET----------LTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1200 AGCTYLPVGVDQP---AERLSRIcARSAMAGLIRTDSDTQDA--------------GVAVSDITAMIECAPTDPIRIDPH 1262
Cdd:cd05931 71 AGAIAVPLPPPTPgrhAERLAAI-LADAGPRVVLTTAAALAAvrafaasrpaagtpRLLVVDLLPDTSAADWPPPSPDPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLlaLSAL----DFDLsVYDTFGALGCGAQLVTIPEHA 1338
Cdd:cd05931 150 DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV--VSWLplyhDMGL-IGGLLTPLYSGGPSVLMSPAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1339 -RRDAFHWLSLTTEFGITvWNSVPGL-MDMLL--IAAGDKAGS-LPTLRSVFLSGDWI-PLDLPRRLRRAAP-GVR---- 1407
Cdd:cd05931 227 fLRRPLRWLRLISRYRAT-ISAAPNFaYDLCVrrVRDEDLEGLdLSSWRVALNGAEPVrPATLRRFAEAFAPfGFRpeaf 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 -----------LVAMGGATE---------AAIWSNEFVVDDVDPDWASIP-YGYPLANQMFRVVDDNGDDQ-PDYVAGEL 1465
Cdd:cd05931 306 rpsyglaeatlFVSGGPPGTgpvvlrvdrDALAGRAVAVAADDPAARELVsCGRPLPDQEVRIVDPETGRElPDGEVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1466 WIGGAGVALGYHNAPELTSDRF--VHDPTGSRWYRTGDMGcYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLV 1543
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFgaLAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1544 -----AAATVVPIHNCTALGAGIVVTGSGAEQFDDSTPGALRAHLAVR--LPQYMIpkVFVSCPELPLTANGKVDRG 1613
Cdd:cd05931 465 lrpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPADV--VLVRPGSIPRTSSGKIQRR 539
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-924 |
1.45e-26 |
|
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: 119.96 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 7 GPPALHDGDRSVPAVFAEWVGRRPDAVALRTVAATgiddWTYQRLWDHV----REIRDvafSGLSAGIRIPMALPGGADY 82
Cdd:COG1020 467 ATAAPYPADATLHELFEAQAARTPDAVAVVFGDQS----LTYAELNARAnrlaHHLRA---LGVGPGDLVGVCLERSLEM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 83 VagmlaalaaglipVPV---------YLP-STREPQrflARAQHILRDCEPSAVYTCGELVEVLerdpilGALPIRTPAS 152
Cdd:COG1020 540 V-------------VALlavlkagaaYVPlDPAYPA---ERLAYMLEDAGARLVLTQSALAARL------PELGVPVLAL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 153 TADGLAPHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGV 232
Cdd:COG1020 598 DALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASV-WEI 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 233 FMPLLNGGCTTLIPPHDfVRNPRIWLETVSRFRgnwiggpdfayrrcIEAFDGT--ALQSL------DLSCLRLATNGAE 304
Cdd:COG1020 677 FGALLSGATLVLAPPEA-RRDPAALAELLARHR--------------VTVLNLTpsLLRALldaapeALPSLRLVLVGGE 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 305 PVRGTTLRDFTAKFRAAGLRDdvmapQYGLAEAGLGVTgsqtvrvwveksfdadalergiAVEVAQPNPADGRS---RAL 381
Cdd:COG1020 742 ALPPELVRRWRARLPGARLVN-----LYGPTETTVDST----------------------YYEVTPPDADGGSVpigRPI 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 382 vscgdgafgWDIQIVDPDRHMTLT-DGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYL-RTGDAGfRYQ--G 457
Cdd:COG1020 795 ---------ANTRVYVLDAHLQPVpVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLyRTGDLA-RWLpdG 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 458 ELYVCGRYRDLIIVGGrnhF---PNDIEkTVEEAHCGVApggACAVQPDAPQANGEWWLVLETGSPVEDLDDLSRILRRR 534
Cdd:COG1020 865 NLEFLGRADDQVKIRG---FrieLGEIE-AALLQHPGVR---EAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALA 937
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 535 ILAHHETAPERVVWVPcrTLPTTTSGKIRRRetlnrltagqlevvHEVSPRAQAPDTPAAPDDPPTELAQHLAAMLGVEP 614
Cdd:COG1020 938 LLLPPYMVPAAVVLLL--PLPLTGNGKLDRL--------------ALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVV 1001
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 615 YELAPDADLTTLGLTSMMTAQIVEWSSSQSRRLDFADLYAEPTLRSWQRLFDAAPPVQTGTSSVAASGPWPTTPLQQAYW 694
Cdd:COG1020 1002 VVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLA 1081
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 695 VGRGAEQPLGGVGCQTYFELVGARVDAGRLAAALDALTRRHPMLRATFPDPGRCLITPEAVRLPLAVHDLTDAPVTTRDT 774
Cdd:COG1020 1082 LLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAA 1161
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 775 HLAEIRRRLRTHRFDIETGDTWTVELTRLPHgciVHFAVDLIIADVTSIGTMLRDLAASYRGEKLPAPSATFADLIQSTS 854
Cdd:COG1020 1162 AAAAELLAAAALLLLLALLLLALLLLLLLLL---LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLL 1238
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 855 PPPQACADRLPEGPQLPRVQEADISFLRHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQ 924
Cdd:COG1020 1239 ALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLA 1308
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
26-566 |
1.63e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 116.96 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 26 VGRRPDAVALRTvaatGIDDWTYQRLWDHV-REIRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPST 104
Cdd:PRK08316 21 ARRYPDKTALVF----GDRSWTYAELDAAVnRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 105 REPQRFlaraqhILRDCEPSAVYTCGELVEVLE------RDPILGALPIRTPASTADGLAP-----HPGGTTADADH--G 171
Cdd:PRK08316 97 GEELAY------ILDHSGARAFLVDPALAPTAEaalallPVDTLILSLVLGGREAPGGWLDfadwaEAGSVAEPDVElaD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQ--AAFAANVWNGDDDmhMVSWLPLYH--DMGIFwgvFMPLLNGGCTTLIPP 247
Cdd:PRK08316 171 DDLAQILYTSGTESLPKGAMLTHRALIAEyvSCIVAGDMSADDI--PLHALPLYHcaQLDVF---LGPYLYVGATNVILD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 248 HDfvrNPRIWLETVSRFRGN--------WIG---GPDFAYRrcieafdgtalqslDLSCLRLATNGAEPVRGTTLRDFTA 316
Cdd:PRK08316 246 AP---DPELILRTIEAERITsffapptvWISllrHPDFDTR--------------DLSSLRKGYYGASIMPVEVLKELRE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 317 KFRAAGLRDdvmapQYGLAEAGLGVTgsqtvrvwveksfdadalergiaveVAQPNPADGRsraLVSCGDGAFGWDIQIV 396
Cdd:PRK08316 309 RLPGLRFYN-----CYGQTEIAPLAT-------------------------VLGPEEHLRR---PGSAGRPVLNVETRVV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 397 DpDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFRY-QGELYVCGRYRDLIIVGGRN 475
Cdd:PRK08316 356 D-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF----RGG---WFHSGDLGVMDeEGYITVVDRKKDMIKTGGEN 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 476 HfpndIEKTVEEA---HCGVAPGGACAVqPDapqangEWWL-------VLETGSPVeDLDDLSRILRRRiLAHHETaPER 545
Cdd:PRK08316 428 V----ASREVEEAlytHPAVAEVAVIGL-PD------PKWIeavtavvVPKAGATV-TEDELIAHCRAR-LAGFKV-PKR 493
|
570 580
....*....|....*....|.
gi 2181016861 546 VVWVPcrTLPTTTSGKIRRRE 566
Cdd:PRK08316 494 VIFVD--ELPRNPSGKILKRE 512
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-1081 |
3.21e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.50 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 8 PPALHDGDRSVPAVFAEWVGRRPDAVALrtvaATGIDDWTYQRLWDHV-REIRDVAFSGLSAGIRIPMALPGGADYVAGM 86
Cdd:PRK12467 1566 THTGYPLARLVHQLIEDQAAATPEAVAL----VFGEQELTYGELNRRAnRLAHRLIALGVGPEVLVGIAVERSLEMVVGL 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 87 LAALAAGLIPVPVYLPSTREpqrflaRAQHILRDCEPSAVYTCGELvevLERDPILGALPIRTPASTADGLAPHPGGTTA 166
Cdd:PRK12467 1642 LAILKAGGAYVPLDPEYPRE------RLAYMIEDSGIELLLTQSHL---QARLPLPDGLRSLVLDQEDDWLEGYSDSNPA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 167 DADHGEHVAFLQYSSGSTGKPKGVVNTHQSILR-----QAAF---AANVWngdddmhmVSWLPLYHDMGIfWGVFMPLLN 238
Cdd:PRK12467 1713 VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNrlcatQEAYqlsAADVV--------LQFTSFAFDVSV-WELFWPLIN 1783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 239 GGCTTLIPPHDFvRNPRIWLETVSRFRGNWIGGPDFAyrrcIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKF 318
Cdd:PRK12467 1784 GARLVIAPPGAH-RDPEQLIQLIERQQVTTLHFVPSM----LQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERL 1858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 319 RAAGLRDdvmapQYGLAEAGLGVTgsqtvrVWVEKSFDadaLERGIAVEVAQPNPadgrsralvscgdgAFGWdiQIVDP 398
Cdd:PRK12467 1859 PDTGLFN-----LYGPTETAVDVT------HWTCRRKD---LEGRDSVPIGQPIA--------------NLST--YILDA 1908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 399 DRHMtLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGRYRDLI-IVGGRn 475
Cdd:PRK12467 1909 SLNP-VPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLyRTGDlARYRADGVIEYLGRIDHQVkIRGFR- 1986
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 476 hfpndIEKTVEEAHCGVAPGGACAVQPDAPQANGEWWL--VLETGSPVEDLDDLSRILRRRILAHHETA-PERVV---WV 549
Cdd:PRK12467 1987 -----IELGEIEARLREQGGVREAVVIAQDGANGKQLVayVVPTDPGLVDDDEAQVALRAILKNHLKASlPEYMVpahLV 2061
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 550 PCRTLPTTTSGKIRRReTLNRLTAGQLEVVHEVspraqapdtpaapddPPTELAQHLAAM----LGVEpyELAPDADLTT 625
Cdd:PRK12467 2062 FLARMPLTPNGKLDRK-ALPAPDASELQQAYVA---------------PQSELEQRLAAIwqdvLGLE--QVGLHDNFFE 2123
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 626 LGLTSMMTAQIVEWSSSQSRRLDFADLYAEPTLRSwqrlFDAAPPVQTGTSSV---AASGPWPTTPLQQAYWVGRGAEQP 702
Cdd:PRK12467 2124 LGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQS----LAAVAQEGDGTVSIdqgPVTGDLPLLPIQQMFFADDIPERH 2199
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 703 LGGvgcQTYFELVGARVDAGRLAAALDALTRRHPMLRATF-PDPGR---CLITPEAVRLPLavhdLTDAPVTTRDT--HL 776
Cdd:PRK12467 2200 HWN---QSVLLEPREALDAELLEAALQALLVHHDALRLGFvQEDGGwsaMHRAPEQERRPL----LWQVVVADKEEleAL 2272
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 777 AEIRRRlrthRFDIETGDTWTVELTRLPHG------CIVHFAVDLIiadvtSIGTMLRDLAASYRGE------KLPAPSA 844
Cdd:PRK12467 2273 CEQAQR----SLDLEEGPLLRAVLATLPDGsqrlllVIHHLVVDGV-----SWRILLEDLQTAYRQLqggqpvKLPAKTS 2343
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 845 TF---ADLIQSTSPPPQACADR------LPEGP-QLPRVQEADISFLRHQ-----HTLSALATKAIDDACHNHGVTRAAV 909
Cdd:PRK12467 2344 AFkawAERLQTYAASAALADELgywqaqLQGAStELPCDHPQGGLQRRHAasvttHLDSEWTRRLLQEAPAAYRTQVNDL 2423
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 910 LLAAYTLVLRRWASQDDFLVNVTTFGR---SPEV--SDVVGDFTEthLY------RAQLDGQISFVDQA--QVTQKGL-- 974
Cdd:PRK12467 2424 LLTALARVIARWTGQASTLIQLEGHGRedlFDEIdlTRTVGWFTS--LYpvklspTASLATSIKTIKEQlrAVPNKGLgf 2501
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 975 -----------RTALRAAPAPDLLATQL-RSGTGHSGIVPVVFTYAADSpllSAEDANTLGAIDEVVSMTPQVlidhqac 1042
Cdd:PRK12467 2502 gvlrylgseaaRQTLQALPVPRITFNYLgQFDGSFDAEKQALFVPSGEF---SGAEQSEEAPLGNWLSINGQV------- 2571
|
1130 1140 1150
....*....|....*....|....*....|....*....
gi 2181016861 1043 rLGDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLERLGGH 1081
Cdd:PRK12467 2572 -YGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEH 2609
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
170-564 |
4.05e-26 |
|
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: 114.48 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 170 HGEHVAFLQYSSGSTGKPKGVVNTHQSILRQA-AFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPH 248
Cdd:cd05919 89 SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 249 dfvRNPRIWLETVSRFRGNWIGGPDFAYRRCIeafDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrddvm 328
Cdd:cd05919 169 ---PTAERVLATLARFRPTVLYGVPTFYANLL---DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF---------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 apqygLAEAGLGVTGSQTVRVWVekSFDADALERGiavevaqpnpadgrsralvSCGDGAFGWDIQIVDPDRHmTLTDGE 408
Cdd:cd05919 233 -----GGPILDGIGATEVGHIFL--SNRPGAWRLG-------------------STGRPVPGYEIRLVDEEGH-TIPPGE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 409 VGEIWVGGPGLPDGYWRQPEQTATTFgartadgLGPYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEE 487
Cdd:cd05919 286 EGDLLVRGPSAAVGYWNNPEKSRATF-------NGGWYRTGDKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQ 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 488 aHCGVAPGGACAVQPDAPQANGEWWLVLETGSPVEDL--DDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSGKIRR 564
Cdd:cd05919 359 -HPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlaRDIHRHLLERLSAH--KVPRRIAFVD--ELPRTATGKLQR 432
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
171-565 |
1.80e-25 |
|
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: 112.79 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSILRqaAFAANVW----NGDDDmhmvsWLpLYHDMGI---FWGVFMPLLNGGcTT 243
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLA--LFAATQRwfgfNEDDV-----WT-LFHSYAFdfsVWEIWGALLHGG-RL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 244 LIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLsclRLATNGAEPVRGTTLRDFTAKFraagl 323
Cdd:cd17643 163 VVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLAL---RYVIFGGEALEAAMLRPWAGRF----- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 324 rdDVMAPQ----YGLAEAglgvtgsqTVRVWVEKsFDADALERGIAVEVAQPNPadgrsralvscgdgafGWDIQIVDPD 399
Cdd:cd17643 235 --GLDRPQlvnmYGITET--------TVHVTFRP-LDAADLPAAAASPIGRPLP----------------GLRVYVLDAD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 400 RHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGP-YLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHF 477
Cdd:cd17643 288 GR-PVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSrMYRTGDlARRLPDGELEYLGRADEQVKIRGFRIE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 478 PNDIEKT------VEEAHCGV---APGG---ACAVQPDAPQAngewwlvletgspvEDLDDLSRILRRRILAHheTAPER 545
Cdd:cd17643 367 LGEIEAAlathpsVRDAAVIVredEPGDtrlVAYVVADDGAA--------------ADIAELRALLKELLPDY--MVPAR 430
|
410 420
....*....|....*....|
gi 2181016861 546 VVWVPcrTLPTTTSGKIRRR 565
Cdd:cd17643 431 YVPLD--ALPLTVNGKLDRA 448
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
2566-2953 |
3.19e-25 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 112.04 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2566 FDRPRFDSAARQLVARHAGLRTTVSPAGT-------DAASSGEVAVVHTAPIEpVVRDHDDVRAAMRD---QIIDLTARP 2635
Cdd:pfam00668 39 LDPERLEKALQELINRHDALRTVFIRQENgepvqviLEERPFELEIIDISDLS-ESEEEEAIEAFIQRdlqSPFDLEKGP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2636 GIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLY----RGETVdQLPPLeTSFAHYVWNHPELLPDADeavlp 2711
Cdd:pfam00668 118 LFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqqllKGEPL-PLPPK-TPYKDYAEWLQQYLQSED----- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2712 rLAASRDYWRARL------PSLPP-APKLADMSLlfeieepRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARV 2784
Cdd:pfam00668 191 -YQKDAAYWLEQLegelpvLQLPKdYARPADRSF-------KGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2785 LSRWSGTDHFCINVTLFDR-DPDvvgIENVVGDFTSLVLLECRVDEPASIWESVRALQRQLMTDLPHRGADAVWLQRELL 2863
Cdd:pfam00668 263 LSRYTGQDDIVVGTPGSGRpSPD---IERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2864 RFHGNPTAALFP--VVFTSGLGL---VDASARAAVRFAEPVFAASQTPQTvLDFQVWESAGALKLSWDFVSQAVSPATAR 2938
Cdd:pfam00668 340 LPRDLSRHPLFDpmFSFQNYLGQdsqEEEFQLSELDLSVSSVIEEEAKYD-LSLTASERGGGLTIKIDYNTSLFDEETIE 418
|
410
....*....|....*
gi 2181016861 2939 TQLESLVDGITGVAT 2953
Cdd:pfam00668 419 RFAEHFKELLEQAIA 433
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1266-1612 |
8.11e-25 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 108.26 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1266 YVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAqlvTIPEHARRDAFHW 1345
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGG---TFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1346 LSLTTEFGITVWNSVPGLMDMLLIAAGDKAgslpTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFV 1425
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALARTLEPES----KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1426 VDDVDPDWAsipyGYPLANQMFRVVDDNGDDQpdyvaGELWIGGAGVALGYHNAPELTSDRfvhdptgsrWYRTGDMGCY 1505
Cdd:cd17633 157 QESRPPNSV----GRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVRGGFSNPDG---------WMSVGDIGYV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1506 WRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALGAGIVVTGSGaeqfDDSTPGALRAHLAV 1585
Cdd:cd17633 219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPD-ARFGEIAVALYSG----DKLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 2181016861 1586 RLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
172-566 |
1.58e-24 |
|
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: 109.35 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDMHMV----SWLplyhdMGIFWGVFMPLLNGGCTTLIP 246
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGlRPDDIHWNiadpGWA-----KGAWSSFFGPWLLGATVFVYE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 247 PHDFVrnPRIWLETVSRFRGNWIGGPDFAYRRCIEAfdgtALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFrAAGLRDD 326
Cdd:cd05972 156 GPRFD--AERILELLERYGVTSFCGPPTAYRMLIKQ----DLSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 327 vmapqYGLAEAGLGVTGSQTVRVwveksfdadalergiavevaQPNpadgrsralvSCGDGAFGWDIQIVDPDRHMtLTD 406
Cdd:cd05972 229 -----YGQTETGLTVGNFPDMPV--------------------KPG----------SMGRPTPGYDVAIIDDDGRE-LPP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 407 GEVGEIWV--GGPGLPDGYWRQPEQTATTFGartadglGPYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEK 483
Cdd:cd05972 273 GEEGDIAIklPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEVES 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 484 TVEEaHCGVAPGGACAVqPD-----APQAngewWLVLETG--SPVEDLDDLSRILRRRILAHheTAPERVVWVPcrTLPT 556
Cdd:cd05972 346 ALLE-HPAVAEAAVVGS-PDpvrgeVVKA----FVVLTSGyePSEELAEELQGHVKKVLAPY--KYPREIEFVE--ELPK 415
|
410
....*....|
gi 2181016861 557 TTSGKIRRRE 566
Cdd:cd05972 416 TISGKIRRVE 425
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1188-1610 |
1.89e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 110.08 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1188 PSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAmAGLIRTDSDTQDAGVAVSDITAMIECAPTDPiRIDPHDAAYV 1267
Cdd:PRK07787 56 LATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG-AQAWLGPAPDDPAGLPHVPVRLHARSWHRYP-EPDPDAPALI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1268 IYTSGSTGEPKGVLVSH---AAALNTIVDVNRRNRIDTHDRLLALsaldFDLS--VYDTFGALGCGAQLVTI--PEHARR 1340
Cdd:PRK07787 134 VYTSGTTGPPKGVVLSRraiAADLDALAEAWQWTADDVLVHGLPL----FHVHglVLGVLGPLRIGNRFVHTgrPTPEAY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1341 DAFHWLSLTTEFGI-TVWNSVPglmdmlliAAGDKAGSLPTLRsVFLSGDwIPLDLPRRLR-RAAPGVRLVAMGGATEAA 1418
Cdd:PRK07787 210 AQALSEGGTLYFGVpTVWSRIA--------ADPEAARALRGAR-LLVSGS-AALPVPVFDRlAALTGHRPVERYGMTETL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1419 IWSNEFVVDDVDPDWAsipyGYPLANQMFRVVDDNGDDQP--DYVAGELWIGGAGVALGYHNAPELTSDRFVHDPtgsrW 1496
Cdd:PRK07787 280 ITLSTRADGERRPGWV----GLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTADG----W 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1497 YRTGDMGCYWRDGTLQFLGRADSQ-VKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALGAGIV--VTGSgaeqfDD 1573
Cdd:PRK07787 352 FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPD-DDLGQRIVayVVGA-----DD 425
|
410 420 430
....*....|....*....|....*....|....*..
gi 2181016861 1574 STPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKV 1610
Cdd:PRK07787 426 VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKV 462
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1177-1551 |
2.45e-24 |
|
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: 110.02 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRIcARSAMAGLIRTDSDT----QDAGVAV---------- 1242
Cdd:cd05904 57 GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQ-VKDSGAKLAFTTAELaeklASLALPVvlldsaefds 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1243 ---SDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSH---AAALNTIVDVnRRNRIDTHDRLLALSAL--DF 1314
Cdd:cd05904 136 lsfSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHrnlIAMVAQFVAG-EGSNSDSEDVFLCVLPMfhIY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1315 DLSVYdTFGALGCGAQLVTIPehaRRDAFHWLSLTTEFGITVWNSVPGLmdMLLIAAGDKAGS--LPTLRSVFLSGDWIP 1392
Cdd:cd05904 215 GLSSF-ALGLLRLGATVVVMP---RFDLEELLAAIERYKVTHLPVVPPI--VLALVKSPIVDKydLSSLRQIMSGAAPLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1393 LDLPRRLRRAAPGVRLVAMGGATEA-AIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVD-DNGDDQPDYVAGELWIGGA 1470
Cdd:cd05904 289 KELIEAFRAKFPNVDLGQGYGMTEStGVVAMCFAPEKDRAKYGSV--GRLVPNVEAKIVDpETGESLPPNQTGELWIRGP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1471 GVALGYHNAPELTSDRFVHDptgsRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVP 1550
Cdd:cd05904 367 SIMKGYLNNPEATAATIDKE----GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIP 442
|
.
gi 2181016861 1551 I 1551
Cdd:cd05904 443 Y 443
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
22-565 |
2.62e-24 |
|
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: 109.74 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 22 FAEWVGRRPDAVALrtvaATGIDDWTYQRLwDHV--REIRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPV 99
Cdd:cd17651 1 FERQAARTPDAPAL----VAEGRRLTYAEL-DRRanRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 100 ylpstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLERDPILGALPIRTPASTADGLAPHPggttadADHGEHVAFLQY 179
Cdd:cd17651 76 ------DPAYPAERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDP------ALDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 180 SSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGiFWGVFMPLLNGGCTTLIPPHdfVRN-PRIWL 258
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVS-VQEIFSTLCAGATLVLPPEE--VRTdPPALA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 259 ETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSClrLATNGAEPVRGTTLRDFTAKFRAAGLRDdvmapQYGLAEAG 338
Cdd:cd17651 221 AWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRY--LLTGGEQLVLTEDLREFCAGLPGLRLHN-----HYGPTETH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 339 LgVTGsqtvrvwveKSFDADALERGIAVEVAQPNPadgrsralvscgdgafGWDIQIVDPDRHmTLTDGEVGEIWVGGPG 418
Cdd:cd17651 294 V-VTA---------LSLPGDPAAWPAPPPIGRPID----------------NTRVYVLDAALR-PVPPGVPGELYIGGAG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 419 LPDGYWRQPEQTATTFGARTADGLGPYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVApGGA 497
Cdd:cd17651 347 LARGYLNRPELTAERFVPDPFVPGARMYRTGDlARWLPDGELEFLGRADDQVKIRGFRIELGEIE-AALARHPGVR-EAV 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 498 CAVQPDAPqanGEWWLV----LETGSPVeDLDDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSGKIRRR 565
Cdd:cd17651 425 VLAREDRP---GEKRLVayvvGDPEAPV-DAAELRAALATHLPEY--MVPSAFVLLD--ALPLTPNGKLDRR 488
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1191-1615 |
2.94e-24 |
|
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: 110.45 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1191 IVAVLGVMMAGCTYLPVGV----DQPAERLSRICARSAMAG--LIRTDSDTQDA-----------GVAVSDITAMIECAP 1253
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVpptyDEPNARLRKLRHIWQLLGspVVLTDAELVAEfagletlsglpGIRVLSIEELLDTAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1254 TDPIRI-DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALD-----FDLSVYDTFgaLGC 1327
Cdd:cd05906 158 DHDLPQsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDhvgglVELHLRAVY--LGC 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1328 gAQLVTIPEHARRDAFHWLSLTTEFGITV-W--NSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRL----- 1399
Cdd:cd05906 236 -QQVHVPTEEILADPLRWLDLIDRYRVTItWapNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLlrlle 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1400 RRAAPGVRLVAMGGATEAA---IWSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGY 1476
Cdd:cd05906 315 PYGLPPDAIRPAFGMTETCsgvIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGY 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1477 HNAPELTSDRFVHDptgsRWYRTGDMGcYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAA--ATVVPIHNC 1554
Cdd:cd05906 395 YNNPEANAEAFTED----GWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDP 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1555 TALGAGIVVTGSGAEQFDDSTPGALRA------HLAVRLPQYMIPkvfVSCPELPLTANGKVDRGKI 1615
Cdd:cd05906 470 GAETEELAIFFVPEYDLQDALSETLRAirsvvsREVGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1255-1615 |
4.92e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 109.70 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1255 DPIRIDPHDAAYVIYTSGSTGEPKGVLVSHA----------AALNTIVDVNRRnridthdrllALSALD----FDLSVYD 1320
Cdd:PRK05605 212 SHPRPTPDDVALILYTSGTTGKPKGAQLTHRnlfanaaqgkAWVPGLGDGPER----------VLAALPmfhaYGLTLCL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1321 TFgALGCGAQLVTIP--------EHARRDAFHWLSlttefgitvwnSVPGLMDMLLIAAGDKAGSLPTLRSVFlSGdwiP 1392
Cdd:PRK05605 282 TL-AVSIGGELVLLPapdidlilDAMKKHPPTWLP-----------GVPPLYEKIAEAAEERGVDLSGVRNAF-SG---A 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1393 LDLPRRLRR---AAPGVRLVAMGGATEAA-IWSNEFVVDDVDPDWASIPYgyPLANqmFRVVD--DNGDDQPDYVAGELW 1466
Cdd:PRK05605 346 MALPVSTVElweKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPF--PDTE--VRIVDpeDPDETMPDGEEGELL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1467 IGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAA 1546
Cdd:PRK05605 422 VRGPQVFKGYWNRPEETAKSFLDG-----WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDA 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 1547 TVVPIHNctALGAGIVVTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:PRK05605 497 AVVGLPR--EDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1261-1615 |
6.67e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 106.21 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1261 PHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdfdlsvYDTFG-------ALGCGAQLVt 1333
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPL------FHCFGsvlgvlaCLTHGATMV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1334 IPEharrDAFHWLS-LTT--EFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVA 1410
Cdd:cd05917 74 FPS----PSFDPLAvLEAieKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1411 MGGATEAA-IWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDY-VAGELWIGGAGVALGYHNAPELTsdRFV 1488
Cdd:cd05917 150 AYGMTETSpVSTQTRTDDSIEKRVNTV--GRIMPHTEAKIVDPEGGIVPPVgVPGELCIRGYSVMKGYWNDPEKT--AEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1489 HDptGSRWYRTGDMGCYWRDGTLQFLGRADSQVkIRG-HRVECGEIEHALRGHPLVAAATVVPIHNCT---ALGAGIVVT 1564
Cdd:cd05917 226 ID--GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERygeEVCAWIRLK 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1565 gSGAEqfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05917 303 -EGAE----LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
13-482 |
8.42e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 109.42 E-value: 8.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 13 DGDRSVPAVFAEWVGRRPDAVALRTVAATGIDDWTYQRLWDHVREIRdVAF--SGLSAGIRI-------P---------M 74
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALA-AGLlaLGVKPGDRVailsdnrPewviadlaiL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 75 ALpgGAdyvagmlaalaaglIPVPVYlPSTREPQrflarAQHILRDCEPSAVYTCGE-----LVEVLERDPIL------- 142
Cdd:COG1022 87 AA--GA--------------VTVPIY-PTSSAEE-----VAYILNDSGAKVLFVEDQeqldkLLEVRDELPSLrhivvld 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 143 -GALPIRTPASTADGLAPHPGGTTADAD--------HGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDD 213
Cdd:COG1022 145 pRGLRDDPRLLSLDELLALGREVADPAElearraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 214 MHMVSWLPLYHDMGIFWGVFMpLLNGGCTTLIP-PHDFVRN------------PRIW----------LETVSRFRGnWIG 270
Cdd:COG1022 225 DRTLSFLPLAHVFERTVSYYA-LAAGATVAFAEsPDTLAEDlrevkptfmlavPRVWekvyagiqakAEEAGGLKR-KLF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 271 gpDFAYRRCIEAFDgTALQSLDLSC------------------------LRLATNGAEPVRGTTLRdFtakFRAAGLRdd 326
Cdd:COG1022 303 --RWALAVGRRYAR-ARLAGKSPSLllrlkhaladklvfsklrealggrLRFAVSGGAALGPELAR-F---FRALGIP-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 327 VMapQ-YGLAEAGLGVTgsqtvrVWVEKSFDADAlergiaveVAQPNPadgrsralvscgdgafGWDIQIvdpdrhmtlt 405
Cdd:COG1022 374 VL--EgYGLTETSPVIT------VNRPGDNRIGT--------VGPPLP----------------GVEVKI---------- 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 406 dGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIV-GGRNHFPNDIE 482
Cdd:COG1022 412 -AEDGEILVRGPNVMKGYYKNPEATAEAF---DADG---WLHTGDIGeLDEDGFLRITGRKKDLIVTsGGKNVAPQPIE 483
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
391-673 |
8.53e-24 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 104.45 E-value: 8.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 391 WDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYLRTGDAGFRYQGELYVCGRYRDLII 470
Cdd:COG3433 20 IPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 471 VGGRNHFPNDIEKTVEEAHCGVAPGGACAVQPDAPQANGEWWLVLETGSPVEDLDDLSRILRRRILAHHETAPERVVWVP 550
Cdd:COG3433 100 ERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 551 CRTLPTTTSGKIRRRETLNRLTAGQLEVVHEVSPRAQAPDTPAapddpptELAQHLAAMLGVEPYELAPDADLTTLGLTS 630
Cdd:COG3433 180 ALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEE-------ELRADVAELLGVDPEEIDPDDNLFDLGLDS 252
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2181016861 631 MMTAQIVEWSSSQSRRLDFADLYAEPTLRSWQRLFDAAPPVQT 673
Cdd:COG3433 253 IRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1177-1612 |
9.80e-24 |
|
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: 107.18 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVG-VDQPAErlsricarsaMAGLIrtdsdtQDAGVAVSDITAMIEcaptd 1255
Cdd:cd05935 26 GDRVGICLQNSPQYVIAYFAIWRANAVVVPINpMLKERE----------LEYIL------NDSGAKVAVVGSELD----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1256 piridphDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdFDLS--VYDTFGALGCGAQLVT 1333
Cdd:cd05935 85 -------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPL-FHVTgfVGSLNTAVYVGGTYVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1334 IpehARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGG 1413
Cdd:cd05935 157 M---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1414 ATEAAIWSNefvvddVDPDWA--SIPYGYPLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHD 1490
Cdd:cd05935 233 LTETMSQTH------TNPPLRpkLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1491 pTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTA---LGAGIVVT-GS 1566
Cdd:cd05935 307 -KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVgeeVKAFIVLRpEY 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2181016861 1567 GAEQFDDSTPGALRAHLAvrlpQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05935 386 RGKVTEEDIIEWAREQMA----AYKYPREVEFVDELPRSASGKILW 427
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1114-1987 |
1.05e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.41 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAATHPARLALRWRPDDyrgerhgdviAQDRSQLTYGELDELARSVARAVAARHAAGSVIGIQLPKGPSQIVA 1193
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADD----------PGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1194 VLGVMMAGCTYLPV-----GVDQPAERLSRICArSAMAGLIRTDSDTQDAGVAVSDITA----------MIECAPTDPIR 1258
Cdd:PRK05691 81 FFGCLYAGVIAVPAyppesARRHHQERLLSIIA-DAEPRLLLTVADLRDSLLQMEELAAanapellcvdTLDPALAEAWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1259 ---IDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSAldfdLSVYDTFGALGCGAQ----- 1330
Cdd:PRK05691 160 epaLQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSW----LPLYHDMGLIGGLLQpifsg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1331 ---LVTIPEHARRDAFHWLSLTTEFGITVwNSVPGLMDMLL---IAAGDKAG-SLPTLRSVFLSGDWIPLDLPRRL--RR 1401
Cdd:PRK05691 236 vpcVLMSPAYFLERPLRWLEAISEYGGTI-SGGPDFAYRLCserVSESALERlDLSRWRVAYSGSEPIRQDSLERFaeKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1402 AAPGVR---LVAMGGATEAAIW----------------SNEFVVDDVDPDWAS--IPYGYPLANQMFRVVDDN-GDDQPD 1459
Cdd:PRK05691 315 AACGFDpdsFFASYGLAEATLFvsggrrgqgipaleldAEALARNRAEPGTGSvlMSCGRSQPGHAVLIVDPQsLEVLGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1460 YVAGELWIGGAGVALGYHNAPELTSDRFV-HDptGSRWYRTGDMGcYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALR 1538
Cdd:PRK05691 395 NRVGEIWASGPSIAHGYWRNPEASAKTFVeHD--GRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1539 GHPLVA-----AATVVPIHNCTALGAGIVVTGSGAEQFD-DSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK05691 472 REVEVVrkgrvAAFAVNHQGEEGIGIAAEISRSVQKILPpQALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1613 ---------GKIAARLEAAARAP-QPLDTSSTLTVVERLVAEVWSDVLGAPITGREDNFFAQGGDSLRATEAVARLTRRG 1682
Cdd:PRK05691 552 sacrlrladGSLDSYALFPALQAvEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDEL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1683 VAGAEVGQLLSHQTLGQFSAAcvLADPASEASESAADVgEPVTPGEGFPLTRLQQ-------------AYTL-GAAGLNG 1748
Cdd:PRK05691 632 GIDLNLRQLFEAPTLAAFSAA--VARQLAGGGAAQAAI-ARLPRGQALPQSLAQNrlwllwqldpqsaAYNIpGGLHLRG 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1749 stcaptyfaVVLAAAPESAgidldrFARVVTRcvdeFAMLRCAL---DADTTQRVQvDAGPVPVHDLDIQDDPD------ 1819
Cdd:PRK05691 709 ---------ELDEAALRAS------FQRLVER----HESLRTRFyerDGVALQRID-AQGEFALQRIDLSDLPEaerear 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1820 --LLLRRMAAAPFDPHSVPVIQCFAPSRSPRHVGLLIS--YLGLDARSLSTVVTTIIAEYQS--QPRPRQVDPTAAVFAR 1893
Cdd:PRK05691 769 aaQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTlhHIVADGWSLNILLDEFSRLYAAacQGQTAELAPLPLGYAD 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1894 FASesaWGENDVDNSVAG-------------PPLLPLH-DQRRDPFERVTFARRSFTIEEQAAATLREHAAHLGVTPTAL 1959
Cdd:PRK05691 849 YGA---WQRQWLAQGEAArqlaywkaqlgdeQPVLELAtDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMV 925
|
970 980
....*....|....*....|....*....
gi 2181016861 1960 VFEAFaHALASIGAGQR-FAVTVPKSYRP 1987
Cdd:PRK05691 926 LLAAF-QALLHRYSGQGdIRIGVPNANRP 953
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
684-1078 |
1.41e-23 |
|
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: 106.52 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 684 WPTTPLQQaywvG---RGAEQPLGGVGC-QTYFELVGaRVDAGRLAAALDALTRRHPMLRATF--PDPGRCL-ITPEAVR 756
Cdd:cd19543 2 YPLSPMQE----GmlfHSLLDPGSGAYVeQMVITLEG-PLDPDRFRAAWQAVVDRHPILRTSFvwEGLGEPLqVVLKDRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 757 LPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRLP---HGCIvhFAVDLIIADVTSIGTMLRDLAAS 833
Cdd:cd19543 77 LPWRELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGddrYRLV--WSFHHILLDGWSLPILLKELFAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 834 YR----GEKLPAPSAT-FADLI-----QSTSPPPQACADRL---PEGPQLPRVQEADIS----FLRHQHTLSALATKAID 896
Cdd:cd19543 155 YAalgeGQPPSLPPVRpYRDYIawlqrQDKEAAEAYWREYLagfEEPTPLPKELPADADgsyePGEVSFELSAELTARLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 897 DACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRSPEVSDV---VGDFTETHLYRAQLDGQISFVDQAQVTQKg 973
Cdd:cd19543 235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQA- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 974 LRTALRA---APAPDLlatQLRSGTGHSGIVP-VVF-TYAADSPLLSAEDANTLGAIDevVSMTPQV-----LIdhqaCR 1043
Cdd:cd19543 314 QQLELREheyVPLYEI---QAWSEGKQALFDHlLVFeNYPVDESLEEEQDEDGLRITD--VSAEEQTnypltVV----AI 384
|
410 420 430
....*....|....*....|....*....|....*
gi 2181016861 1044 LGDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLERL 1078
Cdd:cd19543 385 PGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQV 419
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1114-1612 |
1.65e-23 |
|
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: 107.41 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAATHPARLALRwrpddyrgerhgdviaQDRSQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIV 1192
Cdd:cd05920 17 LGDLLARSAARHPDRIAVV----------------DGDRRLTYRELDRRADRLAAGLRGLgIRPGDRVVVQLPNVAEFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1193 AVLGVMMAGCtyLPVgVDQPAERLSRI---CARSAMAGLIRtdSDTQDAGVAVSDITAMIECAPtdpiridphDAAYVIY 1269
Cdd:cd05920 81 LFFALLRLGA--VPV-LALPSHRRSELsafCAHAEAVAYIV--PDRHAGFDHRALARELAESIP---------EVALFLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1270 TSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLAL--SALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFhwlS 1347
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAF---P 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1348 LTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRrAAPGVRLVAMGGATEAAIwsNEFVVD 1427
Cdd:cd05920 224 LIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVP-PVLGCTLQQVFGMAEGLL--NYTRLD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1428 DvDPDWASIPYGYPL-ANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFvhDPTGsrWYRTGDMGCYW 1506
Cdd:cd05920 301 D-PDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF--TPDG--FYRTGDLVRRT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1507 RDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALG----AGIVVTGSGAEQFddstpgALRAH 1582
Cdd:cd05920 376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPD-ELLGerscAFVVLRDPPPSAA------QLRRF 448
|
490 500 510
....*....|....*....|....*....|.
gi 2181016861 1583 LAVR-LPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05920 449 LRERgLAAYKLPDRIEFVDSLPLTAVGKIDK 479
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
712-1076 |
1.70e-23 |
|
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: 106.29 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 712 FELVGArVDAGRLAAALDALTRRHPMLRATFPDPG---RCLITPEAvRLPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRF 788
Cdd:cd19531 30 LRLRGP-LDVAALERALNELVARHEALRTTFVEVDgepVQVILPPL-PLPLPVVDLSGLPEAEREAEAQRLAREEARRPF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 789 DIETGDTWTVELTRL-PHGCIVHFAVDLIIADVTSIGTMLRDLAASYRGE------KLPAPSATFAD-------LIQSts 854
Cdd:cd19531 108 DLARGPLLRATLLRLgEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlagrpsPLPPLPIQYADyavwqreWLQG-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 855 pppqacaDRL--------------PEGPQLP--RVQEADISFL--RHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTL 916
Cdd:cd19531 186 -------EVLerqlaywreqlagaPPVLELPtdRPRPAVQSFRgaRVRFTLPAELTAALRALARREGATLFMTLLAAFQV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 917 VLRRWASQDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFVDQ-AQVtqkglRTALRAAPA----P-DLLAT 989
Cdd:cd19531 259 LLHRYSGQDDIVVGTPVAGRNrAELEGLIGFFVNTLVLRTDLSGDPTFRELlARV-----RETALEAYAhqdlPfEKLVE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 990 QL---RSgTGHSGIVPVVFTY-AADSPLLSAEDantlgaidevVSMTPqVLIDHQACRL---------GDDVVLSWDYRA 1056
Cdd:cd19531 334 ALqpeRD-LSRSPLFQVMFVLqNAPAAALELPG----------LTVEP-LEVDSGTAKFdltlsltetDGGLRGSLEYNT 401
|
410 420
....*....|....*....|
gi 2181016861 1057 GCFPPGVVDDMFEAYVTLLE 1076
Cdd:cd19531 402 DLFDAATIERMAGHFQTLLE 421
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
171-566 |
1.87e-23 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 107.83 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSI---LRQAAFAANVWNGDDDMHMVSWLPLYHdmgifwgVFMPLLN-------GG 240
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMlanLEQAKAAYGPLLHPGKELVVTALPLYH-------IFALTVNcllfielGG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 241 CTTLIP-PHD---FV----RNPRIWLETVSRFRGNWIGGPDFayrrcieafdgtalQSLDLSCLRLATNGAEPVR---GT 309
Cdd:PRK08974 278 QNLLITnPRDipgFVkelkKYPFTAITGVNTLFNALLNNEEF--------------QELDFSSLKLSVGGGMAVQqavAE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 310 TLRDFTAKFRAAGlrddvmapqYGLAEAGLGVTGSqtvrvwvekSFDADALERGIAVEVaqPNPadgrsralvscgdgaf 389
Cdd:PRK08974 344 RWVKLTGQYLLEG---------YGLTECSPLVSVN---------PYDLDYYSGSIGLPV--PST---------------- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 390 gwDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAG-FRYQGELYVCGRYRDL 468
Cdd:PRK08974 388 --EIKLVDDDGN-EVPPGEPGELWVKGPQVMLGYWQRPEATDEVI----KDG---WLATGDIAvMDEEGFLRIVDRKKDM 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 469 IIVGGRNHFPNDIEKTVeEAHCGVAPGGACAVQPDapqANGEW---WLVLETGSPVEdlDDLSRILRRrilahHETA--- 542
Cdd:PRK08974 458 ILVSGFNVYPNEIEDVV-MLHPKVLEVAAVGVPSE---VSGEAvkiFVVKKDPSLTE--EELITHCRR-----HLTGykv 526
|
410 420
....*....|....*....|....
gi 2181016861 543 PERVVWvpCRTLPTTTSGKIRRRE 566
Cdd:PRK08974 527 PKLVEF--RDELPKSNVGKILRRE 548
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
19-565 |
2.10e-23 |
|
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: 106.98 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 19 PAVFAEWVGRRPDAVALRTVAAT----GIDDWTYqRLWDHVREirdvafSGLSAGIRIPMALPGGADYVAGMLAALAAGL 94
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTltyrELDERAN-RLAHLLRA------RGVGPEDRVAVLLPRSADLVVALLAVLKAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 95 IPVPVylpstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLERDPILGALPirtpastADGLAPHPGGTTADADHGEHV 174
Cdd:cd17646 74 AYLPL------DPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLG-------DEALAAPPATPPLVPPRPDNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGGCtTLIPPHDFVRNP 254
Cdd:cd17646 141 AYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSV-WELFWPLVAGAR-LVVARPGGHRDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 255 RIWLETVSRFRgnwIGGPDFayrrcIEAFDGTALQSLDLSC---LRLATNGAEPVRGTTLRDFTAKFRAAglrddvMAPQ 331
Cdd:cd17646 219 AYLAALIREHG---VTTCHF-----VPSMLRVFLAEPAAGScasLRRVFCSGEALPPELAARFLALPGAE------LHNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 332 YGLAEAGLGVTgsqtvrvwvekSFDADALERGIAVEVAQPNPadgrsralvscgdgafGWDIQIVDPDRHmTLTDGEVGE 411
Cdd:cd17646 285 YGPTEAAIDVT-----------HWPVRGPAETPSVPIGRPVP----------------NTRLYVLDDALR-PVPVGVPGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 412 IWVGGPGLPDGYWRQPEQTATTFgarTADGLGP----YlRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEkTVE 486
Cdd:cd17646 337 LYLGGVQLARGYLGRPALTAERF---VPDPFGPgsrmY-RTGDlARWRPDGALEFLGRSDDQVKIRGFRVEPGEIE-AAL 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 487 EAHCGVApgGACAVQPDAPQANGEW--WLVLETGSPVEDLDDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSGKIRR 564
Cdd:cd17646 412 AAHPAVT--HAVVVARAAPAGAARLvgYVVPAAGAAGPDTAALRAHLAERLPEY--MVPAAFVVLD--ALPLTANGKLDR 485
|
.
gi 2181016861 565 R 565
Cdd:cd17646 486 A 486
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1252-1610 |
3.44e-23 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 107.06 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1252 APTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdfdlsVYDT---FGA---- 1324
Cdd:PRK13295 187 AILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM-----AHQTgfmYGLmmpv 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1325 -LGCGAQLVTIPEHARrdafhWLSLTTEFGIT-VWNSVPGLMDmLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRA 1402
Cdd:PRK13295 262 mLGATAVLQDIWDPAR-----AAELIRTEGVTfTMASTPFLTD-LTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1403 ApGVRLVAMGGATEAAIWSneFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPEL 1482
Cdd:PRK13295 336 L-GAKIVSAWGMTENGAVT--LTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1483 TSDrfvhDPTGsrWYRTGDMGCYWRDGTLQFLGRAdSQVKIRG-HRVECGEIEHALRGHPLVAAATVVPIHNcTALG--- 1558
Cdd:PRK13295 413 NGT----DADG--WFDTGDLARIDADGYIRISGRS-KDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPD-ERLGera 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1559 AGIVVTGSGAE-QFDDSTPGALRAHLAVrlpQYmIPKVFVSCPELPLTANGKV 1610
Cdd:PRK13295 485 CAFVVPRPGQSlDFEEMVEFLKAQKVAK---QY-IPERLVVRDALPRTPSGKI 533
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1263-1611 |
3.54e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 104.39 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSH---------AAALNTIVDVNRRNRID-----THDRLLALSALDFDLSVYDTFGALGCG 1328
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQedifrmlmgGADFGTGEFTPSEDAHKaaaaaAGTVMFPAPPLMHGTGSWTAFGGLLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1329 AQLVTIPEhaRRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGS--LPTLRSVFLSGDWIPLDLPRRLRRAAPGV 1406
Cdd:cd05924 84 QTVVLPDD--RFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPydLSSLFAISSGGALLSPEVKQGLLELVPNI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1407 RLVAMGGATEAAiwSNEFVVDDvdpdwASIPYGYP--LANQMFRVVDDNGDDQPDYVAGELWIGGAG-VALGYHNAPELT 1483
Cdd:cd05924 162 TLVDAFGSSETG--FTGSGHSA-----GSGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1484 SDRFVhDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALGAGIVV 1563
Cdd:cd05924 235 AETFP-EVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPD-ERWGQEVVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2181016861 1564 TGSGAEQFDDSTpGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd05924 313 VVQLREGAGVDL-EELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1263-1612 |
3.84e-23 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 103.50 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSH----AAALNTIVdvnrrnridthdrLLALSALDFDLSVYDTFGALGCGAQLVTIpeHA 1338
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHgnliAANLQLIH-------------AMGLTEADVYLNMLPLFHIAGLNLALATF--HA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1339 --------RRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVflSGdwipLDLP---RRLRRAAPGvR 1407
Cdd:cd17637 66 gganvvmeKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV--LG----LDAPetiQRFEETTGA-T 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 LVAMGGATEAaiwSNEFVVDDVD--PDWAsipyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSD 1485
Cdd:cd17637 139 FWSLYGQTET---SGLVTLSPYRerPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1486 RFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQ--VKIRGHRVECGEIEHALRGHPLVAAATV--VPIhncTALGAGI 1561
Cdd:cd17637 212 TFRNG-----WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVigVPD---PKWGEGI 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 1562 ---VVTGSGAEqfddSTPGALRAHLAVRLPQYMIPK--VFVScpELPLTANGKVDR 1612
Cdd:cd17637 284 kavCVLKPGAT----LTADELIEFVGSRIARYKKPRyvVFVE--ALPKTADGSIDR 333
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
155-566 |
4.00e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 106.77 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 155 DGLAPHPGGTTADAD-HGEHVAFLQYSSGSTGKPKGVVNTHQSILR-----QAAFAANVWNGDDDMhmVSWLPLYHDMGI 228
Cdd:PRK05677 189 DALAKGAGQPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcRALMGSNLNEGCEIL--IAPLPLYHIYAF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 229 FWGVFMPLLNGGCTTLIP-PHD---FVRNPRIWletvsRFRGnWIGGPDFAYRRC-IEAFdgtalQSLDLSCLRLATNGA 303
Cdd:PRK05677 267 TFHCMAMMLIGNHNILISnPRDlpaMVKELGKW-----KFSG-FVGLNTLFVALCnNEAF-----RKLDFSALKLTLSGG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 304 epvrgttlrdftakfraaglrddvMAPQYGLAEAGLGVTGSQTVRVW--VEKSfdadalergiavEVAQPNPADGRSraL 381
Cdd:PRK05677 336 ------------------------MALQLATAERWKEVTGCAICEGYgmTETS------------PVVSVNPSQAIQ--V 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 382 VSCGDGAFGWDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGD-AGFRYQGELY 460
Cdd:PRK05677 378 GTIGIPVPSTLCKVIDDDGN-ELPLGEVGELCVKGPQVMKGYWQRPEATDEIL---DSDG---WLKTGDiALIQEDGYMR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 461 VCGRYRDLIIVGGRNHFPNDIEKTVeEAHCGVAPGGACAVqPDapQANGEWWLVLETGSPVEDLDD--LSRILRRRIlah 538
Cdd:PRK05677 451 IVDRKKDMILVSGFNVYPNELEDVL-AALPGVLQCAAIGV-PD--EKSGEAIKVFVVVKPGETLTKeqVMEHMRANL--- 523
|
410 420
....*....|....*....|....*....
gi 2181016861 539 heTAPERVVWVPCR-TLPTTTSGKIRRRE 566
Cdd:PRK05677 524 --TGYKVPKAVEFRdELPTTNVGKILRRE 550
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1153-1612 |
7.87e-23 |
|
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: 105.28 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1153 QLTYGEL-DELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIRT 1231
Cdd:cd05923 28 RLTYSELrARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1232 DsdtqDAGVAVSDITAMIE-------------CAPTDPIR---IDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVN 1295
Cdd:cd05923 108 V----DAQVMDAIFQSGVRvlalsdlvglgepESAGPLIEdppREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1296 RR--NRIDTHDRLLALSALDFDLSVYDTF-GALGCGAQLVTIPEHARRDAfhwLSLTTEFGITVWNSVPGLMDMLLIAAG 1372
Cdd:cd05923 184 TQagLRHGRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEEFDPADA---LKLIEQERVTSLFATPTHLDALAAAAE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1373 DKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGvRLVAMGGATEAAiwsNEFVVDDVDPDWASIPyGYplaNQMFRVVDD 1452
Cdd:cd05923 261 FAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEAM---NSLYMRDARTGTEMRP-GF---FSEVRIVRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1453 NGDDQ---PDYVAGELWIGGAGVA--LGYHNAPELTSDRFVhdptgSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHR 1527
Cdd:cd05923 333 GGSPDealANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-----DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGEN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1528 VECGEIEHALRGHPLVAAATVVPIHNCTalgAGIVVTGSGAEQFDDSTPGALRAH-LAVRLPQYMIPKVFVSCPELPLTA 1606
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIGVADER---WGQSVTACVVPREGTLSADELDQFcRASELADFKRPRRYFFLDELPKNA 484
|
....*.
gi 2181016861 1607 NGKVDR 1612
Cdd:cd05923 485 MNKVLR 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-1118 |
1.15e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 107.74 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 16 RSVPAVFAEWVGRRPDAVALrtvaATGIDDWTYQRLWDHV-REIRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGL 94
Cdd:PRK12316 3057 RGVHRLFEEQVERTPDAVAL----AFGEQRLSYAELNRRAnRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGG 3132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 95 IPVPVYLPSTREPQRFL---ARAQHILRDCEPSAVYTCGELVEVLERDPilgalpirtpastaDGLAPHPGGTTADadhG 171
Cdd:PRK12316 3133 AYVPLDPEYPEERLAYMledSGAQLLLSQSHLRLPLAQGVQVLDLDRGD--------------ENYAEANPAIRTM---P 3195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDmGIFWGVFMPLLNGGCTTLIPPHDFv 251
Cdd:PRK12316 3196 ENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVLAGPEDW- 3273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 252 RNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTalqslDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLrddvmapq 331
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH-----RCTSLKRIVCGGEALPADLQQQVFAGLPLYNL-------- 3340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 332 YGLAEAGLGVTGSQtvrvwveksfdadalergiAVEVAQPNPADGRSRALVSCGDGAFGWDIQIVdpdrhmtltdGEVGE 411
Cdd:PRK12316 3341 YGPTEATITVTHWQ-------------------CVEEGKDAVPIGRPIANRACYILDGSLEPVPV----------GALGE 3391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 412 IWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHC 490
Cdd:PRK12316 3392 LYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDlARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLE-HP 3470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 491 GVAPGGACAVQPDAPQAngewWLVLETGSPvedldDLSRILRRRIlahHETAPERVV---WVPCRTLPTTTSGKIRRReT 567
Cdd:PRK12316 3471 WVREAVVLAVDGRQLVA----YVVPEDEAG-----DLREALKAHL---KASLPEYMVpahLLFLERMPLTPNGKLDRK-A 3537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 568 LNRLTAGQLEVVHevspraQAPDTPAApddppTELAQHLAAMLGVEpyELAPDADLTTLGLTSMMTAQIVEWSSSQSRRL 647
Cdd:PRK12316 3538 LPRPDAALLQQDY------VAPVNELE-----RRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRARQAGIRF 3604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 648 DFADLYAEPTLRSWQRLFDAAPPVQTGTSSVaaSGPWPTTPLQQAYWVGRGAEQplggvgcQTYFELV----GARVDAGR 723
Cdd:PRK12316 3605 TPKDLFQHQTIQGLARVARVGGGVAVDQGPV--SGETLLLPIQQQFFEEPVPER-------HHWNQSLllkpREALDAAA 3675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 724 LAAALDALTRRHPMLRATF-PDPGRCLITPEAVRLPLAV---HDLTDAPVTTRdthLAEIRRRlrthRFDIETGDTWTVE 799
Cdd:PRK12316 3676 LEAALQALVEHHDALRLRFvEDAGGWTAEHLPVELGGALlwrAELDDAEELER---LGEEAQR----SLDLADGPLLRAL 3748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 800 LTRLPHGC-IVHFAVDLIIADVTSIGTMLRDLAASY----RGE--KLPAPSATFAD--LIQSTSPPPQACADRLP----- 865
Cdd:PRK12316 3749 LATLADGSqRLLLVIHHLVVDGVSWRILLEDLQQAYqqllQGEapRLPAKTSSFKAwaERLQEHARGEALKAELAywqeq 3828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 866 -EG--PQLPRVQEADISFLRHQHTLSA-----LATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRS 937
Cdd:PRK12316 3829 lQGvsSELPCDHPQGALQNRHAASVQTrldreLTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGRE 3908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 938 PEVSDV-----VGDFTETHLYR----AQLDGQISFVDQA--QVTQKGL-------------RTALRAAPAPDLLATQLRS 993
Cdd:PRK12316 3909 DLFADIdlsrtVGWFTSLFPVRlspvEDLGASIKAIKEQlrAIPNKGIgfgllrylgdeesRRTLAGLPVPRITFNYLGQ 3988
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 994 GTGHSGIVPVVFTYAADSpllSAEDANTLGAIDEVVSMTPQVlidhqacrLGDDVVLSWDYRAGCFPPGVVDDMFEAYVT 1073
Cdd:PRK12316 3989 FDGSFDEEMALFVPAGES---AGAEQSPDAPLDNWLSLNGRV--------YGGELSLDWTFSREMFEEATIQRLADDYAA 4057
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*...
gi 2181016861 1074 LLERLGGHDWSTP---ATPGLSAHSRLARAHRNatTTPAPAGLLYDAF 1118
Cdd:PRK12316 4058 ELTALVEHCCDAErhgVTPSDFPLAGLDQARLD--ALPLPLGEIEDIY 4103
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
171-566 |
1.31e-22 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 105.10 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSILR---------QAAFAANvwNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGC 241
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNIVAnvlqmeawlQPAFEKK--PRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 TTLIPphdfvrNPR-I--WLETVSRFRGNWIGGPDFAYRRCIEAFDgtaLQSLDLSCLRLATNGAepvrgttlrdftakf 318
Cdd:PRK07059 281 NILIP------NPRdIpgFIKELKKYQVHIFPAVNTLYNALLNNPD---FDKLDFSKLIVANGGG--------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 319 raaglrddvMAPQYGLAEAGLGVTG---------SQTVRVWVEKSFDADALERGIAVevaqPNPADgrsralvscgdgaf 389
Cdd:PRK07059 337 ---------MAVQRPVAERWLEMTGcpitegyglSETSPVATCNPVDATEFSGTIGL----PLPST-------------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 390 gwDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATtfgARTADGlgpYLRTGDAGF-RYQGELYVCGRYRDL 468
Cdd:PRK07059 390 --EVSIRDDDGN-DLPLGEPGEICIRGPQVMAGYWNRPDETAK---VMTADG---FFRTGDVGVmDERGYTKIVDRKKDM 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 469 IIVGGRNHFPNDIEKTVEEaHCGVAPGGACAVqPDApqangewwlvlETGSPVE------DLDdlsrILRRRILAH-HE- 540
Cdd:PRK07059 461 ILVSGFNVYPNEIEEVVAS-HPGVLEVAAVGV-PDE-----------HSGEAVKlfvvkkDPA----LTEEDVKAFcKEr 523
|
410 420
....*....|....*....|....*...
gi 2181016861 541 -TAPERVVWVPCRT-LPTTTSGKIRRRE 566
Cdd:PRK07059 524 lTNYKRPKFVEFRTeLPKTNVGKILRRE 551
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
172-566 |
1.92e-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: 102.81 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQA-AFAANVWNGDDDmhmvSWL---PLYHDMGIfwGVFMPLLNGGCTTLIPP 247
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAiGSALNLGLTEDD----NWLcalPLFHISGL--SILMRSVIYGMTVYLVD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 248 HdFvrNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTalQSLDLSCLRLatnGAEPVRGTTLRdfTAKfraagLRDDV 327
Cdd:cd05912 151 K-F--DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEG--YPNNLRCILL---GGGPAPKPLLE--QCK-----EKGIP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 328 MAPQYGLAEaglgvTGSQTVRVWVEksfdaDALERgiavevaqpnpadgrsraLVSCGDGAFGWDIQIVDPDRhmtlTDG 407
Cdd:cd05912 216 VYQSYGMTE-----TCSQIVTLSPE-----DALNK------------------IGSAGKPLFPVELKIEDDGQ----PPY 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 408 EVGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGF-RYQGELYVCGRYRDLIIVGGRNHFPNDIEkTVE 486
Cdd:cd05912 264 EVGEILLKGPNVTKGYLNRPDATEESF----ENG---WFKTGDIGYlDEEGFLYVLDRRSDLIISGGENIYPAEIE-EVL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 487 EAHCGVAPGGaCAVQPDApqangEW------WLVLEtgSPVeDLDDLSRILRRRiLAHHETaPERVVWVpcRTLPTTTSG 560
Cdd:cd05912 336 LSHPAIKEAG-VVGIPDD-----KWgqvpvaFVVSE--RPI-SEEELIAYCSEK-LAKYKV-PKKIYFV--DELPRTASG 402
|
....*.
gi 2181016861 561 KIRRRE 566
Cdd:cd05912 403 KLLRHE 408
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
156-577 |
3.23e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 104.31 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 156 GLAPHPGGTTADadhgehVAFLQYSSGSTGKPKGVVNTHQSiLRQAAFAANVW---NGDDDMHMVSWLPLYHDMGIFWGV 232
Cdd:PRK05605 209 SDVSHPRPTPDD------VALILYTSGTTGKPKGAQLTHRN-LFANAAQGKAWvpgLGDGPERVLAALPMFHAYGLTLCL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 233 FMPLLNGGCTTLIPPHDfvrnPRIWLETVSRFRGNWIGGPDFAYRRCIEAfdgTALQSLDLSCLRLATNGAEPVRGTTLR 312
Cdd:PRK05605 282 TLAVSIGGELVLLPAPD----IDLILDAMKKHPPTWLPGVPPLYEKIAEA---AEERGVDLSGVRNAFSGAMALPVSTVE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 313 DFTAkfRAAGLrddvMAPQYGLAEAGLGVTGsqtvrvwveksfdadalergiavevaqpNPADGRSRAlvscgdGAFG-- 390
Cdd:PRK05605 355 LWEK--LTGGL----LVEGYGLTETSPIIVG----------------------------NPMSDDRRP------GYVGvp 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 391 ---WDIQIVDPDR-HMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartadgLGPYLRTGDAGFRYQ-GELYVCGRY 465
Cdd:PRK05605 395 fpdTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-------LDGWFRTGDVVVMEEdGFIRIVDRI 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 466 RDLIIVGGRNHFPNDIEKTVEEaHCGVAPGGACAVQPDAPQANGEWWLVLETGSPVeDLDDLSRILRRRILAHheTAPER 545
Cdd:PRK05605 468 KELIITGGFNVYPAEVEEVLRE-HPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAL-DPEGLRAYCREHLTRY--KVPRR 543
|
410 420 430
....*....|....*....|....*....|..
gi 2181016861 546 VVWVpcRTLPTTTSGKIRRRETLNRLTAGQLE 577
Cdd:PRK05605 544 FYHV--DELPRDQLGKVRRREVREELLEKLGA 573
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1260-1611 |
4.09e-22 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 103.18 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALsaldfdLSVYDTFGALGCG--AQLVTI--- 1334
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGA------LPFFHSFGLTGCLwlPLLSGIkvv 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1335 ----PEHARRDAfhwlSLTTEFGITVWNSVPGLMDMLLIAAgdKAGSLPTLRSVFLSGDwiplDLPRRLRRAAP---GVR 1407
Cdd:cd05909 219 fhpnPLDYKKIP----ELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAE----KLKDTLRQEFQekfGIR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 LVAMGGATEAA-IWSnefvVDDVDPDWASIPYGYPLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSD 1485
Cdd:cd05909 289 ILEGYGTTECSpVIS----VNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1486 RFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTALGAGIVV-- 1563
Cdd:cd05909 365 AFGDG-----WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGEKIVLlt 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2181016861 1564 TGSgaeqfdDSTPGALRAHL-AVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd05909 440 TTT------DTDPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
174-564 |
4.41e-22 |
|
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: 100.27 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTH-QSILRQAAFAANVWNGDDDMHMVSwLPLYHDMGIFWGVFMPLLNGgcTTLIPPHDFvr 252
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCADLTEDDRYLII-NPFFHTFGYKAGIVACLLTG--ATVVPVAVF-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 NPRIWLETVSRFRGNWIGGPDFAYRRCIeafDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKfraagLRDDVMAPQY 332
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLL---DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSE-----LGFETVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 333 GLAEAGLGvtgsqtvrvwveksfdadALERgiavevaqpnPADGRSRALVSCGDGAFGWDIQIVDPdrhmtltdgevGEI 412
Cdd:cd17638 149 GLTEAGVA------------------TMCR----------PGDDAETVATTCGRACPGFEVRIADD-----------GEV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 413 WVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCG 491
Cdd:cd17638 190 LVRGYNVMQGYLDDPEATAEAI---DADG---WLHTGDVGeLDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAE-HPG 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 492 VAPGGACAVQPDAPQANGEWWLVLETGSPVeDLDDLSRILRRRiLAHHETaPERVVWVpcRTLPTTTSGKIRR 564
Cdd:cd17638 263 VAQVAVIGVPDERMGEVGKAFVVARPGVTL-TEEDVIAWCRER-LANYKV-PRFVRFL--DELPRNASGKVMK 330
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
115-469 |
5.88e-22 |
|
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: 102.70 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 115 QHILRDCEPSAVYTCGELVEVLER--DPI--LGALPIRTPASTADGLAPHPGGTTADADHGEHVAFLQYSSGSTGKPKGV 190
Cdd:cd05904 97 AKQVKDSGAKLAFTTAELAEKLASlaLPVvlLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 191 VNTHQSILRQAAFAANVWNGDDDMHMV--SWLPLYHDMGiFWGVFMPLLNGGCTTLIPPhDFvrNPRIWLETVSRFR--G 266
Cdd:cd05904 177 MLTHRNLIAMVAQFVAGEGSNSDSEDVflCVLPMFHIYG-LSSFALGLLRLGATVVVMP-RF--DLEELLAAIERYKvtH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 267 NWIGGPDFayrrcIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAPQ-YGLAEAGLGVTgsq 345
Cdd:cd05904 253 LPVVPPIV-----LALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKF------PNVDLGQgYGMTESTGVVA--- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 346 tvrvwveksfdadalergiavevAQPNPADGRSRAlVSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWR 425
Cdd:cd05904 319 -----------------------MCFAPEKDRAKY-GSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLN 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2181016861 426 QPEQTATTFgarTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLI 469
Cdd:cd05904 375 NPEATAATI---DKEG---WLHTGDLCyIDEDGYLFIVDRLKELI 413
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1153-1613 |
1.18e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 102.43 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1153 QLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVG----------------------V 1209
Cdd:PRK06178 58 VITYAELDELSDRFAALLRQRgVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSplfrehelsyelndagaevllaL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1210 DQPAERLSRICARSAMAGLIRTD-SDT-------------QDAGVAVSDITAMIECAPTDPIRI-----DPHDAAYVIYT 1270
Cdd:PRK06178 138 DQLAPVVEQVRAETSLRHVIVTSlADVlpaeptlplpdslRAPRLAAAGAIDLLPALRACTAPVplpppALDALAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1271 SGSTGEPKGVLVSHA-----AALNTIVDVnrrnRIDTHDRLLALSAL------DFDLsVYDTFgalgCGAQLVTIpehAR 1339
Cdd:PRK06178 218 GGTTGMPKGCEHTQRdmvytAAAAYAVAV----VGGEDSVFLSFLPEfwiageNFGL-LFPLF----SGATLVLL---AR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1340 RDAFHWLSLTTEFGIT----VWNSVPGLMDMLLIAAGDkagsLPTLRSVFLSGDWIPL--DLPRRLRRAAPGVRLVAMGG 1413
Cdd:PRK06178 286 WDAVAFMAAVERYRVTrtvmLVDNAVELMDHPRFAEYD----LSSLRQVRVVSFVKKLnpDYRQRWRALTGSVLAEAAWG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1414 ATE---AAIWSNEFVVDDVDPDWASIPYGYPLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVH 1489
Cdd:PRK06178 362 MTEthtCDTFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1490 DptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV--PIHNCTALGAGIVVTGSG 1567
Cdd:PRK06178 442 G-----WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVgrPDPDKGQVPVAFVQLKPG 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2181016861 1568 AEQfddsTPGALRAHLAVRLPQYMIPKVFVsCPELPLTANGKVDRG 1613
Cdd:PRK06178 517 ADL----TAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQ 557
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
174-565 |
2.02e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 101.65 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILRQAAFAAN-VWNGDDDMHMV-SWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDFv 251
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEGEEVVlGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDM- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 252 rnpRIWLETVSRFRGNWIGGPDFAYrrcIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTakfRAAGLRddvMAPQ 331
Cdd:PRK06710 287 ---KMVFEAIKKHKVTLFPGAPTIY---IALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFE---TVTGGK---LVEG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 332 YGLAEAGlGVTGSQTVrvWveksfdadalERGIAVEVAQPNPADgrsralvscgdgafgwDIQIVDPDRHMTLTDGEVGE 411
Cdd:PRK06710 355 YGLTESS-PVTHSNFL--W----------EKRVPGSIGVPWPDT----------------EAMIMSLETGEALPPGEIGE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 412 IWVGGPGLPDGYWRQPEQTAttfgARTADGlgpYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHC 490
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETA----AVLQDG---WLHTGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE-HE 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 491 GVAPGGACAVqPDAPQANG-EWWLVLETGSPVEDlDDLSRILRRRILAHheTAPErvVWVPCRTLPTTTSGKIRRR 565
Cdd:PRK06710 478 KVQEVVTIGV-PDPYRGETvKAFVVLKEGTECSE-EELNQFARKYLAAY--KVPK--VYEFRDELPKTTVGKILRR 547
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1116-1612 |
2.71e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 100.62 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1116 DAFRENAATHPARLALrwrpddyrgerhgdvIAQDRsQLTYGELDELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVL 1195
Cdd:PRK07638 5 KEYKKHASLQPNKIAI---------------KENDR-VLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIEFLQLFA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1196 GVMMAGCTYLPVGVD-QPAERLSRIcARSAmAGLIRTD-------SDTQDAGVAVSDITAMIECAPTDPIRID--PHDAA 1265
Cdd:PRK07638 69 GAAMAGWTCVPLDIKwKQDELKERL-AISN-ADMIVTEryklndlPDEEGRVIEIDEWKRMIEKYLPTYAPIEnvQNAPF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1266 YVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHW 1345
Cdd:PRK07638 147 YMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRKFIPNQVLDK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1346 LSltTEfGITVWNSVPGLMDMLLiaagdKAGSLP-TLRSVFLSG-DWiPLDLPRRLRRAAPGVRLVAMGGATEAAiwsne 1423
Cdd:PRK07638 227 LE--TE-NISVMYTVPTMLESLY-----KENRVIeNKMKIISSGaKW-EAEAKEKIKNIFPYAKLYEFYGASELS----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1424 FVVDDVDPDWASIPY--GYPLANQMFRVVDDNGDD-QPDYVaGELWIGGAGVALGYHNapeltSDRFVHDPTGSRWYRTG 1500
Cdd:PRK07638 293 FVTALVDEESERRPNsvGRPFHNVQVRICNEAGEEvQKGEI-GTVYVKSPQFFMGYII-----GGVLARELNADGWMTVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1501 DMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI-HNCTALGAGIVVTGSGAEQfddstpgAL 1579
Cdd:PRK07638 367 DVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVpDSYWGEKPVAIIKGSATKQ-------QL 439
|
490 500 510
....*....|....*....|....*....|...
gi 2181016861 1580 RAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK07638 440 KSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
47-564 |
3.21e-21 |
|
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: 99.76 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 47 TYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVyLPSTREPQrflarAQHILRDCEPSA 125
Cdd:cd05903 3 TYSELDTRADRLaAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI-LPFFREHE-----LAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 126 VYTCGELvevlerdpilgalpirtpastadglaphpgGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQA-AFA 204
Cdd:cd05903 77 FVVPERF------------------------------RQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIrQYA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 205 ANVWNGDDDMHMVSwLPLYHDMGIFWGVFMPLLNGGCTTLipphDFVRNPRIWLETVSRFRGNWIGG-PDFAYRRC-IEA 282
Cdd:cd05903 127 ERLGLGPGDVFLVA-SPMAHQTGFVYGFTLPLLLGAPVVL----QDIWDPDKALALMREHGVTFMMGaTPFLTDLLnAVE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 283 FDGTalqslDLSCLRLATNGAEPVRGTTLRdftakfRAAGLRDDVMAPQYGLAEAGlGVTGSQTvrvwveksfDADALER 362
Cdd:cd05903 202 EAGE-----PLSRLRTFVCGGATVPRSLAR------RAAELLGAKVCSAYGSTECP-GAVTSIT---------PAPEDRR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 363 GIavevaqpnpADGRSRAlvscgdgafGWDIQIVDpDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGl 442
Cdd:cd05903 261 LY---------TDGRPLP---------GVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA----PEG- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 443 gpYLRTGDAGFRYQ-GELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVAPggACAV-QPDApqANGE---WWLVLET 517
Cdd:cd05903 317 --WFRTGDLARLDEdGYLRITGRSKDIIIRGGENIPVLEVEDLLLG-HPGVIE--AAVVaLPDE--RLGEracAVVVTKS 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2181016861 518 GSPVeDLDDLSRILRRRILAHHETaPERVVWVPcrTLPTTTSGKIRR 564
Cdd:cd05903 390 GALL-TFDELVAYLDRQGVAKQYW-PERLVHVD--DLPRTPSGKVQK 432
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
14-573 |
3.25e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 100.98 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 14 GDRSVPAVFAEWVGRRPDAVALrtvaatgIDD----WTYQRLwDHVREIrdVAFSGLSAGI----RIPMALPGGADYVAG 85
Cdd:PRK06087 21 GDASLADYWQQTARAMPDKIAV-------VDNhgasYTYSAL-DHAASR--LANWLLAKGIepgdRVAFQLPGWCEFTII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 86 MLAALAAGLIPVPVyLPSTREpqrflARAQHILRDCEpSAVYTCGELVEvlERDPILGALPIR---------------TP 150
Cdd:PRK06087 91 YLACLKVGAVSVPL-LPSWRE-----AELVWVLNKCQ-AKMFFAPTLFK--QTRPVDLILPLQnqlpqlqqivgvdklAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 151 ASTADGLAP----HPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSIL-RQAAFAANV-WNGDDDMHMVSwlPLYH 224
Cdd:PRK06087 162 ATSSLSLSQiiadYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILaSERAYCARLnLTWQDVFMMPA--PLGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 225 DMGIFWGVFMPLLNGGCTTLIppHDFvrNPRIWLETVSRFRGNW-IGGPDFAYR--RCIEAfdgtalQSLDLSCLRLATN 301
Cdd:PRK06087 240 ATGFLHGVTAPFLIGARSVLL--DIF--TPDACLALLEQQRCTCmLGATPFIYDllNLLEK------QPADLSALRFFLC 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 302 GAEPVRGTTLRDftakfraaglrddvmAPQYG--LAEaglgVTGSQTvrvwveksfdadalergiAVEVAQPNPADGRSR 379
Cdd:PRK06087 310 GGTTIPKKVARE---------------CQQRGikLLS----VYGSTE------------------SSPHAVVNLDDPLSR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 380 ALVSCGDGAFGWDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTattfgARTADGLGPYLrTGDAGFR-YQGE 458
Cdd:PRK06087 353 FMHTDGYAAAGVEIKVVDEARK-TLPPGCEGEEASRGPNVFMGYLDEPELT-----ARALDEEGWYY-SGDLCRMdEAGY 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 459 LYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVapGGACAV-QPDapQANGE---WWLVLETGSPVEDLDDLSRILRRR 534
Cdd:PRK06087 426 IKITGRKKDIIVRGGENISSREVEDILLQ-HPKI--HDACVVaMPD--ERLGErscAYVVLKAPHHSLTLEEVVAFFSRK 500
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2181016861 535 ILAHHETaPERVVWVpcRTLPTTTSGKIR----RRETLNRLTA 573
Cdd:PRK06087 501 RVAKYKY-PEHIVVI--DKLPRTASGKIQkfllRKDIMRRLTQ 540
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1149-1562 |
3.55e-21 |
|
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: 99.74 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1149 QDRSQLTYGEL-DELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAG 1227
Cdd:cd17640 1 KPPKRITYKDLyQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1228 LIrtdsdtqdagvavsditamiecaptdpIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNrrNRIDTH--DR 1305
Cdd:cd17640 81 LV---------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLS--DIVPPQpgDR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1306 LLALSAL--DFDLSVYDTFGALGCgAQLVTIPEHARRDafhwlslTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRS 1383
Cdd:cd17640 132 FLSILPIwhSYERSAEYFIFACGC-SQAYTSIRTLKDD-------LKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1384 ----VFLSGDWIPL------DLPRRLRR--AAPGVRLVAMGGATEAA-------IWSNefVVDDVdpdwasipyGYPLAN 1444
Cdd:cd17640 204 flflFFLSGGIFKFgisgggALPPHVDTffEAIGIEVLNGYGLTETSpvvsarrLKCN--VRGSV---------GRPLPG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1445 QMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDrfVHDPTGsrWYRTGDMGCYWRDGTLQFLGRA-DSQVK 1522
Cdd:cd17640 273 TEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK--VLDSDG--WFNTGDLGWLTCGGELVLTGRAkDTIVL 348
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2181016861 1523 IRGHRVECGEIEHALRGHPLVAAATVVPiHNCTALGAGIV 1562
Cdd:cd17640 349 SNGENVEPQPIEEALMRSPFIEQIMVVG-QDQKRLGALIV 387
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1082-1610 |
3.60e-21 |
|
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: 101.11 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1082 DWSTPATPG----LSAHSRLARAHRNATTTpapagLLYDAFRENAATHPARLALRWRPDDYRGERHgdviaqdrsqLTYG 1157
Cdd:cd17634 24 DWITPYQKVkntsFAPGAPSIKWFEDATLN-----LAANALDRHLRENGDRTAIIYEGDDTSQSRT----------ISYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1158 EL-DELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPV-GVDQPAERLSRICARSAM---------- 1225
Cdd:cd17634 89 ELhREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfGGFAPEAVAGRIIDSSSRllitadggvr 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1226 AG-------------------------LIRTDSDTQDAGVAVSDITAMIECAPT--DPIRIDPHDAAYVIYTSGSTGEPK 1278
Cdd:cd17634 169 AGrsvplkknvddalnpnvtsvehvivLKRTGSDIDWQEGRDLWWRDLIAKASPehQPEAMNAEDPLFILYTSGTTGKPK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1279 GVLVSHAAALnTIVDVNRRNRIDTHDRLLALSALDFDLSV---YDTFGALGCGAQLVT---IPEHARRDAFhWlSLTTEF 1352
Cdd:cd17634 249 GVLHTTGGYL-VYAATTMKYVFDYGPGDIYWCTADVGWVTghsYLLYGPLACGATTLLyegVPNWPTPARM-W-QVVDKH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1353 GITVWNSVPGLMDMLLiAAGDKA---GSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVR--LVAMGGATEA--AIWSNEFV 1425
Cdd:cd17634 326 GVNILYTAPTAIRALM-AAGDDAiegTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETggFMITPLPG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1426 VDDVDPDWASIPY-GYPLAnqmfrVVDDNGDDQPDYVAGEL-----WIGGAGVALGYHNAPELTSDRfvhdpTGSRWYRT 1499
Cdd:cd17634 405 AIELKAGSATRPVfGVQPA-----VVDNEGHPQPGGTEGNLvitdpWPGQTRTLFGDHERFEQTYFS-----TFKGMYFS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1500 GDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTALGA--GIVVTGSGAEQfDDSTPG 1577
Cdd:cd17634 475 GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQApyAYVVLNHGVEP-SPELYA 553
|
570 580 590
....*....|....*....|....*....|...
gi 2181016861 1578 ALRAHLAVRLPQYMIPKVFVSCPELPLTANGKV 1610
Cdd:cd17634 554 ELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-571 |
4.71e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 100.50 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 5 TPGPPALHDGDRSVPAVFAEWVGRRPDAVAL----RTVAATGIDDWTyQRLWDHVREIrdvafsGLSAGIRIPMALPGGA 80
Cdd:PRK06178 22 IPREPEYPHGERPLTEYLRAWARERPQRPAIifygHVITYAELDELS-DRFAALLRQR------GVGAGDRVAVFLPNCP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 81 DYVAGMLAALAAGLIPVPVYlPSTREpqrflARAQHILRDCEPSAVYTCGELVEVLErdPILGALPIRTPAST--ADGLA 158
Cdd:PRK06178 95 QFHIVFFGILKLGAVHVPVS-PLFRE-----HELSYELNDAGAEVLLALDQLAPVVE--QVRAETSLRHVIVTslADVLP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 159 PHP--------------------------GGTTADADHG---EHVAFLQYSSGSTGKPKGVVNTHQSILRQAA-FAANVW 208
Cdd:PRK06178 167 AEPtlplpdslraprlaaagaidllpalrACTAPVPLPPpalDALAALNYTGGTTGMPKGCEHTQRDMVYTAAaAYAVAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 209 NGDDDMHMVSWLPlyhdmgIFW------GVFMPLLNGGCTTLIPPHDfvrnPRIWLETVSRFRGNWIGGP-DFAyrrcIE 281
Cdd:PRK06178 247 VGGEDSVFLSFLP------EFWiagenfGLLFPLFSGATLVLLARWD----AVAFMAAVERYRVTRTVMLvDNA----VE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 282 AFDGTALQSLDLSCLRlATNGAEPVRGTTlRDFTAKFRAagLRDDVmapqygLAEAGLGVTGSQTvrvwveksfdADALE 361
Cdd:PRK06178 313 LMDHPRFAEYDLSSLR-QVRVVSFVKKLN-PDYRQRWRA--LTGSV------LAEAAWGMTETHT----------CDTFT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 362 RGIavevaQPNPADGRSRAlVSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADG 441
Cdd:PRK06178 373 AGF-----QDDDFDLLSQP-VFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL----RDG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 442 lgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVApggACAVQPDAPQANGE---WWLVLET 517
Cdd:PRK06178 443 ---WLHTGDIGkIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQ-HPAVL---GSAVVGRPDPDKGQvpvAFVQLKP 515
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 518 GSPVeDLDDLSRILRRRILAHheTAPE-RVVwvpcRTLPTTTSGKIRRRETLNRL 571
Cdd:PRK06178 516 GADL-TAAALQAWCRENMAVY--KVPEiRIV----DALPMTATGKVRKQDLQALA 563
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
47-565 |
5.02e-21 |
|
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: 99.09 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 47 TYQRLWDHVREIRD-VAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVylpstrEPQRFLARAQHILRDCEPSA 125
Cdd:cd05935 3 TYLELLEVVKKLASfLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPI------NPMLKERELEYILNDSGAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 126 VYTCGELvevlerdpilgalpirtpastadglaphpggttadadhgEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAA 205
Cdd:cd05935 77 AVVGSEL---------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 206 NVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDfvrnPRIWLETVSRFRGN-WIGGPDFAyrrcIEAFD 284
Cdd:cd05935 118 VWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWD----RETALELIEKYKVTfWTNIPTML----VDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 285 GTALQSLDLSCLRLATNGAEPVR---GTTLRDFTAKFRAAGlrddvmapqYGLAEaglgvTGSQTvrvwveksfdadale 361
Cdd:cd05935 190 TPEFKTRDLSSLKVLTGGGAPMPpavAEKLLKLTGLRFVEG---------YGLTE-----TMSQT--------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 362 rgiavevaQPNPAdGRSRaLVSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADG 441
Cdd:cd05935 241 --------HTNPP-LRPK-LQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESF---IEIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 442 LGPYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEKTVeeaHCGVAPGGACAV-QPDapQANGE---WWLVLE 516
Cdd:cd05935 308 GRRFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL---YKHPAI*EVCVIsVPD--ERVGEevkAFIVLR 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2181016861 517 TGSPVE-DLDDLSRILRRRILAHHetAPERVVWVpcRTLPTTTSGKIRRR 565
Cdd:cd05935 383 PEYRGKvTEEDIIEWAREQMAAYK--YPREVEFV--DELPRSASGKILWR 428
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
20-565 |
5.07e-21 |
|
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: 99.58 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 20 AVFAEWVGRRPDAVALRTvaatGIDDWTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVP 98
Cdd:cd12117 1 ELFEEQAARTPDAVAVVY----GDRSLTYAELNERANRLaRRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 99 VylpstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLERDpilgalpiRTPASTADGLAPHPGGTTADADHGEHVAFLQ 178
Cdd:cd12117 77 L------DPELPAERLAFMLADAGAKVLLTDRSLAGRAGGL--------EVAVVIDEALDAGPAGNPAVPVSPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 179 YSSGSTGKPKGVVNTHQSILRqaaFAANVWNGDDDMHMVSWL--PLYHDMGIF--WGvfmPLLNGGCTTLIPPH------ 248
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR---LVKNTNYVTLGPDDRVLQtsPLAFDASTFeiWG---ALLNGARLVLAPKGtlldpd 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 249 ---DFVRNPRI---WL-------------ETVSRFRGNWIGG---PDFAYRRCIEAFDGTALqsldlsclrlaTNGAEPV 306
Cdd:cd12117 217 algALIAEEGVtvlWLtaalfnqladedpECFAGLRELLTGGevvSPPHVRRVLAACPGLRL-----------VNGYGPT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 307 RGTTlrdFTAKFRAAGLRDdvmapqyglaeaglgvtgsqtvrvwveksfDADALERGIAVevaqpnpadGRSRALVSCGD 386
Cdd:cd12117 286 ENTT---FTTSHVVTELDE------------------------------VAGSIPIGRPI---------ANTRVYVLDED 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 387 GafgwdiQIVDPdrhmtltdGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYLRTGD-AGFRYQGELYVCGRY 465
Cdd:cd12117 324 G------RPVPP--------GVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDlARWLPDGRLEFLGRI 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 466 RDLIIVGGRNHFPNDIEKTVeEAHCGVApggACAVQPDaPQANGEWWLV-LETGSPVEDLDDLSRILRRRIlahhetaPE 544
Cdd:cd12117 390 DDQVKIRGFRIELGEIEAAL-RAHPGVR---EAVVVVR-EDAGGDKRLVaYVVAEGALDAAELRAFLRERL-------PA 457
|
570 580
....*....|....*....|....
gi 2181016861 545 RVV---WVPCRTLPTTTSGKIRRR 565
Cdd:cd12117 458 YMVpaaFVVLDELPLTANGKVDRR 481
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1263-1612 |
6.29e-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: 96.95 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAA-LNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHARRD 1341
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1342 AFhwLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWiPLDLPRRLRRAAPGVRLVAMGGATEaaiwS 1421
Cdd:cd17635 82 SL--FKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR-AIAADVRFIEATGLTNTAQVYGLSE----T 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1422 NEFVVDDVDPDWASI-PYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTG 1500
Cdd:cd17635 155 GTALCLPTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-----WVNTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1501 DMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALGAGIVVTGSGAEQFDDSTPGALR 1580
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISD-EEFGELVGLAVVASAELDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|..
gi 2181016861 1581 AHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
30-565 |
6.48e-21 |
|
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: 99.29 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 30 PDAVALRTVAATgiddWTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVylpstrEPQ 108
Cdd:cd12116 1 PDATAVRDDDRS----LSYAELDERANRLaARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPL------DPD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 109 RFLARAQHILRDCEPSAVYTCGELVEVLERDpiLGALPIRTPASTADGLAPHPggttadADHGEHVAFLQYSSGSTGKPK 188
Cdd:cd12116 71 YPADRLRYILEDAEPALVLTDDALPDRLPAG--LPVLLLALAAAAAAPAAPRT------PVSPDDLAYVIYTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 189 GVVNTHQSILRQ-AAFAANVWNGDDDmHMVSWLPLYHDMGIFwGVFMPLLNGGcTTLIPPHDFVRNPRIWLETVSRFRGN 267
Cdd:cd12116 143 GVVVSHRNLVNFlHSMRERLGLGPGD-RLLAVTTYAFDISLL-ELLLPLLAGA-RVVIAPRETQRDPEALARLIEAHSIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 268 WI-GGPdfAYRRCIEAFDGTALQSLDLSClrlatnGAEPVRGTTLRDFTAKFRAAglrddvmAPQYGLAEAglgvtgsqt 346
Cdd:cd12116 220 VMqATP--ATWRMLLDAGWQGRAGLTALC------GGEALPPDLAARLLSRVGSL-------WNLYGPTET--------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 347 vRVWveksfdADALErgiaVEVAQPNPADGRSRAlvscgdgafGWDIQIVDPDRhMTLTDGEVGEIWVGGPGLPDGYWRQ 426
Cdd:cd12116 276 -TIW------STAAR----VTAAAGPIPIGRPLA---------NTQVYVLDAAL-RPVPPGVPGELYIGGDGVAQGYLGR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 427 PEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVAPgGACAVQPDA 504
Cdd:cd12116 335 PALTAERFVPDPFAGPGSRLyRTGDlVRRRADGRLEYLGRADGQVKIRGHRIELGEIE-AALAAHPGVAQ-AAVVVREDG 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 505 PQANGEWWLVLETGSPVeDLDDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSGKIRRR 565
Cdd:cd12116 413 GDRRLVAYVVLKAGAAP-DAAALRAHLRATLPAY--MVPSAFVRLD--ALPLTANGKLDRK 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2421-2946 |
8.03e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.57 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2421 DGRWSRPAVPAsslpTDATVVA------------TLAEIWQRHLAIPTPGVDDDFFLLGGDSLVATRVYADLRAAGFgQL 2488
Cdd:PRK12316 992 NGKLDRKALPA----PEASVAQqgyvaprnalerTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGI-QL 1066
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2489 AFVDLFNHSTLGELAAHAgpRTGPEVSVAAESTRGgthdpnRFPLTVVQnayragregalilggvaaHCYFEFELAD--- 2565
Cdd:PRK12316 1067 SPRDLFQHQTIRSLALVA--KAGQATAADQGPASG------EVALAPVQ------------------RWFFEQAIPQrqh 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2566 ------------FDRPRFDSAARQLVARHAGLRTT-VSPAGT-----DAASSGEVAVVHTAPIEPVVRDHDDvrAAMRDq 2627
Cdd:PRK12316 1121 wnqslllqarqpLDPDRLGRALERLVAHHDALRLRfREEDGGwqqayAAPQAGEVLWQRQAASEEELLALCE--EAQRS- 1197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2628 iIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDqLPPLETSFAHYVwnhpellpDADE 2707
Cdd:PRK12316 1198 -LDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDAD-LPARTSSYQAWA--------RRLH 1267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2708 AVLPRLAASRDYWRARLPSLPPA-----PKLAdmsllfeiEEPRFER-ATATIPAVDWSQVTRSCRAEGVT-VASFLLAN 2780
Cdd:PRK12316 1268 EHAGARAEELDYWQAQLEDAPHElpcenPDGA--------LENRHERkLELRLDAERTRQLLQEAPAAYRTqVNDLLLTA 1339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2781 YARVLSRWSGTDHFCINVTLFDRDP--DVVGIENVVGDFTSLVLLecRVDEPASIWESVRALQRQLMTdLPHRGadavwL 2858
Cdd:PRK12316 1340 LARVTCRWSGQASVLVQLEGHGREDlfEDIDLSRTVGWFTSLFPV--RLTPAADLGESIKAIKEQLRA-VPDKG-----I 1411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2859 QRELLRFHGNPTAA----LFP---VVFTSgLGLVDASARAAVRF--AEPVFAASQTPQTVL------DFQVWEsaGALKL 2923
Cdd:PRK12316 1412 GYGLLRYLAGEEAAarlaALPqprITFNY-LGQFDRQFDEAALFvpATESAGAAQDPCAPLanwlsiEGQVYG--GELSL 1488
|
570 580
....*....|....*....|...
gi 2181016861 2924 SWDFVSQAVSPATartqLESLVD 2946
Cdd:PRK12316 1489 HWSFSREMFAEAT----VQRLAD 1507
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
171-566 |
8.67e-21 |
|
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: 98.29 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSILRQA-AFAANVWNGDDDMHMVSwLPLYHDMGIFWgVFMPLLNGGCTTLIPPHD 249
Cdd:TIGR01923 110 MDQIATLMFTSGTTGKPKAVPHTFRNHYASAvGSKENLGFTEDDNWLLS-LPLYHISGLSI-LFRWLIEGATLRIVDKFN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 FVrnpriwLETVSRFRGNWIGG-PDFAYRRCIEAFDGTALQSLDLsclrlatnGAEPVRGTTLRdftakfraaglrddvM 328
Cdd:TIGR01923 188 QL------LEMIANERVTHISLvPTQLNRLLDEGGHNENLRKILL--------GGSAIPAPLIE---------------E 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 APQYGLAE-AGLGVTGSQTVRVWVEKSFDADALERGiavevaqpnpadgrsRALVSCgdgafgwDIQIVDPDRhmtltdG 407
Cdd:TIGR01923 239 AQQYGLPIyLSYGMTETCSQVTTATPEMLHARPDVG---------------RPLAGR-------EIKIKVDNK------E 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 408 EVGEIWVGGPGLPDGYWRQPEQTattfGARTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVE 486
Cdd:TIGR01923 291 GHGEIMVKGANLMKGYLYQGELT----PAFEQQG---WFNTGDIGeLDGEGFLYVLGRRDDLIISGGENIYPEEIETVLY 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 487 EaHCGVAPGGaCAVQPDApqangEW------WLVLETGSPVEDLDDL--SRILRRRILAHHETAPErvvwvpcrtLPTTT 558
Cdd:TIGR01923 364 Q-HPGIQEAV-VVPKPDA-----EWgqvpvaYIVSESDISQAKLIAYltEKLAKYKVPIAFEKLDE---------LPYNA 427
|
....*...
gi 2181016861 559 SGKIRRRE 566
Cdd:TIGR01923 428 SGKILRNQ 435
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
172-482 |
1.76e-20 |
|
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: 97.51 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLI--PPHD 249
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLdkIPSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 FVRN------------PRIW-------LETVSRFRGNW----IGGPDF-------AYRRCIEAFDGTalqsldlscLRLA 299
Cdd:cd05914 169 KIIAlafaqvtptlgvPVPLviekifkMDIIPKLTLKKfkfkLAKKINnrkirklAFKKVHEAFGGN---------IKEF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 300 TNGAEPVRGTTLRDF-TAKFRAAglrddvmaPQYGLAEAGLGVTGSqtvrVWVEKSFDadalergiavevaqpnpadgrs 378
Cdd:cd05914 240 VIGGAKINPDVEEFLrTIGFPYT--------IGYGMTETAPIISYS----PPNRIRLG---------------------- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 379 ralvSCGDGAFGWDIQIVDPDrhmtlTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAG-FRYQG 457
Cdd:cd05914 286 ----SAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAF---DKDG---WFHTGDLGkIDAEG 350
|
330 340
....*....|....*....|....*.
gi 2181016861 458 ELYVCGRYRDLIIVG-GRNHFPNDIE 482
Cdd:cd05914 351 YLYIRGRKKEMIVLSsGKNIYPEEIE 376
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
23-572 |
1.85e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 98.01 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 23 AEWVGRR----PDAVALrtvaATGIDDWTYQRLWDHVREIRDVAFS--GLSAGIRIPMALPGGADYVAGMLAALAAGLIP 96
Cdd:PRK06839 5 AYWIEKRaylhPDRIAI----ITEEEEMTYKQLHEYVSKVAAYLIYelNVKKGERIAILSQNSLEYIVLLFAIAKVECIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 97 VPVYLPSTREPQRFLARAQHILRD-CEPSAVYTCGELVEVLERDPILGalpIRTPASTADGlapHPGGttADADHGEHVA 175
Cdd:PRK06839 81 VPLNIRLTENELIFQLKDSGTTVLfVEKTFQNMALSMQKVSYVQRVIS---ITSLKEIEDR---KIDN--FVEKNESASF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 176 FLQYSSGSTGKPKGVVNTHQSILRQAAfaANVWNGDDDMHMVS--WLPLYHDMGIFWGVFMPLLNGGctTLIPPHDFvrN 253
Cdd:PRK06839 153 IICYTSGTTGKPKGAVLTQENMFWNAL--NNTFAIDLTMHDRSivLLPLFHIGGIGLFAFPTLFAGG--VIIVPRKF--E 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 254 PRIWLETVSRFRGNWIGGPDFAYRRCIEAFDgtaLQSLDLSCLRLATNGAEPVRGTTLRDFTAKfraaGLRddvMAPQYG 333
Cdd:PRK06839 227 PTKALSMIEKHKVTVVMGVPTIHQALINCSK---FETTNLQSVRWFYNGGAPCPEELMREFIDR----GFL---FGQGFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 334 LAEAglgvtgSQTVRVWVEKSFdadalergiavevaqpnpadgrSRALVSCGDGAFGWDIQIVDPDRHmTLTDGEVGEIW 413
Cdd:PRK06839 297 MTET------SPTVFMLSEEDA----------------------RRKVGSIGKPVLFCDYELIDENKN-KVEVGEVGELL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 414 VGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGV 492
Cdd:PRK06839 348 IRGPNVMKEYWNRPDATEETI----QDG---WLCTGDlARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINK-LSDV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 493 APGGACAVQP----DAPQAngewWLVLETGSPVEDLDDLSRILRRriLAHHETaPERVVWVpcRTLPTTTSGKIRRRETL 568
Cdd:PRK06839 420 YEVAVVGRQHvkwgEIPIA----FIVKKSSSVLIEKDVIEHCRLF--LAKYKI-PKEIVFL--KELPKNATGKIQKAQLV 490
|
....
gi 2181016861 569 NRLT 572
Cdd:PRK06839 491 NQLK 494
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
154-454 |
1.94e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 98.49 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 154 ADGLAPHPGGTTADadhgeHVAFLQYSSGSTGKPKGVVNTHQSILrQAAFAANVW-NGDDDMHMVSWLPLYHDMGIFWGV 232
Cdd:PRK08314 177 AAGLAPPPHTAGPD-----DLAVLPYTSGTTGVPKGCMHTHRTVM-ANAVGSVLWsNSTPESVVLAVLPLFHVTGMVHSM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 233 FMPLLNGGCTTLIPphdfvrnprIW-----LETVSRFR-GNWIGGPDFAyrrcIEAFDGTALQSLDLSCLRLATNGaepv 306
Cdd:PRK08314 251 NAPIYAGATVVLMP---------RWdreaaARLIERYRvTHWTNIPTMV----VDFLASPGLAERDLSSLRYIGGG---- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 307 rGTTLRDFTAK--FRAAGLRddvMAPQYGLAEaglgvTGSQTvrvwveksfdadalergiavevaQPNPADgrsRALVSC 384
Cdd:PRK08314 314 -GAAMPEAVAErlKELTGLD---YVEGYGLTE-----TMAQT-----------------------HSNPPD---RPKLQC 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 385 -GDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgaRTADGLgPYLRTGDAGFR 454
Cdd:PRK08314 359 lGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAF--IEIDGK-RFFRTGDLGRM 426
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1263-1610 |
1.98e-20 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 95.26 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdfdlsvYDTFG-ALGCGAQLV---TIPEHA 1338
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPF------FHTFGyKAGIVACLLtgaTVVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1339 RRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAA 1418
Cdd:cd17638 75 VFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1419 IWSneFVVDDVDPDWASIPYGYPLANQMFRVVDDngddqpdyvaGELWIGGAGVALGYHNAPELTSDRFvhDPTGsrWYR 1498
Cdd:cd17638 155 VAT--MCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI--DADG--WLH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1499 TGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VPIHNCTALGAGIVVTGSGAEQFDDSTP 1576
Cdd:cd17638 219 TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVigVPDERMGEVGKAFVVARPGVTLTEEDVI 298
|
330 340 350
....*....|....*....|....*....|....
gi 2181016861 1577 GALRAHLAvrlpQYMIPKVFVSCPELPLTANGKV 1610
Cdd:cd17638 299 AWCRERLA----NYKVPRFVRFLDELPRNASGKV 328
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
30-566 |
2.06e-20 |
|
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: 97.73 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 30 PDAVALRTVAATgiddWTYQRLWDHVREIRDVAF-SGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVylpSTREPQ 108
Cdd:cd12114 1 PDATAVICGDGT----LTYGELAERARRVAGALKaAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV---DIDQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 109 rflARAQHILRDCEPSAVYTCGELVEVLE---RDPILGALPIRTPAstadglAPHPGGTTADAdhgehVAFLQYSSGSTG 185
Cdd:cd12114 74 ---ARREAILADAGARLVLTDGPDAQLDVavfDVLILDLDALAAPA------PPPPVDVAPDD-----LAYVIFTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 186 KPKGVVNTHQSILR-----QAAFAAnvwNGDDDMHMVSwlPLYHDMGIFwGVFMPLLNGGcTTLIPPHDFVRNPRIWLET 260
Cdd:cd12114 140 TPKGVMISHRAALNtildiNRRFAV---GPDDRVLALS--SLSFDLSVY-DIFGALSAGA-TLVLPDEARRRDPAHWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 261 VSRFR--------------GNWIGGPDFAYR--RCIeafdgtaLQSLDLSCLRLAtngaepvrgTTLRDFT--AKFRAAG 322
Cdd:cd12114 213 IERHGvtlwnsvpallemlLDVLEAAQALLPslRLV-------LLSGDWIPLDLP---------ARLRALApdARLISLG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 323 lrddvmapqyGLAEAGlgvtgsqtvrVWveksfdadalerGIAVEVAQPNPAD-----GRSRAlvscgdgafGWDIQIVD 397
Cdd:cd12114 277 ----------GATEAS----------IW------------SIYHPIDEVPPDWrsipyGRPLA---------NQRYRVLD 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 398 PD-RHmtLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgARTADGLGPYlRTGDAG-FRYQGELYVCGRYRDLIIVGGRN 475
Cdd:cd12114 316 PRgRD--CPDWVPGELWIGGRGVALGYLGDPELTAARF-VTHPDGERLY-RTGDLGrYRPDGTLEFLGRRDGQVKVRGYR 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 476 HFPNDIEKTVeEAHCGVApGGACAVQPDAPQANGEWWLVLETGSPVEDLDDLSRILRRRILAHHEtaPERVVWVpcRTLP 555
Cdd:cd12114 392 IELGEIEAAL-QAHPGVA-RAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMI--PSRVIAL--EALP 465
|
570
....*....|.
gi 2181016861 556 TTTSGKIRRRE 566
Cdd:cd12114 466 LTANGKVDRAA 476
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1254-1612 |
3.14e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 98.57 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1254 TDPIRIDPHD--------AAYVIYTSGSTGEPKGVLVSHAAALnTIVDVNRRNRidthdrlLALSALDFDLS---VYDTF 1322
Cdd:PRK06060 129 SEAARVAPGGyepmggdaLAYATYTSGTTGPPKAAIHRHADPL-TFVDAMCRKA-------LRLTPEDTGLCsarMYFAY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1323 G---------ALGCGAQLVTIPEHARRDAfhwlSLTTEFGITVWNSVPGLMDMLLIAAgdKAGSLPTLRSVFLSGDWIPL 1393
Cdd:PRK06060 201 GlgnsvwfplATGGSAVINSAPVTPEAAA----ILSARFGPSVLYGVPNFFARVIDSC--SPDSFRSLRCVVSAGEALEL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1394 DLPRRLRRAAPGVRLVAMGGATEAAiwsNEFVVDDVDpDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVA 1473
Cdd:PRK06060 275 GLAERLMEFFGGIPILDGIGSTEVG---QTFVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1474 LGYHNAPE-LTSDrfvhdptgSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIH 1552
Cdd:PRK06060 351 KGYWNRPDsPVAN--------EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1553 NCTalGAGIV---VTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK06060 423 EST--GASTLqafLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVR 483
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
172-566 |
3.31e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 97.64 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMH-----MVSWLPLYHDMGIFWG--VFMPLlnGGCTTL 244
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEegcevVITALPLYHIFALTANglVFMKI--GGCNHL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 245 IpphdfvRNPR---IWLETVSRFRGNWIGGPDFAYRRCIE--AFDgtalqSLDLSCLRLATNGAepvrgttlrdftakfr 319
Cdd:PRK08751 286 I------SNPRdmpGFVKELKKTRFTAFTGVNTLFNGLLNtpGFD-----QIDFSSLKMTLGGG---------------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 320 aaglrddvMAPQYGLAEAGLGVTGSQTVRVW--VEKSfdadalergiavEVAQPNPADGRSRalvscgDGAFGWDIQIVD 397
Cdd:PRK08751 339 --------MAVQRSVAERWKQVTGLTLVEAYglTETS------------PAACINPLTLKEY------NGSIGLPIPSTD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 398 P----DRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATtfgARTADGlgpYLRTGD-AGFRYQGELYVCGRYRDLIIVG 472
Cdd:PRK08751 393 AcikdDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAK---VMDADG---WLHTGDiARMDEQGFVYIVDRKKDMILVS 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 473 GRNHFPNDIEKTVeEAHCGVAPGGACAVqPDapQANGEWW-LVLETGSPVEDLDDLSRILRRRILAHHETapeRVVWVPc 551
Cdd:PRK08751 467 GFNVYPNEIEDVI-AMMPGVLEVAAVGV-PD--EKSGEIVkVVIVKKDPALTAEDVKAHARANLTGYKQP---RIIEFR- 538
|
410
....*....|....*
gi 2181016861 552 RTLPTTTSGKIRRRE 566
Cdd:PRK08751 539 KELPKTNVGKILRRE 553
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1260-1615 |
4.64e-20 |
|
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: 96.13 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDL-SVYDTFGALGCGAQLVtipeHA 1338
Cdd:cd05907 85 DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFeRRAGLYVPLLAGARIY----FA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1339 RRDAFHWLSLtTEFGITVWNSVPGLMDMllIAAGDKAGSLPTLRSVFLsgDWIPLDlprRLRRAAPG-----VRLV---- 1409
Cdd:cd05907 161 SSAETLLDDL-SEVRPTVFLAVPRVWEK--VYAAIKVKAVPGLKRKLF--DLAVGG---RLRFAASGgaplpAELLhffr 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1410 AMG-------GATE--AAIwsneFVVDDVDPDWASIpyGYPLANQMFRVVDDngddqpdyvaGELWIGGAGVALGYHNAP 1480
Cdd:cd05907 233 ALGipvyegyGLTEtsAVV----TLNPPGDNRIGTV--GKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1481 ELTSDRFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRA-DSQVKIRGHRVECGEIEHALRGHPLVAAATVV----Pihnct 1555
Cdd:cd05907 297 EATAEALDADG----WLHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVIgdgrP----- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1556 ALGAGIVVTGSGAEQF------DDSTPGALRAHLAVR-------------LPQYMIPKVFVSCPELP------LTANGKV 1610
Cdd:cd05907 368 FLVALIVPDPEALEAWaeehgiAYTDVAELAANPAVRaeieaaveaanarLSRYEQIKKFLLLPEPFtiengeLTPTLKL 447
|
....*
gi 2181016861 1611 DRGKI 1615
Cdd:cd05907 448 KRPVI 452
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1237-1615 |
6.59e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 96.75 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1237 DAGVAVSDITAMIECAPTDPIRidPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdFDL 1316
Cdd:PRK06155 157 PAGWSTAPLPPLDAPAPAAAVQ--PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPL-FHT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1317 SVYDTF-GALGCGAQLVTIPehaRRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGdwIPLDL 1395
Cdd:PRK06155 234 NALNAFfQALLAGATYVLEP---RFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1396 PRRLRrAAPGVRLVAMGGATEAaiwsnEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGA---GV 1472
Cdd:PRK06155 309 HAAFR-ERFGVDLLDGYGSTET-----NFVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1473 ALGYHNAPELTSDRFvhdptGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIH 1552
Cdd:PRK06155 383 ATGYFGMPEKTVEAW-----RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1553 ncTALGAGIVVTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:PRK06155 458 --SELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1224-1612 |
8.20e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 95.80 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1224 AMAGLIRTDSDTQDA--GVAVSDITAMIECAPTDPI---RIDPHDAAYVIYTSGSTGEPKGVLVS---H-----AAALNT 1290
Cdd:PRK03640 98 AEVKCLITDDDFEAKliPGISVKFAELMNGPKEEAEiqeEFDLDEVATIMYTSGTTGKPKGVIQTygnHwwsavGSALNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1291 ivdvnrrnRIDTHDRLLA---------LSALdFDLSVYdtfgalGCGAQLVTipehaRRDAFHWLSLTTEFGITVWNSVP 1361
Cdd:PRK03640 178 --------GLTEDDCWLAavpifhisgLSIL-MRSVIY------GMRVVLVE-----KFDAEKINKLLQTGGVTIISVVS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1362 glmDML--LIAAGDKAGSLPTLRSVFLSGDWIPLDLprrLRRA-APGVRLVAMGGATEAAiwsNEFVVddVDPDWA---- 1434
Cdd:PRK03640 238 ---TMLqrLLERLGEGTYPSSFRCMLLGGGPAPKPL---LEQCkEKGIPVYQSYGMTETA---SQIVT--LSPEDAltkl 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1435 -SIpyGYPLANQMFRVVDDnGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVhdptgSRWYRTGDMGCYWRDGTLQF 1513
Cdd:PRK03640 307 gSA--GKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-----DGWFKTGDIGYLDEEGFLYV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1514 LGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCT--ALGAGIVVTGSGAeqfddsTPGALRAHLAVRLPQYM 1591
Cdd:PRK03640 379 LDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwgQVPVAFVVKSGEV------TEEELRHFCEEKLAKYK 452
|
410 420
....*....|....*....|.
gi 2181016861 1592 IPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK03640 453 VPKRFYFVEELPRNASGKLLR 473
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
28-565 |
1.12e-19 |
|
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: 95.01 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 28 RRPDAVALRTvaatGIDDWTYQRLWDHVREIRD-VAFSGLSAGIRIPMALPGGADYVAG--MLAALAAGLIPVPVYLPSt 104
Cdd:cd05945 3 ANPDRPAVVE----GGRTLTYRELKERADALAAaLASLGLDAGDPVVVYGHKSPDAIAAflAALKAGHAYVPLDASSPA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 105 repqrflARAQHILRDCEPSAVYTcgelvevlerdpilgalpirtpastadglAPHPggttadadhgehVAFLQYSSGST 184
Cdd:cd05945 78 -------ERIREILDAAKPALLIA-----------------------------DGDD------------NAYIIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 185 GKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFwGVFMPLLNGGCTTLIPpHDFVRNPRIWLETVSRF 264
Cdd:cd05945 110 GRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVM-DLYPALASGATLVPVP-RDATADPKQLFRFLAEH 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 265 RGN-WIGGPDFAyRRCI--EAFDGTALQSLDLS--ClrlatngAEPVRGTTLRDFTAKFRAAGLRDdvmapQYGLAEAGL 339
Cdd:cd05945 188 GITvWVSTPSFA-AMCLlsPTFTPESLPSLRHFlfC-------GEVLPHKTARALQQRFPDARIYN-----TYGPTEATV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 340 GVTGSQtvrvwveksFDADALERGIAVEVAQPNPadgrsralvscgdgafGWDIQIVDPDRHmTLTDGEVGEIWVGGPGL 419
Cdd:cd05945 255 AVTYIE---------VTPEVLDGYDRLPIGYAKP----------------GAKLVILDEDGR-PVPPGEKGELVISGPSV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 420 PDGYWRQPEQTATTFgaRTADGLGPYlRTGDAGFRY-QGELYVCGRYRDLIIVGGrnhfpNDIEKT-VEEAHCGVAPGGA 497
Cdd:cd05945 309 SKGYLNNPEKTAAAF--FPDEGQRAY-RTGDLVRLEaDGLLFYRGRLDFQVKLNG-----YRIELEeIEAALRQVPGVKE 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 498 CAVqpdAPQANGEW------WLVLETGSPVEDLDDLSRILRRRILAHheTAPERvvWVPCRTLPTTTSGKIRRR 565
Cdd:cd05945 381 AVV---VPKYKGEKvteliaFVVPKPGAEAGLTKAIKAELAERLPPY--MIPRR--FVYLDELPLNANGKIDRK 447
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-566 |
1.41e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 94.28 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHqsilRQAAFAANV---WNG--DDDMHMVSwLPLYHDMGIFWGVFMPLLNGGCTTLIPPHd 249
Cdd:cd05934 84 ASILYTSGTTGPPKGVVITH----ANLTFAGYYsarRFGlgEDDVYLTV-LPLFHINAQAVSVLAALSVGATLVLLPRF- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 fvrNPRIWLETVSRFR---GNWIGGP-DFAYRRCIEAFDGTAlqsldlsCLRLAtnGAEPVRGTTLRDFTAKFraaGLRd 325
Cdd:cd05934 158 ---SASRFWSDVRRYGatvTNYLGAMlSYLLAQPPSPDDRAH-------RLRAA--YGAPNPPELHEEFEERF---GVR- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 326 dvMAPQYGLAEAGlgvtgsqtvrvwveksfdadaleRGIAVEVAQPNPADgrsralvSCGDGAFGWDIQIVDPDRHmTLT 405
Cdd:cd05934 222 --LLEGYGMTETI-----------------------VGVIGPRDEPRRPG-------SIGRPAPGYEVRIVDDDGQ-ELP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 406 DGEVGEIWV---GGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDI 481
Cdd:cd05934 269 AGEPGELVIrglRGWGFFKGYYNMPEATAEAM----RNG---WFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 482 EKTVeEAHCGVApggACAVQPdAPQANGE----WWLVLETGSPVeDLDDLSRILRRRiLAHHEtapervvwVP-----CR 552
Cdd:cd05934 342 ERAI-LRHPAVR---EAAVVA-VPDEVGEdevkAVVVLRPGETL-DPEELFAFCEGQ-LAYFK--------VPryirfVD 406
|
410
....*....|....
gi 2181016861 553 TLPTTTSGKIRRRE 566
Cdd:cd05934 407 DLPKTPTEKVAKAQ 420
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-565 |
1.93e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 94.43 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 65 GLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPSTREPQRFLARaqHILRDCEPSAVYTCGELVEVLerDPILGA 144
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLR--YLVADAGGRIVLADAGAADRL--RDALPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 145 LPIRTPASTADGLAPHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYH 224
Cdd:cd05922 90 SPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 225 DMGiFWGVFMPLLNGGctTLIPPHDFVRNPRIWlETVSRFRGNWIGG--PDFAYRRCIeAFDGTALQSLdlsclRLATNG 302
Cdd:cd05922 170 DYG-LSVLNTHLLRGA--TLVLTNDGVLDDAFW-EDLREHGATGLAGvpSTYAMLTRL-GFDPAKLPSL-----RYLTQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 303 AEPVRGTTLRDFTAKFRaaGLRDDVMapqYGLAEAGLGVTgsqTVrvwveksfdadalergiavevaqpnPADGRSRALV 382
Cdd:cd05922 240 GGRLPQETIARLRELLP--GAQVYVM---YGQTEATRRMT---YL-------------------------PPERILEKPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 383 SCGDGAFGWDIQIVDPDRHMTLTdGEVGEIWVGGPGLPDGYWRQPEqtattfGARTADGLGPYLRTGDAGFRYQ-GELYV 461
Cdd:cd05922 287 SIGLAIPGGEFEILDDDGTPTPP-GEPGEIVHRGPNVMKGYWNDPP------YRRKEGRGGGVLHTGDLARRDEdGFLFI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 462 CGRYRDLIIVGGRNHFPNDIektvEEAHCGVAPGGACAVQPDAPQAnGEWWLVLETGSPVEDLDDLSRILRRRILAHHET 541
Cdd:cd05922 360 VGRRDRMIKLFGNRISPTEI----EAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDVLRSLAERLPPYKVP 434
|
490 500
....*....|....*....|....
gi 2181016861 542 APERVVwvpcRTLPTTTSGKIRRR 565
Cdd:cd05922 435 ATVRVV----DELPLTASGKVDYA 454
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
43-564 |
2.58e-19 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 94.52 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 43 IDD---WTYQRLWDHVREIRD-VAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPSTREPQRFlaraqhIL 118
Cdd:TIGR02262 25 IDDissLSYGELEAQVRRLAAaLRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAY------ML 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 119 RDCEPSAVYTCGELVEVLErdPILGALPI--------RTPAST---ADGLAPHPGGTTADADHGEHVAFLQYSSGSTGKP 187
Cdd:TIGR02262 99 EDSRARVVFVSGALLPVIK--AALGKSPHlehrvvvgRPEAGEvqlAELLATESEQFKPAATQADDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 188 KGVVNTHQSILRQAA-FAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDfvrNPRIWLETVSRFRG 266
Cdd:TIGR02262 177 KGVVHTHSNPYWTAElYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERP---TPDAVFDRLRRHQP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 267 NWIGGPDFAYRRCIEAFDgtaLQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaGLrdDVMApqyglaeaglGVTGSQT 346
Cdd:TIGR02262 254 TIFYGVPTLYAAMLADPN---LPSEDQVRLRLCTSAGEALPAEVGQRWQARF---GV--DIVD----------GIGSTEM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 347 VRVWVekSFDADALERGIAvevAQPNPadgrsralvscgdgafGWDIQIVDpDRHMTLTDGEVGEIWVGGPGLPDGYWRQ 426
Cdd:TIGR02262 316 LHIFL--SNLPGDVRYGTS---GKPVP----------------GYRLRLVG-DGGQDVADGEPGELLISGPSSATMYWNN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 427 PEQTATTFgartadgLGPYLRTGDAGFRYQGELYV-CGRYRDLIIVGGRNHFPNDIEKTVeEAHCGVAPGgacAVQPDA- 504
Cdd:TIGR02262 374 RAKSRDTF-------QGEWTRSGDKYVRNDDGSYTyAGRTDDMLKVSGIYVSPFEIESAL-IQHPAVLEA---AVVGVAd 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 505 ------PQAngewWLVLETGSPVEDlDDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSGKIRR 564
Cdd:TIGR02262 443 edglikPKA----FVVLRPGQTALE-TELKEHVKDRLAPY--KYPRWIVFVD--DLPKTATGKIQR 499
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
168-565 |
2.63e-19 |
|
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: 94.15 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 168 ADHGEHVAFLQYSSGSTGKPKGVVNTHQSIL----------------RQAAFAANVWngddDMHMVSwlplyhdmgifwg 231
Cdd:cd05918 102 TSSPSDAAYVIFTSGSTGKPKGVVIEHRALStsalahgralgltsesRVLQFASYTF----DVSILE------------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 232 VFMPLLNGGCTtLIPPhDFVRNPRIwLETVSRFRGNWIG-GPDFAyrrcieafdgTALQSLDLSCLRLATNGAEPVRGTT 310
Cdd:cd05918 165 IFTTLAAGGCL-CIPS-EEDRLNDL-AGFINRLRVTWAFlTPSVA----------RLLDPEDVPSLRTLVLGGEALTQSD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 311 LRDFTAKFRAAGLrddvmapqYGLAEAGLGVTGSQTVRvwveksfDADALERGIAVevaqpnpadgrsralvscgdGAFG 390
Cdd:cd05918 232 VDTWADRVRLINA--------YGPAECTIAATVSPVVP-------STDPRNIGRPL--------------------GATC 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 391 WdiqIVDPDRHMTLTD-GEVGEIWVGGPGLPDGYWRQPEQTATTF----GARTADGLGPY---LRTGDAGfRYQ--GELY 460
Cdd:cd05918 277 W---VVDPDNHDRLVPiGAVGELLIEGPILARGYLNDPEKTAAAFiedpAWLKQEGSGRGrrlYRTGDLV-RYNpdGSLE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 461 VCGRYRDLIIVGG------------RNHFPNDIEKTVEEAHCGVAPG-----GACAVQPDAPQANGEWWLVLEtgsPVED 523
Cdd:cd05918 353 YVGRKDTQVKIRGqrvelgeiehhlRQSLPGAKEVVVEVVKPKDGSSspqlvAFVVLDGSSSGSGDGDSLFLE---PSDE 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2181016861 524 LDDLSRILR---RRILAHHETaPErvVWVPCRTLPTTTSGKIRRR 565
Cdd:cd05918 430 FRALVAELRsklRQRLPSYMV-PS--VFLPLSHLPLTASGKIDRR 471
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1246-1611 |
2.89e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 96.15 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1246 TAMIECAPTDPIRIDphDAAYVIYTSGSTGEPKGVLVSH------AAALNTIVDVNRRNRIdthdrllaLSAL----DFD 1315
Cdd:PRK08633 768 ARLLKRLYGPTFKPD--DTATIIFSSGSEGEPKGVMLSHhnilsnIEQISDVFNLRNDDVI--------LSSLpffhSFG 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1316 LSVyDTFGALGCGAQLVTIPEHArrDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVfLSGdwiPLDL 1395
Cdd:PRK08633 838 LTV-TLWLPLLEGIKVVYHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLV-VAG---AEKL 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1396 PRRLRRAAP---GVRLVAMGGATE----AAIWSNEFVVDDVDPDWASIP--YGYPLANQMFRVVD-DNGDDQPDYVAGEL 1465
Cdd:PRK08633 911 KPEVADAFEekfGIRILEGYGATEtspvASVNLPDVLAADFKRQTGSKEgsVGMPLPGVAVRIVDpETFEELPPGEDGLI 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1466 WIGGAGVALGYHNAPELTSDrFVHDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALR----GHP 1541
Cdd:PRK08633 991 LIGGPQVMKGYLGDPEKTAE-VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkalgGEE 1069
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1542 LVAAATVVP-------IhnctalgagIVVTGSGAEQFDdstpGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:PRK08633 1070 VVFAVTAVPdekkgekL---------VVLHTCGAEDVE----ELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1177-1615 |
5.65e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 93.39 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVD-QPAER--------LSRICARSAMAGLIrtDSDTQDAGVA-VSDIT 1246
Cdd:PRK06839 53 GERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRlTENELifqlkdsgTTVLFVEKTFQNMA--LSMQKVSYVQrVISIT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1247 AMIECAPTDPIRIDP--HDAAYVI-YTSGSTGEPKG-VLVSHAAALNTIvdvNRRNRID--THDRLLALSALdFDLSVYD 1320
Cdd:PRK06839 131 SLKEIEDRKIDNFVEknESASFIIcYTSGTTGKPKGaVLTQENMFWNAL---NNTFAIDltMHDRSIVLLPL-FHIGGIG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1321 --TFGALGCGAQLVtIPEhaRRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRR 1398
Cdd:PRK06839 207 lfAFPTLFAGGVII-VPR--KFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMRE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1399 LRRAapGVRLVAMGGATEAAIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHN 1478
Cdd:PRK06839 284 FIDR--GFLFGQGFGMTETSPTVFMLSEEDARRKVGSI--GKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWN 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1479 APELTSDRfVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VPIHNCTA 1556
Cdd:PRK06839 360 RPDATEET-IQDG----WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVvgRQHVKWGE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 1557 LGAGIVVTGSGAEqfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:PRK06839 435 IPIAFIVKKSSSV----LIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
172-572 |
5.89e-19 |
|
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: 93.16 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPphdfv 251
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHP----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 252 rNP---RIWLETVSRFRGNWIGGPDFAYRRCIEafdgtALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaGLRddvm 328
Cdd:cd05909 222 -NPldyKKIPELIYDKKATILLGTPTFLRGYAR-----AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF---GIR---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 apqygLAEaGLGVTGSQTVrvwveksfdadalergIAVEVAQPNPADGrsralvSCGDGAFGWDIQIVDPDRHMTLTDGE 408
Cdd:cd05909 289 -----ILE-GYGTTECSPV----------------ISVNTPQSPNKEG------TVGRPLPGMEVKIVSVETHEEVPIGE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 409 VGEIWVGGPGLPDGYWRQPEQTATTFGartaDGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEktvEE 487
Cdd:cd05909 341 GGLLLVRGPNVMLGYLNEPELTSFAFG----DG---WYDTGDIGkIDGEGFLTITGRLSRFAKIAGEMVSLEAIE---DI 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 488 AHCGVAPGGACAV--QPDAPQanGEwWLVLETGSPVEDLDDLSRILRrrilaHHETAPervVWVPCR-----TLPTTTSG 560
Cdd:cd05909 411 LSEILPEDNEVAVvsVPDGRK--GE-KIVLLTTTTDTDPSSLNDILK-----NAGISN---LAKPSYihqveEIPLLGTG 479
|
410
....*....|..
gi 2181016861 561 KIRRReTLNRLT 572
Cdd:cd05909 480 KPDYV-TLKALA 490
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
383-572 |
6.06e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 93.10 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 383 SCGDGAFGWDIQIVDPDRHMTltDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAG-FRYQGELYV 461
Cdd:PRK03640 308 SAGKPLFPCELKIEKDGVVVP--PFEEGEIVVKGPNVTKGYLNREDATRETF----QDG---WFKTGDIGyLDEEGFLYV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 462 CGRYRDLIIVGGRNHFPNDIEKtVEEAHCGVAPGGACAVqPDApqangEWWLV----LETGSPVeDLDDLSRILRRRiLA 537
Cdd:PRK03640 379 LDRRSDLIISGGENIYPAEIEE-VLLSHPGVAEAGVVGV-PDD-----KWGQVpvafVVKSGEV-TEEELRHFCEEK-LA 449
|
170 180 190
....*....|....*....|....*....|....*
gi 2181016861 538 HHETaPERVVWVpcRTLPTTTSGKIRRRETLNRLT 572
Cdd:PRK03640 450 KYKV-PKRFYFV--EELPRNASGKLLRHELKQLVE 481
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2352-2849 |
6.63e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.23 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2352 ATLISAAVLDPGLLASDSKTLRPADRwwRLIADHgWRPTHMIqdgpgltLIAHRP-------DKPGMPTPPAEQRRDGrW 2424
Cdd:PRK12467 956 AYLVPAAVADGAEHQATRDELKAQLR--QVLPDY-MVPAHLL-------LLDSLPltpngklDRKALPKPDASAVQAT-F 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2425 SRPAVPasslptdatVVATLAEIWQRHLAIPTPGVDDDFFLLGGDSLVATRVYADLRAAGFGQLAFVDLFNHSTLGELAA 2504
Cdd:PRK12467 1025 VAPQTE---------LEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQ 1095
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2505 HAGPRtgpEVSVAAESTRGGTHDPnrFPLTVVQNayRAGREGALILGGVAAHCYFEFEL-ADFDRPRFDSAARQLVARHA 2583
Cdd:PRK12467 1096 AVAAQ---QQGAQPALPDVDRDQP--LPLSYAQE--RQWFLWQLEPGSAAYHIPQALRLkGPLDIEALERSFDALVARHE 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2584 GLRTTVspagtdaASSGEVAVVHTAPIEPVVRDHDDVRAAMRD-------------QIIDLTARPGIDFGVQTRGDGRTV 2650
Cdd:PRK12467 1169 SLRTTF-------VQEDGRTRQVIHPVGSLTLEEPLLLAADKDeaqlkvyveaearQPFDLEQGPLLRVGLLRLAADEHV 1241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2651 VGISMDNTMLDGASMMIALSELDHLYRGE---TVDQLPPLETSFAHY-VWNHPELlpDADEAvlprlAASRDYWRARLPS 2726
Cdd:PRK12467 1242 LVLTLHHIVSDGWSMQVLVDELVALYAAYsqgQSLQLPALPIQYADYaVWQRQWM--DAGER-----ARQLAYWKAQLGG 1314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2727 LPPA-------PKLADMSLlfeieepRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRWSGTDHFCINVT 2799
Cdd:PRK12467 1315 EQPVlelptdrPRPAVQSH-------RGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVP 1387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 2800 LFDRDPdvVGIENVVGDFTSLVLLECRVDEPASIWESVR-----ALQRQLMTDLP 2849
Cdd:PRK12467 1388 IANRNR--AETEGLIGFFVNTQVLRAEVDGQASFQQLLQqvkqaALEAQAHQDLP 1440
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1259-1612 |
8.61e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 90.87 E-value: 8.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1259 IDPhDAAYVIYTSGSTGEPKGVLVShAAALNTIVDVnrrnridTHDRLlalsaldfdlsvydtfGalGCGAQLVTIPEH- 1337
Cdd:PRK07824 33 IDD-DVALVVATSGTTGTPKGAMLT-AAALTASADA-------THDRL----------------G--GPGQWLLALPAHh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1338 ------------ARRDAFHwLSLTTEFGITVWNSVPGLMD-----------MLLIAAGDKAG--SLPTLRSVFLSGDwiP 1392
Cdd:PRK07824 86 iaglqvlvrsviAGSEPVE-LDVSAGFDPTALPRAVAELGggrrytslvpmQLAKALDDPAAtaALAELDAVLVGGG--P 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1393 LDLPRRLRRAAPGVRLVAMGGATEAaiwSNEFVVDdvdpdwasipyGYPLANQMFRVVDdngddqpdyvaGELWIGGAGV 1472
Cdd:PRK07824 163 APAPVLDAAAAAGINVVRTYGMSET---SGGCVYD-----------GVPLDGVRVRVED-----------GRIALGGPTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1473 ALGYHNAPEltsdrfvHDP-TGSRWYRTGDMGCYwRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI 1551
Cdd:PRK07824 218 AKGYRNPVD-------PDPfAEPGWFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGL 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 1552 HNcTALG----AGIVVTGSGAEqfddsTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK07824 290 PD-DRLGqrvvAAVVGDGGPAP-----TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDR 348
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2411-2946 |
8.74e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.84 E-value: 8.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2411 MPTPPaeqrrDGRWSRPAVPA--SSLPTDATVVAT------LAEIWQRHLAIPTPGVDDDFFLLGGDSLVATRVYADLRA 2482
Cdd:PRK12467 2066 MPLTP-----NGKLDRKALPApdASELQQAYVAPQseleqrLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQ 2140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2483 AGFgQLAFVDLFNHSTLGELAAHAgpRTGPEVSVAAESTRGGThdpnrFPLTVVQNAYragregalilggvaahcyFEFE 2562
Cdd:PRK12467 2141 AGI-RFTPKDLFQHQTVQSLAAVA--QEGDGTVSIDQGPVTGD-----LPLLPIQQMF------------------FADD 2194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2563 LAD---------------FDRPRFDSAARQLVARHAGLRTTVS--PAGTDAASSGEVAVVHTAPIEPVVRDHDDVRA--- 2622
Cdd:PRK12467 2195 IPErhhwnqsvllepreaLDAELLEAALQALLVHHDALRLGFVqeDGGWSAMHRAPEQERRPLLWQVVVADKEELEAlce 2274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2623 -AMRDqiIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYR----GETVDQlpPLETSfAHYVWN 2697
Cdd:PRK12467 2275 qAQRS--LDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRqlqgGQPVKL--PAKTS-AFKAWA 2349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2698 hpELLpdADEAVLPRLAASRDYWRARLPSLPPAPKLADMSllfEIEEPRFERATATIPAVDWSQ--VTRSCRAEGVTVAS 2775
Cdd:PRK12467 2350 --ERL--QTYAASAALADELGYWQAQLQGASTELPCDHPQ---GGLQRRHAASVTTHLDSEWTRrlLQEAPAAYRTQVND 2422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2776 FLLANYARVLSRWSGTDHFCINVTLFDRDP--DVVGIENVVGDFTSLVLLecRVDEPASIWESVRALQRQLMTdLPHRGa 2853
Cdd:PRK12467 2423 LLLTALARVIARWTGQASTLIQLEGHGREDlfDEIDLTRTVGWFTSLYPV--KLSPTASLATSIKTIKEQLRA-VPNKG- 2498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2854 davwLQRELLRFHGNPTA-----AL-FPVVFTSGLGLVDAS----ARAAVRFAEPVFAASQTPQTVLDF------QVWes 2917
Cdd:PRK12467 2499 ----LGFGVLRYLGSEAArqtlqALpVPRITFNYLGQFDGSfdaeKQALFVPSGEFSGAEQSEEAPLGNwlsingQVY-- 2572
|
570 580 590
....*....|....*....|....*....|....*.
gi 2181016861 2918 AGALKLSWDFVSQAVSPATA-------RTQLESLVD 2946
Cdd:PRK12467 2573 GGELNLGWTFSQEMFDEATIqrladayAEELRALIE 2608
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1076-1612 |
1.00e-18 |
|
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: 93.32 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1076 ERLGGHDWSTPATP--GLSAHSRLARAHRNATTTpapagLLYDAFRENAATHPARLALRWRpddyrGERhGDViaqdRSq 1153
Cdd:cd05968 28 VKDVGIEWYEPPYQtlDLSGGKPWAAWFVGGRMN-----IVEQLLDKWLADTRTRPALRWE-----GED-GTS----RT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1154 LTYGELD-ELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPV----GVDQPAERLsricARSAMAGL 1228
Cdd:cd05968 92 LTYGELLyEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIfsgfGKEAAATRL----QDAEAKAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1229 IRTD-----------------SDTQDAGV----------------AVSDI--TAMIECAPTDPIRIDPHDAAYVIYTSGS 1273
Cdd:cd05968 168 ITADgftrrgrevnlkeeadkACAQCPTVekvvvvrhlgndftpaKGRDLsyDEEKETAGDGAERTESEDPLMIIYTSGT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1274 TGEPKGVLVSHA-----AALNTIVDVNRRNridtHDRLLALSALDFDLSVYDTFGALGCGAQLVT---IPEHARRDAFhW 1345
Cdd:cd05968 248 TGKPKGTVHVHAgfplkAAQDMYFQFDLKP----GDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPDHPKADRL-W 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1346 lSLTTEFGITVWNSVPGLMDMlLIAAGD---KAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRL--VAMGGATEAA-- 1418
Cdd:cd05968 323 -RMVEDHEITHLGLSPTLIRA-LKPRGDapvNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNpiINYSGGTEISgg 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1419 IWSNeFVVDDVDPdwasIPYGYPLANQMFRVVDDNGDDQPDYVaGEL-----WIggaGVALGYHNAPeltsDRFvHDPTG 1493
Cdd:cd05968 401 ILGN-VLIKPIKP----SSFNGPVPGMKADVLDESGKPARPEV-GELvllapWP---GMTRGFWRDE----DRY-LETYW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1494 SRW---YRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLV--AAATVVP-------IHNCTALGAGI 1561
Cdd:cd05968 467 SRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVleSAAIGVPhpvkgeaIVCFVVLKPGV 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1562 VVTGSGAEQfddstpgaLRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05968 547 TPTEALAEE--------LMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
172-566 |
1.10e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 92.96 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSIL--RQAAFAANVWNGDDDMH--------MVSWLPLYHdmgifwgVFMPLLNGGC 241
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVanMLQVRACLSQLGPDGQPlmkegqevMIAPLPLYH-------IYAFTANCMC 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 TTLIPPHD-FVRNPRI---WLETVSRFRGNWIGGPDFAYrrcIEAFDGTALQSLDLSCLRLATNGaepvrGTTLRDFTAK 317
Cdd:PRK12492 280 MMVSGNHNvLITNPRDipgFIKELGKWRFSALLGLNTLF---VALMDHPGFKDLDFSALKLTNSG-----GTALVKATAE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 318 fRAAGLRDDVMAPQYGLAEAGlgvtgsqtvrvwveksfdadalergiavEVAQPNPADGRSRaLVSCGDGAFGWDIQIVD 397
Cdd:PRK12492 352 -RWEQLTGCTIVEGYGLTETS----------------------------PVASTNPYGELAR-LGTVGIPVPGTALKVID 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 398 pDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNH 476
Cdd:PRK12492 402 -DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL---DAEG---WFKTGDiAVIDPDGFVRIVDRKKDLIIVSGFNV 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 477 FPNDIEKTVeEAHCGVApggACAVQPDAPQANGEWW-LVLETGSPVEDLDDLSRILRRRILAHheTAPERVVWVpcRTLP 555
Cdd:PRK12492 475 YPNEIEDVV-MAHPKVA---NCAAIGVPDERSGEAVkLFVVARDPGLSVEELKAYCKENFTGY--KVPKHIVLR--DSLP 546
|
410
....*....|.
gi 2181016861 556 TTTSGKIRRRE 566
Cdd:PRK12492 547 MTPVGKILRRE 557
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1254-1612 |
1.60e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 92.50 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1254 TDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHaaalNTIVDVNR----RNRIDTHDRLLALSALD----FDLSVYDTFgAL 1325
Cdd:PRK06087 179 TTAITTHGDELAAVLFTSGTEGLPKGVMLTH----NNILASERaycaRLNLTWQDVFMMPAPLGhatgFLHGVTAPF-LI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1326 GCGAQLVTI--PEHA----RRDAFHWLSLTTEFgitvwnsvpgLMDMLLIAAGDKAgSLPTLRSVFLSGDWIPLDLPRRL 1399
Cdd:PRK06087 254 GARSVLLDIftPDAClallEQQRCTCMLGATPF----------IYDLLNLLEKQPA-DLSALRFFLCGGTTIPKKVAREC 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1400 RRAapGVRLVAMGGATEAAiwSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNA 1479
Cdd:PRK06087 323 QQR--GIKLLSVYGSTESS--PHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1480 PELTSDrfVHDPTGsrWYRTGDMGCYWRDGTLQFLGRaDSQVKIR-GHRVECGEIEHALRGHPLVAAATVVPIHNcTALG 1558
Cdd:PRK06087 399 PELTAR--ALDEEG--WYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPD-ERLG 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 1559 AGIVVTGSGAEQFDDSTPGALRAHLAV-RLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK06087 473 ERSCAYVVLKAPHHSLTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASGKIQK 527
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1099-1612 |
2.30e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 91.87 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1099 RAHRNATTTPAPAG-LLYDAFRENAATHPARLALrwrpddyrgerhgdVIAQDRSQLTYGELDELARSVARAVAAR-HAA 1176
Cdd:PRK05852 2 RFMGGAAPMASDFGpRIADLVEVAATRLPEAPAL--------------VVTADRIAISYRDLARLVDDLAGQLTRSgLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVgvdQPAERLSRICARSAMAG------------------------LIRTD 1232
Cdd:PRK05852 68 GDRVALRMGSNAEFVVALLAASRADLVVVPL---DPALPIAEQRVRSQAAGarvvlidadgphdraepttrwwplTVNVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1233 SDTQDAGVAVS---DITAMIECAPTDPIRIDPHDAaYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLAL 1309
Cdd:PRK05852 145 GDSGPSGGTLSvhlDAATEPTPATSTPEGLRPDDA-MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1310 SALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGD 1389
Cdd:PRK05852 224 MPLYHGHGLIAALLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1390 WIPLD----LPRRLRRAAPGVRLVAMGGATEAAIWSN-EFVVDDVDPDWASIPYGYPLANQmFRVVDDNGDDQPDYVAGE 1464
Cdd:PRK05852 304 SAPLTaetaQALQTEFAAPVVCAFGMTEATHQVTTTQiEGIGQTENPVVSTGLVGRSTGAQ-IRIVGSDGLPLPAGAVGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1465 LWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVA 1544
Cdd:PRK05852 383 VWLRGTTVVRGYLGDPTITAANFTDG-----WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVM 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1545 AATVVPIHNCT---ALGAGIVVTGSGAeqfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK05852 458 EAAVFGVPDQLygeAVAAVIVPRESAP-----PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1263-1612 |
3.99e-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: 90.23 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALnTIVDVNRRN--RIDTHDRLLALSALDFdlsvydTFG-------ALGCGAQLVT 1333
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPL-ASADRYAVNvlRLREDDRFVGSPPLAF------TFGlggvllfPFGVGASGVL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1334 IPehaRRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLpRRLRRAAPGVRLVAMGG 1413
Cdd:cd05958 171 LE---EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAAL-HRAWKEATGIPIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1414 ATEA--AIWSNEfvVDDVDPDWASIPY-GYPLanqmfRVVDDNGDDQPDYVAGELWIGGAgvaLGYHNAPELTSDRFVHD 1490
Cdd:cd05958 247 STEMfhIFISAR--PGDARPGATGKPVpGYEA-----KVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1491 ptgsRWYRTGDMgcYWR--DGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVpihNCTALGAGIVVTG--- 1565
Cdd:cd05958 317 ----GWNITGDT--YSRdpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVV---GHPDESRGVVVKAfvv 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2181016861 1566 SGAEQFDDSTPG-ALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05958 388 LRPGVIPGPVLArELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQR 435
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1263-1615 |
4.12e-18 |
|
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: 89.71 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLA------LSALDFDL-SVYdtfgaLGCGAQLvtip 1335
Cdd:cd05912 78 DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCalplfhISGLSILMrSVI-----YGMTVYL---- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1336 eHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLiaAGDKAGSLPTLRSVFLSGDWIPLDLprrLRRAAP-GVRLVAMGGA 1414
Cdd:cd05912 149 -VDKFDAEQVLHLINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILLGGGPAPKPL---LEQCKEkGIPVYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1415 TEAAIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNgddQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgs 1494
Cdd:cd05912 223 TETCSQIVTLSPEDALNKIGSA--GKPLFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENG---- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1495 rWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV----------VPIhnctalgAGIVvt 1564
Cdd:cd05912 294 -WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVvgipddkwgqVPV-------AFVV-- 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1565 gsgAEQfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05912 364 ---SER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1254-1544 |
4.23e-18 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 90.74 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1254 TDPiriDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRR--NRIDTHDRLLALSALD--FDLSVYDTF----GAL 1325
Cdd:cd17639 83 TDG---KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRvpELLGPDDRYLAYLPLAhiFELAAENVClyrgGTI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1326 GCGAQLVTIPEHARR---DAfhwlsltTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTL-RSVFLSGDWIPLDLPRRLR- 1400
Cdd:cd17639 160 GYGSPRTLTDKSKRGckgDL-------TEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLkRTLFWTAYQSKLKALKEGPg 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1401 ------------RAAPGVRLVAM--GGATEAAIwSNEFV---------------------VDDVDpDWASIPYGYPLANQ 1445
Cdd:cd17639 233 tplldelvfkkvRAALGGRLRYMlsGGAPLSAD-TQEFLnivlcpviqgygltetcaggtVQDPG-DLETGRVGPPLPCC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1446 MFRVVD--------DNGDDQpdyvaGELWIGGAGVALGYHNAPELTSDRFvhdpTGSRWYRTGDMGCYWRDGTLQFLGRA 1517
Cdd:cd17639 311 EIKLVDweeggystDKPPPR-----GEILIRGPNVFKGYYKNPEKTKEAF----DGDGWFHTGDIGEFHPDGTLKIIDRK 381
|
330 340
....*....|....*....|....*...
gi 2181016861 1518 DSQVKIR-GHRVECGEIEHALRGHPLVA 1544
Cdd:cd17639 382 KDLVKLQnGEYIALEKLESIYRSNPLVN 409
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1154-1612 |
6.77e-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: 89.50 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1154 LTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPV----GVDQPAERLsricaRSAMAGL 1228
Cdd:cd05973 1 LTFGELRALSARFANALQELgVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGPKAIEHRL-----RTSGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1229 IRTDSDTQDagvavsditamiecaptdpiRIDpHDAAYVIYTSGSTGEPKGV------LVSHAAALNTIVDVNRRNRIDT 1302
Cdd:cd05973 76 VVTDAANRH--------------------KLD-SDPFVMMFTSGTTGLPKGVpvplraLAAFGAYLRDAVDLRPEDSFWN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1303 hdrlLALSALDFDLsVYDTFGALGCGAQlvTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLiAAGDKAGSLPTLR 1382
Cdd:cd05973 135 ----AADPGWAYGL-YYAITGPLALGHP--TILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLM-AAGAEVPARPKGR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1383 SVFLSGDWIPLDlPRRLR--RAAPGVRLVAMGGATEAAIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDY 1460
Cdd:cd05973 207 LRRVSSAGEPLT-PEVIRwfDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSA--GRAMPGWRVAVLDDDGDELGPG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1461 VAGELWIGGAGVAL----GYHNAPELTSDrfvhdptgSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHA 1536
Cdd:cd05973 284 EPGRLAIDIANSPLmwfrGYQLPDTPAID--------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1537 LRGHPLVAAATVV--PIHNCTALGAGIVVTGSGAEqfddSTPG---ALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd05973 356 LIEHPAVAEAAVIgvPDPERTEVVKAFVVLRGGHE----GTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQ 431
|
.
gi 2181016861 1612 R 1612
Cdd:cd05973 432 R 432
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1246-1612 |
7.21e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 90.34 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1246 TAMIECAPTDPIR-IDPHDAAYVIYTSGSTGEPKGVLVSHAAALntivdvnrrnridTHdRLLALSALDF---DL----- 1316
Cdd:PRK04319 188 ALMEQASDEFDIEwTDREDGAILHYTSGSTGKPKGVLHVHNAML-------------QH-YQTGKYVLDLhedDVywcta 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1317 -------SVYDTFGALGCGAQLVTipEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAG--SLPTLRSVFLS 1387
Cdd:PRK04319 254 dpgwvtgTSYGIFAPWLNGATNVI--DGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKkyDLSSLRHILSV 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1388 GDwiPLDlPRRLR--RAAPGVRLVAMGGATE-AAIWSNEFVVDDVDPdwASIpyGYPLANQMFRVVDDNGDDQPDYVAGE 1464
Cdd:PRK04319 332 GE--PLN-PEVVRwgMKVFGLPIHDNWWMTEtGGIMIANYPAMDIKP--GSM--GKPLPGIEAAIVDDQGNELPPNRMGN 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1465 LWI--GGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPL 1542
Cdd:PRK04319 405 LAIkkGWPSMMRGIWNNPEKYESYFAGD-----WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPA 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1543 VAAATVV----PIhnctaLGAGI---VVTGSGAEQfDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK04319 480 VAEAGVIgkpdPV-----RGEIIkafVALRPGYEP-SEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1228-1612 |
7.28e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 90.13 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1228 LIRTDSDTQDAGVAVSDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHA----AALNTIVDVNRRNridtH 1303
Cdd:PRK08008 139 LTRVALPADDGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYnlrfAGYYSAWQCALRD----D 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1304 DRLLALSA---LDFDLSVydTFGALGCGAQLVTIPEHARRdAFhWlSLTTEFGITVWNSVPGLMDMLLI---AAGDKAGS 1377
Cdd:PRK08008 215 DVYLTVMPafhIDCQCTA--AMAAFSAGATFVLLEKYSAR-AF-W-GQVCKYRATITECIPMMIRTLMVqppSANDRQHC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1378 LptlRSVF----LSgDWIPLDLPRRLrraapGVRLVAMGGATEAAIWsnefVVDDVDPD---WASIpyGYPLANQMFRVV 1450
Cdd:PRK08008 290 L---REVMfylnLS-DQEKDAFEERF-----GVRLLTSYGMTETIVG----IIGDRPGDkrrWPSI--GRPGFCYEAEIR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1451 DDNGDDQPDYVAGELWIGG-AGVAL--GYHNAPELTSDrfVHDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHR 1527
Cdd:PRK08008 355 DDHNRPLPAGEIGEICIKGvPGKTIfkEYYLDPKATAK--VLEADG--WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGEN 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1528 VECGEIEHALRGHPLVAAATVVPIHNCT---ALGAgIVVTGSGAEQfddsTPGALRAHLAVRLPQYMIPKVFVSCPELPL 1604
Cdd:PRK08008 431 VSCVELENIIATHPKIQDIVVVGIKDSIrdeAIKA-FVVLNEGETL----SEEEFFAFCEQNMAKFKVPSYLEIRKDLPR 505
|
....*...
gi 2181016861 1605 TANGKVDR 1612
Cdd:PRK08008 506 NCSGKIIK 513
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1103-1549 |
7.51e-18 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 90.54 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1103 NATTTPAPAGLLYDAFRENAATHPARLALRWRPDDyrgerhgdvIAQDrsqLTYGELDELARSVARA-VAARHAAGSVIG 1181
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDG---------IWQS---LTWAEFAERVRALAAGlLALGVKPGDRVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1182 IQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERL--------SRIC----------ARSAMAGL------IRTDSDTQD 1237
Cdd:COG1022 70 ILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVayilndsgAKVLfvedqeqldkLLEVRDELpslrhiVVLDPRGLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1238 AGVAVSDITAMIE--CAPTDPIRID-------PHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLA 1308
Cdd:COG1022 150 DDPRLLSLDELLAlgREVADPAELEarraavkPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1309 ---LS-ALDFDLSVYdtfgALGCGAQLV------TIPEHARrdafhwlslttEFGITVWNSVPGLMDMLLIAAGDKAGSL 1378
Cdd:COG1022 230 flpLAhVFERTVSYY----ALAAGATVAfaespdTLAEDLR-----------EVKPTFMLAVPRVWEKVYAGIQAKAEEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1379 PTL-RSVF--------------LSGDWIPLDLP-----------RRLRRA------------AP-GVRLV----AMG--- 1412
Cdd:COG1022 295 GGLkRKLFrwalavgrryararLAGKSPSLLLRlkhaladklvfSKLREAlggrlrfavsggAAlGPELArffrALGipv 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1413 ----GATE--AAIWSNEFvvDDVDPDwaSIpyGYPLANQMFRVVDDngddqpdyvaGELWIGGAGVALGYHNAPELTSDR 1486
Cdd:COG1022 375 legyGLTEtsPVITVNRP--GDNRIG--TV--GPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEA 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 1487 FVHDptgsRWYRTGDMGCYWRDGTLQFLGRADSQVKIR-GHRVECGEIEHALRGHPLVAAATVV 1549
Cdd:COG1022 439 FDAD----GWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| ArgR-Cyc_NRPS-like |
cd20480 |
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ... |
710-1078 |
8.29e-18 |
|
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to Cyc-domains there are various other subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380470 [Multi-domain] Cd Length: 406 Bit Score: 88.71 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 710 TYFELVGARVDAGRLAAALDALTRRHPMLRATFPDPGRCLITPEAVRLPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRfd 789
Cdd:cd20480 28 IYQEFDYENISVDTLERCLTVLINHHPMLHALLSDDFYLHINSKNQIDAFAVNDLSSASEQEAAEQLARTRATLTKSR-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 790 ieTGDTWTVELTRLPHGCI-VHFAVDLIIADVTSIGTMLRDLAASYRGEKLPAPSATFA---------DLIQSTSPPPQA 859
Cdd:cd20480 106 --SKATISVVLSLLPANKIrLHVRFNSVVVDHPSVNLFFEQLCQLLRGSLLSFLAQEQVilahnqlviSELQSTGLSSAF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 860 CAD---RLPEGPQLPRVQE----ADISFLRHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVT 932
Cdd:cd20480 184 WNEqilQLPSSANLPTVCEpeklRETGITRRTLTLSSDKWQQLVTISKQHNVTPELTLASIFSAVLSLWGNQKDMMLRFD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 933 TFGRSpEVSDVVGDFTETHLyrAQLDG-QISFVDQAQVTQKGLRTA--LRAAPAPDLLATQLRSGTGHSGIVPVVFTYAA 1009
Cdd:cd20480 264 LNKKN-DVAGVIGQFTQPLL--VGLSGfGQSFLSLVKENQKHFEQAypFRQIPIFDLVRQLAKLSESHRYPANIAFSSQL 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 1010 DSPLLSA-------EDANTLGAIDEVVSMtpqvlidhqacrlgDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLERL 1078
Cdd:cd20480 341 SGNNTLGrsgwgcrQSANTWLSLHAFISQ--------------GGLILQWDSQDALFPKDMIQDMLTSYSKLLESL 402
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
27-574 |
9.02e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 89.48 E-value: 9.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 27 GRRPDAVALRTVAaTGIDdWTYQRLWDHV-REIRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPV-YLPST 104
Cdd:PRK09088 6 RLQPQRLAAVDLA-LGRR-WTYAELDALVgRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 105 REPQRFLARAQH--ILRDCEPSAVYTCGELVEVLerdpilgalpirtpASTADGLAPHPggtTADADHgEHVAFLQYSSG 182
Cdd:PRK09088 84 SELDALLQDAEPrlLLGDDAVAAGRTDVEDLAAF--------------IASADALEPAD---TPSIPP-ERVSLILFTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 183 STGKPKGVVNTHQSiLRQAAFAANVWNGDDdmHMVSWL---PLYHDMGIFWGVFMPLLNGGCTTLIPPHDFVRNPRiWLE 259
Cdd:PRK09088 146 TSGQPKGVMLSERN-LQQTAHNFGVLGRVD--AHSSFLcdaPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG-RLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 260 TVSRFRGNWIGGPDFAYR-RCIEAFDGTALQSLDLSCLRLATNGAEPVRGttlrdftakFRAAGLRddvMAPQYGLAEAG 338
Cdd:PRK09088 222 DPALGITHYFCVPQMAQAfRAQPGFDAAALRHLTALFTGGAPHAAEDILG---------WLDDGIP---MVDGFGMSEAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 339 lgvtgsqTVRvwveksfdadalerGIAVEvaqpnPADGRSRAlVSCGDGAFGWDIQIVDpDRHMTLTDGEVGEIWVGGPG 418
Cdd:PRK09088 290 -------TVF--------------GMSVD-----CDVIRAKA-GAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPN 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 419 LPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVApggA 497
Cdd:PRK09088 342 LSPGYWRRPQATARAF---TGDG---WFRTGDIARRdADGFFWVVDRKKDMFISGGENVYPAEIE-AVLADHPGIR---E 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 498 CAV--QPDAPQAN-GEWWLVLETGSPVeDLDDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSGKIRRRETLNRLTAG 574
Cdd:PRK09088 412 CAVvgMADAQWGEvGYLAIVPADGAPL-DLERIRSHLSTRLAKY--KVPKHLRLVD--ALPRTASGKLQKARLRDALAAG 486
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
708-1076 |
9.09e-18 |
|
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: 88.67 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 708 CQTYFELVGaRVDAGRLAAALDALTRRHPMLR-ATFPDPGrcliTPEAVR--LPLAVHDLTDAPVTTRDTHLAEIRRrLR 784
Cdd:cd19532 26 VTFSYRLTG-PLDVARLERAVRAVGQRHEALRtCFFTDPE----DGEPMQgvLASSPLRLEHVQISDEAEVEEEFER-LK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 785 THRFDIETGDTwtVELTRLPHGCIVHFavdLIIA------DVTSIGTMLRDLAASYRGEKLPAPSATFADLIQ------- 851
Cdd:cd19532 100 NHVYDLESGET--MRIVLLSLSPTEHY---LIFGyhhiamDGVSFQIFLRDLERAYNGQPLLPPPLQYLDFAArqrqdye 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 852 ---------------STSPPPqacadrLPEGPqLPRVQE----ADISFLRHQHTLSALATKAIDDACHNHGVTRAAVLLA 912
Cdd:cd19532 175 sgaldedlaywksefSTLPEP------LPLLP-FAKVKSrpplTRYDTHTAERRLDAALAARIKEASRKLRVTPFHFYLA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 913 AYTLVLRRWASQDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKGLRTALRAAPAP-DLLATQ 990
Cdd:cd19532 248 ALQVLLARLLDVDDICIGIADANRTdEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPfDVLLDE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 991 L---RSGTgHSGIVPVVFTY----AADSPL-------LSAEDANTlgAIDEVVSMTPQVlidhqacrlGDDVVLSWDYRA 1056
Cdd:cd19532 328 LgvpRSAT-HSPLFQVFINYrqgvAESRPFgdcelegEEFEDART--PYDLSLDIIDNP---------DGDCLLTLKVQS 395
|
410 420
....*....|....*....|
gi 2181016861 1057 GCFPPGVVDDMFEAYVTLLE 1076
Cdd:cd19532 396 SLYSEEDAELLLDSYVNLLE 415
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1263-1611 |
9.36e-18 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 87.36 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdFDLSV-YDTFGALGCGAQLVTIPehaRRD 1341
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTlMFTLATFHAGGTNVFVR---RVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1342 AFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDW---IPLDLPRRLRRaapgvrlvaMGGATEAA 1418
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWndmATVDTSPWGRK---------PGGYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1419 IwSNEFVVDDVDPDWASIpYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVhdptgSRWYR 1498
Cdd:cd17636 148 V-MGLATFAALGGGAIGG-AGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-----GGWHH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1499 TGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VP----IHNCTAlgagIVVTGSGAEqfd 1572
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVigVPdprwAQSVKA----IVVLKPGAS--- 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 2181016861 1573 dSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:cd17636 294 -VTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
165-567 |
1.00e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 89.83 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 165 TADADHGEHVAfLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGifwgvfMPLLNGGC--- 241
Cdd:PRK12583 195 QASLDRDDPIN-IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFG------MVLANLGCmtv 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 -TTLIPPHDFVrNPRIWLETVSRFRGNWIGGPDFAYrrcIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDftakfra 320
Cdd:PRK12583 268 gACLVYPNEAF-DPLATLQAVEEERCTALYGVPTMF---IAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRR------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 321 agLRDDVMAPQ----YGLAEAGLGVTgsQTVRvwveksfdADALERGIAvevaqpnpADGRSRALVSCgdgafgwdiQIV 396
Cdd:PRK12583 337 --VMDEMHMAEvqiaYGMTETSPVSL--QTTA--------ADDLERRVE--------TVGRTQPHLEV---------KVV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 397 DPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATtfgARTADGlgpYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRN 475
Cdd:PRK12583 388 DPDGA-TVPRGEIGELCTRGYSVMKGYWNNPEATAE---SIDEDG---WMHTGDlATMDEQGYVRIVGRSKDMIIRGGEN 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 476 HFPNDIEKTVEEaHCGVApggacAVQ----PDapQANGE---WWLVLETGSPVeDLDDLSRILRRRIlAHHETaPERVVW 548
Cdd:PRK12583 461 IYPREIEEFLFT-HPAVA-----DVQvfgvPD--EKYGEeivAWVRLHPGHAA-SEEELREFCKARI-AHFKV-PRYFRF 529
|
410 420
....*....|....*....|..
gi 2181016861 549 VPcrTLPTTTSGKI---RRRET 567
Cdd:PRK12583 530 VD--EFPMTVTGKVqkfRMREI 549
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
175-482 |
1.42e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 89.16 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLqYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDM--HMvswLPLYHDMGIFWGVFMPLLNGGCTTLIPPHD-- 249
Cdd:PRK07514 160 AIL-YTSGTTGRSKGAMLSHGNLLSNALTLVDYWRfTPDDVliHA---LPIFHTHGLFVATNVALLAGASMIFLPKFDpd 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 --FVRNPRiwlETVsrfrgnWIGGPDFaYRRCIE--AFDGTALQSLdlsclRLATNGAEPVRGTTLRDFTAKFRAAGLRd 325
Cdd:PRK07514 236 avLALMPR---ATV------MMGVPTF-YTRLLQepRLTREAAAHM-----RLFISGSAPLLAETHREFQERTGHAILE- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 326 dvmapQYGLAEAGLGVTgsqtvrvwveksfdadalergiavevaqpNPADGRSRAlvscgdGAFGW-----DIQIVDPDR 400
Cdd:PRK07514 300 -----RYGMTETNMNTS-----------------------------NPYDGERRA------GTVGFplpgvSLRVTDPET 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 401 HMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGfRYQGELYVC--GRYRDLIIVGGRNHFP 478
Cdd:PRK07514 340 GAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF---RADG---FFITGDLG-KIDERGYVHivGRGKDLIISGGYNVYP 412
|
....
gi 2181016861 479 NDIE 482
Cdd:PRK07514 413 KEVE 416
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1224-1608 |
2.33e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 88.65 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1224 AMAGLIRTDSDTQD----AGVAVSDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNR 1299
Cdd:PRK06164 139 AIAVVDDAADATPApapgARVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1300 IDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPEHarrDAFHWLSLTTEFGITvwnSVPGLMDML--LIAAGDKAGS 1377
Cdd:PRK06164 219 YDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVF---DAARTARALRRHRVT---HTFGNDEMLrrILDTAGERAD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1378 LPTLRsVFLSGDWIPL--DLPRRLRraAPGVRLVAMGGATEAAIWsneFVVDDVDPDWAS--IPYGYPLANQM-FRVVD- 1451
Cdd:PRK06164 293 FPSAR-LFGFASFAPAlgELAALAR--ARGVPLTGLYGSSEVQAL---VALQPATDPVSVriEGGGRPASPEArVRARDp 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1452 DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECG 1531
Cdd:PRK06164 367 QDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG----YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPA 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1532 EIEHALRGHPLVAAATVVPI-HNCTALGAGIVVTGSGAEqfddSTPGALRAHLAVRLPQYMIPKVFVSCPELPLT--ANG 1608
Cdd:PRK06164 443 EIEHALEALPGVAAAQVVGAtRDGKTVPVAFVIPTDGAS----PDEAGLMAACREALAGFKVPARVQVVEAFPVTesANG 518
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
687-905 |
2.37e-17 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 84.32 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 687 TPLQQAYWVgrgAEQPLGGVGCQTYFELVGaRVDAGRLAAALDALTRRHPMLRATFP-DPGRCL-ITPEAVRLPLAVHDL 764
Cdd:COG4908 2 SPAQKRFLF---LEPGSNAYNIPAVLRLEG-PLDVEALERALRELVRRHPALRTRFVeEDGEPVqRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 765 TDAPVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRL-PHGCIVHFAVDLIIADVTSIGTMLRDLAASYRGE------ 837
Cdd:COG4908 78 SALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLgEDEHVLLLTIHHIISDGWSLGILLRELAALYAALlegepp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 838 KLPAPSATFADLI---------------------QSTSPPPQAcadRLPEGPQLPRVQEADISflRHQHTLSALATKAID 896
Cdd:COG4908 158 PLPELPIQYADYAawqrawlqsealekqleywrqQLAGAPPVL---ELPTDRPRPAVQTFRGA--TLSFTLPAELTEALK 232
|
....*....
gi 2181016861 897 DACHNHGVT 905
Cdd:COG4908 233 ALAKAHGAT 241
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
143-565 |
2.93e-17 |
|
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: 87.56 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 143 GALPIRTPASTADGLAPHPggTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDMHMVSWLP 221
Cdd:cd05969 62 EAIRDRLENSEAKVLITTE--ELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDlHPDDIYWCTADP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 222 LYhDMGIFWGVFMPLLNgGCTTLIPPHDFvrNPRIWLETVSRFRGN-WIGGPDfAYRRCIEAFDGTAlQSLDLSCLRLAT 300
Cdd:cd05969 140 GW-VTGTVYGIWAPWLN-GVTNVVYEGRF--DAESWYGIIERVKVTvWYTAPT-AIRMLMKEGDELA-RKYDLSSLRFIH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 301 NGAEPVRGTTLRDFTAKFraaGLRddvMAPQYGLAEaglgvTGSQTVRVWVekSFDADALERGiavevaQPNPadgrsra 380
Cdd:cd05969 214 SVGEPLNPEAIRWGMEVF---GVP---IHDTWWQTE-----TGSIMIANYP--CMPIKPGSMG------KPLP------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 381 lvscgdgafGWDIQIVDPDRHmTLTDGEVGEIWVgGPGLPD---GYWRQPEQTATTFgartADGlgpYLRTGDAGFR-YQ 456
Cdd:cd05969 268 ---------GVKAAVVDENGN-ELPPGTKGILAL-KPGWPSmfrGIWNDEERYKNSF----IDG---WYLTGDLAYRdED 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 457 GELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVAPGGACAVqPDA-----PQAngewWLVLETG-SPVEDLDDLSRI 530
Cdd:cd05969 330 GYFWFVGRADDIIKTSGHRVGPFEVESALME-HPAVAEAGVIGK-PDPlrgeiIKA----FISLKEGfEPSDELKEEIIN 403
|
410 420 430
....*....|....*....|....*....|....*
gi 2181016861 531 LRRRILAHHeTAPERVVWvpCRTLPTTTSGKIRRR 565
Cdd:cd05969 404 FVRQKLGAH-VAPREIEF--VDNLPKTRSGKIMRR 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-1134 |
3.28e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.84 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2 MSSTPGPPALhdgDRSVPAVFAEWVGRRPDAVALrTVAATGID----DWTYQRLWDHVREirdvafSGLSAGIRIPMALP 77
Cdd:PRK05691 2177 LAGEAGEARL---DQTLHGLFAAQAARTPQAPAL-TFAGQTLSyaelDARANRLARALRE------RGVGPQVRVGLALE 2246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 78 GGADYVAGMLAALAAGLIPVPVylpstrEPQRFLARAQHILRDCEPSAVYTCGELVEVLerdpilGALPIRTP----AST 153
Cdd:PRK05691 2247 RSLEMVVGLLAILKAGGAYVPL------DPEYPLERLHYMIEDSGIGLLLSDRALFEAL------GELPAGVArwclEDD 2314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 154 ADGLAPHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILR--QAAFAANVWNGDD-DMHMVSwlpLYHDMGIfW 230
Cdd:PRK05691 2315 AAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMhcQAVIERFGMRADDcELHFYS---INFDAAS-E 2390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 231 GVFMPLLNGGcttlipphdfvrnpriwlETVSRFRGNW---------------IGGPDFAYRRCIEAFDGTALQSLDLsc 295
Cdd:PRK05691 2391 RLLVPLLCGA------------------RVVLRAQGQWgaeeicqlireqqvsILGFTPSYGSQLAQWLAGQGEQLPV-- 2450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 296 lRLATNGAEPVRGTTLRDFTAKFraaglrddvmAPQYGLAEAGlgvtGSQTVrVWVEKSFDADALERGIA-VEVAQpnpA 374
Cdd:PRK05691 2451 -RMCITGGEALTGEHLQRIRQAF----------APQLFFNAYG----PTETV-VMPLACLAPEQLEEGAAsVPIGR---V 2511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 375 DGRSRALvscgdgafgwdiqIVDPDRhMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGAR--TADGlGPYLRTGD-A 451
Cdd:PRK05691 2512 VGARVAY-------------ILDADL-ALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADpfAADG-GRLYRTGDlV 2576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 452 GFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVAPGGACAVQ-PDAPQANGewWLVLETGSPVEDLDDLsri 530
Cdd:PRK05691 2577 RLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE-HPAVREAVVLALDtPSGKQLAG--YLVSAVAGQDDEAQAA--- 2650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 531 LRRRILAHHETA-PERVV---WVPCRTLPTTTSGKIRRREtlnrLTAGQLEVV--HEVSPRaqapdtpaapDDPPTELAQ 604
Cdd:PRK05691 2651 LREALKAHLKQQlPDYMVpahLILLDSLPLTANGKLDRRA----LPAPDPELNrqAYQAPR----------SELEQQLAQ 2716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 605 HLAAMLGVEPYELapDADLTTLGLTSMMTAQIVewSSSQSRRLDFA--DLYAEPTLRSWQRLFDAAPPVQTGTSSVaaSG 682
Cdd:PRK05691 2717 IWREVLNVERVGL--GDNFFELGGDSILSIQVV--SRARQLGIHFSprDLFQHQTVQTLAAVATHSEAAQAEQGPL--QG 2790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 683 PWPTTPLQQAYWVGRGAEQPLGGvgcQTYFELVGARVDAGRLAAALDALTRRHPMLRATFPD-PGRCLITPEAVRLPLAV 761
Cdd:PRK05691 2791 ASGLTPIQHWFFDSPVPQPQHWN---QALLLEPRQALDPALLEQALQALVEHHDALRLRFSQaDGRWQAEYRAVTAQELL 2867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 762 HDLTDAPVTTRDTHLAEIRRRLrthrfDIETGDTWTVELTRLPHG------CIVHFAVDLIiadvtSIGTMLRDLAASYR 835
Cdd:PRK05691 2868 WQVTVADFAECAALFADAQRSL-----DLQQGPLLRALLVDGPQGqqrlllAIHHLVVDGV-----SWRVLLEDLQALYR 2937
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 836 ------GEKLPAPSATFADLiqSTSPPPQACADRLPE----------GP--QLPRVQEADISFLRHQHTLSALAtkaidD 897
Cdd:PRK05691 2938 qlsagaEPALPAKTSAFRDW--AARLQAYAGSESLREelgwwqaqlgGPraELPCDRPQGGNLNRHAQTVSVRL-----D 3010
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 898 ACHNHGVTRAA----------VLLAAYTLVLRRWASQDDFLVNVTTFGRSPEVSDV-----VGDFTETHLYRAQLDgqiS 962
Cdd:PRK05691 3011 AERTRQLLQQApaayrtqvndLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIdltrsVGWFTSAYPLRLTPA---P 3087
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 963 FVDQAQVTQ-KGLRTALRAAPAPDL-------LATQL-RSGTGHSGIVPVVFTYA-------ADSPLLSAEDANTLGAID 1026
Cdd:PRK05691 3088 GDDAARGESiKAIKEQLRAVPHKGLgygvlryLADAAvREAMAALPQAPITFNYLgqfdqsfASDALFRPLDEPAGPAHD 3167
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1027 EVVSMTPQVLIDHQAcrLGDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLERLGGH---DWSTPATPGLSAHSRLARAHRN 1103
Cdd:PRK05691 3168 PDAPLPNELSVDGQV--YGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHclaDGAGGLTPSDFPLAQLTQAQLD 3245
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1104 ATTTPAPA------------------------GLLY--DAFRENAATHPARLALRWR 1134
Cdd:PRK05691 3246 ALPVPAAEiedvypltpmqeglllhtllepgtGLYYmqDRYRINSALDPERFAQAWQ 3302
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
2556-2773 |
3.66e-17 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 83.55 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2556 HCYFEFElADFDRPRFDSAARQLVARHAGLRTTVSPAGTDA----ASSGEVAV-VHTAPIEPVVRDHDDVRAAMRDQI-- 2628
Cdd:COG4908 21 PAVLRLE-GPLDVEALERALRELVRRHPALRTRFVEEDGEPvqriDPDADLPLeVVDLSALPEPEREAELEELVAEEAsr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2629 -IDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQ---LPPLETSFAHYV-WNHpellp 2703
Cdd:COG4908 100 pFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEpppLPELPIQYADYAaWQR----- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2704 daDEAVLPRLAASRDYWRARLPSLPPAPKLADMSLLFEIEEPRFERATATIPAVDWSQVTRSCRAEGVTV 2773
Cdd:COG4908 175 --AWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKAHGATV 242
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1259-1612 |
4.35e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 87.91 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1259 IDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdfdlsvYDTFGA----LGC---GAQL 1331
Cdd:PRK12583 198 LDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL------YHCFGMvlanLGCmtvGACL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1332 VTIPEHArrDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAM 1411
Cdd:PRK12583 272 VYPNEAF--DPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1412 GGATEAAIWSNEFVV-DDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDrfVHD 1490
Cdd:PRK12583 350 YGMTETSPVSLQTTAaDDLERRVETV--GRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAE--SID 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1491 PTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VPihnCTALGAGIVV----- 1563
Cdd:PRK12583 426 EDG--WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVfgVP---DEKYGEEIVAwvrlh 500
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2181016861 1564 TGSGAEQFDdstpgaLRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK12583 501 PGHAASEEE------LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
179-465 |
4.78e-17 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 88.83 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 179 YSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGgcttliPPHDFVRNP---R 255
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEG------IKVVYHPDPtdaL 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 256 IWLETVSRFRGNW-IGGPDF--AYRRCIEAfdgtalQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaGLRddvmapqy 332
Cdd:PRK08633 863 GIAKLVAKHRATIlLGTPTFlrLYLRNKKL------HPLMFASLRLVVAGAEKLKPEVADAFEEKF---GIR-------- 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 333 gLAEaGLGVTG-SQTVRVWVEKSFDADALE-----RGiavEVAQPNPadgrsralvscgdgafGWDIQIVDPDRHMTLTD 406
Cdd:PRK08633 926 -ILE-GYGATEtSPVASVNLPDVLAADFKRqtgskEG---SVGMPLP----------------GVAVRIVDPETFEELPP 984
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 407 GEVGEIWVGGPGLPDGYWRQPEQTATTFgaRTADGLGPYLrTGDAGF-RYQGELYVCGRY 465
Cdd:PRK08633 985 GEDGLILIGGPQVMKGYLGDPEKTAEVI--KDIDGIGWYV-TGDKGHlDEDGFLTITDRY 1041
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
2531-2850 |
8.50e-17 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 85.43 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2531 FPLTVVQnayragrEG--ALILGGVAAHCY-FEFELA-DFDRPRFDSAARQLVARHAGLRTTVSPagtDAASSGEVAVVH 2606
Cdd:cd19545 2 YPCTPLQ-------EGlmALTARQPGAYVGqRVFELPpDIDLARLQAAWEQVVQANPILRTRIVQ---SDSGGLLQVVVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2607 TAPIEpvVRDHDDVRAAMRDQ---IIDLTArPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQ 2683
Cdd:cd19545 72 ESPIS--WTESTSLDEYLEEDraaPMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2684 LPPLeTSFAHYVWNHpellpdadeavlpRLAASRDYWRARL-----PSLPPAPKLADMSllfeieeprfeRATATIPA-V 2757
Cdd:cd19545 149 PPPF-SRFVKYLRQL-------------DDEAAAEFWRSYLagldpAVFPPLPSSRYQP-----------RPDATLEHsI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2758 DWSQVTRScraeGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDPDVVGIENVVGDFTSLVLLECRVDEPASIWESV 2837
Cdd:cd19545 204 SLPSSASS----GVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFL 279
|
330
....*....|...
gi 2181016861 2838 RALQRQLMTDLPH 2850
Cdd:cd19545 280 QTVQKDLLDMIPF 292
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1253-1615 |
1.05e-16 |
|
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: 86.40 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1253 PTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTF-GALGCGAQl 1331
Cdd:cd05970 176 PTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIyGQWIAGAA- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1332 VTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMdMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRrAAPGVRLVAM 1411
Cdd:cd05970 255 VFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIY-RFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK-EKTGIKLMEG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1412 GGATEAAIWSNEFVVDDVDPDWASIPY-GYPLanqmfRVVDDNGDDQPDYVAGELWIGGA-----GVALGYHNAPELTSD 1485
Cdd:cd05970 333 FGQTETTLTIATFPWMEPKPGSMGKPApGYEI-----DLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1486 RFvHDPtgsrWYRTGDMGcyWRD--GTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLV--AAATVVP--IHNcTALGA 1559
Cdd:cd05970 408 VW-HDG----YYHTGDAA--WMDedGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVleCAVTGVPdpIRG-QVVKA 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1560 GIVVTgsgaeqfDDSTPG-----ALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05970 480 TIVLA-------KGYEPSeelkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
15-573 |
1.07e-16 |
|
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: 86.35 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 15 DRSVPAVFAEWVGRRPDAVALrtvaatgIDD---WTYQRLWdhvREIRDVAFS----GLSAGIRIPMALPGGADYVAGML 87
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAV-------VDGerrLSYAELD---RRADRLAAGllalGLRPGDRVVVQLPNVAEFVIVFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 88 AALAAGLIPVPVyLPSTREpqrflARAQHILRDCEPSAVYTCGE---------LVEVLERDPILGALPIRTPASTA---D 155
Cdd:COG1021 94 ALFRAGAIPVFA-LPAHRR-----AEISHFAEQSEAVAYIIPDRhrgfdyralARELQAEVPSLRHVLVVGDAGEFtslD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 156 GLAPHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDMHMVSwLPLYHDM-----GIF 229
Cdd:COG1021 168 ALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGlDADTVYLAA-LPAAHNFplsspGVL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 230 wGVFMpllNGGCTTLIP-PhdfvrNPRIWLETVSRFRGNWIG-GPdFAYRRCIEAfdgTALQSLDLSCLRLATNGAepvr 307
Cdd:COG1021 247 -GVLY---AGGTVVLAPdP-----SPDTAFPLIERERVTVTAlVP-PLALLWLDA---AERSRYDLSSLRVLQVGG---- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 308 gttlrdftAKFrAAGLRDDVmapqyglaEAGLGVTGSQtvrvwvekSFdadalerGIAvE--VAQPNPADGRSRAL---- 381
Cdd:COG1021 310 --------AKL-SPELARRV--------RPALGCTLQQ--------VF-------GMA-EglVNYTRLDDPEEVILttqg 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 382 --VSCGDgafgwDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGD-AGFRYQGE 458
Cdd:COG1021 357 rpISPDD-----EVRIVDEDGN-PVPPGEVGELLTRGPYTIRGYYRAPEHNARAF---TPDG---FYRTGDlVRRTPDGY 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 459 LYVCGRYRDLIIVGGRNHFPNDIEKTVeEAHCGVApggACAV--QPDApqANGE---WWLVLETGSPveDLDDLSRILRR 533
Cdd:COG1021 425 LVVEGRAKDQINRGGEKIAAEEVENLL-LAHPAVH---DAAVvaMPDE--YLGErscAFVVPRGEPL--TLAELRRFLRE 496
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2181016861 534 RILAHHEtAPERVVWVPcrTLPTTTSGKIRRRETLNRLTA 573
Cdd:COG1021 497 RGLAAFK-LPDRLEFVD--ALPLTAVGKIDKKALRAALAA 533
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1103-1610 |
2.31e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 85.37 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1103 NATTTPAPAGLLYDAFRENAATHPARLALRWRpddyrgerhgdviaqDRSqLTYGELDELARSVAravaarhaaGSVIGI 1182
Cdd:PRK08316 2 MERSTRARRQTIGDILRRSARRYPDKTALVFG---------------DRS-WTYAELDAAVNRVA---------AALLDL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1183 QLPKGPSqiVAVLG------------VMMAGCTYLPVG-----------VDQPAERLsrICARSAMAGLIRTDSD----- 1234
Cdd:PRK08316 57 GLKKGDR--VAALGhnsdayallwlaCARAGAVHVPVNfmltgeelayiLDHSGARA--FLVDPALAPTAEAALAllpvd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1235 ---------TQDAGVAVSDITAMIECAPTDP--IRIDPHDAAYVIYTSGSTGEPKGVLVSHAAAL----NTIVDVnrrnR 1299
Cdd:PRK08316 133 tlilslvlgGREAPGGWLDFADWAEAGSVAEpdVELADDDLAQILYTSGTESLPKGAMLTHRALIaeyvSCIVAG----D 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1300 IDTHDRLL-AL-----SALDFDLSVYDTFGALGCGAQLVTIPEHARRDAFHwlSLTTEFGI-TVWNSvpglmdMLLIAAG 1372
Cdd:PRK08316 209 MSADDIPLhALplyhcAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAE--RITSFFAPpTVWIS------LLRHPDF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1373 DKAgSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVD--PDWAsipyGYPLANQMFRVV 1450
Cdd:PRK08316 281 DTR-DLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAPLATVLGPEEHLrrPGSA----GRPVLNVETRVV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1451 DDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVEC 1530
Cdd:PRK08316 356 DDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG-----WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVAS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1531 GEIEHALRGHPLVAAATV--VP----IHNCTAlgagIVVTGSGAeqfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPL 1604
Cdd:PRK08316 431 REVEEALYTHPAVAEVAVigLPdpkwIEAVTA----VVVPKAGA----TVTEDELIAHCRARLAGFKVPKRVIFVDELPR 502
|
....*.
gi 2181016861 1605 TANGKV 1610
Cdd:PRK08316 503 NPSGKI 508
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1250-1568 |
2.63e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 85.28 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1250 ECAPTDPIRidPHDAAYVIYTSGSTGEPKGVLVSHA---AALNTIVDVNRRNRIDTHDRLLALSALD----FDLSVYDTf 1322
Cdd:PLN02574 188 DFVPKPVIK--QDDVAAIMYSSGTTGASKGVVLTHRnliAMVELFVRFEASQYEYPGSDNVYLAALPmfhiYGLSLFVV- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1323 GALGCGAQLVTIpehARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAA-GDKAGSLPTLRSVF-----LSGDWIpldlp 1396
Cdd:PLN02574 265 GLLSLGSTIVVM---RRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQVScgaapLSGKFI----- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1397 RRLRRAAPGVRLVAMGGATE-AAIWSNEFVVDDVDpDWASIpyGYPLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVAL 1474
Cdd:PLN02574 337 QDFVQTLPHVDFIQGYGMTEsTAVGTRGFNTEKLS-KYSSV--GLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMK 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1475 GYHNAPELTSDRFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHN- 1553
Cdd:PLN02574 414 GYLNNPKATQSTIDKDG----WLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDk 489
|
330
....*....|....*.
gi 2181016861 1554 -CTALGAGIVVTGSGA 1568
Cdd:PLN02574 490 eCGEIPVAFVVRRQGS 505
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1261-1615 |
2.79e-16 |
|
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: 84.85 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1261 PHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDtfGALGC---GAQLVTIP-- 1335
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIA--FHLAPliaGMNQYLMPtr 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1336 EHARRDAFhWLSLTTEFGITVWNSvPGLMDMLLIAA--GDKAGS--LPTLRSVFLSGDWIPLDL---------PRRLRR- 1401
Cdd:cd05908 183 LFIRRPIL-WLKKASEHKATIVSS-PNFGYKYFLKTlkPEKANDwdLSSIRMILNGAEPIDYELchefldhmsKYGLKRn 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1402 ----------AAPGVRLVAMGGATEAAIWSNEFV--------VDDVDPDWAS-IPYGYPLANQMFRVVDDNGDDQPDYVA 1462
Cdd:cd05908 261 ailpvyglaeASVGASLPKAQSPFKTITLGRRHVthgepepeVDKKDSECLTfVEVGKPIDETDIRICDEDNKILPDGYI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1463 GELWIGGAGVALGYHNAPELTSDRFVHDPtgsrWYRTGDMGcYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPL 1542
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFTDDG----WLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1543 VAAATVVPI--HNCTALGAGIVVTGSGAEQFDDSTPGA--LRAHLAVRlPQYMIPKVfVSCPELPLTANGKVDRGKI 1615
Cdd:cd05908 416 VELGRVVACgvNNSNTRNEEIFCFIEHRKSEDDFYPLGkkIKKHLNKR-GGWQINEV-LPIRRIPKTTSGKVKRYEL 490
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
178-566 |
3.05e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 85.25 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 178 QYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDmHMVSWLPLYHDMGIFWGVfMPLLNGGCTTLIPPHDFvrNPRI 256
Cdd:PRK08315 205 QYTSGTTGFPKGATLTHRNILNNGYFIGEAMKlTEED-RLCIPVPLYHCFGMVLGN-LACVTHGATMVYPGEGF--DPLA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 257 WLETVSRFRGNWIGG-----------PDFAyrrcieafdgtalqSLDLSCLR---LAtnGAE-PVRgtTLRDFTAKFraa 321
Cdd:PRK08315 281 TLAAVEEERCTALYGvptmfiaeldhPDFA--------------RFDLSSLRtgiMA--GSPcPIE--VMKRVIDKM--- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 322 GLRDDVMApqYGLAEAGLGVTgsQTvRVwveksfdADALERGIA-VEVAQPNPadgrsralvscgdgafgwDIQIVDPDR 400
Cdd:PRK08315 340 HMSEVTIA--YGMTETSPVST--QT-RT-------DDPLEKRVTtVGRALPHL------------------EVKIVDPET 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 401 HMTLTDGEVGEIWVGGPGLPDGYWRQPEQTAttfGARTADGlgpYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPN 479
Cdd:PRK08315 390 GETVPRGEQGELCTRGYSVMKGYWNDPEKTA---EAIDADG---WMHTGDlAVMDEEGYVNIVGRIKDMIIRGGENIYPR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 480 DIektvEE---AHCGVApggacAVQ----PDAPQanGE---WWLVLETGSPVeDLDDLSRILRRRIlAHHETaPERVVWV 549
Cdd:PRK08315 464 EI----EEflyTHPKIQ-----DVQvvgvPDEKY--GEevcAWIILRPGATL-TEEDVRDFCRGKI-AHYKI-PRYIRFV 529
|
410 420
....*....|....*....|
gi 2181016861 550 PcrTLPTTTSGKIRR---RE 566
Cdd:PRK08315 530 D--EFPMTVTGKIQKfkmRE 547
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1707-2131 |
3.11e-16 |
|
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: 86.06 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1707 ADPASEASESAADVGEPVTPGEGFPLTRLQQAYTLGAAGLNGSTCAPTYFAVVLAAAPESAGIDLDRFARVVTRCVDEFA 1786
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1787 MLRCALDADTTQRVQVDAGPVPVHDLDIQDDPDLLLRRMAAAPFDPHSVPVIQCFAPSRSPRHVGLL---ISYLGLDARS 1863
Cdd:COG1020 81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLalhHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1864 LSTVVTTIIAEYQSQPRPRQVDPTAAVFARFASESAWGENDVDNSV-----------AGPPLLPLHDQRRDPFERVTFAR 1932
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARqlaywrqqlagLPPLLELPTDRPRPAVQSYRGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1933 RSFTIEEQAAATLREHAAHLGVTPTALVFEAFAHALASIGAGQRFAVTVPKSYRPDyaPADREVLGNFTRLALCEVDyga 2012
Cdd:COG1020 241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVD--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2013 VRPGS--AEAVAAAQRELWRAVSHD----GDITGGLAATRTAGGYPvVFTSTLGLTHQDASGL-------TNVRTLTQTP 2079
Cdd:COG1020 316 LSGDPsfAELLARVRETLLAAYAHQdlpfERLVEELQPERDLSRNP-LFQVMFVLQNAPADELelpgltlEPLELDSGTA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 2080 GVWLDCQTEDEVAGIRMSWDIATNVVAAESISVAFSRFEEAVRRHAGQAEPP 2131
Cdd:COG1020 395 KFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQP 446
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1263-1611 |
3.41e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 84.94 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSH---------------AAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGC 1327
Cdd:PRK07798 164 DDLYLLYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWAAFAALFS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1328 GaQLVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGS--LPTLRSVFLSGDWIPLDLPRRLRRAAPG 1405
Cdd:PRK07798 244 G-QTVVLLPDVRFDADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPydLSSLFAIASGGALFSPSVKEALLELLPN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1406 VRLVAMGGATEAAIWSNEFVVDDvdpdwaSIPYGYPL--ANQMFRVVDDNGDDQPDYVAGELWIGGAG-VALGYHNAPEL 1482
Cdd:PRK07798 323 VVLTDSIGSSETGFGGSGTVAKG------AVHTGGPRftIGPRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1483 TSDRFvhdPT--GSRWYRTGDMGCYWRDGTLQFLGRaDSQVkIR--GHRVECGEIEHALRGHPLVAAATVVPIHNcTALG 1558
Cdd:PRK07798 397 TAETF---PTidGVRYAIPGDRARVEADGTITLLGR-GSVC-INtgGEKVFPEEVEEALKAHPDVADALVVGVPD-ERWG 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 1559 ---AGIVVTGSGAeqfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:PRK07798 471 qevVAVVQLREGA----RPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2564-2851 |
4.62e-16 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 83.65 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2564 ADFDRPRFDSAARQLVARHAGLRTTVSPAGTDAAssgeVAVVHTAPIEPVVRD---HDDVRAAMRDQIIDLTARPGIDFG 2640
Cdd:cd19536 34 RRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQP----VQVVHRQAQVPVTELdltPLEEQLDPLRAYKEETKIRRFDLG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2641 ---------VQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGET---VDQLPPlETSFAHYVWNHPELLPDAdea 2708
Cdd:cd19536 110 raplvraalVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLeykPLSLPP-AQPYRDFVAHERASIQQA--- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2709 vlprlaASRDYWRARLP--SLPPAPKLADMsllfEIEEPRFERATATIPAVDWSQVTRScRAEGVTVASFLLANYARVLS 2786
Cdd:cd19536 186 ------ASERYWREYLAgaTLATLPALSEA----VGGGPEQDSELLVSVPLPVRSRSLA-KRSGIPLSTLLLAAWALVLS 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 2787 RWSGTDHFCINVTLFDRDPDVVGIENVVGDFtsLVLLECRVDEPASIW-ESVRALQRQLMTDLPHR 2851
Cdd:cd19536 255 RHSGSDDVVFGTVVHGRSEETTGAERLLGLF--LNTLPLRVTLSEETVeDLLKRAQEQELESLSHE 318
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
712-1078 |
4.64e-16 |
|
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: 83.58 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 712 FELVGArVDAGRLAAALDALTRRHPMLRATF--PDPGRCLITPEAVRLPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRFD 789
Cdd:cd19539 30 WRLTGP-LDVEALREALRDVVARHEALRTLLvrDDGGVPRQEILPPGPAPLEVRDLSDPDSDRERRLEELLRERESRGFD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 790 IEtgDTWTVELTRLPHGCIVHFAVDL---IIADVTSIGTMLRDLAASYRGEK------LPAPSATFADLI-----QSTSP 855
Cdd:cd19539 109 LD--EEPPIRAVLGRFDPDDHVLVLVahhTAFDAWSLDVFARDLAALYAARRkgpaapLPELRQQYKEYAawqreALAAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 856 PPQACADR----------LPEGPQLPRVQEADISFLRHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQD 925
Cdd:cd19539 187 RAAELLDFwrrrlrgaepTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 926 DFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKGLRTALR--AAPAPDLLAT--QLRSGTGHsGI 1000
Cdd:cd19539 267 DIVVGTPVAGRNhPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRhqELPFQQLVAElpVDRDAGRH-PL 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1001 VPVVFTYAADSPLLSAEDANTLGAIDEVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLERL 1078
Cdd:cd19539 346 VQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQL 423
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
175-566 |
6.50e-16 |
|
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: 83.25 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILRQAA---FAANVWNGDDDmhmVSWLPL-YHDMGIFWGVFMPLLNGGCTTLipPHDF 250
Cdd:cd05971 91 ALIIYTSGTTGPPKGALHAHRVLLGHLPgvqFPFNLFPRDGD---LYWTPAdWAWIGGLLDVLLPSLYFGVPVL--AHRM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 251 VR-NPRIWLETVSRFRGNWIGGPDFAYRrcIEAFDGTALQSLDLSCLRLATnGAEPVRGTTLRDFTAKFRAAglrddvMA 329
Cdd:cd05971 166 TKfDPKAALDLMSRYGVTTAFLPPTALK--MMRQQGEQLKHAQVKLRAIAT-GGESLGEELLGWAREQFGVE------VN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 330 PQYGLAEAGLgVTGSQTVrvwveksfdadalergiaveVAQPNPAdgrsralvSCGDGAFGWDIQIVDpDRHMTLTDGEV 409
Cdd:cd05971 237 EFYGQTECNL-VIGNCSA--------------------LFPIKPG--------SMGKPIPGHRVAIVD-DNGTPLPPGEV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 410 GEIWVGgpgLPD-----GYWRQPEQTATTFgartadgLGPYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEK 483
Cdd:cd05971 287 GEIAVE---LPDpvaflGYWNNPSATEKKM-------AGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 484 TVEEaHCGVAPGGACAVqPDApqANGEW---WLVLETGspVEDLDDLSRILR---RRILAHHETaPERVVWVPcrTLPTT 557
Cdd:cd05971 357 CLLK-HPAVLMAAVVGI-PDP--IRGEIvkaFVVLNPG--ETPSDALAREIQelvKTRLAAHEY-PREIEFVN--ELPRT 427
|
....*....
gi 2181016861 558 TSGKIRRRE 566
Cdd:cd05971 428 ATGKIRRRE 436
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
162-565 |
7.46e-16 |
|
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: 83.19 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 162 GGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN---GDDDMHmvsWLPLYHDMGIfWGVFMPLLN 238
Cdd:cd17649 84 GAGLLLTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGltpGDRELQ---FASFNFDGAH-EQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 239 GGCTtLIPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDgtALQSLDLSCLRLATNGAEPVRGTTLRDftakf 318
Cdd:cd17649 160 GACV-VLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEAD--RTGDGRPPSLRLYIFGGEALSPELLRR----- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 319 raAGLRDDVMAPQYGLAEAGLgvtgsqTVRVWVEKSFDADAlerGIAVEVAQPNPadGRSralvscgdgafgwdIQIVDP 398
Cdd:cd17649 232 --WLKAPVRLFNAYGPTEATV------TPLVWKCEAGAARA---GASMPIGRPLG--GRS--------------AYILDA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 399 DRHMtLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGRYRDLIIVGGRNH 476
Cdd:cd17649 285 DLNP-VPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLyRTGDlARWRDDGVIEYLGRVDHQVKIRGFRI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 477 FPNDIEKTVEEaHCGVAPGGACAVQPDAPQAngewwLV--LETGSPVEDLDDLSRI---LRRRILAHheTAPERVVWVPc 551
Cdd:cd17649 364 ELGEIEAALLE-HPGVREAAVVALDGAGGKQ-----LVayVVLRAAAAQPELRAQLrtaLRASLPDY--MVPAHLVFLA- 434
|
410
....*....|....
gi 2181016861 552 rTLPTTTSGKIRRR 565
Cdd:cd17649 435 -RLPLTPNGKLDRK 447
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
170-487 |
8.32e-16 |
|
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: 83.18 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 170 HGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYH------DMGIF-WGVFMpllngGCT 242
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHsyersaEYFIFaCGCSQ-----AYT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 243 TL---------IPPHDFVRNPRIWLETVSRFRGNWIGGPdfAYRRCIeafdgtALQSLDLSCLRLATNGaepvrGTTLRD 313
Cdd:cd17640 161 SIrtlkddlkrVKPHYIVSVPRLWESLYSGIQKQVSKSS--PIKQFL------FLFFLSGGIFKFGISG-----GGALPP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 314 FTAKF-RAAGLRddvMAPQYGLAEAGLGVTGSQTvrvwveksfdadalergiavevaqPNPADGrsralvSCGDGAFGWD 392
Cdd:cd17640 228 HVDTFfEAIGIE---VLNGYGLTETSPVVSARRL------------------------KCNVRG------SVGRPLPGTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 393 IQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATtfgARTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIV 471
Cdd:cd17640 275 IKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK---VLDSDG---WFNTGDLGwLTCGGELVLTGRAKDTIVL 348
|
330
....*....|....*..
gi 2181016861 472 -GGRNHFPNDIEKTVEE 487
Cdd:cd17640 349 sNGENVEPQPIEEALMR 365
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1237-1610 |
1.05e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 83.17 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1237 DAGVAVSDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPK-GVLVSHAAAL---NTIVDVNRrnriDT--HDRLLALS 1310
Cdd:PRK07470 138 RAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKaAVLTHGQMAFvitNHLADLMP----GTteQDASLVVA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1311 ALdfdlsvydTFGA-------LGCGAQLVTIPEHaRRDAFHWLSLTTEFGITVWNSVPGLMDMLL----IAAGDKAgslp 1379
Cdd:PRK07470 214 PL--------SHGAgihqlcqVARGAATVLLPSE-RFDPAEVWALVERHRVTNLFTVPTILKMLVehpaVDRYDHS---- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1380 TLRSVFLSGdwIPL---DLPRRLRRAAPG-VRLVAMGGAT------EAAIWSnefvVDDvDPDWASIPYGYPLANQMFRV 1449
Cdd:PRK07470 281 SLRYVIYAG--APMyraDQKRALAKLGKVlVQYFGLGEVTgnitvlPPALHD----AED-GPDARIGTCGFERTGMEVQI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1450 VDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRAdSQVKIRG-HRV 1528
Cdd:PRK07470 354 QDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG-----WFRTGDLGHLDARGFLYITGRA-SDMYISGgSNV 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1529 ECGEIEHALRGHPLVAAATV--VPIHNCTALGAGIVVTGSGAeqfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTA 1606
Cdd:PRK07470 428 YPREIEEKLLTHPAVSEVAVlgVPDPVWGEVGVAVCVARDGA----PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSG 503
|
....
gi 2181016861 1607 NGKV 1610
Cdd:PRK07470 504 YGKI 507
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
718-1007 |
1.33e-15 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. 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: 82.31 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 718 RVDAGRLAAALDALTRRHPMLRATF--PDPGRCLITPEAVRLPLAVHDLTDApvTTRDTHLAEIRRRLRTHRFDIETGDT 795
Cdd:cd20483 35 KPDVNLLQKALSELVRRHEVLRTAYfeGDDFGEQQVLDDPSFHLIVIDLSEA--ADPEAALDQLVRNLRRQELDIEEGEV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 796 WTVELTRLPHgciVHFAVDLI---IA-DVTSIGTMLRDLAASY---RGEK----LPAPSATFAD-------LIQSTS--- 854
Cdd:cd20483 113 IRGWLVKLPD---EEFALVLAshhIAwDRGSSKSIFEQFTALYdalRAGRdlatVPPPPVQYIDftlwhnaLLQSPLvqp 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 855 ------------PP-----PQACADRlPEGPQLPRVqeadisflRHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLV 917
Cdd:cd20483 190 lldfwkeklegiPDaskllPFAKAER-PPVKDYERS--------TVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 918 LRRWASQDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKGLRTALRAAPAP-DLLATQL---R 992
Cdd:cd20483 261 LYRYTEDEDLTIGMVDGDRPhPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPfDYIVDALdvpR 340
|
330
....*....|....*
gi 2181016861 993 SgTGHSGIVPVVFTY 1007
Cdd:cd20483 341 S-TSHFPIGQIAVNY 354
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
172-565 |
1.56e-15 |
|
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: 82.13 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSIlrqaAFAANVWngDDDMHMVSWLPLYHDMG-----IFWGVFM-PLLNGGcTTLI 245
Cdd:cd17650 93 EDLAYVIYTSGTTGKPKGVMVEHRNV----AHAAHAW--RREYELDSFPVRLLQMAsfsfdVFAGDFArSLLNGG-TLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 246 PPHDFVRNPRIWLETVSRFRgnwIGGPDFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRaAGLRd 325
Cdd:cd17650 166 CPDEVKLDPAALYDLILKSR---ITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFG-QGMR- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 326 dvMAPQYGLAEAGLGVTGSQTvrvwveksfDADALERGIAVEVAQPNPADGrsralvscgdgafgwdIQIVDPDRHMTLT 405
Cdd:cd17650 241 --IINSYGVTEATIDSTYYEE---------GRDPLGDSANVPIGRPLPNTA----------------MYVLDERLQPQPV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 406 dGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEkT 484
Cdd:cd17650 294 -GVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDlARWRADGNVELLGRVDHQVKIRGFRIELGEIE-S 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 485 VEEAHCGVAPgGACAVQPDapqANGEWWLVLETgSPVEDLDdlSRILRRRILAHHETAPERVVWVPCRTLPTTTSGKIRR 564
Cdd:cd17650 372 QLARHPAIDE-AVVAVRED---KGGEARLCAYV-VAAATLN--TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
.
gi 2181016861 565 R 565
Cdd:cd17650 445 R 445
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1201-1551 |
1.58e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 82.23 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1201 GCTYLPVGVDQPAERLSRICARSAMA-GLIRTDSDTQDAGVAVSditaMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKG 1279
Cdd:PRK09029 77 GARVLPLNPQLPQPLLEELLPSLTLDfALVLEGENTFSALTSLH----LQLVEGAHAVAWQPQRLATMTLTSGSTGLPKA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1280 VLVSHAAALNTIVDVNRRNRIDTHDRLLaLSaldfdLSVYDTFGA------LGCGAQLVtIPEHArrDAFHWLSlttefG 1353
Cdd:PRK09029 153 AVHTAQAHLASAEGVLSLMPFTAQDSWL-LS-----LPLFHVSGQgivwrwLYAGATLV-VRDKQ--PLEQALA-----G 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1354 ITVWNSVPGLMDMLLiaaGDKAGSLpTLRSVFLSGDWIPLDLPRRLRraAPGVRLVAMGGATEAAiwSNEFVV-----DD 1428
Cdd:PRK09029 219 CTHASLVPTQLWRLL---DNRSEPL-SLKAVLLGGAAIPVELTEQAE--QQGIRCWCGYGLTEMA--STVCAKradglAG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1429 VdpdwasipyGYPLANQMFRVVDDngddqpdyvagELWIGGAGVALGYHNAPELTSdrfVHDPTGsrWYRTGDMGCyWRD 1508
Cdd:PRK09029 291 V---------GSPLPGREVKLVDG-----------EIWLRGASLALGYWRQGQLVP---LVNDEG--WFATRDRGE-WQN 344
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2181016861 1509 GTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI 1551
Cdd:PRK09029 345 GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPV 387
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
171-562 |
1.60e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 80.99 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPHDF 250
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 251 vRNP----RIWlETVSRFRGNWIGGPDFAYRRCIEAFDGTalqslDLSCLRLATNGAEPVRGTTLRDFTAkfrAAGLRdd 326
Cdd:cd05944 81 -RNPglfdNFW-KLVERYRITSLSTVPTVYAALLQVPVNA-----DISSLRFAMSGAAPLPVELRARFED---ATGLP-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 327 vMAPQYGLAEAGLGVTgsqtvrvwveKSFDADALERGiavEVAQPNPAdGRSRALVSCGDGAFGWDIQIvdpdrhmtltd 406
Cdd:cd05944 149 -VVEGYGLTEATCLVA----------VNPPDGPKRPG---SVGLRLPY-ARVRIKVLDGVGRLLRDCAP----------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 407 GEVGEIWVGGPGLPDGYwrqpeqtATTFGARTADGLGPYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTV 485
Cdd:cd05944 203 DEVGEICVAGPGVFGGY-------LYTEGNKNAFVADGWLNTGDLGrLDADGYLFITGRAKDLIIRGGHNIDPALIEEAL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 486 eEAHCGVAPGGACAvQPDA-----PQAngewWLVLETGSPVEDlDDLSRILRRRIlaHHETAPERVVWvPCRTLPTTTSG 560
Cdd:cd05944 276 -LRHPAVAFAGAVG-QPDAhagelPVA----YVQLKPGAVVEE-EELLAWARDHV--PERAAVPKHIE-VLEELPVTAVG 345
|
..
gi 2181016861 561 KI 562
Cdd:cd05944 346 KV 347
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1250-1612 |
1.62e-15 |
|
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: 83.07 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1250 ECAPTDpirIDPHDAAYVIYTSGSTGEPKGVLVS------HAAAlntivdvnrrnridTHDRLlalsaldFDLSVYDTF- 1322
Cdd:TIGR02188 228 YCEPEP---MDSEDPLFILYTSGSTGKPKGVLHTtggyllYAAM--------------TMKYV-------FDIKDGDIFw 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1323 ----------------GALGCGAQLV------TIPEHARrdafhWLSLTTEFGITVWNSVPGLMDMlLIAAGD---KAGS 1377
Cdd:TIGR02188 284 ctadvgwitghsyivyGPLANGATTVmfegvpTYPDPGR-----FWEIIEKHKVTIFYTAPTAIRA-LMRLGDewvKKHD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1378 LPTLR---SVflsGDWIpldlprrlrraAPgvrlvamggatEAAIWSNEFVVDD----VDPDW---------ASIP---- 1437
Cdd:TIGR02188 358 LSSLRllgSV---GEPI-----------NP-----------EAWMWYYKVVGKErcpiVDTWWqtetggimiTPLPgatp 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1438 -----YGYPLANQMFRVVDDNGDDQPD-YVAGELWIGGA--GVALGYHNAPEltsdRFVHD--PTGSRWYRTGDMGCYWR 1507
Cdd:TIGR02188 413 tkpgsATLPFFGIEPAVVDEEGNPVEGpGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTyfSPFPGYYFTGDGARRDK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1508 DGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTAlGAGIV--VTGSGAEQFDDSTPGALRAHLAV 1585
Cdd:TIGR02188 489 DGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIK-GQAIYafVTLKDGYEPDDELRKELRKHVRK 567
|
410 420
....*....|....*....|....*..
gi 2181016861 1586 RLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:TIGR02188 568 EIGPIAKPDKIRFVPGLPKTRSGKIMR 594
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
2551-2850 |
1.82e-15 |
|
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: 81.66 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2551 GGVAAHCYFEFEL-ADFDRPRFDSAARQLVARHAGLRTTVSPAGTD-------AASSGEVAVVH-TAPIEPVVRDHDDVR 2621
Cdd:cd19539 20 GGPAYNIPGAWRLtGPLDVEALREALRDVVARHEALRTLLVRDDGGvprqeilPPGPAPLEVRDlSDPDSDRERRLEELL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2622 AAMRDQIIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGET---VDQLPPLETSFAHYVWNH 2698
Cdd:cd19539 100 RERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpAAPLPELRQQYKEYAAWQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2699 PELLPDadeavlPRLAASRDYWRARLPSLPPAPKLADmsllfeieEPRFERATAT-------IPAVDWSQVTRSCRAEGV 2771
Cdd:cd19539 180 REALAA------PRAAELLDFWRRRLRGAEPTALPTD--------RPRPAGFPYPgadlrfeLDAELVAALRELAKRARS 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 2772 TVASFLLANYARVLSRWSGTDHFCINVTLFDRDPDvvGIENVVGDFTSLVLLECRVDEPASIWESVRALQRQLMTDLPH 2850
Cdd:cd19539 246 SLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRH 322
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1246-1615 |
1.96e-15 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 82.75 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1246 TAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVS---HAAALNTivdvNRRNRIDTHDRLLALSALDFDLSV---Y 1319
Cdd:cd05967 214 ELLAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDnggHAVALNW----SMRNIYGIKPGDVWWAASDVGWVVghsY 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1320 DTFGALGCGAQLVTIPEHARR--DAFHWLSLTTEFGITVWNSVPGLMDMllIAAGDKAG------SLPTLRSVFLSGDwi 1391
Cdd:cd05967 290 IVYGPLLHGATTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRA--IRKEDPDGkyikkyDLSSLRTLFLAGE-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1392 PLDLP-RRLRRAAPGVRLVAMGGATEA--AIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIG 1468
Cdd:cd05967 366 RLDPPtLEWAENTLGVPVIDHWWQTETgwPITANPVGLEPLPIKAGSP--GKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1469 GA---GVALGYHNAPELTSDRFVHDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAA 1545
Cdd:cd05967 444 LPlppGCLLTLWKNDERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 1546 ATVVPIHNCTA--LGAGIVVTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:cd05967 522 CAVVGVRDELKgqVPLGLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1243-1612 |
2.14e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 82.34 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1243 SDITAMIECAPTDPIRI--DPHDAAYVIYTSGSTGEPKGVLVSH--AAALNTIVDVNRRNRIDThdRLLALSALDF--DL 1316
Cdd:PRK06188 147 VDLLAAAAKFGPAPLVAaaLPPDIAGLAYTGGTTGKPKGVMGTHrsIATMAQIQLAEWEWPADP--RFLMCTPLSHagGA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1317 SVYDTfgaLGCGAQLVTIPEHarrDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIpldLP 1396
Cdd:PRK06188 225 FFLPT---LLRGGTVIVLAKF---DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPM---SP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1397 RRLRRA--APGVRLVAMGGATEAAIWSNEFVVDDVDPD----WASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGA 1470
Cdd:PRK06188 296 VRLAEAieRFGPIFAQYYGQTEAPMVITYLRKRDHDPDdpkrLTSC--GRPTPGLRVALLDEDGREVAQGEVGEICVRGP 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1471 GVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVP 1550
Cdd:PRK06188 374 LVMDGYWNRPEETAEAFRDG-----WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1551 IHN------CTAlgagIVVTGSGAeqfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK06188 449 VPDekwgeaVTA----VVVLRPGA----AVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDK 508
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1448-1712 |
2.43e-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: 79.41 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1448 RVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDR--FVHDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRG 1525
Cdd:COG3433 28 RALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARapFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1526 HRVECGEIEHALRGHPLVAAATVVPIHNCTALGAGIVVTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLT 1605
Cdd:COG3433 108 IRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1606 ANGKVDRGKIAARLEAAARAPQPLDTSSTLTVVERLVAEVWSDVLGAPIT--GREDNFFAQGGDSLRATEAVARLTRRGV 1683
Cdd:COG3433 188 ALKVVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLGVDPEeiDPDDNLFDLGLDSIRLMQLVERWRKAGL 267
|
250 260
....*....|....*....|....*....
gi 2181016861 1684 AgAEVGQLLSHQTLGQFSAACVLADPASE 1712
Cdd:COG3433 268 D-VSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
174-568 |
2.83e-15 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 82.02 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILRQ-AAFAANVWNGDDD-MHMVSwlPLYHDMGIFWGVFMPLLNGGCTTLippHDfV 251
Cdd:PRK13295 199 VTQLIYTSGTTGEPKGVMHTANTLMANiVPYAERLGLGADDvILMAS--PMAHQTGFMYGLMMPVMLGATAVL---QD-I 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 252 RNPRIWLETVSRFRGNW-IGGPDFAYRRCieafDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAaglrddVMAP 330
Cdd:PRK13295 273 WDPARAAELIRTEGVTFtMASTPFLTDLT----RAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGA------KIVS 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 331 QYGLAEAGLGVTGSQtvrvwveksfdADALERGIAvevaqpnpADGRSRAlvscgdgafGWDIQIVDPDrHMTLTDGEVG 410
Cdd:PRK13295 343 AWGMTENGAVTLTKL-----------DDPDERAST--------TDGCPLP---------GVEVRVVDAD-GAPLPAGQIG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 411 EIWVGGPGLPDGYWRQPEQTATTfgartADGlgpYLRTGDAGF-RYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaH 489
Cdd:PRK13295 394 RLQVRGCSNFGGYLKRPQLNGTD-----ADG---WFDTGDLARiDADGYIRISGRSKDVIIRGGENIPVVEIEALLYR-H 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 490 CGVAPGGACAVqPDAPQanGE---WWLVLETGSPVeDLDDLSRILRRRILAhHETAPERVVWVPcrTLPTTTSGKI---R 563
Cdd:PRK13295 465 PAIAQVAIVAY-PDERL--GEracAFVVPRPGQSL-DFEEMVEFLKAQKVA-KQYIPERLVVRD--ALPRTPSGKIqkfR 537
|
....*
gi 2181016861 564 RRETL 568
Cdd:PRK13295 538 LREML 542
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
685-971 |
3.45e-15 |
|
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: 80.43 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 685 PTTPLQQAYWVGRGAEQPLGGVgcQTYFELVGaRVDAGRLAAALDALTRRHPMLRATF---PDPGRCL-ITPEAVRLPL- 759
Cdd:cd19542 3 PCTPMQEGMLLSQLRSPGLYFN--HFVFDLDS-SVDVERLRNAWRQLVQRHDILRTVFvesSAEGTFLqVVLKSLDPPIe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 760 AVHDLTDAPVTTRDTHLAEIRRRLR-THRFDIETGDTWTVELT-RLPHGcivhfavdliIADVTSIGTMLRDLAASYRGe 837
Cdd:cd19542 80 EVETDEDSLDALTRDLLDDPTLFGQpPHRLTLLETSSGEVYLVlRISHA----------LYDGVSLPIILRDLAAAYNG- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 838 KLPAPSATFADLIQSTSPPPQ--ACA---DRL--PEGPQLPRVQEADISFLRHQHTLSALATkaIDDACHNHGVTRAAVL 910
Cdd:cd19542 149 QLLPPAPPFSDYISYLQSQSQeeSLQywrKYLqgASPCAFPSLSPKRPAERSLSSTRRSLAK--LEAFCASLGVTLASLF 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 911 LAAYTLVLRRWASQDDFLVNVTTFGRS---PEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQ 971
Cdd:cd19542 227 QAAWALVLARYTGSRDVVFGYVVSGRDlpvPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQ 290
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1243-1557 |
4.79e-15 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 81.70 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1243 SDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSH------AAALNTIVDvnrrnRIDTHDRLLALSALD--F 1314
Cdd:PLN02387 231 SEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHgnivatVAGVMTVVP-----KLGKNDVYLAYLPLAhiL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1315 DLSVYDTFGALGC----GAQLV------TIPEHARRDAfhwlsltTEFGITVWNSVPGLMDML----LIAAGDKAGSLPT 1380
Cdd:PLN02387 306 ELAAESVMAAVGAaigyGSPLTltdtsnKIKKGTKGDA-------SALKPTLMTAVPAILDRVrdgvRKKVDAKGGLAKK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1381 L-------RSVFLSGDWIPLDLPRRLR---------RAAPGVRLVAM--GGA------------------------TE-- 1416
Cdd:PLN02387 379 LfdiaykrRLAAIEGSWFGAWGLEKLLwdalvfkkiRAVLGGRIRFMlsGGAplsgdtqrfiniclgapigqgyglTEtc 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1417 -AAIWSnefvvddvDPDWASI-PYGYPLANQMFRVVD-DNG----DDQPdYVAGELWIGGAGVALGYHNAPELTSDRFVH 1489
Cdd:PLN02387 459 aGATFS--------EWDDTSVgRVGPPLPCCYVKLVSwEEGgyliSDKP-MPRGEIVIGGPSVTLGYFKNQEKTDEVYKV 529
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 1490 DPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIR-GHRVECGEIEHALRGHPLVAAATVV--PIHN-CTAL 1557
Cdd:PLN02387 530 DERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHadPFHSyCVAL 601
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
2558-2850 |
4.99e-15 |
|
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: 80.32 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2558 YFE---FEL-ADFDRPRFDSAARQLVARHAGLRTTVSPAGTDAAssgeVAVVH-TAPIEpvVRDHD-------------- 2618
Cdd:cd19543 24 YVEqmvITLeGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEP----LQVVLkDRKLP--WRELDlshlseaeqeaele 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2619 DVRAAMRDQIIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQLPPLET--SFAHYV- 2695
Cdd:cd19543 98 ALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPvrPYRDYIa 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2696 WnhpelLPDADeavlprLAASRDYWRARLPSLPPAPKLADMSLLFEIEEPRFERATATIPAVDWSQVTRSCRAEGVTVAS 2775
Cdd:cd19543 178 W-----LQRQD------KEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNT 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 2776 FLLANYARVLSRWSGTDHFCINVTLFDRDPDVVGIENVVGDFTSLVLLECRVDEPASIWESVRALQRQLMTDLPH 2850
Cdd:cd19543 247 VVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREH 321
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1234-1615 |
5.57e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 80.98 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1234 DTQDAGVAVSDITAmiECAPTDPIRIDPHDA-AYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSAL 1312
Cdd:PRK07786 147 SSDDSVLGYEDLLA--EAGPAHAPVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1313 DFDLSVYDTFGA-LGCGAQLVTIPEHARrDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLpTLRSVFLSGDWI 1391
Cdd:PRK07786 225 LFHIAGIGSMLPgLLLGAPTVIYPLGAF-DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1392 PLDLPRRLRRAAPGVRLVAMGGATEAAIWSNEFVVDDVDPDWASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAG 1471
Cdd:PRK07786 303 SDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAIRKLGSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPT 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1472 VALGYHNAPELTSDRFvhdptGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV-- 1549
Cdd:PRK07786 381 LMSGYWNNPEATAEAF-----AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIgr 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 1550 PIHNCTALGAGIVVTGSGAeqfDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:PRK07786 456 ADEKWGEVPVAVAAVRNDD---AALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1237-1610 |
6.59e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 81.15 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1237 DAGVAVSDITAMIECAPTD----PIRIDPHDAAYVIYTSGSTGEPKGVLVSHAaalNTIVD---VNRRNRIDTHDRLLAl 1309
Cdd:PRK07529 184 KAHARILDFDAELARQPGDrlfsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHG---NEVANawlGALLLGLGPGDTVFC- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1310 saldfDLSVYDTFGALGC-------GAQLVTIPEHARRD----AFHWlSLTTEFGITVWNSVPGLMDMLL---IAAGDka 1375
Cdd:PRK07529 260 -----GLPLFHVNALLVTglaplarGAHVVLATPQGYRGpgviANFW-KIVERYRINFLSGVPTVYAALLqvpVDGHD-- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1376 gsLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGGATEAA-IWSNEFVVDDVDPdwASIpyGYPLANQMFRVV--DD 1452
Cdd:PRK07529 332 --ISSLRYALCGAAPLPVEVFRRFEAAT-GVRIVEGYGLTEATcVSSVNPPDGERRI--GSV--GLRLPYQRVRVVilDD 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1453 NGDDQPDYVA---GELWIGGAGVALGYHNaPELTSDRFVHDptgsRWYRTGDMGCYWRDGTLQFLGRADSQVkIR-GHRV 1528
Cdd:PRK07529 405 AGRYLRDCAVdevGVLCIAGPNVFSGYLE-AAHNKGLWLED----GWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNI 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1529 ECGEIEHALRGHPLVAAATVV--PIHNCTALGAGIVVTGSGAeqfdDSTPGALRAHLAVRLPQ-YMIPKVFVSCPELPLT 1605
Cdd:PRK07529 479 DPAAIEEALLRHPAVALAAAVgrPDAHAGELPVAYVQLKPGA----SATEAELLAFARDHIAErAAVPKHVRILDALPKT 554
|
....*
gi 2181016861 1606 ANGKV 1610
Cdd:PRK07529 555 AVGKI 559
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
167-468 |
8.60e-15 |
|
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: 80.54 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 167 DADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAA--FAANVWNGDDDMhmVSWLPLYHDMGIFWGVFMPLLNGGC--- 241
Cdd:cd17641 153 AAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAayLAADPLGPGDEY--VSVLPLPWIGEQMYSVGQALVCGFIvnf 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 ----TTL------IPPHDFVRNPRIWLETVSRFRGNWIGGPDFAyRRCIEAFDGTALQSLD--------LSCLRLATNGA 303
Cdd:cd17641 231 peepETMmedlreIGPTFVLLPPRVWEGIAADVRARMMDATPFK-RFMFELGMKLGLRALDrgkrgrpvSLWLRLASWLA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 304 EPVRgttlrdftakFRAagLRDdvmapQYGLAEAGLGVTGSQTVRVWVEKSFdadaleRGIAVEVAQPNPADGRSRALVS 383
Cdd:cd17641 310 DALL----------FRP--LRD-----RLGFSRLRSAATGGAALGPDTFRFF------HAIGVPLKQLYGQTELAGAYTV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 384 CGDGAfgwdiqiVDPDRHMTLTDG------EVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAG-FRYQ 456
Cdd:cd17641 367 HRDGD-------VDPDTVGVPFPGtevridEVGEILVRSPGVFVGYYKNPEATAEDF---DEDG---WLHTGDAGyFKEN 433
|
330
....*....|..
gi 2181016861 457 GELYVCGRYRDL 468
Cdd:cd17641 434 GHLVVIDRAKDV 445
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
159-573 |
8.67e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 80.77 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 159 PHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLN 238
Cdd:PRK07529 200 PGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLAR 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 239 GGCTTLIPPHDFvRNP----RIWlETVSRFRGNWIGGPDFAY----RRCIEAFDgtalqsldLSCLRLATNGAEPVRGTT 310
Cdd:PRK07529 280 GAHVVLATPQGY-RGPgviaNFW-KIVERYRINFLSGVPTVYaallQVPVDGHD--------ISSLRYALCGAAPLPVEV 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 311 LRDFTAkfrAAGLRddvMAPQYGLAEAglgvTGSQTVrvwveksfdadalergiavevaqpNPADGRSRalvscgDGAFG 390
Cdd:PRK07529 350 FRRFEA---ATGVR---IVEGYGLTEA----TCVSSV------------------------NPPDGERR------IGSVG 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 391 W-------DIQIVDPDRHMtLTD---GEVGEIWVGGPGLPDGYwRQPEQTAttfGARTADGlgpYLRTGDAGFR-YQGEL 459
Cdd:PRK07529 390 LrlpyqrvRVVILDDAGRY-LRDcavDEVGVLCIAGPNVFSGY-LEAAHNK---GLWLEDG---WLNTGDLGRIdADGYF 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 460 YVCGRYRDLIIVGGRNHFPndieKTVEEA---HCGVAPGGACAvQPDA-----PQANGEwwLVLETGSPVEDLDDLsriL 531
Cdd:PRK07529 462 WLTGRAKDLIIRGGHNIDP----AAIEEAllrHPAVALAAAVG-RPDAhagelPVAYVQ--LKPGASATEAELLAF---A 531
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2181016861 532 RRRIlahHETA--PERVVWVPcrTLPTTTSGKI-----RRRETLNRLTA 573
Cdd:PRK07529 532 RDHI---AERAavPKHVRILD--ALPKTAVGKIfkpalRRDAIRRVLRA 575
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1263-1551 |
1.16e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 79.43 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAaalntivdvNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVT-IPEH---- 1337
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHG---------TFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSvIPDMdptr 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1338 -ARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRA-APGVRLVAMGGAT 1415
Cdd:cd05910 157 pARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMlSDEAEILTPYGAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1416 EA----AIWSNEFVVDDVDP--DWASIPYGYPLANQMFRVVD---------DNGDDQPDYVAGELWIGGAGVALGYHNAP 1480
Cdd:cd05910 237 EAlpvsSIGSRELLATTTAAtsGGAGTCVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRP 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1481 ELTSDRFVHDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI 1551
Cdd:cd05910 317 VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1261-1612 |
1.52e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 78.29 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1261 PHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLSVYDTFGA-LGCGAQLVTIPEHAR 1339
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1340 RD--AFH--WlSLTTEFGITVWNSVPGLMDMLLIAAGDKagSLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGGAT 1415
Cdd:cd05944 81 RNpgLFDnfW-KLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDAT-GLPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1416 EAAIwsnefVVDDVDPDWA----SIPYGYPLANQMFRVVDDNGDDQ----PDYVaGELWIGGAGVALGYHNApELTSDRF 1487
Cdd:cd05944 157 EATC-----LVAVNPPDGPkrpgSVGLRLPYARVRIKVLDGVGRLLrdcaPDEV-GEICVAGPGVFGGYLYT-EGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1488 VHDptgsRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV--PIHNCTALGAGIVVTG 1565
Cdd:cd05944 230 VAD----GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqPDAHAGELPVAYVQLK 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2181016861 1566 SGAEqfddSTPGALRAHLAVRLPQY-MIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05944 306 PGAV----VEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFK 349
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1261-1615 |
1.64e-14 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 79.46 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1261 PHDAAYVIYTSGSTGEPKGVLVSHAA----ALNTIVDVNrrnrIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPE 1336
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSAlivqSLAKIAIVG----YGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1337 HARRDAFHWLSlttEFGITVWNSVPGLM-DMLLIAAGDKAG-SLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGA 1414
Cdd:PLN02860 247 FDAKAALQAIK---QHNVTSMITVPAMMaDLISLTRKSMTWkVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1415 TEAA-----IWSNEFVVDDVDPDWASIPYGYPLANQMF----------RVVDDNGDDQPDYVaGELWIGGAGVALGY-HN 1478
Cdd:PLN02860 324 TEACssltfMTLHDPTLESPKQTLQTVNQTKSSSVHQPqgvcvgkpapHVELKIGLDESSRV-GRILTRGPHVMLGYwGQ 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1479 APELTSDRfvhdpTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALG 1558
Cdd:PLN02860 403 NSETASVL-----SNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPD-SRLT 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 1559 AGIVVTGSGAEQF---DDSTPGA----------LRAHLAVR-LPQYMIPKVFVSCPE-LPLTANGKVDRGKI 1615
Cdd:PLN02860 477 EMVVACVRLRDGWiwsDNEKENAkknltlssetLRHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEV 548
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
179-564 |
1.94e-14 |
|
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: 77.69 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 179 YSSGSTGKPKGVVNTHQSilrqaAFAANV--------WNGDDDMHMVswLPLYHDMGIFWGVFMPLLNGGCTTLippHDF 250
Cdd:cd17635 8 FTSGTTGEPKAVLLANKT-----FFAVPDilqkeglnWVVGDVTYLP--LPATHIGGLWWILTCLIHGGLCVTG---GEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 251 VRNPRIwLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDLSCLRLAtnGAEPVRgttlrDFTAKFRAAGLRDDVMAp 330
Cdd:cd17635 78 TTYKSL-FKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYG--GSRAIA-----ADVRFIEATGLTNTAQV- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 331 qYGLAEaglgvTGSQTVRVWVEKSFDADAlergiaveVAQPNPadgrsralvscgdgafGWDIQIVDPDRHMTLTDGEvG 410
Cdd:cd17635 149 -YGLSE-----TGTALCLPTDDDSIEINA--------VGRPYP----------------GVDVYLAATDGIAGPSASF-G 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 411 EIWVGGPGLPDGYWRQPEQTATTFgartadgLGPYLRTGDAGFRYQGE-LYVCGRYRDLIIVGGRNHFPNDIEKTVEEah 489
Cdd:cd17635 198 TIWIKSPANMLGYWNNPERTAEVL-------IDGWVNTGDLGERREDGfLFITGRSSESINCGGVKIAPDEVERIAEG-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 490 cgvAPG---GACAVQPDAPQanGEWWLVLETGSPVEDLDDLSRILR--RRILAHHeTAPERVVWVpcRTLPTTTSGKIRR 564
Cdd:cd17635 269 ---VSGvqeCACYEISDEEF--GELVGLAVVASAELDENAIRALKHtiRRELEPY-ARPSTIVIV--TDIPRTQSGKVKR 340
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
177-565 |
2.74e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 78.39 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSILRQAA--FAANVWNGDDDMHMVSwlPLYHDMGIFWGVFMPLLNGGctTLIPPHDFvrNP 254
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWKSIdhVIALGLTASERLLVVG--PLYHVGAFDLPGIAVLWVGG--TLRIHREF--DP 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 255 RIWLETVSRFR--GNWiggpdFAYRRCIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAGLRDdvmapQY 332
Cdd:PRK06145 228 EAVLAAIERHRltCAW-----MAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYID-----AY 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 333 GLAEAGLGVTgsqtvrvwveksfdadALERGIAVEVAQpnpADGRSRALVscgdgafgwDIQIVDPDRHMtLTDGEVGEI 412
Cdd:PRK06145 298 GLTETCSGDT----------------LMEAGREIEKIG---STGRALAHV---------EIRIADGAGRW-LPPNMKGEI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 413 WVGGPGLPDGYWRQPEQTATTFgartadgLGPYLRTGDAGF-RYQGELYVCGRYRDLIIVGGRNHFPNDIEKT------V 485
Cdd:PRK06145 349 CMRGPKVTKGYWKDPEKTAEAF-------YGDWFRSGDVGYlDEEGFLYLTDRKKDMIISGGENIASSEVERViyelpeV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 486 EEAHCGVAPGGACAVQPDAPqangewwLVLETGSPVEdLDDLSRILRRRiLAHHETAPERVVwvpCRTLPTTTSGKIRRR 565
Cdd:PRK06145 422 AEAAVIGVHDDRWGERITAV-------VVLNPGATLT-LEALDRHCRQR-LASFKVPRQLKV---RDELPRNPSGKVLKR 489
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1259-1612 |
2.76e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 78.94 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1259 IDPHDAAYVIYTSGSTGEPKGVLVSHAaalNTIVDVNRRNRID----THDRLLALSALD----FDLSVYDT-FGALGCGA 1329
Cdd:PRK08974 203 LVPEDLAFLQYTGGTTGVAKGAMLTHR---NMLANLEQAKAAYgpllHPGKELVVTALPlyhiFALTVNCLlFIELGGQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1330 QLVTIPeharRDAFHWLSLTTEFGITVWNSVPGLMDMLL--------------IAAGdkaGSLPTLRSVflSGDWipldl 1395
Cdd:PRK08974 280 LLITNP----RDIPGFVKELKKYPFTAITGVNTLFNALLnneefqeldfsslkLSVG---GGMAVQQAV--AERW----- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1396 prrlrRAAPGVRLVAMGGATEAA--IWSNEFVVDDVDpdwASIpyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVA 1473
Cdd:PRK08974 346 -----VKLTGQYLLEGYGLTECSplVSVNPYDLDYYS---GSI--GLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVM 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1474 LGYHNAPELTSDrFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVA--AATVVPI 1551
Cdd:PRK08974 416 LGYWQRPEATDE-VIKDG----WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLevAAVGVPS 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 1552 HNCTALGAGIVVtgsgaeQFDDS-TPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK08974 491 EVSGEAVKIFVV------KKDPSlTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILR 546
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
18-573 |
2.79e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 78.73 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 18 VPAVFAEwvGRRPDAVALrTVAATGIDdWTYQRLWDHVreirdvafSGLSAGIRIPMALPGGaDYVAGMlaalaaglIPV 97
Cdd:PLN02574 43 VSFIFSH--HNHNGDTAL-IDSSTGFS-ISYSELQPLV--------KSMAAGLYHVMGVRQG-DVVLLL--------LPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 98 PVYLP-------------STREPQRFLARAQHILRDCEPSAVYTCGELVEVLerdPILGALPIRTPA-----STADGLAP 159
Cdd:PLN02574 102 SVYFPviflavlslggivTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKL---SPLGVPVIGVPEnydfdSKRIEFPK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 160 HPGGTTADADHG-------EHVAFLQYSSGSTGKPKGVVNTHQSILRQAA----FAANVW--NGDDDMHMVSwLPLYHDM 226
Cdd:PLN02574 179 FYELIKEDFDFVpkpvikqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrFEASQYeyPGSDNVYLAA-LPMFHIY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 227 GIFWGVfMPLLNGGcTTLIPPHDFVRNPRIwlETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSLDlsCLRLATNGAEPV 306
Cdd:PLN02574 258 GLSLFV-VGLLSLG-STIVVMRRFDASDMV--KVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLK--SLKQVSCGAAPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 307 RGTTLRDFTAKFraaglrddvmaPQYGLAEaGLGVTGSQTVRVwveKSFDADALERGIAVEVAQPNpadgrsralvscgd 386
Cdd:PLN02574 332 SGKFIQDFVQTL-----------PHVDFIQ-GYGMTESTAVGT---RGFNTEKLSKYSSVGLLAPN-------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 387 gafgWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGD-AGFRYQGELYVCGRY 465
Cdd:PLN02574 383 ----MQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI---DKDG---WLRTGDiAYFDEDGYLYIVDRL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 466 RDLIIVGGRNHFPNDIEKTVEEaHCGVAPGgacAVQPDAPQANGE---WWLVLETGSPVEDLDDLSRILRrrilahhETA 542
Cdd:PLN02574 453 KEIIKYKGFQIAPADLEAVLIS-HPEIIDA---AVTAVPDKECGEipvAFVVRRQGSTLSQEAVINYVAK-------QVA 521
|
570 580 590
....*....|....*....|....*....|....*
gi 2181016861 543 PER----VVWVpcRTLPTTTSGKIRRRETLNRLTA 573
Cdd:PLN02574 522 PYKkvrkVVFV--QSIPKSPAGKILRRELKRSLTN 554
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1439-1612 |
3.46e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 78.71 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1439 GYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDrfVHDPTGsrWYRTGDMGCYWRDGTLQFLGRAD 1518
Cdd:PRK12492 389 GIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAE--ALDAEG--WFKTGDIAVIDPDGFVRIVDRKK 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1519 SQVKIRGHRVECGEIEHALRGHPLVAaatvvpihNCTALGAGIVVTGSGAEQFDDSTPGA-----LRAHLAVRLPQYMIP 1593
Cdd:PRK12492 465 DLIIVSGFNVYPNEIEDVVMAHPKVA--------NCAAIGVPDERSGEAVKLFVVARDPGlsveeLKAYCKENFTGYKVP 536
|
170
....*....|....*....
gi 2181016861 1594 KVFVSCPELPLTANGKVDR 1612
Cdd:PRK12492 537 KHIVLRDSLPMTPVGKILR 555
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1266-1612 |
4.36e-14 |
|
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: 77.80 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1266 YVIYTSGSTGEPKGVLVSHAAALntivdvnrrnridTHDRLLALSALDFDL---SVY-------------DTFGALGCGA 1329
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPGGP-------------PDNDTLMAAALGFGPgadSVYlspaplyhaapfrWSMTALFMGG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1330 QLVTIPehaRRDAFHWLSLTTEFGITVWNSVPGLMDML--LIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRrAAPGVR 1407
Cdd:cd05929 196 TLVLME---KFDPEEFLRLIERYRVTFAQFVPTMFVRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWI-DWGGPI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 LVAMGGATEAaiwsNEFVVDDVDpDWASIP--YGYPLANQMfRVVDDNGDDQPDYVAGELWIGGAGvALGYHNAPELTSD 1485
Cdd:cd05929 272 IWEYYGGTEG----QGLTIINGE-EWLTHPgsVGRAVLGKV-HILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1486 RFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALGA---GIV 1562
Cdd:cd05929 345 ARNEGG----WSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPD-EELGQrvhAVV 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1563 VTGSGAEQfDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05929 420 QPAPGADA-GTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYR 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2425-2957 |
4.90e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.44 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2425 SRPAVPASSLPTDATVVATLAEIWQRHLAIPTPGVDDDFFLLGGDSLVATRVYADLRAAGFGQLAFVDLFNHSTLGELAA 2504
Cdd:PRK05691 572 LQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSA 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2505 HAGPRT---GPEVSVAAESTRGGThdpnrFPLTVVQN-------------AYRAgrEGALILGGvaahcyfefelaDFDR 2568
Cdd:PRK05691 652 AVARQLaggGAAQAAIARLPRGQA-----LPQSLAQNrlwllwqldpqsaAYNI--PGGLHLRG------------ELDE 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2569 PRFDSAARQLVARHAGLRTT------VSPAGTDAASSGEVAVVHTA--PIEPVVRDHDDVRAAMRDQIIDLTARPGIDFG 2640
Cdd:PRK05691 713 AALRASFQRLVERHESLRTRfyerdgVALQRIDAQGEFALQRIDLSdlPEAEREARAAQIREEEARQPFDLEKGPLLRVT 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2641 VQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLY----RGETVDqLPPLETSFAHY-VWNHPELlpDADEAvlprlAA 2715
Cdd:PRK05691 793 LVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYaaacQGQTAE-LAPLPLGYADYgAWQRQWL--AQGEA-----AR 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2716 SRDYWRARLPSLPPAPKLADMSLLFEIEEPRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRWSGTDHFC 2795
Cdd:PRK05691 865 QLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIR 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2796 INVTLFDRDPdvVGIENVVGDFTSLVLLECRVDEP---ASIWESVR--ALQRQLMTDLPhrgadavwLQRELLRFHGNPT 2870
Cdd:PRK05691 945 IGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRlpfTALLAQVRqaTLGAQAHQDLP--------FEQLVEALPQARE 1014
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2871 AALFPVVFTSGLGLVDASARAAVRFAEPVFAASQTPQTVLDFQVWESA-GALKLSWDFVSQAVSPATARTQLESLVDGIT 2949
Cdd:PRK05691 1015 QGLFQVMFNHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRnGRLTLSFDYAAELFDAATIERLAEHFLALLE 1094
|
....*...
gi 2181016861 2950 GVATRSRR 2957
Cdd:PRK05691 1095 QVCEDPQR 1102
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2567-2958 |
5.22e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.05 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2567 DRPRFDSAARQLVARHAGLRTTVSPAG------TDAASSGEVAVVHTAPIEPVVRDHdDVRAAMRDQI---IDLTARPGI 2637
Cdd:PRK12467 85 DVSALRRAFDALVARHESLRTRFVQDEegfrqvIDASLSLTIPLDDLANEQGRARES-QIEAYINEEVarpFDLANGPLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2638 DFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVD---QLPPLETSFAHY-VWNHPELlpDADEAvlprl 2713
Cdd:PRK12467 164 RVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGrepSLPALPIQYADYaIWQRSWL--EAGER----- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2714 AASRDYWRARLPSLPPApkladMSLLFEIEEP-----RFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRW 2788
Cdd:PRK12467 237 ERQLAYWQEQLGGEHTV-----LELPTDRPRPavpsyRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2789 SGTDHFCINVTLFDRDPdvVGIENVVGDFTSLVLLECRVDEPASIWE-----SVRALQRQLMTDLP-HRGADAVWLQREL 2862
Cdd:PRK12467 312 SGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLEllqqvKRTALGAQAHQDLPfEQLVEALQPERSL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2863 LRfhgNPtaaLFPVVFT-----SGLGLVDASARAAVRFaEPVFAASQTPQTVLDFQVWESAGALKLSWDFVSQAVSPATA 2937
Cdd:PRK12467 390 SH---SP---LFQVMFNhqntaTGGRDREGAQLPGLTV-EELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTI 462
|
410 420
....*....|....*....|....
gi 2181016861 2938 R---TQLESLVDGItgVATRSRRI 2958
Cdd:PRK12467 463 ErlaTHWRNLLEAI--VAEPRRRL 484
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1239-1530 |
5.31e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.02 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1239 GVAVSDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLA---LSALdFD 1315
Cdd:PRK09274 151 GTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtfpLFAL-FG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1316 LsvydtfgALGCGAqlvTIPE-HARRDAF----HWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDW 1390
Cdd:PRK09274 230 P-------ALGMTS---VIPDmDPTRPATvdpaKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1391 IPLDLPRRLRRA-APGVRLVAMGGATEA----AIWSNEfVVDDVDPDWAS---IPYGYPLANQMFRVV--DDNG----DD 1456
Cdd:PRK09274 300 VPIAVIERFRAMlPPDAEILTPYGATEAlpisSIESRE-ILFATRAATDNgagICVGRPVDGVEVRIIaiSDAPipewDD 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 1457 Q---PDYVAGELWIGGAGVALGYHNAPELTSDRFVHDPTGSRWYRTGDMGcyWRD--GTLQFLGRadsqvkiRGHRVEC 1530
Cdd:PRK09274 379 AlrlATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRMGDLG--YLDaqGRLWFCGR-------KAHRVET 448
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
15-659 |
5.58e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.05 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 15 DRSVPAVFAEWVGRRPDAVALrtvaATGIDDWTY-------QRLWDHVREIrdvafsGLSAGIRIPMALPGGADYVAGML 87
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPAL----VFGDQQLSYaelnrraNRLAHRLIAI------GVGPDVLVGVAVERSVEMIVALL 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 88 AALAAGLIPVPVYLPSTREpqrflaRAQHILRDcepSAVYTCGELVEVLERDPILGALPirtpASTADGLA--PHPGGTT 165
Cdd:PRK12467 3164 AVLKAGGAYVPLDPEYPRE------RLAYMIED---SGVKLLLTQAHLLEQLPAPAGDT----ALTLDRLDlnGYSENNP 3230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 166 ADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDmGIFWGVFMPLLNGGCTTLI 245
Cdd:PRK12467 3231 STRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFD-GAQERFLWTLICGGCLVVR 3309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 246 PPHdfVRNPRiwlETVSRFRGNWIGGPDF--AYRRCIEAF-DGTALQSLDLSCLrlatnGAEPVRGTTLRDFTAKFRAAG 322
Cdd:PRK12467 3310 DND--LWDPE---ELWQAIHAHRISIACFppAYLQQFAEDaGGADCASLDIYVF-----GGEAVPPAAFEQVKRKLKPRG 3379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 323 LRDdvmapQYGLAEAGLgvtgsqTVRVWvekSFDADALERGIAVEVaqpnpadGRSRALVSCG--DGAFGwdiqivdpdr 400
Cdd:PRK12467 3380 LTN-----GYGPTEAVV------TVTLW---KCGGDAVCEAPYAPI-------GRPVAGRSIYvlDGQLN---------- 3428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 401 hmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFP 478
Cdd:PRK12467 3429 --PVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLyRTGDlARYRADGVIEYLGRIDHQVKIRGFRIEL 3506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 479 NDIEKTVEEaHCGVAPggacAVQPDAPQANGEW---WLVLEtgSPVEDLDDlsrILRRRILAhheTAPERVV---WVPCR 552
Cdd:PRK12467 3507 GEIEARLLQ-HPSVRE----AVVLARDGAGGKQlvaYVVPA--DPQGDWRE---TLRDHLAA---SLPDYMVpaqLLVLA 3573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 553 TLPTTTSGKIRRReTLNRltagqlevvhevsPRAQAPDTPAAPDdppTELAQHLAAM----LGVEpyELAPDADLTTLGL 628
Cdd:PRK12467 3574 AMPLGPNGKVDRK-ALPD-------------PDAKGSREYVAPR---SEVEQQLAAIwadvLGVE--QVGVTDNFFELGG 3634
|
650 660 670
....*....|....*....|....*....|..
gi 2181016861 629 TSMMTAQIVE-WSSSQSRRLDFADLYAEPTLR 659
Cdd:PRK12467 3635 DSLLALQVLSrIRQSLGLKLSLRDLMSAPTIA 3666
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1108-1615 |
8.37e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 76.96 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1108 PAPAG---LLYDAFR--ENAATHPARLALRWRpddyrgERhgDVIAQDRSQLTYGELDELARSVARAVAAR-HAAGSVIG 1181
Cdd:PRK13383 18 PSPRAvlrLLREASRggTNPYTLLAVTAARWP------GR--TAIIDDDGALSYRELQRATESLARRLTRDgVAPGRAVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1182 IQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLIrTDSDTQDAGVAVSDITAMIecaptDPIRIDP 1261
Cdd:PRK13383 90 VMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVV-ADNEFAERIAGADDAVAVI-----DPATAGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1262 HDAA----------YVIYTSGSTGEPKGV-----LVSHAAALNTIVDvnrRNRIDTHDRLLALSALdfdlsvydtFGALG 1326
Cdd:PRK13383 164 EESGgrpavaapgrIVLLTSGTTGKPKGVprapqLRSAVGVWVTILD---RTRLRTGSRISVAMPM---------FHGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1327 CGAQLVTIP------EHARRDAFHWLSLTTEFGITVWNSVPGLMDMLL-IAAGDKA-GSLPTLRSVFLSGDWIPLDLPRR 1398
Cdd:PRK13383 232 LGMLMLTIAlggtvlTHRHFDAEAALAQASLHRADAFTAVPVVLARILeLPPRVRArNPLPQLRVVMSSGDRLDPTLGQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1399 LRRAAPGVrLVAMGGATEAAIWSNEFVVDDVDpdwASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHN 1478
Cdd:PRK13383 312 FMDTYGDI-LYNGYGSTEVGIGALATPADLRD---APETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1479 ApeltSDRFVHDPTGSrwyrTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VPIHNCTA 1556
Cdd:PRK13383 388 G----GGKAVVDGMTS----TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVigVPDERFGH 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 1557 LGAGIVVTGSGAeqfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:PRK13383 460 RLAAFVVLHPGS----GVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
22-583 |
8.89e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 77.12 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 22 FAEWVGR----RPDAVALRTVAATGiddwTYQRLWDHVREIRDV-AFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIP 96
Cdd:PRK07786 19 WVNQLARhalmQPDAPALRFLGNTT----TWRELDDRVAALAGAlSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 97 VPVYLPSTREPQRFLARaqhilrDCEPSAVYTCGELV----EVLERDPILGALPIRTPASTADGLAPHPGGTTADADHG- 171
Cdd:PRK07786 95 VPVNFRLTPPEIAFLVS------DCGAHVVVTEAALApvatAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 -----EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGD--DDMHMVSwLPLYHDMGIfwGVFMPLLNGGCTTL 244
Cdd:PRK07786 169 vdipnDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADinSDVGFVG-VPLFHIAGI--GSMLPGLLLGAPTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 245 IPPHDfVRNPRIWLETVSRFRGNWIggpdFAYRRCIEAF-DGTALQSLDLScLRLATNGAEPVRGTTLRDFTAKFRAAGL 323
Cdd:PRK07786 246 IYPLG-AFDPGQLLDVLEAEKVTGI----FLVPAQWQAVcAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 324 rddvmapqygLAEAGlgvtgsQTVRVWVEKSFDADALERGIAvEVAQPNPAdgrsralVScgdgafgwdIQIVDPDRHmT 403
Cdd:PRK07786 320 ----------LAAFG------QTEMSPVTCMLLGEDAIRKLG-SVGKVIPT-------VA---------ARVVDENMN-D 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 404 LTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGL---GPYLRTGDAGFryqgeLYVCGRYRDLIIVGGRNHFPND 480
Cdd:PRK07786 366 VPVGEVGEIVYRAPTLMSGYWNNPEATAEAF----AGGWfhsGDLVRQDEEGY-----VWVVDRKKDMIISGGENIYCAE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 481 IEkTVEEAHCGVApggACAVQPDAPQANGE---WWLVLETGSPVEDLDDLSRILRRRiLAHHEtAPERVVWVPcrTLPTT 557
Cdd:PRK07786 437 VE-NVLASHPDIV---EVAVIGRADEKWGEvpvAVAAVRNDDAALTLEDLAEFLTDR-LARYK-HPKALEIVD--ALPRN 508
|
570 580
....*....|....*....|....*.
gi 2181016861 558 TSGKIRRRETLNRLTAGQLEVVHEVS 583
Cdd:PRK07786 509 PAGKVLKTELRERYGACVNVERRSAS 534
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1122-1610 |
9.21e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 76.85 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1122 AATHPARLALRwrpddYRGErhgdviaqdrsQLTYGELDE-LARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMA 1200
Cdd:PRK06145 12 ARRTPDRAALV-----YRDQ-----------EISYAEFHQrILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1201 GCTYLPVGVDQPAERLSRIcARSAMAGLIRTDSDTQ-----DAGVAVSDITAM----------IECAPTDPIRidPHDAA 1265
Cdd:PRK06145 76 GAVFLPINYRLAADEVAYI-LGDAGAKLLLVDEEFDaivalETPKIVIDAAAQadsrrlaqggLEIPPQAAVA--PTDLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1266 YVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdFDLSVYDTFGaLGCGAQLVTIPEHARRDAFHW 1345
Cdd:PRK06145 153 RLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPL-YHVGAFDLPG-IAVLWVGGTLRIHREFDPEAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1346 LSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGATEAAiwSNEFV 1425
Cdd:PRK06145 231 LAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETC--SGDTL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1426 VD---DVDPDWASipyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDM 1502
Cdd:PRK06145 309 MEagrEIEKIGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-----WFRSGDV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1503 GCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHN------CTAlgagIVVTGSGAEQfddsTP 1576
Cdd:PRK06145 381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDdrwgerITA----VVVLNPGATL----TL 452
|
490 500 510
....*....|....*....|....*....|....
gi 2181016861 1577 GALRAHLAVRLPQYMIPKVFVSCPELPLTANGKV 1610
Cdd:PRK06145 453 EALDRHCRQRLASFKVPRQLKVRDELPRNPSGKV 486
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
168-565 |
9.75e-14 |
|
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: 76.58 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 168 ADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAA---NVWNGDDDMHMVSwlpLYHDMGIfWGVFMPLLNGGctTL 244
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPParlDVGPGSRVAQVLS---IAFDACI-GEIFSTLCNGG--TL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 245 IPphdfvRNPRIWLETVSRFRGNWIGGPdfayrrcieafdgTALQSL---DLSCLRLATNGAEPVrgttlrdfTAKFRAA 321
Cdd:cd17653 175 VL-----ADPSDPFAHVARTVDALMSTP-------------SILSTLspqDFPNLKTIFLGGEAV--------PPSLLDR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 322 GLRDDVMAPQYGLAEAGLGVTGSQtvrvwveksfdadaLERGIAVEVAQPNPadgrsralvscgdgafGWDIQIVDPDRh 401
Cdd:cd17653 229 WSPGRRLYNAYGPTECTISSTMTE--------------LLPGQPVTIGKPIP----------------NSTCYILDADL- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 402 MTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTA-DGLGPYlRTGDAGF-RYQGELYVCGRYRDLIIVGGrnhFPN 479
Cdd:cd17653 278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwPGSRMY-RTGDYGRwTEDGGLEFLGREDNQVKVRG---FRI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 480 DIEKTVEEAHcgvapggacAVQPDAPQA-----NGEwwLV-LETGSPVeDLDDLSRILRRRILAHHetAPERVVWVPcrT 553
Cdd:cd17653 354 NLEEIEEVVL---------QSQPEVTQAaaivvNGR--LVaFVTPETV-DVDGLRSELAKHLPSYA--VPDRIIALD--S 417
|
410
....*....|..
gi 2181016861 554 LPTTTSGKIRRR 565
Cdd:cd17653 418 FPLTANGKVDRK 429
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
113-692 |
9.91e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 77.78 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 113 RAQHILRDCEPSAVYTCGELVevlerdPILGALPIRTPASTADGLAPhPGGTTADADHGEHVAFLQYSSGSTGKPKGVVN 192
Cdd:PRK10252 546 RLKMMLEDARPSLLITTADQL------PRFADVPDLTSLCYNAPLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMV 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 193 THQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGGCTTLIPPhDFVRNPrIWLETVsrFRGNWIGGP 272
Cdd:PRK10252 619 GQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSV-WEFFWPFIAGAKLVMAEP-EAHRDP-LAMQQF--FAEYGVTTT 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 273 DFAyRRCIEAFDGT-ALQSLDLSCLRLA---TNG-AEPvrgTTLRDFTAKFRAAGLRDdvmapQYGLAEAGLGVTgsqtv 347
Cdd:PRK10252 694 HFV-PSMLAAFVASlTPEGARQSCASLRqvfCSGeALP---ADLCREWQQLTGAPLHN-----LYGPTEAAVDVS----- 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 348 rvWVEKSFDADALERGIAVEVAQPNpadgrsralvscgdgafgWDIQIVDPDRHMT-LTDGEVGEIWVGGPGLPDGYWRQ 426
Cdd:PRK10252 760 --WYPAFGEELAAVRGSSVPIGYPV------------------WNTGLRILDARMRpVPPGVAGDLYLTGIQLAQGYLGR 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 427 PEQTATTFgarTADGLGP----YlRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVeEAHCGVAPGG--ACA 499
Cdd:PRK10252 820 PDLTASRF---IADPFAPgermY-RTGDvARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAM-QALPDVEQAVthACV 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 500 VQPDAPQANGEW----WLVLETGSPVeDLDDLSRILRRRILAHheTAPerVVWVPCRTLPTTTSGKIRRretlNRLTAGQ 575
Cdd:PRK10252 895 INQAAATGGDARqlvgYLVSQSGLPL-DTSALQAQLRERLPPH--MVP--VVLLQLDQLPLSANGKLDR----KALPLPE 965
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 576 LEVvhEVSPRAQAPDTpaapddpPTELAQHLAAMLGVEPyeLAPDADLTTLGLTSMMTAQ-IVEWSSSQSRRLDFADLYA 654
Cdd:PRK10252 966 LKA--QVPGRAPKTGT-------ETIIAAAFSSLLGCDV--VDADADFFALGGHSLLAMKlAAQLSRQFARQVTPGQVMV 1034
|
570 580 590
....*....|....*....|....*....|....*...
gi 2181016861 655 EPTLRSWQRLFDAAPPVQtgtssvAASGPWPTTPLQQA 692
Cdd:PRK10252 1035 ASTVAKLATLLDAEEDES------RRLGFGTILPLREG 1066
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1256-1610 |
1.35e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 76.54 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1256 PIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALdFDLS--VYDTFGALGCGAQLVT 1333
Cdd:PRK08314 184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTgmVHSMNAPIYAGATVVL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1334 IPEHARRDAfhwLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGG 1413
Cdd:PRK08314 263 MPRWDREAA---ARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELT-GLDYVEGYG 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1414 ATE--AAIWSNEfvvddvdPDWASIP-YGYPLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVh 1489
Cdd:PRK08314 339 LTEtmAQTHSNP-------PDRPKLQcLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1490 DPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHN---------CTALGAG 1560
Cdd:PRK08314 411 EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDprrgetvkaVVVLRPE 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 1561 IVVTGSGAEQFDDStpgalRAHLAVrlpqYMIPKV--FVScpELPLTANGKV 1610
Cdd:PRK08314 491 ARGKTTEEEIIAWA-----REHMAA----YKYPRIveFVD--SLPKSGSGKI 531
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1177-1610 |
1.37e-13 |
|
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: 76.18 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRIcARSAMAGLIRTDSD-TQDAGVAVSDITAMIECAptd 1255
Cdd:cd12118 54 GDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI-LRHSEAKVLFVDREfEYEDLLAEGDPDFEWIPP--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1256 pirIDPHDAAYVIYTSGSTGEPKGVLVSH-AAALNTIVDVnRRNRIDTHdrllalsaldfdlSVY----DTFGALG-C-- 1327
Cdd:cd12118 130 ---ADEWDPIALNYTSGTTGRPKGVVYHHrGAYLNALANI-LEWEMKQH-------------PVYlwtlPMFHCNGwCfp 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1328 ------GAQLVTIPEHARRDAFHWLSlttEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPldlPRRLRR 1401
Cdd:cd12118 193 wtvaavGGTNVCLRKVDAKAIYDLIE---KHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPP---AAVLAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1402 AAP-GVRLVAMGGATE------AAIWSnefvvddvdPDWASIP------------YGYPLANQMfRVVD-DNGDDQP-DY 1460
Cdd:cd12118 267 MEElGFDVTHVYGLTEtygpatVCAWK---------PEWDELPteerarlkarqgVRYVGLEEV-DVLDpETMKPVPrDG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1461 V-AGELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRG 1539
Cdd:cd12118 337 KtIGEIVFRGNIVMKGYLKNPEATAEAFRGG-----WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYK 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1540 HPLVAAATVV--PIHNCTALGAGIVVTGSGAEqfddSTPGALRAHLAVRLPQYMIPKVFVSCPeLPLTANGKV 1610
Cdd:cd12118 412 HPAVLEAAVVarPDEKWGEVPCAFVELKEGAK----VTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
18-565 |
1.51e-13 |
|
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: 76.76 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 18 VPAVFAEWVGRRPDAVALRTVAATG-IDDWTYQRLWDHVRE----IRDVafsGLSAGIRIPMALPGGADYVAGMLAALAA 92
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEDGtSRTLTYGELLYEVKRlangLRAL---GVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 93 GLIPVPVYLPSTREPQRflARaqhiLRDCEPSAVYTC------GELVEVLE-------RDP------ILGALPIRTPAST 153
Cdd:cd05968 140 GGIVVPIFSGFGKEAAA--TR----LQDAEAKALITAdgftrrGREVNLKEeadkacaQCPtvekvvVVRHLGNDFTPAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 154 ADGLAPHPGGTTADAD----HGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAA----NVWNGDddmhMVSWLPlyhD 225
Cdd:cd05968 214 GRDLSYDEEKETAGDGaertESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMyfqfDLKPGD----LLTWFT---D 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 226 MGIF---WGVFMPLLNGGCTTL---IPPHDfvRNPRIWlETVSRFRGNWIG-GPDFAyrRCIEAFDGTALQSLDLSCLRL 298
Cdd:cd05968 287 LGWMmgpWLIFGGLILGATMVLydgAPDHP--KADRLW-RMVEDHEITHLGlSPTLI--RALKPRGDAPVNAHDLSSLRV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 299 ATNGAEPVRGTTLRDFtakFRAAGLRDDVMAPQYGLAEAGLGVTGSQTVRVWVEKSFDAdalergiavevaqPNPadgrs 378
Cdd:cd05968 362 LGSTGEPWNPEPWNWL---FETVGKGRNPIINYSGGTEISGGILGNVLIKPIKPSSFNG-------------PVP----- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 379 ralvscgdgafGWDIQIVDPDRhmTLTDGEVGEIWVGGP--GLPDGYWRQPEQTATTFGARTADglgpYLRTGD-AGFRY 455
Cdd:cd05968 421 -----------GMKADVLDESG--KPARPEVGELVLLAPwpGMTRGFWRDEDRYLETYWSRFDN----VWVHGDfAYYDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 456 QGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVAPGGACAVQPDAPQANGEWWLVLETGspVEDLDDLSRILRRRI 535
Cdd:cd05968 484 EGYFYILGRSDDTINVAGKRVGPAEIE-SVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPG--VTPTEALAEELMERV 560
|
570 580 590
....*....|....*....|....*....|..
gi 2181016861 536 LAHHETA--PERVVWVPcrTLPTTTSGKIRRR 565
Cdd:cd05968 561 ADELGKPlsPERILFVK--DLPKTRNAKVMRR 590
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
171-566 |
1.69e-13 |
|
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: 76.38 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAfAANVWNG--DDDMHMVswlplYHDMG---IFWGVFMPLLNGGCTTLI 245
Cdd:cd05970 184 GEDILLVYFSSGTTGMPKMVEHDFTYPLGHIV-TAKYWQNvrEGGLHLT-----VADTGwgkAVWGKIYGQWIAGAAVFV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 246 ppHDFVR-NPRIWLETVSRFRGNWIGGPDFAYRRCIEAfdgtALQSLDLSCLRLATNGAEPVRGTTLRDFTAKfraAGLR 324
Cdd:cd05970 258 --YDYDKfDPKALLEKLSKYGVTTFCAPPTIYRFLIRE----DLSRYDLSSLRYCTTAGEALNPEVFNTFKEK---TGIK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 325 ddvMAPQYGLAEAGLGVTGSQtvrvWVEksfdadalergiavevaqPNPAdgrsralvSCGDGAFGWDIQIVDPDRHMTL 404
Cdd:cd05970 329 ---LMEGFGQTETTLTIATFP----WME------------------PKPG--------SMGKPAPGYEIDLIDREGRSCE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 405 TdGEVGEIWV----GGP-GLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFRYQ-GELYVCGRYRDLIIVGGRNHFP 478
Cdd:cd05970 376 A-GEEGEIVIrtskGKPvGLFGGYYKDAEKTAEVW----HDG---YYHTGDAAWMDEdGYLWFVGRTDDLIKSSGYRIGP 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 479 NDIEkTVEEAHCGVApggACAVQ--PDAPQANG-EWWLVLETG-SPVEDLDDLSRILRRRILAHHEtAPERVVWVPcrTL 554
Cdd:cd05970 448 FEVE-SALIQHPAVL---ECAVTgvPDPIRGQVvKATIVLAKGyEPSEELKKELQDHVKKVTAPYK-YPRIVEFVD--EL 520
|
410
....*....|..
gi 2181016861 555 PTTTSGKIRRRE 566
Cdd:cd05970 521 PKTISGKIRRVE 532
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2389-2966 |
1.69e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.52 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2389 PTHMIQDGpGLTLIAH-RPDKPGMPTPPAEQRRDGRwsrpAVPASSLPTdatvvaTLAEIWQRHLAIPTPGVDDDFFLLG 2467
Cdd:PRK05691 2669 PAHLILLD-SLPLTANgKLDRRALPAPDPELNRQAY----QAPRSELEQ------QLAQIWREVLNVERVGLGDNFFELG 2737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2468 GDSLVATRVYADLRAAGFgQLAFVDLFNHSTLGELAAHAgprTGPEVSVAAESTRGGthdpnRFPLTVVQnayragrega 2547
Cdd:PRK05691 2738 GDSILSIQVVSRARQLGI-HFSPRDLFQHQTVQTLAAVA---THSEAAQAEQGPLQG-----ASGLTPIQ---------- 2798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2548 lilggvaaHCYFEFELAD---------------FDRPRFDSAARQLVARHAGLRTTVSPAgtDAASSGEVAVVHTAP--I 2610
Cdd:PRK05691 2799 --------HWFFDSPVPQpqhwnqallleprqaLDPALLEQALQALVEHHDALRLRFSQA--DGRWQAEYRAVTAQEllW 2868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2611 EPVVRDHDDVRAAMRD--QIIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQLPPL- 2687
Cdd:PRK05691 2869 QVTVADFAECAALFADaqRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALp 2948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2688 --ETSFAHYV-----WNHPELLPDADEAVLPRLAASRDYWRARLPSLPPAPKLAD-MSLLFEIEEPR--FERAtatiPAV 2757
Cdd:PRK05691 2949 akTSAFRDWAarlqaYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQtVSVRLDAERTRqlLQQA----PAA 3024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2758 DWSQVTrscraegvtvaSFLLANYARVLSRWSGTDHFCINVTLFDRDP--DVVGIENVVGDFTSL--VLLECRVDEPASI 2833
Cdd:PRK05691 3025 YRTQVN-----------DLLLTALARVLCRWSGQPSVLVQLEGHGREAlfDDIDLTRSVGWFTSAypLRLTPAPGDDAAR 3093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2834 WESVRALQRQLMTdLPHRGadavwLQRELLRFHGNPT-----AAL--FPVVFTSgLGLVDAS--ARAAVRFAEPVFAASQ 2904
Cdd:PRK05691 3094 GESIKAIKEQLRA-VPHKG-----LGYGVLRYLADAAvreamAALpqAPITFNY-LGQFDQSfaSDALFRPLDEPAGPAH 3166
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 2905 TPQTVL------DFQVWesAGALKLSWDFVSQAVSPATARTQLESLvdgitgVATRSRRIEHKLGEGA 2966
Cdd:PRK05691 3167 DPDAPLpnelsvDGQVY--GGELVLRWTYSAERYDEQTIAELAEAY------LAELQALIAHCLADGA 3226
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1260-1612 |
1.84e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 76.33 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAA-ALNTIVDVNRrnridthdRLLALSALDFDLSVYD---------TFGALGCGA 1329
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYSHRSnVLHALMANNG--------DALGTSAADTMLPVVPlfhanswgiAFSAPSMGT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1330 QLVtIPeHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIpldlPRRLRRAAP--GVR 1407
Cdd:PRK06018 247 KLV-MP-GAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAM----PRSMIKAFEdmGVE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 LVAMGGATEAaiwSNEFVVDDVDPDWASIPY----------GYPLANQMFRVVDDNGDDQP--DYVAGELWIGGAGVALG 1475
Cdd:PRK06018 321 VRHAWGMTEM---SPLGTLAALKPPFSKLPGdarldvlqkqGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGPAVAAA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1476 YHNApeltsDRFVHDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCT 1555
Cdd:PRK06018 398 YYRV-----DGEILDDDG--FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPK 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 1556 -----ALgagIVVTGSGaeqfDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK06018 471 wderpLL---IVQLKPG----ETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILK 525
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
179-564 |
1.92e-13 |
|
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: 74.23 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 179 YSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDMHMVSwLPLYHDMGIFWGvFMPLLNGGCTTLIPPHDfvrnPRIW 257
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGlTEADVYLNM-LPLFHIAGLNLA-LATFHAGGANVVMEKFD----PAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 258 LETVSRFRGNWIGgpDFA--YRRCIEAFDGTalqSLDLSCLRLAT--NGAEPVRgTTLRDFTAKFRAAglrddvmapqYG 333
Cdd:cd17637 81 LELIEEEKVTLMG--SFPpiLSNLLDAAEKS---GVDLSSLRHVLglDAPETIQ-RFEETTGATFWSL----------YG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 334 LAEAGLGVTGSqtvrvwveksfdaDALERgiavevaqPNPAdGRSRALVscgdgafgwDIQIVDPDRHmTLTDGEVGEIW 413
Cdd:cd17637 145 QTETSGLVTLS-------------PYRER--------PGSA-GRPGPLV---------RVRIVDDNDR-PVPAGETGEIV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 414 VGGPGLPDGYWRQPEQTATTFgaRtadglGPYLRTGDAG-FRYQGELYVCGRY--RDLIIVGGRNHFPNDIEKTVEEaHC 490
Cdd:cd17637 193 VRGPLVFQGYWNLPELTAYTF--R-----NGWHHTGDLGrFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILE-HP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 491 GVApgGACAVQ-PDApqangEWW------LVLETGSPVEDlDDL-----SRILRRRilahhetAPERVVWVpcRTLPTTT 558
Cdd:cd17637 265 AIA--EVCVIGvPDP-----KWGegikavCVLKPGATLTA-DELiefvgSRIARYK-------KPRYVVFV--EALPKTA 327
|
....*.
gi 2181016861 559 SGKIRR 564
Cdd:cd17637 328 DGSIDR 333
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1439-1612 |
2.71e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 75.57 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1439 GYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFvhDPTGsrWYRTGDMGCYWRDGTLQFLGRAD 1518
Cdd:PRK05677 381 GIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL--DSDG--WLKTGDIALIQEDGYMRIVDRKK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1519 SQVKIRGHRVECGEIEHALRGHPLVAaatvvpihNCTALGAGIVVTGSGAEQFDDSTPGA------LRAHLAVRLPQYMI 1592
Cdd:PRK05677 457 DMILVSGFNVYPNELEDVLAALPGVL--------QCAAIGVPDEKSGEAIKVFVVVKPGEtltkeqVMEHMRANLTGYKV 528
|
170 180
....*....|....*....|
gi 2181016861 1593 PKVFVSCPELPLTANGKVDR 1612
Cdd:PRK05677 529 PKAVEFRDELPTTNVGKILR 548
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
65-636 |
3.16e-13 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.84 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 65 GLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPSTREPQRFLARaqhilrDCEPSAVYTCGELVEVLERDPILGA 144
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAAR------NTEPALVVTSDALRDRFQPSRVAEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 145 LPIRTPASTADGLAPHPGGttadadhGEHVAFLQYSSGSTGKPKGVVNTHQSILR--QAAFAANVWNGDDDMHMVSwLPL 222
Cdd:PRK06060 125 AELMSEAARVAPGGYEPMG-------GDALAYATYTSGTTGPPKAAIHRHADPLTfvDAMCRKALRLTPEDTGLCS-ARM 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 223 YHDMGIFWGVFMPLLNGGcTTLIPPHDFVRNPRIWLETvsRFRGNWIGG-PDFaYRRCIEAFDGTALQSLdlSCLRLATN 301
Cdd:PRK06060 197 YFAYGLGNSVWFPLATGG-SAVINSAPVTPEAAAILSA--RFGPSVLYGvPNF-FARVIDSCSPDSFRSL--RCVVSAGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 302 GAEPVRGTTLRDFtakFRAAGLRDDVmapqyGLAEAGLGVTgSQTVRVWveksfdadalERGIAVEVAQPnpadgrsral 381
Cdd:PRK06060 271 ALELGLAERLMEF---FGGIPILDGI-----GSTEVGQTFV-SNRVDEW----------RLGTLGRVLPP---------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 382 vscgdgafgWDIQIVDPDRHMTLTDGEvGEIWVGGPGLPDGYWRQPEQTATTfgartadglGPYLRTGDAgFRYQGE--- 458
Cdd:PRK06060 322 ---------YEIRVVAPDGTTAGPGVE-GDLWVRGPAIAKGYWNRPDSPVAN---------EGWLDTRDR-VCIDSDgwv 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 459 LYVCgRYRDLIIVGGRNHFPNDIEKTVEEAHcGVAPGGACAVQPDAPQANGEWWLVLETGSPVEdlDDLSRILRRRILAH 538
Cdd:PRK06060 382 TYRC-RADDTEVIGGVNVDPREVERLIIEDE-AVAEAAVVAVRESTGASTLQAFLVATSGATID--GSVMRDLHRGLLNR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 539 HET--APERVVWVpcRTLPTTTSGKIRRRETLNRLTAgqlEVVHEVSPRAQAPDTPAAPDDPPTE-------------LA 603
Cdd:PRK06060 458 LSAfkVPHRFAVV--DRLPRTPNGKLVRGALRKQSPT---KPIWELSLTEPGSGVRAQRDDLSASnmtiaggndggatLR 532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 604 QHLAA-------------------MLG-VEPYELAPDADLTTLGLTSMMTAQI 636
Cdd:PRK06060 533 ERLVAlrqerqrlvvdavcaeaakMLGePDPWSVDQDLAFSELGFDSQMTVTL 585
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
172-469 |
3.40e-13 |
|
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: 74.94 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQ-AAFAANV--WNGDDDMHmVSWLPLYHDMG-------IFWGVFM----PLL 237
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGiAGLGDRVpeLLGPDDRY-LAYLPLAHIFElaaenvcLYRGGTIgygsPRT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 238 ---------NGGCTTLiPPHDFVRNPRIWlETVsrFRG-----NWIGGP-----DFAYRRCIEAF----DGTALQSLDLS 294
Cdd:cd17639 167 ltdkskrgcKGDLTEF-KPTLMVGVPAIW-DTI--RKGvlaklNPMGGLkrtlfWTAYQSKLKALkegpGTPLLDELVFK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 295 CLRLATNGAepVR-----GTTLRDFTAKFRAAGLRDdvMAPQYGLAEAglgvTGSQTVRVWveksfdaDALERGIaveVA 369
Cdd:cd17639 243 KVRAALGGR--LRymlsgGAPLSADTQEFLNIVLCP--VIQGYGLTET----CAGGTVQDP-------GDLETGR---VG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 370 QPnpadgrsraLVSCgdgafgwDIQIVD-PD-RHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLR 447
Cdd:cd17639 305 PP---------LPCC-------EIKLVDwEEgGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAF---DGDG---WFH 362
|
330 340
....*....|....*....|...
gi 2181016861 448 TGDAG-FRYQGELYVCGRYRDLI 469
Cdd:cd17639 363 TGDIGeFHPDGTLKIIDRKKDLV 385
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
15-565 |
3.69e-13 |
|
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: 75.06 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 15 DRSVPAVFAEWVGRRPDAVALrtvaatgIDD---WTYQRLWDHVREI-RDVAFSGLSAGIRIPMALPGGADYVAGMLAAL 90
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAV-------VDGdrrLTYRELDRRADRLaAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 91 AAGLIPVpVYLPSTRepqrfLARAQHILRDCEPSAVYTCGELVEVLERdpilgALPIRTPASTADglaphpggttadadh 170
Cdd:cd05920 87 RLGAVPV-LALPSHR-----RSELSAFCAHAEAVAYIVPDRHAGFDHR-----ALARELAESIPE--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 gehVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFW-GVFMPLLNGGCTTLIPPHD 249
Cdd:cd05920 141 ---VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 fvrnPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGtalQSLDLSCLRLATNGAEPVRGTTLRdftakfRAAGLRDDVMA 329
Cdd:cd05920 218 ----PDAAFPLIEREGVTVTALVPALVSLWLDAAAS---RRADLSSLRLLQVGGARLSPALAR------RVPPVLGCTLQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 330 PQYGLAEAGLGVTgsqtvrvwvekSFDaDALERgiaVEVAQPNPadgrsralVSCGDgafgwDIQIVDPDRHmTLTDGEV 409
Cdd:cd05920 285 QVFGMAEGLLNYT-----------RLD-DPDEV---IIHTQGRP--------MSPDD-----EIRVVDEEGN-PVPPGEE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 410 GEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFRY-QGELYVCGRYRDLIIVGGRNHFPNDIEKTVeEA 488
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAF---TPDG---FYRTGDLVRRTpDGYLVVEGRIKDQINRGGEKIAAEEVENLL-LR 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 489 HCGVAPGGACAVqPDAPQANGEWWLVLETGSPVeDLDDLSRILRRRILAHHEtAPERVVWVPcrTLPTTTSGKIRRR 565
Cdd:cd05920 409 HPAVHDAAVVAM-PDELLGERSCAFVVLRDPPP-SAAQLRRFLRERGLAAYK-LPDRIEFVD--SLPLTAVGKIDKK 480
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
166-483 |
5.65e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 74.55 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 166 ADADHGEHVAFLqYSSGSTGKPKGVVNTHQSILRQAAFAANVWN---GDDDMHMvswLPLYhdmgifwGVFMPLLngGCT 242
Cdd:PRK09274 169 ADLAPDDMAAIL-FTSGSTGTPKGVVYTHGMFEAQIEALREDYGiepGEIDLPT---FPLF-------ALFGPAL--GMT 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 243 TLIPPHDFVR----NPRIWLETVSRFR-GNWIGGPdfAY-----RRCIEafdgtalQSLDLSCLRLATNGAEPVRGTTLR 312
Cdd:PRK09274 236 SVIPDMDPTRpatvDPAKLFAAIERYGvTNLFGSP--ALlerlgRYGEA-------NGIKLPSLRRVISAGAPVPIAVIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 313 DFTAKFRAAGlrdDVMAPqYGLAEAgLGVT--GSQTVrvwVEKSFDADALERGIAVEvaqpNPADGRSRALVSCGDGAfg 390
Cdd:PRK09274 307 RFRAMLPPDA---EILTP-YGATEA-LPISsiESREI---LFATRAATDNGAGICVG----RPVDGVEVRIIAISDAP-- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 391 wdIQIVDPDRhmTLTDGEVGEIWVGGPGLPDGYWRQPEQTAttfGARTADGLGP-YLRTGDAGFR-YQGELYVCGRYRDL 468
Cdd:PRK09274 373 --IPEWDDAL--RLATGEIGEIVVAGPMVTRSYYNRPEATR---LAKIPDGQGDvWHRMGDLGYLdAQGRLWFCGRKAHR 445
|
330
....*....|....*
gi 2181016861 469 IIVGGRNHFPNDIEK 483
Cdd:PRK09274 446 VETAGGTLYTIPCER 460
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1250-1612 |
5.67e-13 |
|
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: 74.91 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1250 ECAPTdpiRIDPHDAAYVIYTSGSTGEPKGVLVSHA-----AALNTivdvnrRNRIDTHDRLLALSALDfdlsV------ 1318
Cdd:cd05966 222 ECEPE---WMDSEDPLFILYTSGSTGKPKGVVHTTGgyllyAATTF------KYVFDYHPDDIYWCTAD----Igwitgh 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1319 -YDTFGALGCGAQLV------TIPEHARrdafhWLSLTTEFGITVWNSVPGLMDMLlIAAGD---KAGSLPTLR---SVf 1385
Cdd:cd05966 289 sYIVYGPLANGATTVmfegtpTYPDPGR-----YWDIVEKHKVTIFYTAPTAIRAL-MKFGDewvKKHDLSSLRvlgSV- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1386 lsGDWIpldlprrlrraAPgvrlvamggatEAAIWSNEFVVDD----VDPDW---------ASIPYGYPL--ANQMF--- 1447
Cdd:cd05966 362 --GEPI-----------NP-----------EAWMWYYEVIGKErcpiVDTWWqtetggimiTPLPGATPLkpGSATRpff 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1448 ----RVVDDNGDDQPDYVAGELWIGGA--GVALGYHNAPEltsdRFVHD--PTGSRWYRTGDmGCYW-RDGTLQFLGRAD 1518
Cdd:cd05966 418 giepAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTyfSKFPGYYFTGD-GARRdEDGYYWITGRVD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1519 SQVKIRGHRVECGEIEHALRGHPLVAAATVVPI-HNCTalGAGIV--VTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKV 1595
Cdd:cd05966 493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRpHDIK--GEAIYafVTLKDGEEPSDELRKELRKHVRKEIGPIATPDK 570
|
410
....*....|....*..
gi 2181016861 1596 FVSCPELPLTANGKVDR 1612
Cdd:cd05966 571 IQFVPGLPKTRSGKIMR 587
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
180-566 |
5.94e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 74.41 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 180 SSGSTGKPKGV-------VNTHQSILRQAAfaanvWNGDDDMHMVSwlPLYHDMGIFWGVFMPLLNggcTTLIPPHDFvr 252
Cdd:PRK13382 204 TSGTTGTPKGArrsgpggIGTLKAILDRTP-----WRAEEPTVIVA--PMFHAWGFSQLVLAASLA---CTIVTRRRF-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 NPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDgTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAPQY 332
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFDRIMDLPA-EVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF------GDVIYNNY 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 333 GLAEAGLgvtgsqtvrvwveksfdadalergiaveVAQPNPADGRsRALVSCGDGAFGWDIQIVDPDrHMTLTDGEVGEI 412
Cdd:PRK13382 345 NATEAGM----------------------------IATATPADLR-AAPDTAGRPAEGTEIRILDQD-FREVPTGEVGTI 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 413 WVGGPGLPDGYwrqpeqtatTFGArTADGLGPYLRTGDAGF-RYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVeEAHCG 491
Cdd:PRK13382 395 FVRNDTQFDGY---------TSGS-TKDFHDGFMASGDVGYlDENGRLFVVGRDDEMIVSGGENVYPIEVEKTL-ATHPD 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 492 VAPGGACAVQPDAPQANGEWWLVLETGSPvEDLDDLSRILRRRiLAHHETaPERVVWVPcrTLPTTTSGKIRRRE 566
Cdd:PRK13382 464 VAEAAVIGVDDEQYGQRLAAFVVLKPGAS-ATPETLKQHVRDN-LANYKV-PRDIVVLD--ELPRGATGKILRRE 533
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1263-1615 |
6.51e-13 |
|
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: 74.42 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALNTIVdVNRRnridthdRLLALSALDFDLSVYDT----------FGALGCGAqLV 1332
Cdd:cd05928 175 EPMAIYFTSGTTGSPKMAEHSHSSLGLGLK-VNGR-------YWLDLTASDIMWNTSDTgwiksawsslFEPWIQGA-CV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1333 TIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLiaAGD-KAGSLPTLRSVFLSGDWIpldLPRRLR--RAAPGVRLV 1409
Cdd:cd05928 246 FVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLV--QQDlSSYKFPSLQHCVTGGEPL---NPEVLEkwKAQTGLDIY 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1410 AMGGATEAAIWSNEFVVDDVDPDW---ASIPYGyplanqmFRVVDDNGDDQPDYVAGELWI-----GGAGVALGYHNAPE 1481
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSmgkASPPYD-------VQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1482 LTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV----PIHNcTAL 1557
Cdd:cd05928 394 KTAATIRGD-----FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVsspdPIRG-EVV 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 1558 GAGIVVTgsgaEQFDDSTPGALRAHL-----AVRLPqYMIP-KV-FVScpELPLTANGKVDRGKI 1615
Cdd:cd05928 468 KAFVVLA----PQFLSHDPEQLTKELqqhvkSVTAP-YKYPrKVeFVQ--ELPKTVTGKIQRNEL 525
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
174-571 |
7.03e-13 |
|
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: 72.36 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWgVFMPLLNGGCTTLIPPHDfvrn 253
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 254 priwletvsrfrgnwiggpDFAYRRCIEAFDGTALQSLDLscLRLATNGAEPVRGTTLR-----------DFTAKFRAAG 322
Cdd:cd17630 77 -------------------ALAEDLAPPGVTHVSLVPTQL--QRLLDSGQGPAALKSLRavllggapippELLERAADRG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 323 LRddvMAPQYGLAEAGLGVTGSQtvrvwveksfdADALERGiavEVAQPNPadgrsralvscgdgafGWDIQIVDPdrhm 402
Cdd:cd17630 136 IP---LYTTYGMTETASQVATKR-----------PDGFGRG---GVGVLLP----------------GRELRIVED---- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 403 tltdgevGEIWVGGPGLPDGYWRQPEQtattfGARTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDI 481
Cdd:cd17630 179 -------GEIWVGGASLAMGYLRGQLV-----PEFNEDG---WFTTKDLGeLHADGRLTVLGRADNMIISGGENIQPEEI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 482 EKtVEEAHCGVApgGACAVqpdaPQANGEWW----LVLETGSPVeDLDDLSRILRRRILAHHetAPERVVWVPcrTLPTT 557
Cdd:cd17630 244 EA-ALAAHPAVR--DAFVV----GVPDEELGqrpvAVIVGRGPA-DPAELRAWLKDKLARFK--LPKRIYPVP--ELPRT 311
|
410
....*....|....
gi 2181016861 558 TSGKIRRRETLNRL 571
Cdd:cd17630 312 GGGKVDRRALRAWL 325
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
172-571 |
9.81e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 74.06 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQA-AFAANVWNGDDDMHMVSwLPLYHDMGIFWGVFMpLLNGGCTTLIPPHD- 249
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSlAKIAIVGYGEDDVYLHT-APLCHIGGLSSALAM-LMVGACHVLLPKFDa 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 --------------FVRNPRIW--LETVSRFRGNWIGGPdfayrrcieafdgtalqsldlsCLRLATNGAEPVRGTTLRD 313
Cdd:PLN02860 250 kaalqaikqhnvtsMITVPAMMadLISLTRKSMTWKVFP----------------------SVRKILNGGGSLSSRLLPD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 314 FTAKFRAAGLrddvmAPQYGLAEAGLGVTgSQTVRVWVEKSFDAdalergIAVEVAQPNPADGRSRALVSCGDGAFGWDI 393
Cdd:PLN02860 308 AKKLFPNAKL-----FSAYGMTEACSSLT-FMTLHDPTLESPKQ------TLQTVNQTKSSSVHQPQGVCVGKPAPHVEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 394 QIVDPDrhmtltDGEVGEIWVGGPGLPDGYWRQPEQTATTfgaRTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVG 472
Cdd:PLN02860 376 KIGLDE------SSRVGRILTRGPHVMLGYWGQNSETASV---LSNDG---WLDTGDIGwIDKAGNLWLIGRSNDRIKTG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 473 GRNHFPNDIEkTVEEAHcgvaPGGACAVQPDAPQAN-GE-----------W-WLVLETGSPVEdlddlSRILRRRILAHH 539
Cdd:PLN02860 444 GENVYPEEVE-AVLSQH----PGVASVVVVGVPDSRlTEmvvacvrlrdgWiWSDNEKENAKK-----NLTLSSETLRHH 513
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2181016861 540 --------ETAPER-VVWVpcRTLPTTTSGKIRR----RETLNRL 571
Cdd:PLN02860 514 creknlsrFKIPKLfVQWR--KPFPLTTTGKIRRdevrREVLSHL 556
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
157-482 |
1.37e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 73.15 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 157 LAPHPGGTTADA--DHGEHVAFLqYSSGSTGKPKGVVNTHQsilrQAAFAANVWNGD-------DDMHMVSwLPLYHDMG 227
Cdd:PRK07470 147 VARHLGARVANAavDHDDPCWFF-FTSGTTGRPKAAVLTHG----QMAFVITNHLADlmpgtteQDASLVV-APLSHGAG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 228 IFwgvfmPLLN--GGCTTLIPPHDFVRNPRIWlETVSRFRGNWIggpdFAYRRCIEAF-DGTALQSLDLSCLRLATNGAE 304
Cdd:PRK07470 221 IH-----QLCQvaRGAATVLLPSERFDPAEVW-ALVERHRVTNL----FTVPTILKMLvEHPAVDRYDHSSLRYVIYAGA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 305 PvrgTTLRDftaKFRAAGLRDDVMAPQYGLAEaglgVTGSQTVrvwveksfdadalergiaVEVAQPNPADGRSRALVSC 384
Cdd:PRK07470 291 P---MYRAD---QKRALAKLGKVLVQYFGLGE----VTGNITV------------------LPPALHDAEDGPDARIGTC 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 385 GDGAFGWDIQIVDpDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFR-YQGELYVCG 463
Cdd:PRK07470 343 GFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF----RDG---WFRTGDLGHLdARGFLYITG 414
|
330
....*....|....*....
gi 2181016861 464 RYRDLIIVGGRNHFPNDIE 482
Cdd:PRK07470 415 RASDMYISGGSNVYPREIE 433
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1260-1615 |
1.79e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 73.13 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAAALntivdvnrrnridthdrLLALSAL-DFDLSVYDTF---------------- 1322
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVISHRGAY-----------------LSTLSAIiGWEMGTCPVYlwtlpmfhcngwtftw 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1323 -----GALGCGAQLVTIPEHARRDAFHwlslttefGITVWNSVPGLMDMLLiaAGDKAGSLPtlRS----VFLSGDWIPL 1393
Cdd:PLN03102 247 gtaarGGTSVCMRHVTAPEIYKNIEMH--------NVTHMCCVPTVFNILL--KGNSLDLSP--RSgpvhVLTGGSPPPA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1394 DLPRRLRRAapGVRLVAMGGATEAA------IWSNEfvvddvdpdWASIPYGYPL---ANQMFRV-----VDDNGDDQPD 1459
Cdd:PLN03102 315 ALVKKVQRL--GFQVMHAYGLTEATgpvlfcEWQDE---------WNRLPENQQMelkARQGVSIlgladVDVKNKETQE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1460 YVA------GELWIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEI 1533
Cdd:PLN03102 384 SVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHG-----WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEV 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1534 EHALRGHPLVAAATVVPIHNCT--ALGAGIVVTGSGAEQFDD------STPGALRAHLAVRLPQYMIPKVFVSCPELPLT 1605
Cdd:PLN03102 459 ENVLYKYPKVLETAVVAMPHPTwgETPCAFVVLEKGETTKEDrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQELPKN 538
|
410
....*....|
gi 2181016861 1606 ANGKVDRGKI 1615
Cdd:PLN03102 539 GNGKILKPKL 548
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1253-1612 |
2.68e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 72.37 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1253 PTDPiridPHDAAYVIYTSGSTGEPKGVLVSHAAAL-NTIVDVN-RRNRIDTHDrlLALSALDFdLSVYDTFGALGC--- 1327
Cdd:PRK06710 201 PCDP----ENDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQwLYNCKEGEE--VVLGVLPF-FHVYGMTAVMNLsim 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1328 -GAQLVTIPEHARRDAFHWLSlttEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGv 1406
Cdd:PRK06710 274 qGYKMVLIPKFDMKMVFEAIK---KHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGG- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1407 RLVAMGGATEAA-IWSNEFVVDDVDPDWASIPygYPLANQMFrVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSd 1485
Cdd:PRK06710 350 KLVEGYGLTESSpVTHSNFLWEKRVPGSIGVP--WPDTEAMI-MSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1486 RFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVV----PIHNCTAlgAGI 1561
Cdd:PRK06710 426 AVLQDG----WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIgvpdPYRGETV--KAF 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1562 VVTGSGAEQFDDSTPGALRAHLAVrlpqYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK06710 500 VVLKEGTECSEEELNQFARKYLAA----YKVPKVYEFRDELPKTTVGKILR 546
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
685-983 |
2.89e-12 |
|
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: 71.90 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 685 PTTPLQQAYwvgrgAEQPLGGVGC--QTYFELVGARVDAGRLAAALDALTRRHPMLRATFP-DPGR---CLITPEAVRLP 758
Cdd:cd19534 3 PLTPIQRWF-----FEQNLAGRHHfnQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRrEDGGwqqRIRGDVEELFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 759 LAVHDLTDAPV-TTRDTHLAEIRRRLrthrfDIETGDTWTVELTRLPHGC----IV--HFAVDLIIADVtsigtMLRDLA 831
Cdd:cd19534 78 LEVVDLSSLAQaAAIEALAAEAQSSL-----DLEEGPLLAAALFDGTDGGdrllLVihHLVVDGVSWRI-----LLEDLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 832 ASYR----GEKLPAPSAT----FADLIQ--STSPPPqacadrLPEGPQLPRVQEADISFLRHQH------------TLSA 889
Cdd:cd19534 148 AAYEqalaGEPIPLPSKTsfqtWAELLAeyAQSPAL------LEELAYWRELPAADYWGLPKDPeqtygdartvsfTLDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 890 LATKAI-DDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGR-----SPEVSDVVGDFTETHLYRAQLDGQISF 963
Cdd:cd19534 222 EETEALlQEANAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGReeidpGLDLSRTVGWFTSMYPVVLDLEASEDL 301
|
330 340
....*....|....*....|...
gi 2181016861 964 VDQaqvtqkgLRT---ALRAAPA 983
Cdd:cd19534 302 GDT-------LKRvkeQLRRIPN 317
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-673 |
3.05e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 73.45 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 16 RSVPAVFAEWVGRRPDAVALrtvaATGIDDWTYQRLWDHVREIRDVAFS-GLSAGIRIPMALPGGADYVAGMLAALAAGL 94
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAV----VFDEEKLTYAELNRRANRLAHALIArGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 95 IPVPVYLPSTREpqrflaRAQHILRDCEPSAVYTCGELVEVLERDPILGALPIrtpaSTADGLAPHPGGTTADADHGEHV 174
Cdd:PRK12316 4627 AYVPLDPEYPRE------RLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLAL----DRDEDWEGFPAHDPAVRLHPDNL 4696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDmGIFWGVFMPLLNGGCTtlipphdFVRNP 254
Cdd:PRK12316 4697 AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-GSHEGLYHPLINGASV-------VIRDD 4768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 255 RIWLetvsrfrgnwiggPDFAYRRCIEA------FDGTALQSL--------DLSCLRLATNGAEPVRGTTLRDFTAKFRA 320
Cdd:PRK12316 4769 SLWD-------------PERLYAEIHEHrvtvlvFPPVYLQQLaehaerdgEPPSLRVYCFGGEAVAQASYDLAWRALKP 4835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 321 AGLRDdvmapQYGLAEAGLgvtgsqTVRVWVEKSFDADALErgiAVEVAQPNPadGRSRALVscgDGAFGwdiqivdpdr 400
Cdd:PRK12316 4836 VYLFN-----GYGPTETTV------TVLLWKARDGDACGAA---YMPIGTPLG--NRSGYVL---DGQLN---------- 4886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 401 hmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFP 478
Cdd:PRK12316 4887 --PLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLyRTGDlARYRADGVIDYLGRVDHQVKIRGFRIEL 4964
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 479 NDIEK------TVEEAHCGVAPGGACA-----VQPDAPQangewwLVLETGSPVEDLDDLSRILRRRIlahhetaPERVV 547
Cdd:PRK12316 4965 GEIEArlrehpAVREAVVIAQEGAVGKqlvgyVVPQDPA------LADADEAQAELRDELKAALRERL-------PEYMV 5031
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 548 ---WVPCRTLPTTTSGKIRRReTLNRLTAGQLEVVHeVSPRaqapdtpaapddppTELAQHLAAM----LGVEPYELapD 620
Cdd:PRK12316 5032 pahLVFLARMPLTPNGKLDRK-ALPQPDASLLQQAY-VAPR--------------SELEQQVAAIwaevLQLERVGL--D 5093
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 621 ADLTTLGLTSMMTAQIVEWSSSQ-SRRLDFADLYAEPTLRSWQRLFDAAPPVQT 673
Cdd:PRK12316 5094 DNFFELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
171-565 |
3.77e-12 |
|
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: 71.58 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFwGVFMPLLNGGC-----TTLI 245
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVF-ELFGPLATGGKvvladNVLA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 246 PPHDFVRNPRIWLETVsrfrgnwiggPDFAyrrcieafdgTALQSLD-----LSCLRLAtngAEPVRGTTLRDFTAKFRA 320
Cdd:cd12115 183 LPDLPAAAEVTLINTV----------PSAA----------AELLRHDalpasVRVVNLA---GEPLPRDLVQRLYARLQV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 321 AGLRDdvmapQYGLAEAGLGVTGSqtvrvwveksfdadALERGiavevAQPNPADGRSRAlvscgdgafGWDIQIVDpdR 400
Cdd:cd12115 240 ERVVN-----LYGPSEDTTYSTVA--------------PVPPG-----ASGEVSIGRPLA---------NTQAYVLD--R 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 401 HMT-LTDGEVGEIWVGGPGLPDGYWRQPEQTATTF-GARTADGLGPYlRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHF 477
Cdd:cd12115 285 ALQpVPLGVPGELYIGGAGVARGYLGRPGLTAERFlPDPFGPGARLY-RTGDlVRWRPDGLLEFLGRADNQVKVRGFRIE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 478 PNDIEKTVEEaHCGVAPGGACAVQPDAPQANGEWWLVLETGSPVeDLDDLSRILRRRILAHheTAPERVVWVPcrTLPTT 557
Cdd:cd12115 364 LGEIEAALRS-IPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-LVEDLRRHLGTRLPAY--MVPSRFVRLD--ALPLT 437
|
....*...
gi 2181016861 558 TSGKIRRR 565
Cdd:cd12115 438 PNGKIDRS 445
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
28-579 |
5.12e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 71.58 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 28 RRPDAVALRTvaATGIDDWTYQRLwdhVREIRDVAFS----GLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVylpS 103
Cdd:PRK05857 26 QQPEAIALRR--CDGTSALRYREL---VAEVGGLAADlraqSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA---D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 104 TREPQRFLARAQHIlrdCEPSAVYTC-GELVEVLERDPILGALPIRTPASTAD-GLAPHPGGT---TADADHGEHVAF-L 177
Cdd:PRK05857 98 GNLPIAAIERFCQI---TDPAAALVApGSKMASSAVPEALHSIPVIAVDIAAVtRESEHSLDAaslAGNADQGSEDPLaM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 178 QYSSGSTGKPKGVVNTHQS------ILRQAAFAANVWNGDDDMHmvSWLPLYHDMGIFWgVFMPLLNGG-CTTlipphdf 250
Cdd:PRK05857 175 IFTSGTTGEPKAVLLANRTffavpdILQKEGLNWVTWVVGETTY--SPLPATHIGGLWW-ILTCLMHGGlCVT------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 251 vrnpriwletvsrfrgnwiGGPDFAYRRCIEAFDGTA-------LQSLDLSCLRLATNGAEPVR-----GTtlRDFTAKF 318
Cdd:PRK05857 245 -------------------GGENTTSLLEILTTNAVAttclvptLLSKLVSELKSANATVPSLRlvgygGS--RAIAADV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 319 R---AAGLRddvMAPQYGLAEAGLGVTGSQTvrvwveksfDADALERGIAVEVAQPNPAdgrSRALVSCGDGAfgwdiqi 395
Cdd:PRK05857 304 RfieATGVR---TAQVYGLSETGCTALCLPT---------DDGSIVKIEAGAVGRPYPG---VDVYLAATDGI------- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 396 vDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFRYQ-GELYVCGRYRDLIIVGGR 474
Cdd:PRK05857 362 -GPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVL----IDG---WVNTGDLLERREdGFFYIKGRSSEMIICGGV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 475 NHFPNDIEKTVEEAhCGVAPgGACAVQPDAPQANgewwLVLETGSPVEDLDD-LSRILRRRILAHHETAPERVV----WV 549
Cdd:PRK05857 434 NIAPDEVDRIAEGV-SGVRE-AACYEIPDEEFGA----LVGLAVVASAELDEsAARALKHTIAARFRRESEPMArpstIV 507
|
570 580 590
....*....|....*....|....*....|
gi 2181016861 550 PCRTLPTTTSGKIRRRETLNRLTAGQLEVV 579
Cdd:PRK05857 508 IVTDIPRTQSGKVMRASLAAAATADKARVV 537
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
716-949 |
5.44e-12 |
|
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: 70.68 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 716 GARVDAGRLAAALDALTRRHPMLRATFPDPGRCL---ITPEAVR-LPLAVHDLTdapvttrdthlAEIRRRlrthrFDIE 791
Cdd:cd19537 33 SGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLrrsYSSSPPRvQRVDTLDVW-----------KEINRP-----FDLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 792 TGDTWTVELTRlphgciVHFAVDL--IIADVTSIGTMLRDLAASYRGEKLPAPSATFADLIQSTSPPPQACAD------R 863
Cdd:cd19537 97 REDPIRVFISP------DTLLVVMshIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSRPASPEDLDfwseylS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 864 LPEGPQLPRvQEADISF--LRHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGR-SPEV 940
Cdd:cd19537 171 GLPLLNLPR-RTSSKSYrgTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRtSEED 249
|
....*....
gi 2181016861 941 SDVVGDFTE 949
Cdd:cd19537 250 METVGLFLE 258
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1256-1612 |
5.81e-12 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 71.45 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1256 PIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNR-----------RNRIDTHDRLLALSALDFDLSVYDTFGa 1324
Cdd:PRK08751 202 TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagtgkleegCEVVITALPLYHIFALTANGLVFMKIG- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1325 lGCGaQLVTIPeharRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAp 1404
Cdd:PRK08751 281 -GCN-HLISNP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVT- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1405 GVRLVAMGGATEAaiwSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTS 1484
Cdd:PRK08751 354 GLTLVEAYGLTET---SPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1485 DrfVHDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVA--AATVVPIHNCTALGAGIV 1562
Cdd:PRK08751 431 K--VMDADG--WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLevAAVGVPDEKSGEIVKVVI 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1563 VTGSGAEQFDDstpgaLRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK08751 507 VKKDPALTAED-----VKAHARANLTGYKQPRIIEFRKELPKTNVGKILR 551
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1177-1612 |
6.15e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 71.18 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIqLPKGPSQIV-AVLGVMMAGC-----------TYLPVGVDQPAERLSRICARS--------AMAGLIRTDsdtq 1236
Cdd:PRK07768 54 GDAVAV-LAGAPVEIApTAQGLWMRGAsltmlhqptprTDLAVWAEDTLRVIGMIGAKAvvvgepflAAAPVLEEK---- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1237 daGVAVSDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDT-HDRLLALSALDFD 1315
Cdd:PRK07768 129 --GIRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1316 LsvydtfGALG-------CGAQLVTI-PEHARRDAFHWLSLTTEFGITVW---NSVPGLMDMLLI-AAGDKAGSLPTLRS 1383
Cdd:PRK07768 207 M------GMVGfltvpmyFGAELVKVtPMDFLRDPLLWAELISKYRGTMTaapNFAYALLARRLRrQAKPGAFDLSSLRF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1384 VFLSGDWI-PLDLPRRLRRAAP-GVRLVAMG---GATEAAI------WSNEFVVDDVDPDWASI---------------- 1436
Cdd:PRK07768 281 ALNGAEPIdPADVEDLLDAGARfGLRPEAILpayGMAEATLavsfspCGAGLVVDEVDADLLAAlrravpatkgntrrla 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1437 PYGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYhnapeLTSDRFV--HDPTGsrWYRTGDMGCYWRDGTLQFL 1514
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIpaQDADG--WLDTGDLGYLTEEGEVVVC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1515 GRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTALGA-GIVVTGSGAEQFDDSTPGALR--------AHLAV 1585
Cdd:PRK07768 434 GRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSReGFAVAVESNAFEDPAEVRRIRhqvahevvAEVGV 513
|
490 500 510
....*....|....*....|....*....|...
gi 2181016861 1586 R------LPQYMIPKvfvscpelplTANGKVDR 1612
Cdd:PRK07768 514 RprnvvvLGPGSIPK----------TPSGKLRR 536
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
170-574 |
6.37e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 71.17 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 170 HGEHVAFLQYSSGSTGKPKGVVNTHQSILrqAAFAANV--------WNGDDDMHMVswLPLYHdmgIFW--GVFMPLLNG 239
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLV--TSVAQQVdgenpnlyFHSDDVILCV--LPMFH---IYSlnSVLLCGLRV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 240 GCTTLI-PPHDFVRnpriWLETVSRfrgnwiggpdfaYRRCIEAF---------DGTALQSLDLSCLRLATNGAEPVrGT 309
Cdd:PLN02246 250 GAAILImPKFEIGA----LLELIQR------------HKVTIAPFvppivlaiaKSPVVEKYDLSSIRMVLSGAAPL-GK 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 310 TLRD-FTAKFRAAglrddVMAPQYGLAEAGLGVtgsqtvrvwveksfdadALERGIAVEVAQPNPAdgrsralvSCGDGA 388
Cdd:PLN02246 313 ELEDaFRAKLPNA-----VLGQGYGMTEAGPVL-----------------AMCLAFAKEPFPVKSG--------SCGTVV 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 389 FGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTattfgARTADGLGpYLRTGDAGF-RYQGELYVCGRYRD 467
Cdd:PLN02246 363 RNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEAT-----ANTIDKDG-WLHTGDIGYiDDDDELFIVDRLKE 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 468 LIIVGGRNHFPNDIEKTVeEAHCGVAPggaCAVQPDAPQANGE---WWLVLETGSPVEDlDDLSRILRRRILAHHETapE 544
Cdd:PLN02246 437 LIKYKGFQVAPAELEALL-ISHPSIAD---AAVVPMKDEVAGEvpvAFVVRSNGSEITE-DEIKQFVAKQVVFYKRI--H 509
|
410 420 430
....*....|....*....|....*....|
gi 2181016861 545 RVVWVPcrTLPTTTSGKIRRRETLNRLTAG 574
Cdd:PLN02246 510 KVFFVD--SIPKAPSGKILRKDLRAKLAAG 537
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1252-1610 |
6.70e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 71.25 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1252 APTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSH---AAALNTIVDVNRRNRIDTHDRLLAL---SALDFDLSVydtfgAL 1325
Cdd:PRK07867 142 AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHrkvASAGVMLAQRFGLGPDDVCYVSMPLfhsNAVMAGWAV-----AL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1326 GCGAqlvTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIA--AGDKAGSlpTLRSVFlSGDWIPLDLPRRLRRAa 1403
Cdd:PRK07867 217 AAGA---SIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATpeRPDDADN--PLRIVY-GNEGAPGDIARFARRF- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1404 pGVRLVAMGGATEAAI----------WSNEFVVDDV---DPD-WASIPYGyplanqmfrVVDDNGDDQPDYVAGELW-IG 1468
Cdd:PRK07867 290 -GCVVVDGFGSTEGGVaitrtpdtppGALGPLPPGVaivDPDtGTECPPA---------EDADGRLLNADEAIGELVnTA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1469 GAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGcyWRD--GTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAA 1546
Cdd:PRK07867 360 GPGGFEGYYNDPEADAERMRGG-----VYWSGDLA--YRDadGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEV 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1547 TVVPIHNCTA----LGAgiVVTGSGAEqFDdstPGALRAHLAVR--LPQYMIPKVFVSCPELPLTANGKV 1610
Cdd:PRK07867 433 AVYAVPDPVVgdqvMAA--LVLAPGAK-FD---PDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKV 496
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1177-1550 |
7.12e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 71.17 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1177 GSVIGIQLPKGPSQIVAVLGVMMAGCT-------YLP-------------VGVDQPA--ERLSRICARSAMAgLIRTDSD 1234
Cdd:PLN02246 75 GDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTPaeiakqakasgakLIITQSCyvDKLKGLAEDDGVT-VVTIDDP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1235 TqDAGVAVSDITAMIEcAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTI---VDVNRRNridthdrlLALSA 1311
Cdd:PLN02246 154 P-EGCLHFSELTQADE-NELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVaqqVDGENPN--------LYFHS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1312 LDFDLSVYDTF----------GALGCGAQLVTIPehaRRDAFHWLSLTTEFGITVWNSVPGLMdmLLIAAGDKAGS--LP 1379
Cdd:PLN02246 224 DDVILCVLPMFhiyslnsvllCGLRVGAAILIMP---KFEIGALLELIQRHKVTIAPFVPPIV--LAIAKSPVVEKydLS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1380 TLRSVfLSGDwIPL--DLPRRLRRAAPGVRLVAMGGATEAAiwsnefVVDDVDPDWASIPY-------GYPLANQMFRVV 1450
Cdd:PLN02246 299 SIRMV-LSGA-APLgkELEDAFRAKLPNAVLGQGYGMTEAG------PVLAMCLAFAKEPFpvksgscGTVVRNAELKIV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1451 D-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFvhDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVE 1529
Cdd:PLN02246 371 DpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTI--DKDG--WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVA 446
|
410 420
....*....|....*....|.
gi 2181016861 1530 CGEIEHALRGHPLVAAATVVP 1550
Cdd:PLN02246 447 PAELEALLISHPSIADAAVVP 467
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
172-482 |
7.29e-12 |
|
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: 70.57 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSilrqaaFAANVWNGDDDMHMVswlPLYHDMGIF--WGVFMPLLngGCTTLIPPHD 249
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGT------FAAQIDALRQLYGIR---PGEVDLATFplFALFGPAL--GLTSVIPDMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 FVR----NPRIWLETVSRFRGNWIGGPDFAYRRCIEAfdgTALQSLDLSCLRLATNGAEPVRGTTLrdftAKFRAAgLRD 325
Cdd:cd05910 154 PTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARY---CAQHGITLPSLRRVLSAGAPVPIALA----ARLRKM-LSD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 326 D--VMAPqYGLAEAgLGVT--GSQTVRvwvekSFDADALERGIAVEVAQpnPADGRSRALVSCGDGAfgwdiqIVDPDRH 401
Cdd:cd05910 226 EaeILTP-YGATEA-LPVSsiGSRELL-----ATTTAATSGGAGTCVGR--PIPGVRVRIIEIDDEP------IAEWDDT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 402 MTLTDGEVGEIWVGGPGLPDGYWRQPEQTATtfgARTADGLGPYL-RTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPN 479
Cdd:cd05910 291 LELPRGEIGEITVTGPTVTPTYVNRPVATAL---AKIDDNSEGFWhRMGDLGyLDDEGRLWFCGRKAHRVITTGGTLYTE 367
|
...
gi 2181016861 480 DIE 482
Cdd:cd05910 368 PVE 370
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2565-2839 |
9.16e-12 |
|
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: 70.18 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2565 DFDRPRFDSAARQLVARHAGLRTtvspAGTDAASSGEV--AVVHTAPIEPVVR---DHDDVRAA---MRDQIIDLTArpG 2636
Cdd:cd19532 35 PLDVARLERAVRAVGQRHEALRT----CFFTDPEDGEPmqGVLASSPLRLEHVqisDEAEVEEEferLKNHVYDLES--G 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2637 IDFGVQ--TRGDGRT--VVG---ISMdntmlDGASMMIALSELDHLYRGETvdqLPPLETSFAHYVwnhpelLPDADEAV 2709
Cdd:cd19532 109 ETMRIVllSLSPTEHylIFGyhhIAM-----DGVSFQIFLRDLERAYNGQP---LLPPPLQYLDFA------ARQRQDYE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2710 LPRLAASRDYWRARLPSLPPAPKLADMSLLF---EIEEPRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLS 2786
Cdd:cd19532 175 SGALDEDLAYWKSEFSTLPEPLPLLPFAKVKsrpPLTRYDTHTAERRLDAALAARIKEASRKLRVTPFHFYLAALQVLLA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 2787 RWSGTDHFCINVTlfD---RDPDVVGienVVGDFTSLVLLECRVDEPASIWESVRA 2839
Cdd:cd19532 255 RLLDVDDICIGIA--DanrTDEDFME---TIGFFLNLLPLRFRRDPSQTFADVLKE 305
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1237-1516 |
9.71e-12 |
|
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: 70.71 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1237 DAGVAV---SDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVN----RRNRIDTHDRLlaL 1309
Cdd:cd05927 86 DAGVKVyslEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFkileILNKINPTDVY--I 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1310 SALdfdlsvydtfgalgcgaQLVTIPEHarrdAFHWLSLTTEFGI-------------------TVWNSVPGLMDMLL-- 1368
Cdd:cd05927 164 SYL-----------------PLAHIFER----VVEALFLYHGAKIgfysgdirlllddikalkpTVFPGVPRVLNRIYdk 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1369 IAAGDKAGSlPTLRSVF-----------LSGD------W-------IPLDLPRRLR-----------------RAAPGVR 1407
Cdd:cd05927 223 IFNKVQAKG-PLKRKLFnfalnyklaelRSGVvraspfWdklvfnkIKQALGGNVRlmltgsaplspevleflRVALGCP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1408 LVAMGGATE--AAIwsneFVVDDVDPDWASIpyGYPLANQMFRVVD------DNGDDQPdyvAGELWIGGAGVALGYHNA 1479
Cdd:cd05927 302 VLEGYGQTEctAGA----TLTLPGDTSVGHV--GGPLPCAEVKLVDvpemnyDAKDPNP---RGEVCIRGPNVFSGYYKD 372
|
330 340 350
....*....|....*....|....*....|....*..
gi 2181016861 1480 PELTSDRFVHDptGsrWYRTGDMGCYWRDGTLQFLGR 1516
Cdd:cd05927 373 PEKTAEALDED--G--WLHTGDIGEWLPNGTLKIIDR 405
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1263-1615 |
1.04e-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: 70.63 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAAALNTI---VDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALGCGAQLVTIPehaR 1339
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNIVARFshaRDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMY---K 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1340 RDAFHWLSLTTEFGITVWNSVPGLMDML----LIAAGD-------KAGSLPTLRSVflsGDWIpldlprRLRRAAPGVRL 1408
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLVPTLFAFFakstLVDKYDlsnlheiASGGAPLSKEV---GEAV------AKRFKLPGIRQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1409 -VAMGGATEAAIWSNEfvvDDVDPDWAS--IPYGYPlanqmfRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTS 1484
Cdd:cd17642 333 gYGLTETTSAILITPE---GDDKPGAVGkvVPFFYA------KVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATK 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1485 DRFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLV--AAATVVPIHNCTALGAGIV 1562
Cdd:cd17642 404 ALIDKDG----WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIfdAGVAGIPDEDAGELPAAVV 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1563 VTGSG---AEQ-----FDDSTPGALRAHLAVRlpqymipkvFVScpELPLTANGKVDRGKI 1615
Cdd:cd17642 480 VLEAGktmTEKevmdyVASQVSTAKRLRGGVK---------FVD--EVPKGLTGKIDRRKI 529
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1272-1612 |
1.09e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 70.40 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1272 GSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLL-ALSAL-DFDLSVYDTFGALGCGAQLVTIPEHARRDAFhwlSLT 1349
Cdd:PRK10946 192 GSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLcALPAAhNYPMSSPGALGVFLAGGTVVLAPDPSATLCF---PLI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1350 TEFGITVWNSVPGLMDMLL--IAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRrAAPGVRLVAMGGATEAAIwsNEFVVD 1427
Cdd:PRK10946 269 EKHQVNVTALVPPAVSLWLqaIAEGGSRAQLASLKLLQVGGARLSETLARRIP-AELGCQLQQVFGMAEGLV--NYTRLD 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1428 DvdPDWASI-PYGYPLA-NQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFvhDPTGsrWYRTGDMGCY 1505
Cdd:PRK10946 346 D--SDERIFtTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF--DANG--FYCSGDLVSI 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1506 WRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCtALG----AGIVVTgsgaeqfDDSTPGALRA 1581
Cdd:PRK10946 420 DPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDE-LMGekscAFLVVK-------EPLKAVQLRR 491
|
330 340 350
....*....|....*....|....*....|..
gi 2181016861 1582 HLAVR-LPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK10946 492 FLREQgIAEFKLPDRVECVDSLPLTAVGKVDK 523
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
29-562 |
1.11e-11 |
|
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: 70.68 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 29 RPDAVAL--RTVAATGIDDWTYQRLWDHVREIRDVAFS-GLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYlpSTR 105
Cdd:cd17634 66 NGDRTAIiyEGDDTSQSRTISYRELHREVCRFAGTLLDlGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIF--GGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 106 EPQRFLARaqhiLRDCEPSAVYTCGELVE---------VLERDPILGALPIRTPASTADGLAPHPGGTTADADHGEHVA- 175
Cdd:cd17634 144 APEAVAGR----IIDSSSRLLITADGGVRagrsvplkkNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAk 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 176 ----------------FLQYSSGSTGKPKGVVNTHQSILRQAAFA-ANVWN-GDDDMHM----VSWLplyhdMGIFWGVF 233
Cdd:cd17634 220 aspehqpeamnaedplFILYTSGTTGKPKGVLHTTGGYLVYAATTmKYVFDyGPGDIYWctadVGWV-----TGHSYLLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 234 MPLLNGGCTTL---IPPHDfvRNPRIWlETVSRFRGNWIGGPDFAYRRCIEAfDGTALQSLDLSCLRLATNGAEPVRGTT 310
Cdd:cd17634 295 GPLACGATTLLyegVPNWP--TPARMW-QVVDKHGVNILYTAPTAIRALMAA-GDDAIEGTDRSSLRILGSVGEPINPEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 311 LRDFTAKfraaglrddvmapqyglaeagLGVTGSQTVRVW--VEKSFDADALERGiavevAQPNPADGRSRALvscgdga 388
Cdd:cd17634 371 YEWYWKK---------------------IGKEKCPVVDTWwqTETGGFMITPLPG-----AIELKAGSATRPV------- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 389 FGWDIQIVDPDRHmTLTDGEVGEIWVGG--PGLPDGYWRQPEQTATTFgARTADGlgpYLRTGDAGFR-YQGELYVCGRY 465
Cdd:cd17634 418 FGVQPAVVDNEGH-PQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTY-FSTFKG---MYFSGDGARRdEDGYYWITGRS 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 466 RDLIIVGGRNHFPNDIEKTVeEAHCGVAPGGACAVqPDAPQANGEW-WLVLETGspVEDLDDLSRILRRRILAH--HETA 542
Cdd:cd17634 493 DDVINVAGHRLGTAEIESVL-VAHPKVAEAAVVGI-PHAIKGQAPYaYVVLNHG--VEPSPELYAELRNWVRKEigPLAT 568
|
570 580
....*....|....*....|
gi 2181016861 543 PERVVWVpcRTLPTTTSGKI 562
Cdd:cd17634 569 PDVVHWV--DSLPKTRSGKI 586
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1264-1615 |
1.25e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 70.04 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1264 AAYVIYTSGSTGEPKGVLVshaaalntivDVNRRNRIDTHDRLLALSALDFDLSVYDTFGALG----------CG---AQ 1330
Cdd:PRK13390 150 GAVMLYSSGTTGFPKGIQP----------DLPGRDVDAPGDPIVAIARAFYDISESDIYYSSApiyhaaplrwCSmvhAL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1331 LVTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAG--SLPTLRSVFLSGDWIPLDLPRRLRRAApGVRL 1408
Cdd:PRK13390 220 GGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTryDVSSLRAVIHAAAPCPVDVKHAMIDWL-GPIV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1409 VAMGGATEAAIWSnefVVDDvdPDWASIP--YGYPLANQMfRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDr 1486
Cdd:PRK13390 299 YEYYSSTEAHGMT---FIDS--PDWLAHPgsVGRSVLGDL-HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1487 fVHDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VP-------IHNCTAL 1557
Cdd:PRK13390 372 -AQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVigVPdpemgeqVKAVIQL 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1558 GAGIVVTGSGAEQFDDSTpgalRAhlavRLPQYMIPKVFVSCPELPLTANGKVDRGKI 1615
Cdd:PRK13390 451 VEGIRGSDELARELIDYT----RS----RIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1258-1615 |
1.40e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 70.12 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1258 RIDPHDAAYVIYTSGSTGEPKGVLVSH--------AAALNtivDVnrrnridthdrlLALSALDFDLSVYDTF--GALG- 1326
Cdd:PRK07008 172 RFDENQASSLCYTSGTTGNPKGALYSHrstvlhayGAALP---DA------------MGLSARDAVLPVVPMFhvNAWGl 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1327 ------CGAQLVtIPEHARrDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLR 1400
Cdd:PRK07008 237 pysaplTGAKLV-LPGPDL-DGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1401 RAApGVRLVAMGGATEAAiwsnefvvddvdpdwasiPYG-----------YPLANQM--------------FRVVDDNGD 1455
Cdd:PRK07008 315 DEY-GVEVIHAWGMTEMS------------------PLGtlcklkwkhsqLPLDEQRkllekqgrviygvdMKIVGDDGR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1456 DQP-DYVA-GELWIGGAGVALGYHNAPEltsdrfvhDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEI 1533
Cdd:PRK07008 376 ELPwDGKAfGDLQVRGPWVIDRYFRGDA--------SPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1534 EHALRGHPLVAAATVVPIHN--CTALGAGIVVTGSGAEqfddSTPGALRAHLAVRLPQYMIPK--VFVScpELPLTANGK 1609
Cdd:PRK07008 448 ENVAVAHPAVAEAACIACAHpkWDERPLLVVVKRPGAE----VTREELLAFYEGKVAKWWIPDdvVFVD--AIPHTATGK 521
|
....*.
gi 2181016861 1610 VDRGKI 1615
Cdd:PRK07008 522 LQKLKL 527
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-482 |
1.43e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.11 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 112 ARAQHILRDCEPSAVYTCGELVEVLERDPilGALPIRTPASTADGLAPHPG-----GTTAD------ADHGEHVAfLQYS 180
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARALL--KQCPGVRHRLVLDGDGELEGfvgyaEAVAGlpatpiADESLGTD-MLYS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 181 SGSTGKPKGVVN--THQSILRQ---AAFAANVWNGDDDMHMVSWLPLYHDMGIFWgvFMPLLNGGCTTLIPPHdFvrNPR 255
Cdd:PRK13391 163 SGTTGRPKGIKRplPEQPPDTPlplTAFLQRLWGFRSDMVYLSPAPLYHSAPQRA--VMLVIRLGGTVIVMEH-F--DAE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 256 IWLETVSRFR---GNWIggPDFAYR--RCIEAfdgtALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAP 330
Cdd:PRK13391 238 QYLALIEEYGvthTQLV--PTMFSRmlKLPEE----VRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWW------GPIIHE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 331 QYGLAEaGLGVTGSQTvRVWVEKsfdadaleRGiavevaqpnpadgrsralvSCGDGAFGwDIQIVDPDRHMtLTDGEVG 410
Cdd:PRK13391 306 YYAATE-GLGFTACDS-EEWLAH--------PG-------------------TVGRAMFG-DLHILDDDGAE-LPPGEPG 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 411 EIWVGGpGLPDGYWRQPEQTATtfgARTADglGPYLRTGDAGF-RYQGELYVCGRYRDLIIVGGRNHFPNDIE 482
Cdd:PRK13391 355 TIWFEG-GRPFEYLNDPAKTAE---ARHPD--GTWSTVGDIGYvDEDGYLYLTDRAAFMIISGGVNIYPQEAE 421
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
176-561 |
1.61e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 68.95 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 176 FLQYSSGSTGKPKGVVNTHQSILRQ----AAFAANVWNGDDDMHMV-------SWL---PLYHdmGIFWGVFMPLLNGGC 241
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDIFRMlmggADFGTGEFTPSEDAHKAaaaaagtVMFpapPLMH--GTGSWTAFGGLLGGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 TTLIPPHDFvrNPRIWLETVSRFRGN--WIGGPDFAyRRCIEAFDGTalQSLDLSCLRLATNGAEPvrgttlrdFTAKFR 319
Cdd:cd05924 85 TVVLPDDRF--DPEEVWRTIEKHKVTsmTIVGDAMA-RPLIDALRDA--GPYDLSSLFAISSGGAL--------LSPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 320 AAGLR---DDVMAPQYGLAEAGLGVTGsqtvrvwveksfdadalergiaveVAQPNPADGRSRALVscgdgafGWDIQIV 396
Cdd:cd05924 152 QGLLElvpNITLVDAFGSSETGFTGSG------------------------HSAGSGPETGPFTRA-------NPDTVVL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 397 DPDRHMtLTDGEVGEIWVGGPGL-PDGYWRQPEQTATTFgaRTADGLgPYLRTGD-AGFRYQGELYVCGRYRDLIIVGGR 474
Cdd:cd05924 201 DDDGRV-VPPGSGGVGWIARRGHiPLGYYGDEAKTAETF--PEVDGV-RYAVPGDrATVEADGTVTLLGRGSVCINTGGE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 475 NHFPNDIEKTVeEAHCGVAPggaCAV--QPDapqangEWW-------LVLETGSPVeDLDDLSRILRRRILAHheTAPER 545
Cdd:cd05924 277 KVFPEEVEEAL-KSHPAVYD---VLVvgRPD------ERWgqevvavVQLREGAGV-DLEELREHCRTRIARY--KLPKQ 343
|
410
....*....|....*.
gi 2181016861 546 VVWVPcrTLPTTTSGK 561
Cdd:cd05924 344 VVFVD--EIERSPAGK 357
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2567-2832 |
2.24e-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: 68.83 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2567 DRPRFDSAARQLVARHAGLRTTVSpAGTDaasSGEVAVVHTAPIEPVVRD---HDDVRAAMRDQIIDLTARP-GIDFG-- 2640
Cdd:cd20483 37 DVNLLQKALSELVRRHEVLRTAYF-EGDD---FGEQQVLDDPSFHLIVIDlseAADPEAALDQLVRNLRRQElDIEEGev 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2641 -----VQTRGDGRTVVGISmDNTMLDGASMMIALSELDHLY----RGETVDQLPPLETSFAHY-VWnHPELLpdADEAVL 2710
Cdd:cd20483 113 irgwlVKLPDEEFALVLAS-HHIAWDRGSSKSIFEQFTALYdalrAGRDLATVPPPPVQYIDFtLW-HNALL--QSPLVQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2711 PRLaasrDYWRARLPSLPPAPKLADMSLLFEIEEPRFERAT--ATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRW 2788
Cdd:cd20483 189 PLL----DFWKEKLEGIPDASKLLPFAKAERPPVKDYERSTveATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRY 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2181016861 2789 SGTDHFCINVTLFDR-DPDVvgiENVVGDFTSLVLLECRVDEPAS 2832
Cdd:cd20483 265 TEDEDLTIGMVDGDRpHPDF---DDLVGFFVNMLPIRCRMDCDMS 306
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
170-565 |
3.19e-11 |
|
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: 68.66 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 170 HGEHVAFLQYSSGSTGKPKGVVNTHQSILRQA-AFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTLIPPh 248
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASAdRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 249 dfvRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTAlqsLDLSCLRLATNGAEPVRGTTlrdFTAKFRAAGLrdDVM 328
Cdd:cd05958 174 ---ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAG---PDLSSLRKCVSAGEALPAAL---HRAWKEATGI--PII 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 ApqyglaeaglGVTGSQTVRVWVEKSFDAdalergiavevAQPnpadGRSRALVScgdgafGWDIQIVDpDRHMTLTDGE 408
Cdd:cd05958 243 D----------GIGSTEMFHIFISARPGD-----------ARP----GATGKPVP------GYEAKVVD-DEGNPVPDGT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 409 VGEIWVGGpglPDGYWRQPEQTA-TTFGARTADGLGPYLRTGDAGFRYQgelyvcGRYRDLIIVGGRNHFPNDIEKT--- 484
Cdd:cd05958 291 IGRLAVRG---PTGCRYLADKRQrTYVQGGWNITGDTYSRDPDGYFRHQ------GRSDDMIVSGGYNIAPPEVEDVllq 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 485 ---VEEahCGV--APGGACAVQPDApqangewWLVLETG-----SPVEDLDDLSrilrRRILAHHETaPERVVWVPcrTL 554
Cdd:cd05958 362 hpaVAE--CAVvgHPDESRGVVVKA-------FVVLRPGvipgpVLARELQDHA----KAHIAPYKY-PRAIEFVT--EL 425
|
410
....*....|.
gi 2181016861 555 PTTTSGKIRRR 565
Cdd:cd05958 426 PRTATGKLQRF 436
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
95-459 |
4.10e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.38 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 95 IPVPVYLPSTRepqrflarAQHILRDCEPSAVYTCGELvevlerDPILGALPIRTPASTADGLAPhpgGTTADADH---G 171
Cdd:PRK04813 80 IPVDVSSPAER--------IEMIIEVAKPSLIIATEEL------PLEILGIPVITLDELKDIFAT---GNPYDFDHavkG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGV-------------------VNTHQSILRQAAFAAnvwngddDMHMVSWLPlyhdmgifwgv 232
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVqishdnlvsftnwmledfaLPEGPQFLNQAPYSF-------DLSVMDLYP----------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 233 fmPLLNGGctTLIP-PHDFVRNPRIWLETVSRFRGN-WIGGPDFAyRRCI--EAFDGTALQSLD--LSClrlatnGAE-P 305
Cdd:PRK04813 205 --TLASGG--TLVAlPKDMTANFKQLFETLPQLPINvWVSTPSFA-DMCLldPSFNEEHLPNLThfLFC------GEElP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 306 VRgtTLRDFTAKFRAAglrddVMAPQYGLAEAGLGVTGsqtVRVwveksfDADALERGIAVEVAQPNPadgrsralvscg 385
Cdd:PRK04813 274 HK--TAKKLLERFPSA-----TIYNTYGPTEATVAVTS---IEI------TDEMLDQYKRLPIGYAKP------------ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 386 dgafGWDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFgaRTADGLGPYlRTGDAGF------RYQGEL 459
Cdd:PRK04813 326 ----DSPLLIIDEEGT-KLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF--FTFDGQPAY-HTGDAGYledgllFYQGRI 397
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1246-1613 |
4.26e-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: 68.23 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1246 TAMIECAPTDPIR---IDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRL---------------- 1306
Cdd:cd05937 68 DPLIHCLKLSGSRfviVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTytcmplyhgtaaflga 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1307 ---------LAL----SALDFDLSVYDT----FGALG--CGAQLVTIPE-----HARRDAFH-------WLSLTTEFGIT 1355
Cdd:cd05937 148 cnclmsggtLALsrkfSASQFWKDVRDSgatiIQYVGelCRYLLSTPPSpydrdHKVRVAWGnglrpdiWERFRERFNVP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1356 V----WNSVPGLMDMLLIAAGD----KAGSLPTLRSVFLSGDWIPldlprrlrraapgvrlVAMGGATEAAIWSNE--FV 1425
Cdd:cd05937 228 EigefYAATEGVFALTNHNVGDfgagAIGHHGLIRRWKFENQVVL----------------VKMDPETDDPIRDPKtgFC 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1426 VddvdpdwaSIPYGYPlANQMFRVVDDNgddqpdyvagelwiggAGVALGYHNAPELTSDRFVHD--PTGSRWYRTGDMG 1503
Cdd:cd05937 292 V--------RAPVGEP-GEMLGRVPFKN----------------REAFQGYLHNEDATESKLVRDvfRKGDIYFRTGDLL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1504 CYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV----VPIHNCTALGAGIVVTGSGAEQfDDSTPGAL 1579
Cdd:cd05937 347 RQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygvkVPGHDGRAGCAAITLEESSAVP-TEFTKSLL 425
|
410 420 430
....*....|....*....|....*....|....*
gi 2181016861 1580 RAHLAVRLPQYMIPkVFVS-CPELPLTANGKVDRG 1613
Cdd:cd05937 426 ASLARKNLPSYAVP-LFLRlTEEVATTDNHKQQKG 459
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1258-1634 |
5.09e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 68.49 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1258 RIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRN-RIDTHDRllALSALDFdlsvYDTFGALGC-----GAQL 1331
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRPGDR--CVSWLPF----YHDMGLVGFlltpvATQL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1332 VT--IP--EHARRdAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGS---LPTLRSVFLSGDWIPLDLPRRL--RRA 1402
Cdd:PRK09192 246 SVdyLPtrDFARR-PLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLAeldLSCWRVAGIGADMIRPDVLHQFaeAFA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1403 APGVRLVA------MGGATEAAIWSNE---FVVDDVD------------PDWASIPY------GYPLANQMFRVVDDNGD 1455
Cdd:PRK09192 325 PAGFDDKAfmpsygLAEATLAVSFSPLgsgIVVEEVDrdrleyqgkavaPGAETRRVrtfvncGKALPGHEIEIRNEAGM 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1456 DQPDYVAGELWIGGAGVALGYHNAPElTSDrfVHDPTGsrWYRTGDMGcYWRDGTLQFLGRADSQVKIRGHRVECGEIEH 1535
Cdd:PRK09192 405 PLPERVVGHICVRGPSLMSGYFRDEE-SQD--VLAADG--WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEW 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1536 ALRGHPLV----AAATVVPIHNCTALGAGIVVTGSgaeqfDDSTPGALRAHLA--VRLPQYMIPKVFVSCPE-LPLTANG 1608
Cdd:PRK09192 479 IAEQEPELrsgdAAAFSIAQENGEKIVLLVQCRIS-----DEERRGQLIHALAalVRSEFGVEAAVELVPPHsLPRTSSG 553
|
410 420
....*....|....*....|....*.
gi 2181016861 1609 KVDRGKIAARLEAAARAPQPLDTSST 1634
Cdd:PRK09192 554 KLSRAKAKKRYLSGAFASLDVAASLA 579
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
28-565 |
8.93e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 67.60 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 28 RRPDAVALrTVAATGIDdWTYQRLwdhVREIRDVA----FSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPV--YL 101
Cdd:PRK05852 28 RLPEAPAL-VVTADRIA-ISYRDL---ARLVDDLAgqltRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLdpAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 102 PSTRE---PQRFLARAQHILRD-----CEPSAVYTCGELVEVLERDPILGALPIRTPASTAdglaPHPGgTTADADHGEH 173
Cdd:PRK05852 103 PIAEQrvrSQAAGARVVLIDADgphdrAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATE----PTPA-TSTPEGLRPD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILRQA-AFAANVWNGDDDMhMVSWLPLYHDMGIFwGVFMPLLNGGCTTLIPPHDFVR 252
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMVPWTHANIASSVrAIITGYRLSPRDA-TVAVMPLYHGHGLI-AALLATLASGGAVLLPARGRFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 NPRIWlETVSRFRGNWIGGPDFAYRRCIEAFDgTALQSLDLSCLRLATNGAEPVRGTTlrdftakfrAAGLRDDVMAP-- 330
Cdd:PRK05852 256 AHTFW-DDIKAVGATWYTAVPTIHQILLERAA-TEPSGRKPAALRFIRSCSAPLTAET---------AQALQTEFAAPvv 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 331 -QYGLAEAGLGVTgsqtvrvwveksfdadalERGIAVEVAQPNPadGRSRALVSCGDGAfgwDIQIVDPDRHmTLTDGEV 409
Cdd:PRK05852 325 cAFGMTEATHQVT------------------TTQIEGIGQTENP--VVSTGLVGRSTGA---QIRIVGSDGL-PLPAGAV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 410 GEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKtVEEA 488
Cdd:PRK05852 381 GEVWLRGTTVVRGYLGDPTITAANF----TDG---WLRTGDLGsLSAAGDLSIRGRIKELINRGGEKISPERVEG-VLAS 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 489 HCGVAPGGACAVqPDAPQANGEWWLVLETGSPVEDLDDLSRILRRRILAHHETAPERVVwvpcRTLPTTTSGKIRRR 565
Cdd:PRK05852 453 HPNVMEAAVFGV-PDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEA----SGLPHTAKGSLDRR 524
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
2567-2927 |
1.17e-10 |
|
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: 66.61 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2567 DRPRFDSAARQLVARHAGLRTTVspagtdAASSGE-VAVVH-TAPIEPVVRDHDDVRAAMRDQII------------DLT 2632
Cdd:cd19531 37 DVAALERALNELVARHEALRTTF------VEVDGEpVQVILpPLPLPLPVVDLSGLPEAEREAEAqrlareearrpfDLA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2633 ARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQ---LPPLETSFAHY-VWNHpELLPDadea 2708
Cdd:cd19531 111 RGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRpspLPPLPIQYADYaVWQR-EWLQG---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2709 vlPRLAASRDYWRARLPSLPPAPKL-ADMsllfeieePR-----FE--RATATIPAVDWSQVTRSCRAEGVTVASFLLAN 2780
Cdd:cd19531 186 --EVLERQLAYWREQLAGAPPVLELpTDR--------PRpavqsFRgaRVRFTLPAELTAALRALARREGATLFMTLLAA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2781 YARVLSRWSGTDHFCINVTLFDRdpDVVGIENVVGDFT-SLVLlecRVD---EP--ASIWESVR-----ALQRQlmtDLP 2849
Cdd:cd19531 256 FQVLLHRYSGQDDIVVGTPVAGR--NRAELEGLIGFFVnTLVL---RTDlsgDPtfRELLARVRetaleAYAHQ---DLP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2850 -HRGADAVWLQRELLRfhgNPtaaLFPVVFTsglgLVDASARAAVRF---AEPVFAASQTPQTVLDFQVWESAGALKLSW 2925
Cdd:cd19531 328 fEKLVEALQPERDLSR---SP---LFQVMFV----LQNAPAAALELPgltVEPLEVDSGTAKFDLTLSLTETDGGLRGSL 397
|
..
gi 2181016861 2926 DF 2927
Cdd:cd19531 398 EY 399
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2966-3055 |
1.49e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.67 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIADTDNADE 3045
Cdd:PRK12316 5068 APRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
|
90
....*....|
gi 2181016861 3046 PDLTVEEGML 3055
Cdd:PRK12316 5148 EKFDDLEELL 5157
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
177-564 |
1.56e-10 |
|
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: 66.55 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMG--IFWGVFMpllNGGcTTLIPPHdfVRNP 254
Cdd:cd12118 138 LNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGwcFPWTVAA---VGG-TNVCLRK--VDAK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 255 RIW----LETVSRFRG-----NWIGGPDFAYRRcieAFDGTalqsldlscLRLATNGAEPvRGTTLrdftAKFRAAGLRd 325
Cdd:cd12118 212 AIYdlieKHKVTHFCGaptvlNMLANAPPSDAR---PLPHR---------VHVMTAGAPP-PAAVL----AKMEELGFD- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 326 dvMAPQYGLAEaglgVTGSQTVRVWVEKSfdaDALergiavevaqpnPADGRSRALVSCGDGAFGWD-IQIVDPDRHMTL 404
Cdd:cd12118 274 --VTHVYGLTE----TYGPATVCAWKPEW---DEL------------PTEERARLKARQGVRYVGLEeVDVLDPETMKPV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 405 T-DGE-VGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFRY-QGELYVCGRYRDLIIVGGRNHFPNDI 481
Cdd:cd12118 333 PrDGKtIGEIVFRGNIVMKGYLKNPEATAEAF----RGG---WFHSGDLAVIHpDGYIEIKDRSKDIIISGGENISSVEV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 482 EKTVEEaHCGVApggACAV--QPDapqangEWW-------LVLETGSPVEDlDDLSRILRRRiLAHHETaPERVVWVPcr 552
Cdd:cd12118 406 EGVLYK-HPAVL---EAAVvaRPD------EKWgevpcafVELKEGAKVTE-EEIIAFCREH-LAGFMV-PKTVVFGE-- 470
|
410
....*....|..
gi 2181016861 553 tLPTTTSGKIRR 564
Cdd:cd12118 471 -LPKTSTGKIQK 481
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1448-1609 |
1.62e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 66.47 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1448 RVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVhdptGSRWYRTGDMGCYWRDGTLqFLGRADSQVKIRGhr 1527
Cdd:PRK08276 326 RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN----PHGWVTVGDVGYLDEDGYL-YLTDRKSDMIISG-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1528 vecG------EIEHALRGHPLVAAATV--VPihnCTALG---AGIVVTGSGAEQfDDSTPGALRAHLAVRLPQYMIPKVF 1596
Cdd:PRK08276 399 ---GvniypqEIENLLVTHPKVADVAVfgVP---DEEMGervKAVVQPADGADA-GDALAAELIAWLRGRLAHYKCPRSI 471
|
170
....*....|...
gi 2181016861 1597 VSCPELPLTANGK 1609
Cdd:PRK08276 472 DFEDELPRTPTGK 484
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
684-986 |
1.72e-10 |
|
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: 65.93 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 684 WPTTPLQQAYwVGRGAEQPLGGVGCQTYFELVGARVDAGRLAAALDALTRRHPMLRATFPDPGrcliTPEAVRLPLA--- 760
Cdd:cd19536 2 YPLSSLQEGM-LFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDG----LGQPVQVVHRqaq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 761 --VHDLTDAPVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRLPHGCIVHFAVDL--IIADVTSIGTMLRDLAASYRG 836
Cdd:cd19536 77 vpVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLVISDhhSILDGWSLYLLVKEILAVYNQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 837 --EKLP---APSATFADLIQST--SPPPQACAD---------RLPEGPQLPRVQEADiSFLRHQHTLSALATKAIDDACH 900
Cdd:cd19536 157 llEYKPlslPPAQPYRDFVAHEraSIQQAASERywreylagaTLATLPALSEAVGGG-PEQDSELLVSVPLPVRSRSLAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 901 NHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRSPEVSD---VVGDFTETHLYRAQLDgQISFVDQAQVTQKGLRTA 977
Cdd:cd19536 236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGaerLLGLFLNTLPLRVTLS-EETVEDLLKRAQEQELES 314
|
330
....*....|.
gi 2181016861 978 L--RAAPAPDL 986
Cdd:cd19536 315 LshEQVPLADI 325
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
170-565 |
1.87e-10 |
|
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: 66.12 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 170 HGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDmGIFWGVFMPLLNGGCTTLIPPHD 249
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFD-ASVWELLMALLAGATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 FVrnpriwletvsrfrgnwiGGPDFAyrRCIEAFDGTALqSLDLSCLRLATNGAEPVRGTTL-------RDFTAKFrAAG 322
Cdd:cd17652 170 LL------------------PGEPLA--DLLREHRITHV-TLPPAALAALPPDDLPDLRTLVvageacpAELVDRW-APG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 323 LRddvMAPQYGLAEAGLGVTgsqtvrvWVEKSFDADALERGIAVEVAQpnpadgrsralvscgdgafgwdIQIVDpDRHM 402
Cdd:cd17652 228 RR---MINAYGPTETTVCAT-------MAGPLPGGGVPPIGRPVPGTR----------------------VYVLD-ARLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 403 TLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGARTADGLGPYL-RTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPND 480
Cdd:cd17652 275 PVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMyRTGDlARWRADGQLEFLGRADDQVKIRGFRIELGE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 481 IEkTVEEAHCGVAPgGACAVQPDAPQANGEWWLVLETGSPVEDLDDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSG 560
Cdd:cd17652 355 VE-AALTEHPGVAE-AVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGY--MVPAAFVVLD--ALPLTPNG 428
|
....*
gi 2181016861 561 KIRRR 565
Cdd:cd17652 429 KLDRR 433
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
164-482 |
2.52e-10 |
|
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: 66.01 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 164 TTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSIL------RQAAFAANVwngDDDMHMVSWLPLYHDMGIFwGVFMPLL 237
Cdd:cd17642 176 KPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVarfshaRDPIFGNQI---IPDTAILTVIPFHHGFGMF-TTLGYLI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 238 NGGCTTLIPPHDfvrnPRIWLETVSRFR--GNWIGGPDFAYrrcieaFDGTAL-QSLDLSCLRLATNGAEPVRGTTLRDF 314
Cdd:cd17642 252 CGFRVVLMYKFE----EELFLRSLQDYKvqSALLVPTLFAF------FAKSTLvDKYDLSNLHEIASGGAPLSKEVGEAV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 315 TAKFRAAGLRDDvmapqYGLAEAGLGVtgsqtvrvwveksfdadalergiaveVAQPNPADGRSralvSCGDGAFGWDIQ 394
Cdd:cd17642 322 AKRFKLPGIRQG-----YGLTETTSAI--------------------------LITPEGDDKPG----AVGKVVPFFYAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 395 IVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTATtfgARTADGlgpYLRTGDAGFrY--QGELYVCGRYRDLIIVG 472
Cdd:cd17642 367 VVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKA---LIDKDG---WLHSGDIAY-YdeDGHFFIVDRLKSLIKYK 439
|
330
....*....|
gi 2181016861 473 GRNHFPNDIE 482
Cdd:cd17642 440 GYQVPPAELE 449
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1229-1610 |
2.54e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 65.99 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1229 IRTDSDTQDAGVAVSDITAMIECAPTDPIR-----IDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTH 1303
Cdd:PRK08315 161 IFLGDEKHPGMLNFDELLALGRAVDDAELAarqatLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1304 DRLLalsaldfdLSV--YDTFG----ALGC---GAQLVTIPEharrdAFHWLS-LTT--EFGITVWNSVPglmdMLLIAA 1371
Cdd:PRK08315 241 DRLC--------IPVplYHCFGmvlgNLACvthGATMVYPGE-----GFDPLAtLAAveEERCTALYGVP----TMFIAE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1372 GD----KAGSLPTLRSVFLSGDWIPLDLPRRLrraapgVRLVAMG------GATEAAIWSNEFVVDD-VDPDWASIpyGY 1440
Cdd:PRK08315 304 LDhpdfARFDLSSLRTGIMAGSPCPIEVMKRV------IDKMHMSevtiayGMTETSPVSTQTRTDDpLEKRVTTV--GR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1441 PLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDrfVHDPTGsrWYRTGDMGCYWRDGTLQFLGRADS 1519
Cdd:PRK08315 376 ALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDADG--WMHTGDLAVMDEEGYVNIVGRIKD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1520 QVkIRGhrvecGE------IEHALRGHPLVAAATVVPIHNCT---ALGAGIVVTgSGAEqfddSTPGALRAHLAVRLPQY 1590
Cdd:PRK08315 452 MI-IRG-----GEniypreIEEFLYTHPKIQDVQVVGVPDEKygeEVCAWIILR-PGAT----LTEEDVRDFCRGKIAHY 520
|
410 420
....*....|....*....|..
gi 2181016861 1591 MIPK--VFVScpELPLTANGKV 1610
Cdd:PRK08315 521 KIPRyiRFVD--EFPMTVTGKI 540
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
177-488 |
2.91e-10 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 65.84 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSILRQAAFAANvwNGDDDM------HMVSWLPLYHDMGIFWGVFMPLLNGGCT-------- 242
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQ--HMDLRPatvgqeSVVSYLPLSHIAAQILDIWLPIKVGGQVyfaqpdal 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 243 --TLIP------PHDFVRNPRIW-----------------------------LETVSRFRGNWIGGPDFAY--RRCIEAF 283
Cdd:cd05933 233 kgTLVKtlrevrPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGESPSPLFYRlaKKLVFKK 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 284 DGTALqSLDlSCLRLATnGAEPVRGTTLRDFTakfraaGLRDDVMApQYGLAEAglgvTGSQTVrvwveksfdadalerg 363
Cdd:cd05933 313 VRKAL-GLD-RCQKFFT-GAAPISRETLEFFL------SLNIPIME-LYGMSET----SGPHTI---------------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 364 iavevAQPNpadgrSRALVSCGDGAFGWDIQIVDPDrhmtlTDGeVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlg 443
Cdd:cd05933 363 -----SNPQ-----AYRLLSCGKALPGCKTKIHNPD-----ADG-IGEICFWGRHVFMGYLNMEDKTEEAI---DEDG-- 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2181016861 444 pYLRTGDAGF-RYQGELYVCGRYRDLIIV-GGRNHFPNDIEKTVEEA 488
Cdd:cd05933 422 -WLHSGDLGKlDEDGFLYITGRIKELIITaGGENVPPVPIEDAVKKE 467
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
100-434 |
2.96e-10 |
|
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: 65.81 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 100 YLPStrEPQRFLARAQHILRDCEPSAVYTCGELVEVLERDPILGALPIRTPASTADGLAPHPGGTTadadhgeHVAFLQY 179
Cdd:cd17655 74 YLPI--DPDYPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSD-------DLAYVIY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 180 SSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGGcTTLIPPHDFVRNPRIWLE 259
Cdd:cd17655 145 TSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASV-TEIFASLLSGN-TLYIVRKETVLDGQALTQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 260 TVSRFRGNWIGGPDfAYRRCIEAFDGtalqSLDLSCLRLATnGAEPVRGTTLRDFTAKFRAAGLRDDVmapqYGLAEAGL 339
Cdd:cd17655 223 YIRQNRITIIDLTP-AHLKLLDAADD----SEGLSLKHLIV-GGEALSTELAKKIIELFGTNPTITNA----YGPTETTV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 340 GVTGSQTVRVWVEksfdadalergiavevaQPNPADGRSRALVScgdgafgwdIQIVDPDRHMTLTdGEVGEIWVGGPGL 419
Cdd:cd17655 293 DASIYQYEPETDQ-----------------QVSVPIGKPLGNTR---------IYILDQYGRPQPV-GVAGELYIGGEGV 345
|
330
....*....|....*
gi 2181016861 420 PDGYWRQPEQTATTF 434
Cdd:cd17655 346 ARGYLNRPELTAEKF 360
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
712-965 |
2.99e-10 |
|
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: 65.52 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 712 FELVGaRVDAGRLAAALDALTRRHPMLRATFPDPGRcliTPEAVRLPLAVHDLTDAPVTTRDTHLAEIRRRLRTHRFDIE 791
Cdd:cd19540 30 LRLTG-ALDVDALRAALADVVARHESLRTVFPEDDG---GPYQVVLPAAEARPDLTVVDVTEDELAARLAEAARRGFDLT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 792 TGDTWTVELTRL-PHGCIVHFAVDLIIADVTSIGTMLRDLAASYRG---------EKLPAPSATFA----DLIQSTSPPP 857
Cdd:cd19540 106 AELPLRARLFRLgPDEHVLVLVVHHIAADGWSMAPLARDLATAYAArragrapdwAPLPVQYADYAlwqrELLGDEDDPD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 858 QACADRL----------PEGPQLP--RVQEADISFL--RHQHTLSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWAS 923
Cdd:cd19540 186 SLAARQLaywretlaglPEELELPtdRPRPAVASYRggTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGA 265
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2181016861 924 QDDFLVNVTTFGRS-PEVSDVVGDFTETHLYRAQLDGQISFVD 965
Cdd:cd19540 266 GDDIPIGTPVAGRGdEALDDLVGMFVNTLVLRTDVSGDPTFAE 308
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1730-2123 |
3.12e-10 |
|
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: 65.12 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1730 FPLTRLQQAYTLGAAGLNGSTCAPTYFAVVLaaapeSAGIDLDRFARVVTRCVDEFAMLRCALDADTTQRVQVDAGPVP- 1808
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFL-----TGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1809 ----VHDLDIQDDPDL----LLRRMAAAPFDPHSVPVI--QCFAPSRSPRHVGLLISYLGLDARSLSTVVTTIIAEYqSQ 1878
Cdd:cd19066 77 frieIIDLRNLADPEArlleLIDQIQQTIYDLERGPLVrvALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVY-DA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1879 PRPRQVDPTAAV--FARFASESAW--GENDVDNSVA--------GPPLLPLH-DQRRDPFERVTFARRSFTIEEQAAATL 1945
Cdd:cd19066 156 AERQKPTLPPPVgsYADYAAWLEKqlESEAAQADLAywtsylhgLPPPLPLPkAKRPSQVASYEVLTLEFFLRSEETKRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1946 REHAAHLGVTPTALVFEAFAHALASIGAGQRFAVTVPKSYRPDyaPADREVLGNFTRLALCEVDYGavRPGSAEAVAAAQ 2025
Cdd:cd19066 236 REVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTS--PDATFPELLKRT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2026 RE-LWRAVSHdGDITGG-----LAATRTAGGYP---VVFTSTLG----LTHQDASGLTNVRTLTQTPGVWLDCQ-TEDEV 2091
Cdd:cd19066 312 KEqSREAIEH-QRVPFIelvrhLGVVPEAPKHPlfePVFTFKNNqqqlGKTGGFIFTTPVYTSSEGTVFDLDLEaSEDPD 390
|
410 420 430
....*....|....*....|....*....|..
gi 2181016861 2092 AGIRMSWDIATNVVAAESISVAFSRFEEAVRR 2123
Cdd:cd19066 391 GDLLLRLEYSRGVYDERTIDRFAERYMTALRQ 422
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
171-565 |
4.23e-10 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 65.41 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNT---HQSILRQAAF------AANVWNGDDDMHMVswlplyhdMGIFWGVFMPLLNGgC 241
Cdd:cd05967 229 ATDPLYILYTSGTTGKPKGVVRDnggHAVALNWSMRniygikPGDVWWAASDVGWV--------VGHSYIVYGPLLHG-A 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 TTLIpphdfvrnpriwletvsrFRGNWIGGPDF-AYRRCIEAFDGTALQSLD--LSCLRLATNGAEPVRGTTLRDFTAKF 318
Cdd:cd05967 300 TTVL------------------YEGKPVGTPDPgAFWRVIEKYQVNALFTAPtaIRAIRKEDPDGKYIKKYDLSSLRTLF 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 319 rAAGLRDDVmaPQYGlaeaglgvtgsqtvrvWVEKSFDADAL------ERGIAVeVAQPNPADGRSRALVSCGDGAFGWD 392
Cdd:cd05967 362 -LAGERLDP--PTLE----------------WAENTLGVPVIdhwwqtETGWPI-TANPVGLEPLPIKAGSPGKPVPGYQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 393 IQIVDPDRHmTLTDGEVGEIWVGGPgLPDGY----WRQPEQTATTFGARTAdglgPYLRTGDAGFR-YQGELYVCGRYRD 467
Cdd:cd05967 422 VQVLDEDGE-PVGPNELGNIVIKLP-LPPGClltlWKNDERFKKLYLSKFP----GYYDTGDAGYKdEDGYLFIMGRTDD 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 468 LIIVGGRNHFPNDIEKTVeEAHCGVApggACAV--QPDAPQanGEWWL---VLETGSPvEDLDDLSRIL----RRRI--L 536
Cdd:cd05967 496 VINVAGHRLSTGEMEESV-LSHPAVA---ECAVvgVRDELK--GQVPLglvVLKEGVK-ITAEELEKELvalvREQIgpV 568
|
410 420
....*....|....*....|....*....
gi 2181016861 537 AhhetAPERVVWVpcRTLPTTTSGKIRRR 565
Cdd:cd05967 569 A----AFRLVIFV--KRLPKTRSGKILRR 591
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1532-1609 |
4.24e-10 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 58.32 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1532 EIEHALRGHPLVAAATVVPIHN--CTALGAGIVVTGSGAEQfddsTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGK 1609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDelKGEAPVAFVVLKPGVEL----LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
175-473 |
4.78e-10 |
|
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: 64.96 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILRQA-----AFAANVWNGDDDMHMVswlPLYHDMGifWGV-FMPLLNGGCTTLIPPH 248
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLVLHAmaallTDGLGLSESDVVLPVV---PMFHVNA--WGLpYAAAMVGAKLVLPGPY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 249 DfvrNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTalqSLDLSCLR-LATNGAEPVRGttlrdFTAKFRAAGLRddV 327
Cdd:cd12119 241 L---DPASLAELIEREGVTFAAGVPTVWQGLLDHLEAN---GRDLSSLRrVVIGGSAVPRS-----LIEAFEERGVR--V 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 328 MApQYGLAEAGLGVTGSQTVRVWVEKSFDADALERgiaveVAQpnpadGRSRALVscgdgafgwDIQIVDPD-RHMTLTD 406
Cdd:cd12119 308 IH-AWGMTETSPLGTVARPPSEHSNLSEDEQLALR-----AKQ-----GRPVPGV---------ELRIVDDDgRELPWDG 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 407 GEVGEIWVGGPGLPDGYWRQPEQTAttfgARTADGlgpYLRTGDAGFRY-QGELYVCGRYRDLIIVGG 473
Cdd:cd12119 368 KAVGELQVRGPWVTKSYYKNDEESE----ALTEDG---WLRTGDVATIDeDGYLTITDRSKDVIKSGG 428
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1121-1610 |
5.62e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 64.95 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1121 NAATHPARLAlrwrpddyrgerhgdvIAQDRSQLTYGELDELARSVARAVAAR-HAAGSVIGIQLPKGPSQIVAVLGVMM 1199
Cdd:PRK07788 58 AARRAPDRAA----------------LIDERGTLTYAELDEQSNALARGLLALgVRAGDGVAVLARNHRGFVLALYAAGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1200 AGCTYLPVGVDQPAERLSRICAR-----------------------SAMAGLIRTDSDTQDAGVAVSDITAMIECAPTDP 1256
Cdd:PRK07788 122 VGARIILLNTGFSGPQLAEVAARegvkalvyddeftdllsalppdlGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1257 IRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVnrRNRID-THDRLLALSALDFDLSVYDTFG-ALGCGAQLVTi 1334
Cdd:PRK07788 202 LPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGL--LSRVPfRAGETTLLPAPMFHATGWAHLTlAMALGSTVVL- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1335 peHARRDAFHWLSLTTEFGITVWNSVPglmDML--LIAAGDKAGS---LPTLRSVFLSGDWIPLDLPRRLRrAAPGVRLV 1409
Cdd:PRK07788 279 --RRRFDPEATLEDIAKHKATALVVVP---VMLsrILDLGPEVLAkydTSSLKIIFVSGSALSPELATRAL-EAFGPVLY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1410 AMGGATE---AAIWSNEfvvddvdpDWASIP--YGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYhnapelTS 1484
Cdd:PRK07788 353 NLYGSTEvafATIATPE--------DLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1485 DRfvHDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALGAGI--- 1561
Cdd:PRK07788 419 GR--DKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDD-EEFGQRLraf 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1562 VVTGSGAEQfddsTPGALRAHLAVRLPQYMIPK--VFVscPELPLTANGKV 1610
Cdd:PRK07788 496 VVKAPGAAL----DEDAIKDYVRDNLARYKVPRdvVFL--DELPRNPTGKV 540
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1263-1612 |
6.09e-10 |
|
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: 64.51 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1263 DAAYVIYTSGSTGEPKGVLVSHAA----ALNTIVDVNRRnRIDTHdrlLALSALDFDLSVYDTFGALGCGAQLVTIPEHA 1338
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSypvgHLSTMYWIGLK-PGDVH---WNISSPGWAKHAWSCFFAPWNAGATVFLFNYA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1339 RRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAagDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAApGVRLVAMGGATEAA 1418
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ--DLASFDVKLREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1419 IWSNEFVVDDVDPDwasiPYGYPLANQMFRVVDDNGDDQPDyvaGE--LWIGG---AGVALGYHNAPELTSDRFvhdptG 1493
Cdd:cd05974 239 ALVGNSPGQPVKAG----SMGRPLPGYRVALLDPDGAPATE---GEvaLDLGDtrpVGLMKGYAGDPDKTAHAM-----R 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1494 SRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTALGA--GIVVTGSGAEQF 1571
Cdd:cd05974 307 GGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVpkAFIVLRAGYEPS 386
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2181016861 1572 DDSTPGALRaHLAVRLPQYMIPKVfVSCPELPLTANGKVDR 1612
Cdd:cd05974 387 PETALEIFR-FSRERLAPYKRIRR-LEFAELPKTISGKIRR 425
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
179-564 |
6.59e-10 |
|
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: 64.46 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 179 YSSGSTGKPKGVVNTHQSILRQAA---FAANV------WNGDDDmhmvSWLplyhdMGIFWGVFMPLLNGGCTTLIppHD 249
Cdd:cd05973 95 FTSGTTGLPKGVPVPLRALAAFGAylrDAVDLrpedsfWNAADP----GWA-----YGLYYAITGPLALGHPTILL--EG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 250 FVRNPRIWlETVSRFRGNWIGGPDFAYRRCIEAfdGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAgLRDdvma 329
Cdd:cd05973 164 GFSVESTW-RVIERLGVTNLAGSPTAYRLLMAA--GAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVP-IHD---- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 330 pQYGLAEAGLGVTGSQTvrvwveksfDADALERGiavevaqpnpadgrsralvSCGDGAFGWDIQIVDPDRHmTLTDGEV 409
Cdd:cd05973 236 -HYGQTELGMVLANHHA---------LEHPVHAG-------------------SAGRAMPGWRVAVLDDDGD-ELGPGEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 410 GEIWVGGPGLP----DGYWRQPeqtattfgarTADGLGPYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKT 484
Cdd:cd05973 286 GRLAIDIANSPlmwfRGYQLPD----------TPAIDGGYYLTGDTVeFDPDGSFSFIGRADDVITMSGYRIGPFDVESA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 485 VEEaHCGVAPGGACAVQPDAPQANGEWWLVLETG-SPVEDL-DDLSRILRRRILAHheTAPERVVWVpcRTLPTTTSGKI 562
Cdd:cd05973 356 LIE-HPAVAEAAVIGVPDPERTEVVKAFVVLRGGhEGTPALaDELQLHVKKRLSAH--AYPRTIHFV--DELPKTPSGKI 430
|
..
gi 2181016861 563 RR 564
Cdd:cd05973 431 QR 432
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1267-1612 |
6.62e-10 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 64.78 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1267 VIYTSGSTGEPKGVLVSH---AAALNTIVDvnrrnRID-THDRLLALSALDFD---LSVYDTFGALGCgaqlvTIPEHAR 1339
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGpggIGTLKAILD-----RTPwRAEEPTVIVAPMFHawgFSQLVLAASLAC-----TIVTRRR 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1340 RDAFHWLSLTTEFGITVWNSVPGLMD--MLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVrLVAMGGATEA 1417
Cdd:PRK13382 271 FDPEATLDLIDRHRATGLAVVPVMFDriMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1418 AiWSNEFVVDDVD--PDWAsipyGYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNApeltSDRFVHDPTGSr 1495
Cdd:PRK13382 350 G-MIATATPADLRaaPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG----STKDFHDGFMA- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1496 wyrTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHN---CTALGAGIVVTGSGAEqfd 1572
Cdd:PRK13382 420 ---SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDeqyGQRLAAFVVLKPGASA--- 493
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2181016861 1573 dsTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK13382 494 --TPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILR 531
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1439-1594 |
1.19e-09 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 63.84 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1439 GYPLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFvhDPTGsrWYRTGDMGCYWRDGTLQFLGRA 1517
Cdd:PLN02330 364 GFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTI--DEDG--WLHTGDIGYIDDDGDIFIVDRI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1518 DSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTA--LGAGIVVTGSGAEQFDDSTPGALRAHLA----VRLPQYM 1591
Cdd:PLN02330 440 KELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAgeIPAACVVINPKAKESEEDILNFVAANVAhykkVRVVQFV 519
|
....*
gi 2181016861 1592 --IPK 1594
Cdd:PLN02330 520 dsIPK 524
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
115-561 |
1.37e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 63.75 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 115 QHILRDCEPSAVYTCGELVEVLErdPILGALP-IRTPASTADGLAPHPGG---------TTADADH--GEHVA---FLQY 179
Cdd:PRK07798 93 RYLLDDSDAVALVYEREFAPRVA--EVLPRLPkLRTLVVVEDGSGNDLLPgavdyedalAAGSPERdfGERSPddlYLLY 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 180 SSGSTGKPKGVVNTHQSILRQAAFAANVWNGDD--DMHMVS----------WL---PLYHDMGiFWGVFMPLLNGGCTTL 244
Cdd:PRK07798 171 TGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPieDEEELAkraaagpgmrRFpapPLMHGAG-QWAAFAALFSGQTVVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 245 IPPHDFvrNPRIWLETVSRFRGNWIG--GPDFAyRRCIEAFDgtALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFRAAG 322
Cdd:PRK07798 250 LPDVRF--DADEVWRTIEREKVNVITivGDAMA-RPLLDALE--ARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 323 LRDDvmapqYGLAEAGLGVTGSqtvrvwveksfdadalergiaveVAQPNPADGRSRAlvscgdgAFGWDIQIVDPDRHM 402
Cdd:PRK07798 325 LTDS-----IGSSETGFGGSGT-----------------------VAKGAVHTGGPRF-------TIGPRTVVLDEDGNP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 403 TLT-DGEVGEIWVGGPgLPDGYWRQPEQTATTFgaRTADGLgPYLRTGD-AGFRYQGELYVCGRYRDLIIVGGRNHFPND 480
Cdd:PRK07798 370 VEPgSGEIGWIARRGH-IPLGYYKDPEKTAETF--PTIDGV-RYAIPGDrARVEADGTITLLGRGSVCINTGGEKVFPEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 481 IEkTVEEAHCGVApgGACAV-QPDapqangEWW------LVLETGSPVEDLDDLSRILRRRiLAHHETaPERVVWVPcrT 553
Cdd:PRK07798 446 VE-EALKAHPDVA--DALVVgVPD------ERWgqevvaVVQLREGARPDLAELRAHCRSS-LAGYKV-PRAIWFVD--E 512
|
....*...
gi 2181016861 554 LPTTTSGK 561
Cdd:PRK07798 513 VQRSPAGK 520
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1180-1612 |
1.97e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 63.12 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1180 IGIQLPKGPSQIVAVLGVMMAGctYLPVGVD---QPAERLSRIcaRSAMAGLIRTDSDTQD--AGVAVSDIT-------- 1246
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGG--YVLVGLNttrRGAALAADI--RRADCQLLVTDAEHRPllDGLDLPGVRvldvdtpa 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1247 ---AMIECAPTDPIR-IDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHD------------RLLALS 1310
Cdd:PRK13388 131 yaeLVAAAGALTPHReVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDvcyvsmplfhsnAVMAGW 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1311 ALdfdlsvydtfgALGCGAqlvTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFlSGDW 1390
Cdd:PRK13388 211 AP-----------AVASGA---AVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAF-GNEA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1391 IPLDLPRRLRRAapGVRLVAMGGATEAAIwsneFVVDDVDPDWASIPYGYP---------LANQMFRVVDDNGD-DQPDY 1460
Cdd:PRK13388 276 SPRDIAEFSRRF--GCQVEDGYGSSEGAV----IVVREPGTPPGSIGRGAPgvaiynpetLTECAVARFDAHGAlLNADE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1461 VAGELW-IGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRG 1539
Cdd:PRK13388 350 AIGELVnTAGAGFFEGYYNNPEATAERMRHG-----MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLR 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1540 HPLVAAATVVPI---HNCTALGAGIVVtgsgaEQFDDSTPGALRAHLAVR--LPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK13388 425 HPAINRVAVYAVpdeRVGDQVMAALVL-----RDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLK 497
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
26-565 |
2.02e-09 |
|
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: 62.91 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 26 VGRRPDAVALrTVAATGIDdWTYQRLWDHVREIRDV-AFSGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVylpst 104
Cdd:cd05923 11 ASRAPDACAI-ADPARGLR-LTYSELRARIEAVAARlHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 105 rEPQRFLARAQHILRDCEPSAVYTC----------GELVEVLErdpiLGALP-IRTPASTADGLAPHPGGTTADAdhgeh 173
Cdd:cd05923 84 -NPRLKAAELAELIERGEMTAAVIAvdaqvmdaifQSGVRVLA----LSDLVgLGEPESAGPLIEDPPREPEQPA----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 vaFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMH--MVSWLPLYHDMGIFwGVFMPLLNGGcTTLIPPHDFv 251
Cdd:cd05923 154 --FVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHnvVLGLMPLYHVIGFF-AVLVAALALD-GTYVVVEEF- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 252 rNPRIWLETVSRFRGNWIggpdFAYRRCIEAFDGTALQS-LDLSCLRLATngaepVRGTTLRDFTAKfRAAGLRDDVMAP 330
Cdd:cd05923 229 -DPADALKLIEQERVTSL----FATPTHLDALAAAAEFAgLKLSSLRHVT-----FAGATMPDAVLE-RVNQHLPGEKVN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 331 QYGLAEAglgvtgsqtvrvwVEKSFDadalergiavevaqPNPADGrsralvSCGDGAFGWDIQIV----DPDRhmTLTD 406
Cdd:cd05923 298 IYGTTEA-------------MNSLYM--------------RDARTG------TEMRPGFFSEVRIVriggSPDE--ALAN 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 407 GEVGEIWVGGPGLP--DGYWRQPEQTATtfgaRTADGlgpYLRTGDAGFRY-QGELYVCGRYRDLIIVGGRNHFPNDIEK 483
Cdd:cd05923 343 GEEGELIVAAAADAafTGYLNQPEATAK----KLQDG---WYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIER 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 484 tVEEAHCGVAPGGACAVqPDapqangEWW-------LVLETGSPVEDLddLSRILRRRILAHHETaPERVVWVpcRTLPT 556
Cdd:cd05923 416 -VLSRHPGVTEVVVIGV-AD------ERWgqsvtacVVPREGTLSADE--LDQFCRASELADFKR-PRRYFFL--DELPK 482
|
....*....
gi 2181016861 557 TTSGKIRRR 565
Cdd:cd05923 483 NAMNKVLRR 491
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1793-2122 |
2.23e-09 |
|
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: 62.40 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1793 DADT-TQRVQ-VDAGPVPVHDLDIQDDP-----DLLLRRMAAAPFDPHSVPVIQCFAPSRSP-RHV-GLLISYLGLDARS 1863
Cdd:cd19539 63 DGGVpRQEILpPGPAPLEVRDLSDPDSDrerrlEELLRERESRGFDLDEEPPIRAVLGRFDPdDHVlVLVAHHTAFDAWS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1864 LSTVVTTIIAEYQS--QPRPRQVDPTAAVFARFASE--SAWGENDVDNSV---------AGPPLLPLHDQRRDPFERVTf 1930
Cdd:cd19539 143 LDVFARDLAALYAArrKGPAAPLPELRQQYKEYAAWqrEALAAPRAAELLdfwrrrlrgAEPTALPTDRPRPAGFPYPG- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1931 ARRSFTIEEQAAATLREHAAHLGVTPTALVFEAFAHALASIgAGQR-FAVTVPKSYRPDyaPADREVLGNFTRLALCEVD 2009
Cdd:cd19539 222 ADLRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRY-TGQTdIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2010 ygaVRPGSA--EAVAAAQRELWRAVSHD----GDITGGLAATRTAGGYPVV-----FTSTLGLTHQDASGLTNVRTLTQT 2078
Cdd:cd19539 299 ---VSDCATfrDLIARVRKALVDAQRHQelpfQQLVAELPVDRDAGRHPLVqivfqVTNAPAGELELAGGLSYTEGSDIP 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2181016861 2079 PGVWLDCQT--EDEVAGIRMSWDIATNVVAAESISVAFSRFEEAVR 2122
Cdd:cd19539 376 DGAKFDLNLtvTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLR 421
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2966-3051 |
2.44e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIADTDNADE 3045
Cdd:PRK12467 3601 APRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGDVPVN 3680
|
....*.
gi 2181016861 3046 PDLTVE 3051
Cdd:PRK12467 3681 LLLDLN 3686
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
180-566 |
2.52e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 62.64 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 180 SSGSTGKPKGVVNTHQSILR-QAAFAANV-WNGDDDMHMVSwlPLYHDMGIF-WGVFMPLlngGCTtLIPPHDFvrNPRI 256
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLApLAGLLSRVpFRAGETTLLPA--PMFHATGWAhLTLAMAL---GST-VVLRRRF--DPEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 257 WLETVSRFRGN-WIGGPDFAYRrcIEAFDGTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAPQYGLA 335
Cdd:PRK07788 287 TLEDIAKHKATaLVVVPVMLSR--ILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAF------GPVLYNLYGST 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 336 EAGLGVtgsqtvrvwveksfdadalergIAvevaqpNPADGRsRALVSCGDGAFGWDIQIVDPDRHmTLTDGEVGEIWVG 415
Cdd:PRK07788 359 EVAFAT----------------------IA------TPEDLA-EAPGTVGRPPKGVTVKILDENGN-EVPRGVVGRIFVG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 416 GpGLP-DGYW--RQPEqtattfgarTADGLgpyLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCG 491
Cdd:PRK07788 409 N-GFPfEGYTdgRDKQ---------IIDGL---LSSGDVGyFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAG-HPD 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 492 VAPGGACAVQPDapqangEW------WLVLETGSPVeDLDDLSRILRRRiLAHHETaPERVVWVPcrTLPTTTSGKIRRR 565
Cdd:PRK07788 475 VVEAAVIGVDDE------EFgqrlraFVVKAPGAAL-DEDAIKDYVRDN-LARYKV-PRDVVFLD--ELPRNPTGKVLKR 543
|
.
gi 2181016861 566 E 566
Cdd:PRK07788 544 E 544
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
116-566 |
3.05e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 62.31 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 116 HILRDCEPSAVytcgeLVEVLERDPILGALPIRTPASTADGLA-PHPGGTtadadhgehvAFLQYSSGSTGKPKGVVnth 194
Cdd:PRK07787 86 HILADSGAQAW-----LGPAPDDPAGLPHVPVRLHARSWHRYPePDPDAP----------ALIVYTSGTTGPPKGVV--- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 195 qsiLRQAAFAANV--------WNGDDDmhMVSWLPLYHDMGIFWGVFMPLLNGGcttliPPHDFVR-NPRIWLETVSRFR 265
Cdd:PRK07787 148 ---LSRRAIAADLdalaeawqWTADDV--LVHGLPLFHVHGLVLGVLGPLRIGN-----RFVHTGRpTPEAYAQALSEGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 266 GNWIGGPDFAYRRCIEAFDGTALQSldlscLRLATNGAEPVRGTTLRDFTAkfrAAGLRddvMAPQYGLAEAGLGVtgsq 345
Cdd:PRK07787 218 TLYFGVPTVWSRIAADPEAARALRG-----ARLLVSGSAALPVPVFDRLAA---LTGHR---PVERYGMTETLITL---- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 346 tvrvwvekSFDADALERGIAVEVAQPnpadgrsralvscgdgafGWDIQIVDPDRHMTLTDGE-VGEIWVGGPGLPDGYW 424
Cdd:PRK07787 283 --------STRADGERRPGWVGLPLA------------------GVETRLVDEDGGPVPHDGEtVGELQVRGPTLFDGYL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 425 RQPEQTATTFgarTADGlgpYLRTGDAGFR-YQGELYVCGRYR-DLIIVGGRNHFPNDIEkTVEEAHCGVAPGGACAVqP 502
Cdd:PRK07787 337 NRPDATAAAF---TADG---WFRTGDVAVVdPDGMHRIVGREStDLIKSGGYRIGAGEIE-TALLGHPGVREAAVVGV-P 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 503 DAPQanGE---WWLVLETGSPVEDLDDLSrilrRRILAHHETaPERVVWVPcrTLPTTTSGKIRRRE 566
Cdd:PRK07787 409 DDDL--GQrivAYVVGADDVAADELIDFV----AQQLSVHKR-PREVRFVD--ALPRNAMGKVLKKQ 466
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1260-1612 |
3.13e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 62.46 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLAL--------SALDFDLSVYdtfgaLGCGAQL 1331
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSIlplhhiypLTFTLLLPLL-----NGAHVVF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1332 VTIPEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLS------------------------ 1387
Cdd:cd05914 162 LDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFKLAKKINNrkirklafkkvheafggnikefvi 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1388 -GDWIPLDLPRRLRRAapGVRLVAMGGATEAA-IWS----NEFVVDDVdpdwasipyGYPLANQMFRVVDDNgddqPDYV 1461
Cdd:cd05914 242 gGAKINPDVEEFLRTI--GFPYTIGYGMTETApIISysppNRIRLGSA---------GKVIDGVEVRIDSPD----PATG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1462 AGELWIGGAGVALGYHNAPELTSDRFvhDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQ-VKIRGHRVECGEIEHALRGH 1540
Cdd:cd05914 307 EGEIIVRGPNVMKGYYKNPEATAEAF--DKDG--WFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNM 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 1541 PLVAAATVVPIHNCTALGAGI-----VVTGSGAEQFDDSTPGALRAHLAVRLPQY-MIPKVFVSCPELPLTANGKVDR 1612
Cdd:cd05914 383 PFVLESLVVVQEKKLVALAYIdpdflDVKALKQRNIIDAIKWEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2973-3032 |
3.35e-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: 55.26 E-value: 3.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 2973 QRVSRICASALGQP--RVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGD 3032
Cdd:pfam00550 1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
144-575 |
3.64e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 62.45 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 144 ALPIRTPASTADGLAPHPGGTTA----DADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSW 219
Cdd:PRK06164 149 ATPAPAPGARVQLFALPDPAPPAaageRAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 220 LPLYHDMGiFWGVFMPLLNGGCTTLIPPHDFVRNPRIwletVSRFRGNWIGGPDFAYRRCIEafdgTALQSLDLSCLRLA 299
Cdd:PRK06164 229 LPFCGVFG-FSTLLGALAGGAPLVCEPVFDAARTARA----LRRHRVTHTFGNDEMLRRILD----TAGERADFPSARLF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 300 TNGAEPVRgttLRDFTAKFRAAGlrddvmAPQYGLaeaglgvTGSQTVrvwveksfdadalergIAVEVAQPNPADGRSR 379
Cdd:PRK06164 300 GFASFAPA---LGELAALARARG------VPLTGL-------YGSSEV----------------QALVALQPATDPVSVR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 380 ALVSCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTAttfGARTADGlgpYLRTGDAGF-RYQGE 458
Cdd:PRK06164 348 IEGGGRPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATA---RALTDDG---YFRTGDLGYtRGDGQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 459 LYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVAPGGACAVQPDApQANGEWWLVLETGSPVeDLDDLSRILRRRILAH 538
Cdd:PRK06164 422 FVYQTRMGDSLRLGGFLVNPAEIEHALEA-LPGVAAAQVVGATRDG-KTVPVAFVIPTDGASP-DEAGLMAACREALAGF 498
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2181016861 539 heTAPERVVWVpcRTLPTTTSG---KIRR---RETLNRLTAGQ 575
Cdd:PRK06164 499 --KVPARVQVV--EAFPVTESAngaKIQKhrlREMAQARLAAE 537
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2567-2936 |
5.42e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2567 DRPRFDSAARQLVARHAGLRTTVSPAGTDAassgevaVVHTAPIEPVVRDHDDVR--------AAMRD-------QIIDL 2631
Cdd:PRK12316 85 DRQALERAFASLVQRHETLRTVFPRGADDS-------LAQVPLDRPLEVEFEDCSglpeaeqeARLRDeaqreslQPFDL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2632 TARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLY----RGETVdQLPPLETSFAHY-VWNHPELlpDAD 2706
Cdd:PRK12316 158 CEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYsayaTGAEP-GLPALPIQYADYaLWQRSWL--EAG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2707 EAvlprlAASRDYWRARLPSLPPAPKLADMSLLFEIEEPRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLS 2786
Cdd:PRK12316 235 EQ-----ERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLH 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2787 RWSGTDHFCINVTLFDRDPdvVGIENVVGDFTSLVLLECRVDEPASIWESVRALQR-----QLMTDLP-HRGADAVWLQR 2860
Cdd:PRK12316 310 RYSGQTDIRVGVPIANRNR--AEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDtvlgaQAHQDLPfERLVEALKVER 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 2861 ELLRfhgNPtaaLFPVVFTSGLGLVDASAR---AAVRFaEPVFAASQTPQTVLDFQVWESAGALKLSWDFVSQAVSPAT 2936
Cdd:PRK12316 388 SLSH---SP---LFQVMYNHQPLVADIEALdtvAGLEF-GQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEART 459
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2966-3048 |
5.70e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 62.49 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIADTDNADE 3045
Cdd:PRK12467 1026 APQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQ 1105
|
...
gi 2181016861 3046 PDL 3048
Cdd:PRK12467 1106 PAL 1108
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
685-979 |
6.95e-09 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 60.85 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 685 PTTPLQQAYWVgrgAEQ--PLGGVgCQT--YFELVGArVDAGRLAAALDALTRRHPMLRATF-PDPG--RCLITPEAvRL 757
Cdd:cd19533 3 PLTSAQRGVWF---AEQldPEGSI-YNLaeYLEITGP-VDLAVLERALRQVIAEAETLRLRFtEEEGepYQWIDPYT-PV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 758 PLAVHDLTDAPVTtRDTHLAEIRRRLRtHRFDIETGDTWTVELTRLPHGCIVHFA-VDLIIADVTSIGTMLRDLAASYRG 836
Cdd:cd19533 77 PIRHIDLSGDPDP-EGAAQQWMQEDLR-KPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIYTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 837 -----EKLPAPSATFADLIQSTSP---PPQACADR---------LPEGPQL-PRVQEADISFLRHQHTLSALATKAIDDA 898
Cdd:cd19533 155 llkgrPAPPAPFGSFLDLVEEEQAyrqSERFERDRafwteqfedLPEPVSLaRRAPGRSLAFLRRTAELPPELTRTLLEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 899 CHNHGVTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRSPEVS-DVVGDFTETHLYRAQLDGQISFVDQAQVTQKGLRTA 977
Cdd:cd19533 235 AEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAArQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSL 314
|
..
gi 2181016861 978 LR 979
Cdd:cd19533 315 LR 316
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2564-2953 |
1.08e-08 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 60.34 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2564 ADFDRPRFDSAARQLVARHAGLRTTVSPAGtdaassGEVAVVHTAPIEPVVR------DHDDVRAAMRDQI------IDL 2631
Cdd:cd19534 32 QGLDPDALRQALRALVEHHDALRMRFRRED------GGWQQRIRGDVEELFRlevvdlSSLAQAAAIEALAaeaqssLDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2632 TARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQLPPLE--TSFAHYVwnhpELLpdADEAV 2709
Cdd:cd19534 106 EEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPLPskTSFQTWA----ELL--AEYAQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2710 LPRLAASRDYWRArLPSLPPAPKLADMSLLFEIEEPRFERATATIPAVDWSQVTRSCRAEGVTVasfLLANYARVLSRWS 2789
Cdd:cd19534 180 SPALLEELAYWRE-LPAADYWGLPKDPEQTYGDARTVSFTLDEEETEALLQEANAAYRTEINDL---LLAALALAFQDWT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2790 GTDHFCINVTLFDRDPDVVGIE--NVVGDFTSL--VLLEcrVDEPASIWESVRALQRQLMTdLPHRGadavwLQRELLRF 2865
Cdd:cd19534 256 GRAPPAIFLEGHGREEIDPGLDlsRTVGWFTSMypVVLD--LEASEDLGDTLKRVKEQLRR-IPNKG-----IGYGILRY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2866 HGNPTAALF------PVVFTSgLGLVDASARAAVRF--AEPVFAASQTPQT----VLDFQVWESAGALKLSWDFVSQAVS 2933
Cdd:cd19534 328 LTPEGTKRLafhpqpEISFNY-LGQFDQGERDDALFvsAVGGGGSDIGPDTprfaLLDINAVVEGGQLVITVSYSRNMYH 406
|
410 420
....*....|....*....|
gi 2181016861 2934 PATARTQLESLVDGITGVAT 2953
Cdd:cd19534 407 EETIQQLADSYKEALEALIE 426
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
179-566 |
1.20e-08 |
|
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: 60.56 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 179 YSSGSTGKPKGVVNTHQSILRQAAFAANVWNG---DDDMHMVSwlplyhDMG----IFWGVFMPLLNGGCTTLippHDFV 251
Cdd:cd05928 181 FTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDltaSDIMWNTS------DTGwiksAWSSLFEPWIQGACVFV---HHLP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 252 R-NPRIWLETVSRFRGNWIGGPDFAYRRCIEafdgTALQSLDLSCLRLATNGAEPVRGTTLRDFTAKfraAGLRddvMAP 330
Cdd:cd05928 252 RfDPLVILKTLSSYPITTFCGAPTVYRMLVQ----QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ---TGLD---IYE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 331 QYGLAEAGLGVTGSQTVRVwveksfdadalergiavevaQPNpadgrsralvSCGDGAFGWDIQIVDpDRHMTLTDGEVG 410
Cdd:cd05928 322 GYGQTETGLICANFKGMKI--------------------KPG----------SMGKASPPYDVQIID-DNGNVLPPGTEG 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 411 EIWVG-GPGLP----DGYWRQPEQTATTFgartadgLGPYLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEKT 484
Cdd:cd05928 371 DIGIRvKPIRPfglfSGYVDNPEKTAATI-------RGDFYLTGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 485 VEEaHCGVAPGgACAVQPDapQANGE---WWLVLETGSPVEDLDDLSRILR---RRILAHHETaPERVVWVpcRTLPTTT 558
Cdd:cd05928 444 LIE-HPAVVES-AVVSSPD--PIRGEvvkAFVVLAPQFLSHDPEQLTKELQqhvKSVTAPYKY-PRKVEFV--QELPKTV 516
|
....*...
gi 2181016861 559 SGKIRRRE 566
Cdd:cd05928 517 TGKIQRNE 524
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
114-489 |
1.61e-08 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 60.08 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 114 AQHILRDCEPSAVYTCGELVEVLER------DPILGALPIRTPASTADG-------LAPHPG----GTTADADHgehVAF 176
Cdd:PRK08008 101 SAWILQNSQASLLVTSAQFYPMYRQiqqedaTPLRHICLTRVALPADDGvssftqlKAQQPAtlcyAPPLSTDD---TAE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSILRQAAFAAnvWNG---DDDMHMvSWLPLYH-DMGIfwGVFMPLLNGGCTTlipphdfvr 252
Cdd:PRK08008 178 ILFTSGTTSRPKGVVITHYNLRFAGYYSA--WQCalrDDDVYL-TVMPAFHiDCQC--TAAMAAFSAGATF--------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 nprIWLETVS--RFrgnWiggpdfayrRCIEAFDGTALQSLDLSCLRLATNGAEPV-RGTTLRD--------------FT 315
Cdd:PRK08008 244 ---VLLEKYSarAF---W---------GQVCKYRATITECIPMMIRTLMVQPPSANdRQHCLREvmfylnlsdqekdaFE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 316 AKFraaGLRddvMAPQYGLAEAGLGVTGSQtvrvwveksfdadalergiavevaqpnPADgrSRALVSCGDGAFGWDIQI 395
Cdd:PRK08008 309 ERF---GVR---LLTSYGMTETIVGIIGDR---------------------------PGD--KRRWPSIGRPGFCYEAEI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 396 VDPDRHmTLTDGEVGEIWVGG-PG--LPDGYWRQPEQTATTFgarTADGlgpYLRTGDAGFR-YQGELYVCGRYRDLIIV 471
Cdd:PRK08008 354 RDDHNR-PLPAGEIGEICIKGvPGktIFKEYYLDPKATAKVL---EADG---WLHTGDTGYVdEEGFFYFVDRRCNMIKR 426
|
410
....*....|....*...
gi 2181016861 472 GGRNHFPNDIEKtVEEAH 489
Cdd:PRK08008 427 GGENVSCVELEN-IIATH 443
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
8-565 |
1.63e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 60.38 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 8 PPALHDGDRSVPAVFAEWVGRRPDAVALrTVAATGiDDWTYQrlwDHVREIRDVAFSGLSAGIR----IPMALPGGADYV 83
Cdd:PLN02330 20 PSVPVPDKLTLPDFVLQDAELYADKVAF-VEAVTG-KAVTYG---EVVRDTRRFAKALRSLGLRkgqvVVVVLPNVAEYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 84 AGMLAALAAGLI---PVPVYLPSTREPQRFLARAQHIL-RDCEPSAVYTCGELVEVLERDPILGALPIRTPASTADglap 159
Cdd:PLN02330 95 IVALGIMAAGGVfsgANPTALESEIKKQAEAAGAKLIVtNDTNYGKVKGLGLPVIVLGEEKIEGAVNWKELLEAAD---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 160 HPGGTTADAD-HGEHVAFLQYSSGSTGKPKGVVNTHQSILrqAAFAANVWNGDDDM----HMVSWLPLYHDMGIFWGVFM 234
Cdd:PLN02330 171 RAGDTSDNEEiLQTDLCALPFSSGTTGISKGVMLTHRNLV--ANLCSSLFSVGPEMigqvVTLGLIPFFHIYGITGICCA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 235 PLLNGGCTTLIPPHDFvrnpRIWLET-----------VSRFRGNWIGGPdfayrrCIEAFDGTALQsldlscLRLATNGA 303
Cdd:PLN02330 249 TLRNKGKVVVMSRFEL----RTFLNAlitqevsfapiVPPIILNLVKNP------IVEEFDLSKLK------LQAIMTAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 304 EPVRGTTLRDFTAKFRAAGLRDdvmapQYGLAEAGlgvtgsqtvrvwveksfdadalergiAVEVAQPNPADGRSRALV- 382
Cdd:PLN02330 313 APLAPELLTAFEAKFPGVQVQE-----AYGLTEHS--------------------------CITLTHGDPEKGHGIAKKn 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 383 SCGDGAFGWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQTattfgARTADGLGpYLRTGDAGF-RYQGELYV 461
Cdd:PLN02330 362 SVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEET-----DRTIDEDG-WLHTGDIGYiDDDGDIFI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 462 CGRYRDLIIVGGRNHFPNDIEK------TVEEAhcgvapggacAVQPDAPQANGE--WWLVLETGSPVEDLDDLSRILRR 533
Cdd:PLN02330 436 VDRIKELIKYKGFQVAPAELEAillthpSVEDA----------AVVPLPDEEAGEipAACVVINPKAKESEEDILNFVAA 505
|
570 580 590
....*....|....*....|....*....|..
gi 2181016861 534 RIlAHHETApeRVVWVpCRTLPTTTSGKIRRR 565
Cdd:PLN02330 506 NV-AHYKKV--RVVQF-VDSIPKSLSGKIMRR 533
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1462-1612 |
1.67e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 60.01 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1462 AGELWIGGAGVALGYHnaPELTSDRfvhdptgsRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHP 1541
Cdd:PRK07445 301 TGNITIQAQSLALGYY--PQILDSQ--------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATG 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 1542 LVAAATVVPIHNCTAlgaGIVVTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK07445 371 LVQDVCVLGLPDPHW---GEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINR 438
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
43-468 |
1.79e-08 |
|
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: 59.79 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 43 IDDWTYQRLWDHVReiRDVAF---SGLSAGIRIPMALPGGADYVAGMLAALAAGLIPVPVYLPSTREPQRflaraqHILR 119
Cdd:cd05932 4 VVEFTWGEVADKAR--RLAAAlraLGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIR------YVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 120 DCEPSAVYTcGELVEVLERDPILGALPIRTPASTADGL-------------APHPGGTTADAdhgEHVAFLQYSSGSTGK 186
Cdd:cd05932 76 HSESKALFV-GKLDDWKAMAPGVPEGLISISLPPPSAAncqyqwddliaqhPPLEERPTRFP---EQLATLIYTSGTTGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 187 PKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHdmgIFWGVFMPL--LNGGCTTLIP--------------PHDF 250
Cdd:cd05932 152 PKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAH---VTERVFVEGgsLYGGVLVAFAesldtfvedvqrarPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 251 VRNPRIWletvSRFRGNWIGG-PDFAYRRCIE-AFDGT-----ALQSLDLSCLRLATNGAEPVRGTTLrdftAKFRAAGL 323
Cdd:cd05932 229 FSVPRLW----TKFQQGVQDKiPQQKLNLLLKiPVVNSlvkrkVLKGLGLDQCRLAGCGSAPVPPALL----EWYRSLGL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 324 RddvMAPQYGLAE----AGLGVTGSQTVRVwveksfdadalergiaveVAQPNPadgrsralvscgdgafGWDIQIvdpd 399
Cdd:cd05932 301 N---ILEAYGMTEnfaySHLNYPGRDKIGT------------------VGNAGP----------------GVEVRI---- 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 400 rhmtltdGEVGEIWVGGPGLPDGYWRQPEQTATTFgarTADGlgpYLRTGDAG-FRYQGELYVCGRYRDL 468
Cdd:cd05932 340 -------SEDGEILVRSPALMMGYYKDPEATAEAF---TADG---FLRTGDKGeLDADGNLTITGRVKDI 396
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2567-2817 |
1.87e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.74 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2567 DRPRFDSAARQLVARHAGLRTTVSPAGtdaASSGEVAVVHTAPIEPVVR-----------DHDDVRAAMRDQIIDLTARP 2635
Cdd:PRK12316 4137 DVERFRAAWQAALDRHDVLRSGFVWQG---ELGRPLQVVHKQVSLPFAEldwrgradlqaALDALAAAERERGFDLQRAP 4213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2636 GIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGEtvdQLPPLETSFAHYVwnhpellpdadeAVLPRL-- 2713
Cdd:PRK12316 4214 LLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGR---PPAQPGGRYRDYI------------AWLQRQda 4278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2714 AASRDYWRARLPSLPPAPKLADmsllfEIEEPRFERATA------TIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSR 2787
Cdd:PRK12316 4279 AASEAFWREQLAALDEPTRLAQ-----AIARADLRSANGygehvrELDATATARLREFARTQRVTLNTLVQAAWLLLLQR 4353
|
250 260 270
....*....|....*....|....*....|
gi 2181016861 2788 WSGTDHFCINVTLFDRDPDVVGIENVVGDF 2817
Cdd:PRK12316 4354 YTGQDTVAFGATVAGRPAELPGIEGQIGLF 4383
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1492-1612 |
2.01e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 59.66 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1492 TGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNctALGAGIVVTGSGAEQF 1571
Cdd:PRK08308 288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKD--PVAGERVKAKVISHEE 365
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2181016861 1572 DDstPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK08308 366 ID--PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
139-338 |
2.67e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 59.98 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 139 DPILGALPIRTPastadglaphpgGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANV--WNGDDDMHM 216
Cdd:PRK06814 772 DKIKGLLAGRFP------------LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARidFSPEDKVFN 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 217 VswLPLYHDMGIFWGVFMPLLNGGCTTLIP-PhdfvRNPRIWLETVSRFRGNWIGGPDF---AYRRCIEAFdgtalqslD 292
Cdd:PRK06814 840 A--LPVFHSFGLTGGLVLPLLSGVKVFLYPsP----LHYRIIPELIYDTNATILFGTDTflnGYARYAHPY--------D 905
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2181016861 293 LSCLRLATNGAEPVRGTTLRDFTAKFraaGLRddvMAPQYGLAEAG 338
Cdd:PRK06814 906 FRSLRYVFAGAEKVKEETRQTWMEKF---GIR---ILEGYGVTETA 945
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
111-452 |
2.71e-08 |
|
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: 59.37 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 111 LARAQHILRDCEPSAVYT------CGELVEVLERDP----ILGALPIRTPASTADgLAPHPGGTTADADHG----EHVAF 176
Cdd:cd05921 91 LAKLKHLFELLKPGLVFAqdaapfARALAAIFPLGTplvvSRNAVAGRGAISFAE-LAATPPTAAVDAAFAavgpDTVAK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 177 LQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN--GDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGC------------- 241
Cdd:cd05921 170 FLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPffGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTlyiddgkpmpggf 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 -TTL-----IPPHDFVRNPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTAL-QSL--DLSCLRLATNGaEPVRgttlr 312
Cdd:cd05921 250 eETLrnlreISPTVYFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLsQDVwdRLQALAVATVG-ERIP----- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 313 dftakfraaglrddvMAPQYGLAEAGlgvtGSQTVRVWVeksfdadaLERGIAVEVaqpnPADGRSRALVSCGdGAFgwd 392
Cdd:cd05921 324 ---------------MMAGLGATETA----PTATFTHWP--------TERSGLIGL----PAPGTELKLVPSG-GKY--- 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 393 iqivdpdrhmtltdgevgEIWVGGPGLPDGYWRQPEQTATTFgartaDGLGPYlRTGDAG 452
Cdd:cd05921 369 ------------------EVRVKGPNVTPGYWRQPELTAQAF-----DEEGFY-CLGDAA 404
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2966-3038 |
2.78e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.18 E-value: 2.78e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIA 3038
Cdd:PRK05691 582 ASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVA 654
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1114-1610 |
3.60e-08 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 59.12 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1114 LYDAFRENAAThPARLALRwrpddyrgerhgdviAQDRSQLTYGELDELARSVARA-VAARHAAGSVIGIQLPKGPSQIV 1192
Cdd:PRK07514 5 LFDALRAAFAD-RDAPFIE---------------TPDGLRYTYGDLDAASARLANLlVALGVKPGDRVAVQVEKSPEALA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1193 AVLGVMMAGCTYLPVGVD-QPAE----------RLSrICARSAMAGLIR-------TDSDTQDAGVAVSDITAMIECAPT 1254
Cdd:PRK07514 69 LYLATLRAGAVFLPLNTAyTLAEldyfigdaepALV-VCDPANFAWLSKiaaaagaPHVETLDADGTGSLLEAAAAAPDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1255 -DPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALsaldfdLSVYDTFG-------ALG 1326
Cdd:PRK07514 148 fETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHA------LPIFHTHGlfvatnvALL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1327 CGAQLVTIPEHARRDAFHWLSLTTefgitVWNSVPGLMDMLLIAAGDKAGSLPTLRsVFLSGDwIPLdLPRRLR--RAAP 1404
Cdd:PRK07514 222 AGASMIFLPKFDPDAVLALMPRAT-----VMMGVPTFYTRLLQEPRLTREAAAHMR-LFISGS-APL-LAETHRefQERT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1405 GVRLVAMGGATEAA-IWSNefvvddvdpdwasiPY---------GYPLANQMFRVVD-DNGDDQPDYVAGELWIGGAGVA 1473
Cdd:PRK07514 294 GHAILERYGMTETNmNTSN--------------PYdgerragtvGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1474 LGYHNAPELTSDRFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV--VPI 1551
Cdd:PRK07514 360 KGYWRMPEKTAEEFRADG----FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVigVPH 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 1552 HNCTALGAGIVVTGSGAeqfdDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKV 1610
Cdd:PRK07514 436 PDFGEGVTAVVVPKPGA----ALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV 490
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
128-565 |
4.47e-08 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 58.54 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 128 TCGELVEVLERDPILGALPIRtPASTADGLAPHPGGTTADADHGEHVAF--------------LQYSSGSTGKPKGVVNT 193
Cdd:cd05929 68 CPAYKSSRAPRAEACAIIEIK-AAALVCGLFTGGGALDGLEDYEAAEGGspetpiedeaagwkMLYSGGTTGRPKGIKRG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 194 H----QSILRQAAFAANVWNGDDDMHMvSWLPLYHDMGIFWgVFMPLLNGGCTTLIPPHDfvrnPRIWLETVSRFRGNWI 269
Cdd:cd05929 147 LpggpPDNDTLMAAALGFGPGADSVYL-SPAPLYHAAPFRW-SMTALFMGGTLVLMEKFD----PEEFLRLIERYRVTFA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 270 GG-PDFAYRrcIEAFDGTALQSLDLSCLRLATNGAEPVrgttlrdftakfrAAGLRDDVMA--PQ-----YGLAEA-GLG 340
Cdd:cd05929 221 QFvPTMFVR--LLKLPEAVRNAYDLSSLKRVIHAAAPC-------------PPWVKEQWIDwgGPiiweyYGGTEGqGLT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 341 VTGSQTvrvWVEksfdadalERGiavevaqpnpadgrsralvSCGDGAFGwDIQIVDPDRHmTLTDGEVGEIWVGGPGlP 420
Cdd:cd05929 286 IINGEE---WLT--------HPG-------------------SVGRAVLG-KVHILDEDGN-EVPPGEIGEVYFANGP-G 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 421 DGYWRQPEQTATtfgARTADGlgpYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVApggACA 499
Cdd:cd05929 333 FEYTNDPEKTAA---ARNEGG---WSTLGDVGyLDEDGYLYLTDRRSDMIISGGVNIYPQEIE-NALIAHPKVL---DAA 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 500 V--QPDaPQANGEWWLVLETG----SPVEDLDDLSRILRRRiLAHHETaPERVVWVpcRTLPTTTSGKIRRR 565
Cdd:cd05929 403 VvgVPD-EELGQRVHAVVQPApgadAGTALAEELIAFLRDR-LSRYKC-PRSIEFV--AELPRDDTGKLYRR 469
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
175-305 |
4.64e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 58.75 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILrqaafaanvwngdddMHMVS--WLPLYHDMGIFW-------------GVFMPLLNg 239
Cdd:PRK04319 208 AILHYTSGSTGKPKGVLHVHNAML---------------QHYQTgkYVLDLHEDDVYWctadpgwvtgtsyGIFAPWLN- 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 240 GCTTLIPPHDFvrNPRIWLETVSRFRGN-WIGGPDfAYRRCIEAFDGTAlQSLDLSCLRLATNGAEP 305
Cdd:PRK04319 272 GATNVIDGGRF--SPERWYRILEDYKVTvWYTAPT-AIRMLMGAGDDLV-KKYDLSSLRHILSVGEP 334
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1439-1612 |
6.14e-08 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 58.49 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1439 GYPLANQMFRVVDDNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDrfVHDPTGsrWYRTGDMGCYWRDGTLQFLGRAD 1518
Cdd:PRK07059 383 GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAK--VMTADG--FFRTGDVGVMDERGYTKIVDRKK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1519 SQVKIRGHRVECGEIEHALRGHP--LVAAATVVP-IHNCTALGAGIVvtgsgaEQFDDSTPGALRAHLAVRLPQYMIPKV 1595
Cdd:PRK07059 459 DMILVSGFNVYPNEIEEVVASHPgvLEVAAVGVPdEHSGEAVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKF 532
|
170
....*....|....*..
gi 2181016861 1596 FVSCPELPLTANGKVDR 1612
Cdd:PRK07059 533 VEFRTELPKTNVGKILR 549
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
390-565 |
6.42e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 58.17 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 390 GWDIQIVDPDRHmTLTDGEVGEIWVGGPGLPD-GYWRQPEqtattfgARTADGLGPYLRTGDAG-FRYQGELYVCGRYRD 467
Cdd:PRK12406 332 GAELRFVDEDGR-PLPQGEIGEIYSRIAGNPDfTYHNKPE-------KRAEIDRGGFITSGDVGyLDADGYLFLCDRKRD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 468 LIIVGGRNHFPNDIEktvEEAHcGVAPGGACAV--QPDApqANGE-WWLVLETGSPVE-DLDDLSRILRRRiLAHHETaP 543
Cdd:PRK12406 404 MVISGGVNIYPAEIE---AVLH-AVPGVHDCAVfgIPDA--EFGEaLMAVVEPQPGATlDEADIRAQLKAR-LAGYKV-P 475
|
170 180
....*....|....*....|..
gi 2181016861 544 ERVVWVPcrTLPTTTSGKIRRR 565
Cdd:PRK12406 476 KHIEIMA--ELPREDSGKIFKR 495
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
685-1082 |
6.81e-08 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 57.69 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 685 PTTPLQQAYwVGRGAEQPLGGVGcQTYFELVGArVDAGRLAAALDALTRRHPMLRATFpdpgrclITPEAVRLPLAVHDL 764
Cdd:cd19545 3 PCTPLQEGL-MALTARQPGAYVG-QRVFELPPD-IDLARLQAAWEQVVQANPILRTRI-------VQSDSGGLLQVVVKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 765 TDAPVTTRDThLAEIRRRLRTHRFDIetgdtwtveLTRLPHGCIVHFAVD---LIIA------DVTSIGTMLRDLAASYR 835
Cdd:cd19545 73 SPISWTESTS-LDEYLEEDRAAPMGL---------GGPLVRLALVEDPDTeryFVWTihhalyDGWSLPLILRQVLAAYQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 836 GEKLPA--PSATFADLIQSTSPppQACAD---------RLPEGPQLPRvqeadisfLRHQHTLSALATKAID-DACHNHG 903
Cdd:cd19545 143 GEPVPQppPFSRFVKYLRQLDD--EAAAEfwrsylaglDPAVFPPLPS--------SRYQPRPDATLEHSISlPSSASSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 904 VTRAAVLLAAYTLVLRRWASQDDFLVNVTTFGRS---PEVSDVVGDFTETHLYRAQLDGQIS---FVD--QAQVT----- 970
Cdd:cd19545 213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNapvPGIEQIVGPTIATVPLRVRIDPEQSvedFLQtvQKDLLdmipf 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 971 -QKGLRTALRAAPapdllatqlrsGTGHSGIVP--VVFTYAADSPLLSAEDANtlgaidevvsmTPQVLIDHQA------ 1041
Cdd:cd19545 293 eHTGLQNIRRLGP-----------DARAACNFQtlLVVQPALPSSTSESLELG-----------IEEESEDLEDfssygl 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2181016861 1042 ---CRL-GDDVVLSWDYRAGCFPPGVVDDMFEAYVTLLERLGGHD 1082
Cdd:cd19545 351 tleCQLsGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
2614-2868 |
6.97e-08 |
|
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: 57.76 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2614 VRDHDDVRAA----MRDQI---IDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGE-TVDQLP 2685
Cdd:cd19533 83 LSGDPDPEGAaqqwMQEDLrkpLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALlKGRPAP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2686 P-LETSFAHYVwnhpelLPDADEAVLPRLAASRDYWRARLPSLPPAPKLADMSLLFEieePRFERATATIPAVDWSQVTR 2764
Cdd:cd19533 163 PaPFGSFLDLV------EEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRS---LAFLRRTAELPPELTRTLLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2765 SCRAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDPdvVGIENVVGDFTSLVLLECRVDEPASIWESVRALQRQL 2844
Cdd:cd19533 234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLG--AAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311
|
250 260
....*....|....*....|....
gi 2181016861 2845 MTDLPHRGADAVWLQRELLRFHGN 2868
Cdd:cd19533 312 RSLLRHQRYRYEDLRRDLGLTGEL 335
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
718-1081 |
8.29e-08 |
|
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: 57.71 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 718 RVDAGRLAAALDALTRRHPMLRATF--PDPGRCLITPEAVRLPLAVHDLTdapvttrdtHL--AEIRRRLRTHR---FDI 790
Cdd:cd20484 35 KLDVEKFKQACQFVLEQHPILKSVIeeEDGVPFQKIEPSKPLSFQEEDIS---------SLkeSEIIAYLREKAkepFVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 791 ETGDTWTVEL-TRLPHGCIVHFAVDLIIADVTSIGTMLRDLAASYR-----GEKLPAPSAT----FADLIQSTSPPPQAC 860
Cdd:cd20484 106 ENGPLMRVHLfSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqgKQPTLASSPAsyydFVAWEQDMLAGAEGE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 861 ADR----------LPeGPQLP--RVQEADISFLRHQHT--LSALATKAIDDACHNHGVTRAAVLLAAYTLVLRRWASQDD 926
Cdd:cd20484 186 EHRaywkqqlsgtLP-ILELPadRPRSSAPSFEGQTYTrrLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 927 FLVNVTTFGRSPE-VSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKGLRTALRAAPAP------DLLATQLRsgtGHSG 999
Cdd:cd20484 265 IIVGMPTMGRPEErFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPfpamvrDLNIPRSQ---ANSP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1000 IVPVVFTY-----AADSPLLSAEDANTLGA--IDEVvsmtpqvlidHQ------ACRL---GDDVVLSWDYRAGCFPPGV 1063
Cdd:cd20484 342 VFQVAFFYqnflqSTSLQQFLAEYQDVLSIefVEGI----------HQegeyelVLEVyeqEDRFTLNIKYNPDLFDAST 411
|
410
....*....|....*...
gi 2181016861 1064 VDDMFEAYVTLLERLGGH 1081
Cdd:cd20484 412 IERMMEHYVKLAEELIAN 429
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1260-1537 |
8.67e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 57.90 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAAALntivdVNRRNRIDTHDRLLALSALDFdLSVYDTFGALGCG-----AQLVTI 1334
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLL-----ANQRACLKFFSPKEDDVMMSF-LPPFHAYGFNSCTlfpllSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1335 PEHARRDAFHWLSLTTEFGITVWNSVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRAAPGVRLVAMGGA 1414
Cdd:PRK06334 255 FAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1415 TEAaiwSNEFVVDDVDPDWASIPYGYPLANQMFRVVDDNGD-DQPDYVAGELWIGGAGVALGYHNAPEltSDRFVHdPTG 1493
Cdd:PRK06334 335 TEC---SPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE-LGG 408
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2181016861 1494 SRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHAL 1537
Cdd:PRK06334 409 ETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1250-1612 |
1.03e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 57.84 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1250 ECAPTdpiRIDPHDAAYVIYTSGSTGEPKGVLVS------HAAAlntivdvnrrnridTHDRLlalsaldFDLSVYDTF- 1322
Cdd:PRK00174 236 ECEPE---PMDAEDPLFILYTSGSTGKPKGVLHTtggylvYAAM--------------TMKYV-------FDYKDGDVYw 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1323 ----------------GALGCGA-QLV-----TIPEHARrdafHWlSLTTEFGITVWNSVPGLMDMLlIAAGD---KAGS 1377
Cdd:PRK00174 292 ctadvgwvtghsyivyGPLANGAtTLMfegvpNYPDPGR----FW-EVIDKHKVTIFYTAPTAIRAL-MKEGDehpKKYD 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1378 LPTLR---SVflsGDWI-PldlprrlrraapgvrlvamggatEAAIWSNEFVVDD----VDPDW---------ASIP--- 1437
Cdd:PRK00174 366 LSSLRllgSV---GEPInP-----------------------EAWEWYYKVVGGErcpiVDTWWqtetggimiTPLPgat 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1438 ------YGYPLANQMFRVVDDNGDDQPDYVAGEL-----WiggAGVALGYHNAPEltsdRFVHD--PTGSRWYRTGDmGC 1504
Cdd:PRK00174 420 plkpgsATRPLPGIQPAVVDEEGNPLEGGEGGNLvikdpW---PGMMRTIYGDHE----RFVKTyfSTFKGMYFTGD-GA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1505 -YWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPI-HNCTalGAGIV--VTGSGAEQFDDSTPGALR 1580
Cdd:PRK00174 492 rRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRpDDIK--GQGIYafVTLKGGEEPSDELRKELR 569
|
410 420 430
....*....|....*....|....*....|..
gi 2181016861 1581 AHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK00174 570 NWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2323-2507 |
1.41e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2323 LPDAEAVLEAITVSDDGwlwmvenseATQATLISAAV-LDPGLLASDSKTLRPADRWWRLIADHgwRPTHMIqdgPG-LT 2400
Cdd:PRK12316 4971 LREHPAVREAVVIAQEG---------AVGKQLVGYVVpQDPALADADEAQAELRDELKAALRER--LPEYMV---PAhLV 5036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2401 LIAHRP-------DKPGMPTPPAEQRRDGRwsrpAVPASSLPTDatvvatLAEIWQRHLAIPTPGVDDDFFLLGGDSLVA 2473
Cdd:PRK12316 5037 FLARMPltpngklDRKALPQPDASLLQQAY----VAPRSELEQQ------VAAIWAEVLQLERVGLDDNFFELGGHSLLA 5106
|
170 180 190
....*....|....*....|....*....|....*..
gi 2181016861 2474 TRVYADLRAAGFGQLAFVDLFNHSTLG---ELAAHAG 2507
Cdd:PRK12316 5107 IQVTSRIQLELGLELPLRELFQTPTLAafvELAAAAG 5143
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2966-3050 |
1.58e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIADTDNADE 3045
Cdd:PRK12316 2512 APQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRA 2591
|
....*
gi 2181016861 3046 PDLTV 3050
Cdd:PRK12316 2592 PVLQK 2596
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2442-2501 |
1.73e-07 |
|
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: 50.25 E-value: 1.73e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 2442 ATLAEIWQRHLAIPTP--GVDDDFFLLGGDSLVATRVYADLRAAgFG-QLAFVDLFNHSTLGE 2501
Cdd:pfam00550 1 ERLRELLAEVLGVPAEeiDPDTDLFDLGLDSLLAVELIARLEEE-FGvEIPPSDLFEHPTLAE 62
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2436-2505 |
1.85e-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: 51.01 E-value: 1.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 2436 TDATVVATLAEIWQRHLAIPTP--GVDDDFFL-LGGDSLVATRVYADLRAAgFG-QLAFVDLFNHSTLGELAAH 2505
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEeiTPDDSFFEdLGLDSLDAVELIAALEEE-FGiELPDTELFEYPTVADLADY 74
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1234-1609 |
2.01e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 56.62 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1234 DTQDAGVAVSDITAMIecaPTDPIRIDPHDAAyVIYTSGSTGEPKGVL-----VSHAAALNTIVDVNRRNRIDTHDRLLA 1308
Cdd:PRK13391 130 GELEGFVGYAEAVAGL---PATPIADESLGTD-MLYSSGTTGRPKGIKrplpeQPPDTPLPLTAFLQRLWGFRSDMVYLS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1309 L-----SALDFDLSVYDTFGALgcgaqlVTIPEHArrDAFHWLSLTTEFGITVWNSVPGLMD-ML-LIAAGDKAGSLPTL 1381
Cdd:PRK13391 206 PaplyhSAPQRAVMLVIRLGGT------VIVMEHF--DAEQYLALIEEYGVTHTQLVPTMFSrMLkLPEEVRDKYDLSSL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1382 RSVFLSGDWIPLDLPRR-LRRAAPGVRlvAMGGATEAAIWSnefVVDDvdPDWASIP--YGYPLANQMfRVVDDNGDDQP 1458
Cdd:PRK13391 278 EVAIHAAAPCPPQVKEQmIDWWGPIIH--EYYAATEGLGFT---ACDS--EEWLAHPgtVGRAMFGDL-HILDDDGAELP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1459 DYVAGELWIGGaGVALGYHNAPELTSDrfVHDPTGSrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALR 1538
Cdd:PRK13391 350 PGEPGTIWFEG-GRPFEYLNDPAKTAE--ARHPDGT-WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLI 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 1539 GHPLVAAATVVPIHNcTALG---AGIVVTGSGAEQfDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGK 1609
Cdd:PRK13391 426 THPKVADAAVFGVPN-EDLGeevKAVVQPVDGVDP-GPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGK 497
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1269-1612 |
2.13e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.78 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1269 YTSGSTGEPKGVLVSHAAALntivdvnrrnridthdrLLALS-ALDFDL---SVYdtfgalgcgaqLVTIPE-HARRDAF 1343
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAY-----------------LMALSnALIWGMnegAVY-----------LWTLPMfHCNGWCF 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1344 HW--------------------LSLTTEFGITVWNSVPGLMDMLLIA-AGDKAGSLPTLRSVFLSGDWIPLDLPRRLRRA 1402
Cdd:PLN02479 254 TWtlaalcgtniclrqvtakaiYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVHVMTAGAAPPPSVLFAMSEK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1403 apGVRLVAMGGATEAAIWSNefvVDDVDPDWASIPygyPL------ANQMFRVVDDNGDDQPD-----------YVAGEL 1465
Cdd:PLN02479 334 --GFRVTHTYGLSETYGPST---VCAWKPEWDSLP---PEeqarlnARQGVRYIGLEGLDVVDtktmkpvpadgKTMGEI 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1466 WIGGAGVALGYHNAPELTSDRFVHDptgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAA 1545
Cdd:PLN02479 406 VMRGNMVMKGYLKNPKANEEAFANG-----WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLE 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1546 ATVV--PIHNCTALGAGIVVTGSGAEQFDDS-TPGALRAHLAVRLPQYMIPKVFVSCPeLPLTANGKVDR 1612
Cdd:PLN02479 481 ASVVarPDERWGESPCAFVTLKPGVDKSDEAaLAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQK 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2407-2507 |
2.16e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2407 DKPGMPTPPAEQRRDGrwsrpAVPASSLPtdatvvATLAEIWQRHLAIPTPGVDDDFFLLGGDSLVATRVYADLRAAGFG 2486
Cdd:PRK12467 3584 DRKALPDPDAKGSREY-----VAPRSEVE------QQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGL 3652
|
90 100
....*....|....*....|.
gi 2181016861 2487 QLAFVDLFNHSTLGELAAHAG 2507
Cdd:PRK12467 3653 KLSLRDLMSAPTIAELAGYSP 3673
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1259-1612 |
2.17e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 56.83 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1259 IDPHDAAYVIYTSGSTGEPKGVLvsHAAALNTIVDVNR-RNRIDTHDRLLALSALD---FDLSVYDTFGALGCGAQLVT- 1333
Cdd:PLN02654 272 VDAEDPLFLLYTSGSTGKPKGVL--HTTGGYMVYTATTfKYAFDYKPTDVYWCTADcgwITGHSYVTYGPMLNGATVLVf 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1334 --IPEHArrDAFHWLSLTTEFGITVWNSVPGLMDMLLiAAGDK------AGSLPTLRSVflsGDwiPLDlPRRLRRAAPG 1405
Cdd:PLN02654 350 egAPNYP--DSGRCWDIVDKYKVTIFYTAPTLVRSLM-RDGDEyvtrhsRKSLRVLGSV---GE--PIN-PSAWRWFFNV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1406 VrlvamgGATEAAI----WSNE---FVVDDVDPDWASIPYG--YPLANQMFRVVDDNGDDQPDYVAGEL-----WIGGAG 1471
Cdd:PLN02654 421 V------GDSRCPIsdtwWQTEtggFMITPLPGAWPQKPGSatFPFFGVQPVIVDEKGKEIEGECSGYLcvkksWPGAFR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1472 VALGYHNAPELTsdrFVHDPTGsrWYRTGDmGCYW-RDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVP 1550
Cdd:PLN02654 495 TLYGDHERYETT---YFKPFAG--YYFSGD-GCSRdKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVG 568
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1551 I-HNCTALGAGIVVTGSGAEQFDDSTPGALRAHLAVRLPQYMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PLN02654 569 IeHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
117-566 |
2.31e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 56.45 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 117 ILRDCEPSAVYTCGELVEVLErdPILGALPIRTPASTADG------------LAPHPGGTTADADHGEHvafLQYSSGST 184
Cdd:PRK08276 78 IVDDSGAKVLIVSAALADTAA--ELAAELPAGVPLLLVVAgpvpgfrsyeeaLAAQPDTPIADETAGAD---MLYSSGTT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 185 GKPKGVVN--THQSIL-----RQAAFAANVWNGDDDMHMVSwLPLYHDMGIFWGvfMPLLNGGCTTLIPPHdFvrNPRIW 257
Cdd:PRK08276 153 GRPKGIKRplPGLDPDeapgmMLALLGFGMYGGPDSVYLSP-APLYHTAPLRFG--MSALALGGTVVVMEK-F--DAEEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 258 LETVSRFR---GNWIggPDFaYRRCIeAFDGTALQSLDLSCLRLATNGAEP----VR-------GTTLRDFtakfraagl 323
Cdd:PRK08276 227 LALIERYRvthSQLV--PTM-FVRML-KLPEEVRARYDVSSLRVAIHAAAPcpveVKramidwwGPIIHEY--------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 324 rddvmapqYGLAEAGlGVTGSQTvrvwveksfdADALERGIAVevaqpnpadgrSRALVScgdgafgwDIQIVDPDRHmT 403
Cdd:PRK08276 294 --------YASSEGG-GVTVITS----------EDWLAHPGSV-----------GKAVLG--------EVRILDEDGN-E 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 404 LTDGEVGEIWVGGPGLPDGYWRQPEQTATtfgARTADGLgpyLRTGDAGfrY---QGELYVCGRYRDLIIVGGRNHFPND 480
Cdd:PRK08276 335 LPPGEIGTVYFEMDGYPFEYHNDPEKTAA---ARNPHGW---VTVGDVG--YldeDGYLYLTDRKSDMIISGGVNIYPQE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 481 IEkTVEEAHCGVAPggaCAV--QPDApqangEWW----LVLETGSPVEDLDDLSRILR---RRILAHHEtAPERVVWVPc 551
Cdd:PRK08276 407 IE-NLLVTHPKVAD---VAVfgVPDE-----EMGervkAVVQPADGADAGDALAAELIawlRGRLAHYK-CPRSIDFED- 475
|
490
....*....|....*
gi 2181016861 552 rTLPTTTSGKIRRRE 566
Cdd:PRK08276 476 -ELPRTPTGKLYKRR 489
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2966-3039 |
2.32e-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: 50.62 E-value: 2.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 2966 ASNDELLQRVSRICASALGQP--RVEPHDNFFQ-LGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIAD 3039
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1139-1612 |
2.35e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 56.56 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1139 RGERHGDVIAQDR----SQLTYGEL-DELARSVARAVAARHAAGSVIGIQLPKGPSQIVAVLGVMMAGCTYLPVGVDQPA 1213
Cdd:PRK05857 23 QARQQPEAIALRRcdgtSALRYRELvAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1214 ERLSRICARSAMAGLI-----RTDSDTQDAGVAV---------SDITAMIECAPTDPIRIDPH----DAAYVIYTSGSTG 1275
Cdd:PRK05857 103 AAIERFCQITDPAAALvapgsKMASSAVPEALHSipviavdiaAVTRESEHSLDAASLAGNADqgseDPLAMIFTSGTTG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1276 EPKGVLVSHAA--ALNTIVDVNRRNRIDTHDRLLALSALDfDLSVYDTFGALGC---GAQLVTIPEHArrdafhwLSLTT 1350
Cdd:PRK05857 183 EPKAVLLANRTffAVPDILQKEGLNWVTWVVGETTYSPLP-ATHIGGLWWILTClmhGGLCVTGGENT-------TSLLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1351 EFGITVWNS---VPGLMDMLLIAAGDKAGSLPTLRSVFLSGD-WIPLDLprRLRRAApGVRLVAMGGATEAAIWSNEFVV 1426
Cdd:PRK05857 255 ILTTNAVATtclVPTLLSKLVSELKSANATVPSLRLVGYGGSrAIAADV--RFIEAT-GVRTAQVYGLSETGCTALCLPT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1427 DDvdPDWASIPYG-----YPLANQMFRVVDDNGDDQPDYVA----GELWIGGAGVALGYHNAPELTSDRFVHDptgsrWY 1497
Cdd:PRK05857 332 DD--GSIVKIEAGavgrpYPGVDVYLAATDGIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLIDG-----WV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1498 RTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNcTALGAGIVVTGSGAEQFDDSTPG 1577
Cdd:PRK05857 405 NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD-EEFGALVGLAVVASAELDESAAR 483
|
490 500 510
....*....|....*....|....*....|....*....
gi 2181016861 1578 ALRAHLAVRLPQ----YMIPKVFVSCPELPLTANGKVDR 1612
Cdd:PRK05857 484 ALKHTIAARFRResepMARPSTIVIVTDIPRTQSGKVMR 522
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
173-564 |
2.82e-07 |
|
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: 55.10 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 173 HVAFlqySSGSTGKPKGVVNTHQSILrqAAFAANVwngdDDMHM------VSWLPLYHDMGIFwGVFMPLLNGGctTLIP 246
Cdd:cd17633 4 YIGF---TSGTTGLPKAYYRSERSWI--ESFVCNE----DLFNIsgedaiLAPGPLSHSLFLY-GAISALYLGG--TFIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 247 PHDFvrNPRIWLETVSRFRG-NWIGGPdfayrrcieafdgTALQSLDL-----SCLRLATNGAEPVRGTTLRDFTAKFRA 320
Cdd:cd17633 72 QRKF--NPKSWIRKINQYNAtVIYLVP-------------TMLQALARtlepeSKIKSIFSSGQKLFESTKKKLKNIFPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 321 AGLRDdvmapQYGLAEAGlgvtgsqtvrvWVEKSFDADALERGiavEVAQPNPadgrsralvscgdgafGWDIQIVDPDr 400
Cdd:cd17633 137 ANLIE-----FYGTSELS-----------FITYNFNQESRPPN---SVGRPFP----------------NVEIEIRNAD- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 401 hmtltDGEVGEIWVGGPGLPDGYWRQPEQTATtfgartadglGPYlRTGDAGF-RYQGELYVCGRYRDLIIVGGRNHFPN 479
Cdd:cd17633 181 -----GGEIGKIFVKSEMVFSGYVRGGFSNPD----------GWM-SVGDIGYvDEEGYLYLVGRESDMIIIGGINIFPT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 480 DIEKTVeEAHCGVAPGGACAVqPDApqANGEWWLVLETGSPVEDlDDLSRILRRRiLAHHETaPERVVWVpcRTLPTTTS 559
Cdd:cd17633 245 EIESVL-KAIPGIEEAIVVGI-PDA--RFGEIAVALYSGDKLTY-KQLKRFLKQK-LSRYEI-PKKIIFV--DSLPYTSS 315
|
....*
gi 2181016861 560 GKIRR 564
Cdd:cd17633 316 GKIAR 320
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
10-245 |
2.82e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.21 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 10 ALHDGDRSVPAVFAEWVGRRPDAVAL--RTVAATGIDDWTYQRLWDHVREI-RDVAFSGLSAGIRIpMALPGGADYVAGM 86
Cdd:PRK12582 43 PLGPYPRSIPHLLAKWAAEAPDRPWLaqREPGHGQWRKVTYGEAKRAVDALaQALLDLGLDPGRPV-MILSGNSIEHALM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 87 LAALAAGLIPV-PVYLPSTREPQRFlARAQHILRDCEPSAVYT-CGELVEVLERDPILGALPIRTPASTADG-------- 156
Cdd:PRK12582 122 TLAAMQAGVPAaPVSPAYSLMSHDH-AKLKHLFDLVKPRVVFAqSGAPFARALAALDLLDVTVVHVTGPGEGiasiafad 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 157 LAPHPGGTTADADHG----EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDM---HMVSWLPLYHDMGif 229
Cdd:PRK12582 201 LAATPPTAAVAAAIAaitpDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNHTMG-- 278
|
250
....*....|....*...
gi 2181016861 230 wG--VFMPLLNGGCTTLI 245
Cdd:PRK12582 279 -GnaNFNGLLWGGGTLYI 295
|
|
| ArgR-Cyc_NRPS-like |
cd20480 |
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ... |
2660-2926 |
2.97e-07 |
|
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to Cyc-domains there are various other subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380470 [Multi-domain] Cd Length: 406 Bit Score: 55.59 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2660 LDGASMMIALSELDHLYRGEtvdqlpPLETSFAHYVWN-HPELLPDAdeavLPRLAASRDYWRARLPSLPPAPKLADMSL 2738
Cdd:cd20480 133 VDHPSVNLFFEQLCQLLRGS------LLSFLAQEQVILaHNQLVISE----LQSTGLSSAFWNEQILQLPSSANLPTVCE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2739 LFEIEEPRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRWSGTDHFCINvtlFDRDP--DVVGIenvVGD 2816
Cdd:cd20480 203 PEKLRETGITRRTLTLSSDKWQQLVTISKQHNVTPELTLASIFSAVLSLWGNQKDMMLR---FDLNKknDVAGV---IGQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2817 FTSLVLLECRVDEpASIWESVRALQRQLMTDLPHRGADAVWLQRELLRF---HGNPTAalfpVVFTSGLGLVDASARaav 2893
Cdd:cd20480 277 FTQPLLVGLSGFG-QSFLSLVKENQKHFEQAYPFRQIPIFDLVRQLAKLsesHRYPAN----IAFSSQLSGNNTLGR--- 348
|
250 260 270
....*....|....*....|....*....|...
gi 2181016861 2894 rfaePVFAASQTPQTVLDFQVWESAGALKLSWD 2926
Cdd:cd20480 349 ----SGWGCRQSANTWLSLHAFISQGGLILQWD 377
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1237-1612 |
3.77e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 55.93 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1237 DAGVAVSDITAMIECAPTDPIRIDPHDAAYVIY-TSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDT-HDRLLALSALDF 1314
Cdd:PRK05851 126 DSSVTVHDLATAAHTNRSASLTPPDSGGPAVLQgTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAaTDVGCSWLPLYH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1315 DLSVydTF---GALGcGAQLVTIPEHARRDA-FHWLSLTTEFGITVwNSVPGLMDMLLIAAGDKAGS--LPTLRSVFLSG 1388
Cdd:PRK05851 206 DMGL--AFlltAALA-GAPLWLAPTTAFSASpFRWLSWLSDSRATL-TAAPNFAYNLIGKYARRVSDvdLGALRVALNGG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1389 DWIPLDLPRRLRRAA------PGVRLVAMGGA-TEAAIWSNE----FVVDDV-DPDWASIP----YGYPLANQMFRVVDD 1452
Cdd:PRK05851 282 EPVDCDGFERFATAMapfgfdAGAAAPSYGLAeSTCAVTVPVpgigLRVDEVtTDDGSGARrhavLGNPIPGMEVRISPG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1453 NGD-DQPDYVAGELWIGGAGVALGYHNAPELTSDRfvhdptgsrWYRTGDMGcYWRDGTLQFLGRADSQVKIRGHRVECG 1531
Cdd:PRK05851 362 DGAaGVAGREIGEIEIRGASMMSGYLGQAPIDPDD---------WFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPT 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1532 EIEHALRGHPLVAAATVVpihnctALGAGIVVTGSG---AEQFDDSTPGALRAHLAVRLPQY--MIPK--VFVSCPELPL 1604
Cdd:PRK05851 432 EIERVAAQVRGVREGAVV------AVGTGEGSARPGlviAAEFRGPDEAGARSEVVQRVASEcgVVPSdvVFVAPGSLPR 505
|
....*...
gi 2181016861 1605 TANGKVDR 1612
Cdd:PRK05851 506 TSSGKLRR 513
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
179-493 |
4.57e-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: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 179 YSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHdMGIFWGVFMPLLNGGCTTLIPPHDfvrnPRIWL 258
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNVFVRRVD----AEEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 259 ETVSRFR--GNWIGGPDFAYrrcIEAFDGTALqsLDLSCLRlATNGAEPVRGTTLRDFTAKFRAAGlrddvmapQYGLAE 336
Cdd:cd17636 82 ELIEAERctHAFLLPPTIDQ---IVELNADGL--YDLSSLR-SSPAAPEWNDMATVDTSPWGRKPG--------GYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 337 aglgVTGSqtvrvWVEKSFDADALerGIAvevaqpnpadGRSRALVScgdgafgwdIQIVDPDRHmTLTDGEVGEIWVGG 416
Cdd:cd17636 148 ----VMGL-----ATFAALGGGAI--GGA----------GRPSPLVQ---------VRILDEDGR-EVPDGEVGEIVARG 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181016861 417 PGLPDGYWRQPEQTAttfgARTADGlgpYLRTGDAGFRYQ-GELYVCGRYRDLIIVGGRNHFPNDIEKTVEEaHCGVA 493
Cdd:cd17636 197 PTVMAGYWNRPEVNA----RRTRGG---WHHTNDLGRREPdGSLSFVGPKTRMIKSGAENIYPAEVERCLRQ-HPAVA 266
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
10-241 |
5.10e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 55.27 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 10 ALHDGDRSVPAVFAEWVGRRPDAVALrtVAATGIDDW---TYQRLWDHVREI------RdvafsGLSAGiRIPMALPG-- 78
Cdd:PRK08180 33 PLGDYPRRLTDRLVHWAQEAPDRVFL--AERGADGGWrrlTYAEALERVRAIaqalldR-----GLSAE-RPLMILSGns 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 79 --------GADYVAgmlaalaaglIPV----PVY-LPSTRepqrfLARAQHILRDCEPSAVYT------CGELVEVLERD 139
Cdd:PRK08180 105 iehallalAAMYAG----------VPYapvsPAYsLVSQD-----FGKLRHVLELLTPGLVFAddgaafARALAAVVPAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 140 PIL----GALPIRTPASTADGLAPhPGGTTADADH----GEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-- 209
Cdd:PRK08180 170 VEVvavrGAVPGRAATPFAALLAT-PPTAAVDAAHaavgPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfl 248
|
250 260 270
....*....|....*....|....*....|..
gi 2181016861 210 GDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGC 241
Cdd:PRK08180 249 AEEPPVLVDWLPWNHTFGGNHNLGIVLYNGGT 280
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1258-1549 |
5.81e-07 |
|
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: 55.12 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1258 RIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRLLALSALDFDLS-VYDTFGALGCGaQLVTIPE 1336
Cdd:cd17641 154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEqMYSVGQALVCG-FIVNFPE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1337 HA-------RRDAFH--------WLSLTTEFGITVWNSVP-------GLMDMLLIAA-----GDKAGSLPTLRSVFlsGD 1389
Cdd:cd17641 233 EPetmmedlREIGPTfvllpprvWEGIAADVRARMMDATPfkrfmfeLGMKLGLRALdrgkrGRPVSLWLRLASWL--AD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1390 WIPLDLPR------RLRRA----------------APGVRLVAMGGATEAAIWSNEFVVDDVDPDwasiPYGYPLANQMF 1447
Cdd:cd17641 311 ALLFRPLRdrlgfsRLRSAatggaalgpdtfrffhAIGVPLKQLYGQTELAGAYTVHRDGDVDPD----TVGVPFPGTEV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1448 RVVDdngddqpdyvAGELWIGGAGVALGYHNAPELTSDRFVHDptgsRWYRTGDMGCYWRDGTLQFLGRA-DSQVKIRGH 1526
Cdd:cd17641 387 RIDE----------VGEILVRSPGVFVGYYKNPEATAEDFDED----GWLHTGDAGYFKENGHLVVIDRAkDVGTTSDGT 452
|
330 340
....*....|....*....|...
gi 2181016861 1527 RVECGEIEHALRGHPLVAAATVV 1549
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVL 475
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2407-2525 |
5.95e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 55.44 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2407 DKPGMPTPPAEQRRDGRWSRPavpasslPTDATVVATLAEIWQRhlaiPTPGVDDDFFLLGGDSLVATRVYADLRAAGFG 2486
Cdd:PRK10252 957 DRKALPLPELKAQVPGRAPKT-------GTETIIAAAFSSLLGC----DVVDADADFFALGGHSLLAMKLAAQLSRQFAR 1025
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2181016861 2487 QLAFVDLFNHSTLGELAA------HAGPRTGPEVSVAAESTRGGT 2525
Cdd:PRK10252 1026 QVTPGQVMVASTVAKLATlldaeeDESRRLGFGTILPLREGDGPT 1070
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
171-565 |
6.53e-07 |
|
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: 54.75 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 171 GEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIfWGVFMPLLNGGCTTLIP---- 246
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAA-EEIYVTLLSGATLVLRPeemr 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 247 --PHDFVRNPRIWLETVSRFRGnwiggpdfAYRRciEAFDGTALQSLDL-SCLRLATNGAEPVRGTTLRDFtakfrAAGL 323
Cdd:cd17644 184 ssLEDFVQYIQQWQLTVLSLPP--------AYWH--LLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQW-----QKNV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 324 RDDV-MAPQYGLAEAGLGVTGSQTVRVWVEKSfdadalergiavevaqPNPADGRSRAlvscgdgafgwDIQIVDPDRHM 402
Cdd:cd17644 249 GNFIqLINVYGPTEATIAATVCRLTQLTERNI----------------TSVPIGRPIA-----------NTQVYILDENL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 403 TLTDGEV-GEIWVGGPGLPDGYWRQPEQTATTFGARTADGlGPYLR---TGDAGfRY--QGELYVCGRYRDLIIVGGRNH 476
Cdd:cd17644 302 QPVPVGVpGELHIGGVGLARGYLNRPELTAEKFISHPFNS-SESERlykTGDLA-RYlpDGNIEYLGRIDNQVKIRGFRI 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 477 FPNDIEKTVEEaHCGVAPggACA-VQPDAPqanGEWWLVL-------ETGSPVEdlddLSRILRRRIlahhetaPERVV- 547
Cdd:cd17644 380 ELGEIEAVLSQ-HNDVKT--AVViVREDQP---GNKRLVAyivphyeESPSTVE----LRQFLKAKL-------PDYMIp 442
|
410 420
....*....|....*....|
gi 2181016861 548 --WVPCRTLPTTTSGKIRRR 565
Cdd:cd17644 443 saFVVLEELPLTPNGKIDRR 462
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1185-1516 |
7.45e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 54.95 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1185 PKGPSQIVAVLGVMMAGCTYLPVGVDQPAERLSRICA------------RSAMAGLIRTDSDTQDAGVAvsdiTAMIEC- 1251
Cdd:PRK05850 67 PQGLEYIVAFLGALQAGLIAVPLSVPQGGAHDERVSAvlrdtspsvvltTSAVVDDVTEYVAPQPGQSA----PPVIEVd 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1252 -------APTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHaaalntivdvnrRNridthdrLLAlsalDFDLSVYDTFGA 1324
Cdd:PRK05850 143 lldldspRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSH------------RN-------VIA----NFEQLMSDYFGD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1325 LGCGAQLVTIpeharrdAFHWLSLTTEFG------ITVWNSVPG-LMD-----------MLLIAAGDKAGS--------L 1378
Cdd:PRK05850 200 TGGVPPPDTT-------VVSWLPFYHDMGlvlgvcAPILGGCPAvLTSpvaflqrparwMQLLASNPHAFSaapnfafeL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1379 PTLRSVflSGDWIPLDL--------------PRRLRR-----AAPGVRLVAMG---GATEA------AIWSNEFVVDDVD 1430
Cdd:PRK05850 273 AVRKTS--DDDMAGLDLggvlgiisgservhPATLKRfadrfAPFNLRETAIRpsyGLAEAtvyvatREPGQPPESVRFD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1431 PDWAS---------------IPYGYPlANQMFRVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRF---VHDP 1491
Cdd:PRK05850 351 YEKLSaghakrcetgggtplVSYGSP-RSPTVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDP 429
|
410 420
....*....|....*....|....*....
gi 2181016861 1492 T----GSRWYRTGDMGCYWrDGTLQFLGR 1516
Cdd:PRK05850 430 SpgtpEGPWLRTGDLGFIS-EGELFIVGR 457
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1191-1615 |
7.72e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 54.70 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1191 IVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLI-RTDSDTQDAGVAVSDITAMieCAPTDP-----IRIDPHDA 1264
Cdd:PRK12406 50 FEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIaHADLLHGLASALPAGVTVL--SVPTPPeiaaaYRISPALL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1265 ---------------------------AYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDR-LLALSALDFDL 1316
Cdd:PRK12406 128 tppagaidwegwlaqqepydgppvpqpQSMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRALIYGLKPgIRALLTGPLYH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1317 SVYDTFG--ALGCGAQLVTIPehaRRDAFHWLSLTTEFGITVWNSVPGLMDML--LIAAGDKAGSLPTLRSVFLSGDWIP 1392
Cdd:PRK12406 208 SAPNAYGlrAGRLGGVLVLQP---RFDPEELLQLIERHRITHMHMVPTMFIRLlkLPEEVRAKYDVSSLRHVIHAAAPCP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1393 LDLPRRLRrAAPGVRLVAMGGATEAAIwsnefVVDDVDPDWASIP--YGYPLANQMFRVVDDNGDDQPDYVAGELWIGGA 1470
Cdd:PRK12406 285 ADVKRAMI-EWWGPVIYEYYGSTESGA-----VTFATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1471 GVAL-GYHNAPEltsDRFVHDPTGsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVaaatvv 1549
Cdd:PRK12406 359 GNPDfTYHNKPE---KRAEIDRGG--FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGV------ 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 1550 piHNCTALG----------AGIVVTGSGAEQfddsTPGALRAHLAVRLPQYMIPKVFVSCPELPltangKVDRGKI 1615
Cdd:PRK12406 428 --HDCAVFGipdaefgealMAVVEPQPGATL----DEADIRAQLKARLAGYKVPKHIEIMAELP-----REDSGKI 492
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
383-562 |
9.28e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 383 SCGDGAFGwDIQIVDPDRHmTLTDGEVGEIWVGGPGLPDGYWRQPEQTATTfgartADGLGPYLRT-GDAGF-RYQGELY 460
Cdd:PRK13390 324 SVGRSVLG-DLHICDDDGN-ELPAGRIGTVYFERDRLPFRYLNDPEKTAAA-----QHPAHPFWTTvGDLGSvDEDGYLY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 461 VCGRYRDLIIVGGRNHFPNDIEK--TVEEAHCGVAPGGAcavqPDaPQANGEWWLVLETGSPVEDLDDLSRIL----RRR 534
Cdd:PRK13390 397 LADRKSFMIISGGVNIYPQETENalTMHPAVHDVAVIGV----PD-PEMGEQVKAVIQLVEGIRGSDELARELidytRSR 471
|
170 180
....*....|....*....|....*...
gi 2181016861 535 IlAHHEtAPERVVWVPcrTLPTTTSGKI 562
Cdd:PRK13390 472 I-AHYK-APRSVEFVD--ELPRTPTGKL 495
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1493-1605 |
9.40e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.50 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1493 GSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV----VPIHNCTALGAGIVVTgsGA 1568
Cdd:PRK08279 437 GDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygveVPGTDGRAGMAAIVLA--DG 514
|
90 100 110
....*....|....*....|....*....|....*...
gi 2181016861 1569 EQFDdstPGALRAHLAVRLPQYMIPkVFVS-CPELPLT 1605
Cdd:PRK08279 515 AEFD---LAALAAHLYERLPAYAVP-LFVRlVPELETT 548
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1260-1611 |
1.15e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 54.59 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1260 DPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNrrNRIDTHDRLLALSALdfdlSVYDTFGaLGCGAQLVTI----- 1334
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVA--ARIDFSPEDKVFNAL----PVFHSFG-LTGGLVLPLLsgvkv 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1335 -----PEHARrdafhwlslttefgitvwnSVPGLM-----------DMLLIAAGDKAGS--LPTLRSVFLSGDwiPL-DL 1395
Cdd:PRK06814 864 flypsPLHYR-------------------IIPELIydtnatilfgtDTFLNGYARYAHPydFRSLRYVFAGAE--KVkEE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1396 PRRLRRAAPGVRLVAMGGATEAAiwsnefvvddvdpdwASIPYGYPLANQM-----------FRVVDDNGDDQpdyvAGE 1464
Cdd:PRK06814 923 TRQTWMEKFGIRILEGYGVTETA---------------PVIALNTPMHNKAgtvgrllpgieYRLEPVPGIDE----GGR 983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1465 LWIGGAGVALGYHNApeltSDRFVHDPTGSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHAlrghplva 1544
Cdd:PRK06814 984 LFVRGPNVMLGYLRA----ENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEEL-------- 1051
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 1545 AATVVP--IHNCTAL-----GAGIVV--TGSGAEQfddstpGALRAHL-AVRLPQYMIPKVFVSCPELPLTANGKVD 1611
Cdd:PRK06814 1052 AAELWPdaLHAAVSIpdarkGERIILltTASDATR------AAFLAHAkAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1266-1612 |
1.65e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 53.80 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1266 YVIYTSGSTGEPKGVL-------VSHAAALNTIVDVNRRnriDTHdrllaLSALDFDLSV---YDTFGALGCGaqLVTI- 1334
Cdd:PRK10524 237 YILYTSGTTGKPKGVQrdtggyaVALATSMDTIFGGKAG---ETF-----FCASDIGWVVghsYIVYAPLLAG--MATIm 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1335 ----PehARRDAFHWLSLTTEFGITVWNSVPGLMDML------LIAAGDkagsLPTLRSVFLSGDwiPLDLPR-RLRRAA 1403
Cdd:PRK10524 307 yeglP--TRPDAGIWWRIVEKYKVNRMFSAPTAIRVLkkqdpaLLRKHD----LSSLRALFLAGE--PLDEPTaSWISEA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1404 PGVRLVAMGGATEAA--IWSNEFVVDDVDPDWAS--IP-YGYPLanqmfRVVDDNgdDQPDYVAGELWIggagVALGYHN 1478
Cdd:PRK10524 379 LGVPVIDNYWQTETGwpILAIARGVEDRPTRLGSpgVPmYGYNV-----KLLNEV--TGEPCGPNEKGV----LVIEGPL 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1479 APELTS------DRFVHdptgSRW-------YRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAA 1545
Cdd:PRK10524 448 PPGCMQtvwgddDRFVK----TYWslfgrqvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 1546 ATVVPIHNC----TALGAGIVVTGSGAEQFDDSTP--GALRAHLAVRLPQYMIPK--VFVScpELPLTANGKVDR 1612
Cdd:PRK10524 524 VAVVGVKDAlkgqVAVAFVVPKDSDSLADREARLAleKEIMALVDSQLGAVARPArvWFVS--ALPKTRSGKLLR 596
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2973-3044 |
1.93e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 53.89 E-value: 1.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 2973 QRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIADTDNAD 3044
Cdd:PRK10252 981 TIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDES 1052
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
2423-2513 |
2.06e-06 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 52.44 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2423 RWSRPAVPASSLPTDATVVATLAEIWQRHLAIP--TPGVDDDFFLLGGDSLVATRVYADLRAAGFgQLAFVDLFNHSTLG 2500
Cdd:COG3433 203 EALLAAASPAPALETALTEEELRADVAELLGVDpeEIDPDDNLFDLGLDSIRLMQLVERWRKAGL-DVSFADLAEHPTLA 281
|
90
....*....|...
gi 2181016861 2501 ELAAHAGPRTGPE 2513
Cdd:COG3433 282 AWWALLAAAQAAA 294
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1153-1583 |
2.69e-06 |
|
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: 52.86 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1153 QLTYGEL-DELARSVARAVAARHAAGSVIGIqLPKGPSQ-IVAVLGVMMAGCTYLPVGVDQPAERLSRICARSAMAGLI- 1229
Cdd:cd05932 6 EFTWGEVaDKARRLAAALRALGLEPGSKIAL-ISKNCAEwFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1230 --RTDSDTQDAGVAVSDIT----------------AMIECAP--TDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALN 1289
Cdd:cd05932 85 gkLDDWKAMAPGVPEGLISislpppsaancqyqwdDLIAQHPplEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1290 TIVDVNRRNRIDTHDRLLA-LSALDFDLSVYDTFGALGCGAQLV------TIPEHARRDA----FHWLSLTTEFGITVWN 1358
Cdd:cd05932 165 AAQAGIEHIGTEENDRMLSyLPLAHVTERVFVEGGSLYGGVLVAfaesldTFVEDVQRARptlfFSVPRLWTKFQQGVQD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1359 SVP-GLMDMLLiaagdkagSLPTLRSvflsgdwipldLPRRLRRAAPG---VRLVAMGGA--TEAAI-WSNEFVVDDVDP 1431
Cdd:cd05932 245 KIPqQKLNLLL--------KIPVVNS-----------LVKRKVLKGLGldqCRLAGCGSApvPPALLeWYRSLGLNILEA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1432 DWASIPYGYPLANQMFR----VVDDNGDDQPDYVA--GELWIGGAGVALGYHNAPELTSDRFVHDPtgsrWYRTGDMGCY 1505
Cdd:cd05932 306 YGMTENFAYSHLNYPGRdkigTVGNAGPGVEVRISedGEILVRSPALMMGYYKDPEATAEAFTADG----FLRTGDKGEL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1506 WRDGTLQFLGRADSQVKI-RGHRVECGEIEHALRGHPLVAAATVVPihncTALGA--GIVVTGSGAE-QFDDSTPGALRA 1581
Cdd:cd05932 382 DADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG----SGLPAplALVVLSEEARlRADAFARAELEA 457
|
..
gi 2181016861 1582 HL 1583
Cdd:cd05932 458 SL 459
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
113-565 |
2.79e-06 |
|
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: 52.86 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 113 RAQHILRDCEPSAVYTCGELVEVLERDPILgALPIRTPASTADGlaphpgGTTADADHGEHVAFLQYSSGSTGKPKGVVN 192
Cdd:cd17656 76 RRIYIMLDSGVRVVLTQRHLKSKLSFNKST-ILLEDPSISQEDT------SNIDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 193 THQSILRQAAFA---ANVWNGDDDMHMV--SWLPLYHDmgifwgVFMPLLNGGcTTLIPPHDFVRNPRIWLETVSRFRGN 267
Cdd:cd17656 149 EHKNMVNLLHFErekTNINFSDKVLQFAtcSFDVCYQE------IFSTLLSGG-TLYIIREETKRDVEQLFDLVKRHNIE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 268 WIGGPD------FAYRRCIEAFdgtalqsldLSCLR-LATNGAEPVRGTTLRDFTAKfraaglRDDVMAPQYGLAEAGLg 340
Cdd:cd17656 222 VVFLPVaflkfiFSEREFINRF---------PTCVKhIITAGEQLVITNEFKEMLHE------HNVHLHNHYGPSETHV- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 341 VTgsqTVRVwveksfdadalergiavevaqpNPADgRSRALVSCGDGAFGWDIQIVDPDRHMTlTDGEVGEIWVGGPGLP 420
Cdd:cd17656 286 VT---TYTI----------------------NPEA-EIPELPPIGKPISNTWIYILDQEQQLQ-PQGIVGELYISGASVA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 421 DGYWRQPEQTATTFGARTADGLGPYLRTGDAGfRY--QGELYVCGRYRDLIIVGGRNHFPNDIEKTVEEahcgvAPGGAC 498
Cdd:cd17656 339 RGYLNRQELTAEKFFPDPFDPNERMYRTGDLA-RYlpDGNIEFLGRADHQVKIRGYRIELGEIEAQLLN-----HPGVSE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 499 AVQPDAPQANGEWWL----VLETGSPVEDLddlsrilrRRILAhhETAPERVV---WVPCRTLPTTTSGKIRRR 565
Cdd:cd17656 413 AVVLDKADDKGEKYLcayfVMEQELNISQL--------REYLA--KQLPEYMIpsfFVPLDQLPLTPNGKVDRK 476
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
172-246 |
3.65e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.79 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQ-------AAFAANvwngddDMHMvSWLPLYHDMGIFWGVFMPLLNGGCTTL 244
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANveqiktiADFTPN------DRFM-SALPLFHSFGLTVGLFTPLLTGAEVFL 437
|
..
gi 2181016861 245 IP 246
Cdd:PRK08043 438 YP 439
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1211-1526 |
3.76e-06 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.82 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1211 QPAERLSRICARSAMAGLIRTDS-DTQDAGVAVSDITAMIEcAPTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAA-- 1287
Cdd:PRK12476 142 EPTVVLTTTAAAEAVEGFLRNLPrLRRPRVIAIDAIPDSAG-ESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgt 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1288 --LNTIVDVNRRNRiDTHdrllALSAL----DFDLSVYdTFGALGCGAQLVTIPEHARRDAFHW---LSLTTEFGITVwN 1358
Cdd:PRK12476 221 nlVQMILSIDLLDR-NTH----GVSWLplyhDMGLSMI-GFPAVYGGHSTLMSPTAFVRRPQRWikaLSEGSRTGRVV-T 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1359 SVPGLMDMLLIAAG-DKAGSLPTLRSVFL-------SGDWI--------PLDLPRRLRRAAPGVRLVAMGGATEAAIWSN 1422
Cdd:PRK12476 294 AAPNFAYEWAAQRGlPAEGDDIDLSNVVLiigsepvSIDAVttfnkafaPYGLPRTAFKPSYGIAEATLFVATIAPDAEP 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1423 EFVVDD-----------VDPDW----ASIPYGYPLANQMFRVVDDN-GDDQPDYVAGELWIGGAGVALGYHNAPELTSDR 1486
Cdd:PRK12476 374 SVVYLDreqlgagravrVAADApnavAHVSCGQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERT 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 1487 F-----------VH---DPTGSRWYRTGDMGCYwRDGTLQFLGRADSQVKIRGH 1526
Cdd:PRK12476 454 FgaklqsrlaegSHadgAADDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGR 506
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2966-3048 |
3.77e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.25 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIADTDNADE 3045
Cdd:PRK05691 1634 EPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGE 1713
|
...
gi 2181016861 3046 PDL 3048
Cdd:PRK05691 1714 RNS 1716
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
14-502 |
4.55e-06 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 52.45 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 14 GDRSVPAVFAEWVGRRPDAVALRTvaatGIDDWTYQRLWDHV-REIRDVAFSGLSAGIRIPMALPGGADYVAGMLAALAA 92
Cdd:PRK06155 19 SERTLPAMLARQAERYPDRPLLVF----GGTRWTYAEAARAAaAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 93 GLIPVPVYLPStREPQrflarAQHILRDCEPSAVYTCGELVEVLER-DP---------ILGALPIRTPASTADGLAPHPG 162
Cdd:PRK06155 95 GAIAVPINTAL-RGPQ-----LEHILRNSGARLLVVEAALLAALEAaDPgdlplpavwLLDAPASVSVPAGWSTAPLPPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 163 GTTADADH---GEHVAFLqYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDMhMVSWLPLYHDMGIfwGVFMPLLN 238
Cdd:PRK06155 169 DAPAPAAAvqpGDTAAIL-YTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEiGADDV-LYTTLPLFHTNAL--NAFFQALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 239 GGCTtlipphdFVRNPRIwleTVSRFrgnWiggPDFAYRRCIEAFDGTALQSLDLS----------CLRLATNGAEPVRg 308
Cdd:PRK06155 245 AGAT-------YVLEPRF---SASGF---W---PAVRRHGATVTYLLGAMVSILLSqparesdrahRVRVALGPGVPAA- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 309 tTLRDFTAKFrAAGLRDdvmapqyglaeaGLGVTGSQTVrvwveksfdadalergIAVEVAQPNPAdgrsralvSCGDGA 388
Cdd:PRK06155 308 -LHAAFRERF-GVDLLD------------GYGSTETNFV----------------IAVTHGSQRPG--------SMGRLA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 389 FGWDIQIVDPDrHMTLTDGEVGEIWVGG--PG-LPDGYWRQPEQTATTFGartadglGPYLRTGDAGFR-YQGELYVCGR 464
Cdd:PRK06155 350 PGFEARVVDEH-DQELPDGEPGELLLRAdePFaFATGYFGMPEKTVEAWR-------NLWFHTGDRVVRdADGWFRFVDR 421
|
490 500 510
....*....|....*....|....*....|....*...
gi 2181016861 465 YRDLIIVGGRNHFPNDIEKTVeEAHCGVApggACAVQP 502
Cdd:PRK06155 422 IKDAIRRRGENISSFEVEQVL-LSHPAVA---AAAVFP 455
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
682-834 |
4.88e-06 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 52.10 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 682 GPWPTTPLQQAYWVgRGAEQPlGGVGCQTYFEL-VGARVDAGRLAAALDALTRRHPMLRATFPDPGRCL----ITPEAVR 756
Cdd:cd19546 3 DEVPATAGQLRTWL-LARLDE-ETRGRHLSVALrLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVhqriLDADAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 757 LPLAVhdltdAPVTTRDthLAEIRRRLRTHRFDIETGDTWTVELTRLP---HgcIVHFAVDLIIADVTSIGTMLRDLAAS 833
Cdd:cd19546 81 PELPV-----VPATEEE--LPALLADRAAHLFDLTRETPWRCTLFALSdteH--VLLLVVHRIAADDESLDVLVRDLAAA 151
|
.
gi 2181016861 834 Y 834
Cdd:cd19546 152 Y 152
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2966-3034 |
5.96e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 5.96e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIgRELSASATLRLLFANPVIGDFA 3034
Cdd:PRK12316 3552 APVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLA 3619
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1493-1609 |
6.23e-06 |
|
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: 51.59 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1493 GSRWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATV----VPIHNCTALGAGIVVTGSga 1568
Cdd:cd05940 321 GDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDGRAGMAAIVLQPN-- 398
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2181016861 1569 EQFDDStpgALRAHLAVRLPQYMIPkVFVS-CPELPLTANGK 1609
Cdd:cd05940 399 EEFDLS---ALAAHLEKNLPGYARP-LFLRlQPEMEITGTFK 436
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1213-1612 |
6.64e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 51.71 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1213 AERLSRICAR--SAMAGLIRTDSDTQDA------GVAVSDITAMIECAPTD---PIrIDPHDAAYVIYTSGSTGEPKGVL 1281
Cdd:PRK05620 122 AEQLGEILKEcpCVRAVVFIGPSDADSAaahmpeGIKVYSYEALLDGRSTVydwPE-LDETTAAAICYSTGTTGAPKGVV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1282 VSHaaalntivdvnrrnridthdRLLALSALDfdLSVYDTFGALGCGAQLVTIPeharrdAFHWLSLTTEF--------- 1352
Cdd:PRK05620 201 YSH--------------------RSLYLQSLS--LRTTDSLAVTHGESFLCCVP------IYHVLSWGVPLaafmsgtpl 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1353 ---GITVwnSVPGLMDMLLIAAGDKAGSLPTLrsvflsgdWIPL------DLPRRLrraapGVRLVAMGGATEAAI---- 1419
Cdd:PRK05620 253 vfpGPDL--SAPTLAKIIATAMPRVAHGVPTL--------WIQLmvhylkNPPERM-----SLQEIYVGGSAVPPIlika 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1420 WSNEFVVDDVDPdW-----------ASIPYG---------------YPLANQmFRVVDD-NGDDQPDYVAGELWIGGAGV 1472
Cdd:PRK05620 318 WEERYGVDVVHV-WgmtetspvgtvARPPSGvsgearwayrvsqgrFPASLE-YRIVNDgQVMESTDRNEGEIQVRGNWV 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1473 ALGYHNAP----------------ELTSDRFVHDPtgsrWYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHA 1536
Cdd:PRK05620 396 TASYYHSPteegggaastfrgedvEDANDRFTADG----WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENY 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1537 LRGHPLVAAATVVPIHN---------CTALGAGIVVTGSGAEQfddstpgaLRAHLAVRLPQYMIPKVFVSCPELPLTAN 1607
Cdd:PRK05620 472 IMAAPEVVECAVIGYPDdkwgerplaVTVLAPGIEPTRETAER--------LRDQLRDRLPNWMLPEYWTFVDEIDKTSV 543
|
....*
gi 2181016861 1608 GKVDR 1612
Cdd:PRK05620 544 GKFDK 548
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
172-565 |
6.68e-06 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 51.79 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAfaanvwngdddMHMvSWLPLYHDMGIFW-------------GVFMPLLN 238
Cdd:cd05966 231 EDPLFILYTSGSTGKPKGVVHTTGGYLLYAA-----------TTF-KYVFDYHPDDIYWctadigwitghsyIVYGPLAN 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 239 gGCTTLI----PPHDfvrNPRIWLETVSRFRGN-WIGGPdfayrrcieafdgTALQSL-----------DLSCLRLATNG 302
Cdd:cd05966 299 -GATTVMfegtPTYP---DPGRYWDIVEKHKVTiFYTAP-------------TAIRALmkfgdewvkkhDLSSLRVLGSV 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 303 AEPVRGTTLRDFtakfraaglRDDVmapqyGLAEAGLGVTGSQTvrvwveksfdadalERG---IAvevaqPNPADGRSR 379
Cdd:cd05966 362 GEPINPEAWMWY---------YEVI-----GKERCPIVDTWWQT--------------ETGgimIT-----PLPGATPLK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 380 AlVSCGDGAFGWDIQIVDPDRHMTLTDGE----VGEIWvggPGLPDGYWRQPEQTATTFGARTAdglGPYLrTGDAGFR- 454
Cdd:cd05966 409 P-GSATRPFFGIEPAILDEEGNEVEGEVEgylvIKRPW---PGMARTIYGDHERYEDTYFSKFP---GYYF-TGDGARRd 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 455 YQGELYVCGRYRDLIIVGGrnHFPNDIEktVEEA---HCGVApggACAV--QPD-----APQAngewWLVLETGSPVED- 523
Cdd:cd05966 481 EDGYYWITGRVDDVINVSG--HRLGTAE--VESAlvaHPAVA---EAAVvgRPHdikgeAIYA----FVTLKDGEEPSDe 549
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2181016861 524 -LDDLSRILRRRILAHheTAPERVVWVPcrTLPTTTSGKIRRR 565
Cdd:cd05966 550 lRKELRKHVRKEIGPI--ATPDKIQFVP--GLPKTRSGKIMRR 588
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
180-566 |
6.74e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 51.54 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 180 SSGSTGKPKGVVNThqsilRQAAFAANVWNGDDDM-------HMVSWLPLYHDMGIfwGVFMPLLNGGCTTLIPPHdfvR 252
Cdd:PRK13383 182 TSGTTGKPKGVPRA-----PQLRSAVGVWVTILDRtrlrtgsRISVAMPMFHGLGL--GMLMLTIALGGTVLTHRH---F 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 NPRIWLETVSRFRGNWIGGPDFAYRRCIEAFDGTALQSlDLSCLRLATNGAEPVRGTTLRDFTAKFraaglrDDVMAPQY 332
Cdd:PRK13383 252 DAEAALAQASLHRADAFTAVPVVLARILELPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTY------GDILYNGY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 333 GLAEAGLGvtgsqtvrvwveksfdadalergiavevAQPNPADGRSrALVSCGDGAFGWDIQIVDPDRHmTLTDGEVGEI 412
Cdd:PRK13383 325 GSTEVGIG----------------------------ALATPADLRD-APETVGKPVAGCPVRILDRNNR-PVGPRVTGRI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 413 WVGGPGLPDGYwrqpeqtATTFGARTADGLGpylRTGDAGF-RYQGELYVCGRYRDLIIVGGRNHFPNDIEKTVeEAHCG 491
Cdd:PRK13383 375 FVGGELAGTRY-------TDGGGKAVVDGMT---STGDMGYlDNAGRLFIVGREDDMIISGGENVYPRAVENAL-AAHPA 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181016861 492 VAPGGACAVQPDAPQANGEWWLVLETGSPVeDLDDLSRILRRRILAHHETAPERVVwvpcRTLPTTTSGKIRRRE 566
Cdd:PRK13383 444 VADNAVIGVPDERFGHRLAAFVVLHPGSGV-DAAQLRDYLKDRVSRFEQPRDINIV----SSIPRNPTGKVLRKE 513
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
2556-2850 |
7.68e-06 |
|
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: 51.28 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2556 HCYFEFEladfDRPRFDS---AARQLVARHAGLRTTVSPAGTDAAssgeVAVVH-TAPI---EPVVRDHDDVRAAMRDQI 2628
Cdd:cd19544 27 RSLLAFD----SRARLDAflaALQQVIDRHDILRTAILWEGLSEP----VQVVWrQAELpveELTLDPGDDALAQLRARF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2629 ------IDLTARPGIDFGV-QTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETvDQLPPLeTSFAHYVWnHPEL 2701
Cdd:cd19544 99 dprryrLDLRQAPLLRAHVaEDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRA-AALPPP-VPYRNFVA-QARL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2702 LPDADEAvlprlaasRDYWRARLpslppapklADmsllfeIEEP--------------RFERATATIPAvDWSQVTRSC- 2766
Cdd:cd19544 176 GASQAEH--------EAFFREML---------GD------VDEPtapfglldvqgdgsDITEARLALDA-ELAQRLRAQa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2767 RAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDPDVVGIENVVGDF--TslvlLECRVD-EPASIWESVRALQRQ 2843
Cdd:cd19544 232 RRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFinT----LPLRVRlGGRSVREAVRQTHAR 307
|
....*..
gi 2181016861 2844 LMTDLPH 2850
Cdd:cd19544 308 LAELLRH 314
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
175-562 |
8.00e-06 |
|
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: 51.25 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILR-QAAFAANVWNGDDDMHMVSWLPLYhdmgifwgVF--------MPLLNGGcTTLI 245
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGSVVNlRTSLSERYFGRDNGDEAVLFFSNY--------VFdffveqmtLALLNGQ-KLVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 246 PPHDFVRNPRIWLETVSRFRGNWIGGpdfayrrcieafDGTALQSLDLSclrlatngaepvRGTTLRDFTAkfraAGlrD 325
Cdd:cd17648 168 PPDEMRFDPDRFYAYINREKVTYLSG------------TPSVLQQYDLA------------RLPHLKRVDA----AG--E 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 326 DVMAPQY--------GLAEAGLGVTgsqtvrvwveksfdadalergiavEVAQPN---PADGRSRALVSCGDGAFGWDIQ 394
Cdd:cd17648 218 EFTAPVFeklrsrfaGLIINAYGPT------------------------ETTVTNhkrFFPGDQRFDKSLGRPVRNTKCY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 395 IVDPDRHMtLTDGEVGEIWVGGPGLPDGYWRQPEQTATTFGA-------RTADGLGPYL-RTGD-AGFRYQGELYVCGRY 465
Cdd:cd17648 274 VLNDAMKR-VPVGAVGELYLGGDGVARGYLNRPELTAERFLPnpfqteqERARGRNARLyKTGDlVRWLPSGELEYLGRN 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 466 RDLIIVGGRNHFPNDIEKTVEEaHCGVApggACAV----QPDAPQANGEWWLV----LETGSPVEdlDDLSRILRRRILA 537
Cdd:cd17648 353 DFQVKIRGQRIEPGEVEAALAS-YPGVR---ECAVvakeDASQAQSRIQKYLVgyylPEPGHVPE--SDLLSFLRAKLPR 426
|
410 420
....*....|....*....|....*
gi 2181016861 538 HheTAPERVvwVPCRTLPTTTSGKI 562
Cdd:cd17648 427 Y--MVPARL--VRLEGIPVTINGKL 447
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1640-1699 |
8.24e-06 |
|
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: 45.63 E-value: 8.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 1640 RLVAEVWSDVLGAPIT--GREDNFFAQGGDSLRATEAVARLTRR-GVAgAEVGQLLSHQTLGQ 1699
Cdd:pfam00550 1 ERLRELLAEVLGVPAEeiDPDTDLFDLGLDSLLAVELIARLEEEfGVE-IPPSDLFEHPTLAE 62
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1256-1525 |
9.98e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 51.27 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1256 PIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVNRRNRIDTHDRllALSALDF--DLSVYDT-FGALGCGAQLV 1332
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDR--GVSWLPFfhDMGLITVlLPALLGHYITF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1333 TIPEHARRDAFHWLSLTTEfgitvwnsVPGLMDMLLIAAGDKAGSLPTLRSVFLSGDwIPLDLP---------------- 1396
Cdd:PRK07769 252 MSPAAFVRRPGRWIRELAR--------KPGGTGGTFSAAPNFAFEHAAARGLPKDGE-PPLDLSnvkgllngsepvspas 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1397 -RRLRRA-AP-GVRLVA------MGGAT---EAAIWSNEFVVDDVDPDW-----------------ASIPYGYPLANQMF 1447
Cdd:PRK07769 323 mRKFNEAfAPyGLPPTAikpsygMAEATlfvSTTPMDEEPTVIYVDRDElnagrfvevpadapnavAQVSAGKVGVSEWA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1448 RVVD-DNGDDQPDYVAGELWIGGAGVALGYHNAPELTSDRFVH-------------DPTGSRWYRTGDMGCYWrDGTLQF 1513
Cdd:PRK07769 403 VIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshaegAPDDALWVRTGDYGVYF-DGELYI 481
|
330
....*....|..
gi 2181016861 1514 LGRADSQVKIRG 1525
Cdd:PRK07769 482 TGRVKDLVIIDG 493
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
2585-2850 |
1.04e-05 |
|
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: 50.77 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2585 LRTTVSPAGTDAASSGEVAVVHTAPIEPVVRDHddvRAAMrdqiIDLTARPGIDFGVQTRGDGRTVVGISMDNTMLDGAS 2664
Cdd:cd19547 71 VRDDLAPPWALLDWSGEDPDRRAELLERLLADD---RAAG----LSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWC 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2665 MMIALSELDHLYRGETVDQLPPLET--SFAHYV-WnhpellpdaDEAVLPRLAASRDYWRARLPSLPPAPkladMSLLFE 2741
Cdd:cd19547 144 LSLIWGDVFRVYEELAHGREPQLSPcrPYRDYVrW---------IRARTAQSEESERFWREYLRDLTPSP----FSTAPA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2742 IEEPRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRDPDVVGIENVVGDFTSLV 2821
Cdd:cd19547 211 DREGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTI 290
|
250 260
....*....|....*....|....*....
gi 2181016861 2822 LLECRVDEPASIWESVRALQRQLMTDLPH 2850
Cdd:cd19547 291 PLRIRLDPDQTVTGLLETIHRDLATTAAH 319
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
138-450 |
1.06e-05 |
|
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: 51.30 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 138 RDPILG-ALPIRTPASTAD-GLAPHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRqaAFAANVWNGDDDMH 215
Cdd:cd17632 187 RERLAAvGIPVTTLTLIAVrGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVAT--FWLKVSSIQDIRPP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 216 ---MVSWLPLYHDMGIFWgVFMPLLNGGCT---------------TLIPPHDFVRNPRIWLETVSRFRGNWIggpdfayR 277
Cdd:cd17632 265 asiTLNFMPMSHIAGRIS-LYGTLARGGTAyfaaasdmstlfddlALVRPTELFLVPRVCDMLFQRYQAELD-------R 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 278 RCIEAFDGTALqsldlsclrlatngAEPVRgttlrdftakfraAGLRDDVMAPQYGLAEAGLGVTGSQtVRVWVEKSFDA 357
Cdd:cd17632 337 RSVAGADAETL--------------AERVK-------------AELRERVLGGRLLAAVCGSAPLSAE-MKAFMESLLDL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 358 DALErGIAVEVAQPNPADGR-SRALVScgdgafgwDIQIVD-PDRHMTLTDGEV--GEIWVGGPGLPDGYWRQPEQTATT 433
Cdd:cd17632 389 DLHD-GYGSTEAGAVILDGViVRPPVL--------DYKLVDvPELGYFRTDRPHprGELLVKTDTLFPGYYKRPEVTAEV 459
|
330
....*....|....*..
gi 2181016861 434 FgarTADGlgpYLRTGD 450
Cdd:cd17632 460 F---DEDG---FYRTGD 470
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
172-453 |
1.45e-05 |
|
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: 50.68 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-----GDDDMHMvSWLPLYHdmgIF-----WGVFMpllNGGC 241
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEilnkiNPTDVYI-SYLPLAH---IFervveALFLY---HGAK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 242 --------TTLIP------PHDFVRNPRIWLETVSRFRGNWIGGP-------DFAYRR---CIEAFDGTA---------- 287
Cdd:cd05927 187 igfysgdiRLLLDdikalkPTVFPGVPRVLNRIYDKIFNKVQAKGplkrklfNFALNYklaELRSGVVRAspfwdklvfn 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 288 -LQSLDLSCLRLATNGAEPVRGTTLRdftaKFRAA-------GlrddvmapqYGLAEaGLGVTGSQTVRVWVeksfdada 359
Cdd:cd05927 267 kIKQALGGNVRLMLTGSAPLSPEVLE----FLRVAlgcpvleG---------YGQTE-CTAGATLTLPGDTS-------- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 360 lergiAVEVAQPNPADgrsralvscgdgafgwDIQIVD-PDR--HMTLTDGEvGEIWVGGPGLPDGYWRQPEQTATTFga 436
Cdd:cd05927 325 -----VGHVGGPLPCA----------------EVKLVDvPEMnyDAKDPNPR-GEVCIRGPNVFSGYYKDPEKTAEAL-- 380
|
330
....*....|....*..
gi 2181016861 437 rTADGlgpYLRTGDAGF 453
Cdd:cd05927 381 -DEDG---WLHTGDIGE 393
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
2243-2341 |
1.58e-05 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 46.93 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2243 ARTLGRRLRVVEVGSRTGLITERLTELVGVVVeeylCLEPNPTLAGIA--AGRRFPAPTRHVDAPDAA---SGVDVVICC 2317
Cdd:COG2227 19 ARLLPAGGRVLDVGCGTGRLALALARRGADVT----GVDISPEALEIAreRAAELNVDFVQGDLEDLPledGSFDLVICS 94
|
90 100
....*....|....*....|....*.
gi 2181016861 2318 GSLHQLPDAEAVLEAIT--VSDDGWL 2341
Cdd:COG2227 95 EVLEHLPDPAALLRELArlLKPGGLL 120
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
163-483 |
1.73e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 50.26 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 163 GTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQA-------AFAANvwngddDmhmvSWL---PLYH--DMGIFW 230
Cdd:PRK09029 126 GAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAegvlslmPFTAQ------D----SWLlslPLFHvsGQGIVW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 231 gvfMPLLNGGCTTLIPPHDFVrnpriwletvsrfrgnwiggpdfayrrciEAFDG--------TALQsldlsclRLATNG 302
Cdd:PRK09029 196 ---RWLYAGATLVVRDKQPLE-----------------------------QALAGcthaslvpTQLW-------RLLDNR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 303 AEPVrgtTLRDF-----------TAKFRAAGLRDDVmapQYGLAEAGLGVTGSQtvrvwveksfdADALeRGiaveVAQP 371
Cdd:PRK09029 237 SEPL---SLKAVllggaaipvelTEQAEQQGIRCWC---GYGLTEMASTVCAKR-----------ADGL-AG----VGSP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 372 NPadGRsralvscgdgafgwDIQIVDpdrhmtltdgevGEIWVGGPGLPDGYWRQPEQTATTfgarTADGlgpYLRTGDA 451
Cdd:PRK09029 295 LP--GR--------------EVKLVD------------GEIWLRGASLALGYWRQGQLVPLV----NDEG---WFATRDR 339
|
330 340 350
....*....|....*....|....*....|..
gi 2181016861 452 GFRYQGELYVCGRYRDLIIVGGRNHFPNDIEK 483
Cdd:PRK09029 340 GEWQNGELTILGRLDNLFFSGGEGIQPEEIER 371
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
2565-2792 |
1.79e-05 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 50.11 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2565 DFDRPRFDSAARQLVARHAGLRTtVSPAGTDAAssgeVAVVHTA-----PIEPVVRDHDDVRAAMRDQI---IDLTARPG 2636
Cdd:cd19540 35 ALDVDALRAALADVVARHESLRT-VFPEDDGGP----YQVVLPAaearpDLTVVDVTEDELAARLAEAArrgFDLTAELP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2637 IDFGVQTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQLP---PLETSFAHY-VWNHpELLPDADEavlPR 2712
Cdd:cd19540 110 LRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPdwaPLPVQYADYaLWQR-ELLGDEDD---PD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2713 LAASR--DYWRARLPSLP---------PAPKLADMsllfeieepRFERATATIPAVDWSQVTRSCRAEGVTVASFLLANY 2781
Cdd:cd19540 186 SLAARqlAYWRETLAGLPeelelptdrPRPAVASY---------RGGTVEFTIDAELHARLAALAREHGATLFMVLHAAL 256
|
250
....*....|.
gi 2181016861 2782 ARVLSRWSGTD 2792
Cdd:cd19540 257 AVLLSRLGAGD 267
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2966-3037 |
3.04e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.17 E-value: 3.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKI 3037
Cdd:PRK05691 4237 APRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1243-1609 |
4.35e-05 |
|
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: 49.19 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1243 SDITAMIECAPTDPIRIDPHDAAYVIYTSGSTGEPK-------GVLVSHaaalntivdvnrrnridthdrlLALSALDFD 1315
Cdd:cd05943 230 EDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQH----------------------LKEHILHCD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1316 LSVYDTF---------------GALGCGAQLVTIPEHARRDAFHWL-SLTTEFGITVWNSVPGLMDMLLIAAGD--KAGS 1377
Cdd:cd05943 288 LRPGDRLfyyttcgwmmwnwlvSGLAVGATIVLYDGSPFYPDTNALwDLADEEGITVFGTSAKYLDALEKAGLKpaETHD 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1378 LPTLRSVFLSG--------DWIPldlprrlRRAAPGVRLVAMGGATEaaIWSNeFVVDDVD-PDWASiPYGYPLANQMFR 1448
Cdd:cd05943 368 LSSLRTILSTGsplkpesfDYVY-------DHIKPDVLLASISGGTD--IISC-FVGGNPLlPVYRG-EIQCRGLGMAVE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1449 VVDDNGDDQPDyVAGELWIGGA--GVALGYHNapeltsdrfvhDPTGSRW-----------YRTGDMGCYWRDGTLQFLG 1515
Cdd:cd05943 437 AFDEEGKPVWG-EKGELVCTKPfpSMPVGFWN-----------DPDGSRYraayfakypgvWAHGDWIEITPRGGVVILG 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1516 RADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNctaLGAG-----IVVTGSGAEqFDDSTPGALRAHLAVRLPQY 1590
Cdd:cd05943 505 RSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEW---KDGDervilFVKLREGVE-LDDELRKRIRSTIRSALSPR 580
|
410
....*....|....*....
gi 2181016861 1591 MIPKVFVSCPELPLTANGK 1609
Cdd:cd05943 581 HVPAKIIAVPDIPRTLSGK 599
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
403-564 |
4.38e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 48.84 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 403 TLTDGEVGEIWVGGPGLPDGYWRQPEQTAttfgartadglgPYLRTGDAG-FRYQGELYVCGRYRDLIIVGGRNHFPNDI 481
Cdd:PRK07445 295 TIPANQTGNITIQAQSLALGYYPQILDSQ------------GIFETDDLGyLDAQGYLHILGRNSQKIITGGENVYPAEV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 482 EKTVEEAHcgvapggacAVQpDAP---QANGEW-WLVLETGSPVEDLDDLSRILRRriLAHHETA---PERvvWVPCRTL 554
Cdd:PRK07445 363 EAAILATG---------LVQ-DVCvlgLPDPHWgEVVTAIYVPKDPSISLEELKTA--IKDQLSPfkqPKH--WIPVPQL 428
|
170
....*....|
gi 2181016861 555 PTTTSGKIRR 564
Cdd:PRK07445 429 PRNPQGKINR 438
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1768-2121 |
4.93e-05 |
|
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: 48.87 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1768 GIDLDRFARVVTRCVDEFAMLRCALDADTTQR-VQV--DAGPVPVHDLDIQDDP--------DLLLRRMAAAPFDPHSVP 1836
Cdd:pfam00668 38 ELDPERLEKALQELINRHDALRTVFIRQENGEpVQVilEERPFELEIIDISDLSeseeeeaiEAFIQRDLQSPFDLEKGP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1837 VIQCFAPSRSPRHVGLLISY--LGLDARSLSTVVTTIIAEYQSQPRPRQ-VDPTAAVFARFA------SESAWGENDVD- 1906
Cdd:pfam00668 118 LFRAGLFRIAENRHHLLLSMhhIIVDGVSLGILLRDLADLYQQLLKGEPlPLPPKTPYKDYAewlqqyLQSEDYQKDAAy 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1907 --NSVAGP-PLLPLHDQRRDPFERvTFA--RRSFTIEEQAAATLREHAAHLGVTPTALVFEAFAHALASIGAGQRFAVTV 1981
Cdd:pfam00668 198 wlEQLEGElPVLQLPKDYARPADR-SFKgdRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1982 PKSYRPDyaPADREVLGNFT-----RLALCEVDygavrpGSAEAVAAAQRELWRAVSHD----GDITGGLAATRTAGGYP 2052
Cdd:pfam00668 277 PGSGRPS--PDIERMVGMFVntlplRIDPKGGK------TFSELIKRVQEDLLSAEPHQgypfGDLVNDLRLPRDLSRHP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2053 -----VVFTSTLGltHQDASGLTNVRTLTQTPGVWLDCQTEDEVA--------GIRMSWDIATNVVAAESISVAFSRFEE 2119
Cdd:pfam00668 349 lfdpmFSFQNYLG--QDSQEEEFQLSELDLSVSSVIEEEAKYDLSltaserggGLTIKIDYNTSLFDEETIERFAEHFKE 426
|
..
gi 2181016861 2120 AV 2121
Cdd:pfam00668 427 LL 428
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
97-566 |
6.24e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 48.52 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 97 VPVYLPSTRepqRFLARAQHILR-DCEpsAVYTCGELVEVLE-RDPILGALPIRTPAsTADGLAPHPGGTTADAD-HGEH 173
Cdd:PRK07867 80 VPVGLNPTR---RGAALARDIAHaDCQ--LVLTESAHAELLDgLDPGVRVINVDSPA-WADELAAHRDAEPPFRVaDPDD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN-GDDDMHMVSwLPLYHDMGIFWGvFMPLLNGGCTTLIPPHDFVR 252
Cdd:PRK07867 154 LFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGlGPDDVCYVS-MPLFHSNAVMAG-WAVALAAGASIALRRKFSAS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 253 NpriWLETVSRF---RGNWIGGPdFAYRRCIEAFDGTALQSLdlsclRLA-TNGAEPVrgtTLRDFTAKFraaglrDDVM 328
Cdd:PRK07867 232 G---FLPDVRRYgatYANYVGKP-LSYVLATPERPDDADNPL-----RIVyGNEGAPG---DIARFARRF------GCVV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 329 APQYGLAEAGLGVTGSQTVRvwveksfdADALERGIAvEVAQPNPADGRSralvsCGDGAFgwdiqivDPDRHmTLTDGE 408
Cdd:PRK07867 294 VDGFGSTEGGVAITRTPDTP--------PGALGPLPP-GVAIVDPDTGTE-----CPPAED-------ADGRL-LNADEA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 409 VGEIW-VGGPGLPDGYWRQPEQTAttfgARTADGLgpyLRTGDAGFR-YQGELYVCGRYRDLIIVGGRNHFPNDIEKTVE 486
Cdd:PRK07867 352 IGELVnTAGPGGFEGYYNDPEADA----ERMRGGV---YWSGDLAYRdADGYAYFAGRLGDWMRVDGENLGTAPIERILL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 487 EaHCGVAPGGACAVqPDApqANGEWWLVLETGSPVEDLDDLSriLRRRILAHHETAPErvvWVP-----CRTLPTTTSGK 561
Cdd:PRK07867 425 R-YPDATEVAVYAV-PDP--VVGDQVMAALVLAPGAKFDPDA--FAEFLAAQPDLGPK---QWPsyvrvCAELPRTATFK 495
|
....*
gi 2181016861 562 IRRRE 566
Cdd:PRK07867 496 VLKRQ 500
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
2986-3045 |
6.30e-05 |
|
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: 48.91 E-value: 6.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2986 PRVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIADTDNADE 3045
Cdd:TIGR03443 866 ATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEE 925
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
172-244 |
6.87e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 48.20 E-value: 6.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGGCTTL 244
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL 159
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
371-473 |
1.25e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.47 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 371 PNPADGRSRALVSCGDGAF--GWDIQIVDPDRHMTLTDGEVGEIWVGGPGLPDGYWRQPEQT----ATTFGAR------- 437
Cdd:PRK05620 345 PSGVSGEARWAYRVSQGRFpaSLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaASTFRGEdvedand 424
|
90 100 110
....*....|....*....|....*....|....*....
gi 2181016861 438 --TADGlgpYLRTGDAGFRYQ-GELYVCGRYRDLIIVGG 473
Cdd:PRK05620 425 rfTADG---WLRTGDVGSVTRdGFLTIHDRARDVIRSGG 460
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
13-227 |
1.29e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 47.56 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 13 DGDRSVPAVFAEWVGRRPDAVALRTvaatGIDDWTYQRLWDHVREIRDVAFS-GLSAGIRIPMALPGGADYVAGMLAALA 91
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLF----EDQSISYAELNARANRYAHWAAArGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 92 aglIPVPVYLPSTREPQRFLAraqHILRDCEPSAVYTCGELVEVLE--RDPILGALPI-------RTPASTADGLA---- 158
Cdd:PRK08279 110 ---LGAVVALLNTQQRGAVLA---HSLNLVDAKHLIVGEELVEAFEeaRADLARPPRLwvaggdtLDDPEGYEDLAaaaa 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 159 --PHPGGTTADADHGEHVAFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWN--GDDDMHMVswLPLYHDMG 227
Cdd:PRK08279 184 gaPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRltPDDVLYCC--LPLYHNTG 254
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2661-2868 |
1.37e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 47.73 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2661 DGASMMIALSELDHLYRGETVDQLPPLE--TSFAHYVWNhpellpDADEAVLPRLAASRDYWRARLPSLPPAPKLADMSL 2738
Cdd:PRK10252 145 DGFSFPAITRRIAAIYCAWLRGEPTPASpfTPFADVVEE------YQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2739 LFEIEEPRFERATATIPAVDWSQVTRScrAEGVTVASFLLANYARVLSRWSGTDHFCINVTLFDRdpdvvgIENVVGDFT 2818
Cdd:PRK10252 219 PGRSASADILRLKLEFTDGAFRQLAAQ--ASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRR------LGSAALTAT 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 2819 SLVL--LECRV--DEPASIWESVRALQRQLMTDLPHRGADAVWLQRELLRFHGN 2868
Cdd:PRK10252 291 GPVLnvLPLRVhiAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGD 344
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
2253-2341 |
1.39e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 43.13 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2253 VEVGSRTGLITERLTELVGVVveEYLCLEPNPTLAGIAAGR-----RFPAPTRHVDAPDAASG----VDVVICCGSLHQL 2323
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGL--EYTGLDISPAALEAARERlaalgLLNAVRVELFQLDLGELdpgsFDVVVASNVLHHL 78
|
90 100
....*....|....*....|
gi 2181016861 2324 PDAEAVLEAIT--VSDDGWL 2341
Cdd:pfam08242 79 ADPRAVLRNIRrlLKPGGVL 98
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2966-3035 |
1.47e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.85 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2966 ASNDELLQRVSRICASALGQPRVEPHDNFFQLGGDSVSATKVVEQiGRELSASATLRLLFANPVIGDFAA 3035
Cdd:PRK12467 2093 APQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAA 2161
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
2251-2333 |
2.64e-04 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 43.83 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2251 RVVEVGSRTGLITERLTELVGVVVeeylCLEPNPTLAGIAAGR----RFPAPTRHVDA---PDAASGVDVVICCGSLHQL 2323
Cdd:COG2226 25 RVLDLGCGTGRLALALAERGARVT----GVDISPEMLELARERaaeaGLNVEFVVGDAedlPFPDGSFDLVISSFVLHHL 100
|
90
....*....|
gi 2181016861 2324 PDAEAVLEAI 2333
Cdd:COG2226 101 PDPERALAEI 110
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1730-2121 |
2.83e-04 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 46.15 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1730 FPLTRLQQAYTLGAAGLNGSTCAPTYFAVvlaaapeSAGIDLDRFARVVTRCVDEFAMLRCALDADTTQR--VQV--DAG 1805
Cdd:cd19542 2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDL-------DSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtfLQVvlKSL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1806 PVPVHDLDIQDD-PDLLLRRMAAAPFDPHSVPVIQCFAPSRSPRHVGLL-ISYLGLDARSLSTVVTTIIAEYQSQPRPRq 1883
Cdd:cd19542 75 DPPIEEVETDEDsLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLrISHALYDGVSLPIILRDLAAAYNGQLLPP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1884 vdptAAVFARFASeSAWGENDVD-----NSV---AGPPLLPLHDQRRDPFERVTFARRSftieeqaAATLREHAAHLGVT 1955
Cdd:cd19542 154 ----APPFSDYIS-YLQSQSQEEslqywRKYlqgASPCAFPSLSPKRPAERSLSSTRRS-------LAKLEAFCASLGVT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1956 PTALVFEAFAHALASIgAGQR---FAVTVpkSYRpDYAPADRE-VLGNFT-----RLALCEvdygavRPGSAEAVAAAQR 2026
Cdd:cd19542 222 LASLFQAAWALVLARY-TGSRdvvFGYVV--SGR-DLPVPGIDdIVGPCIntlpvRVKLDP------DWTVLDLLRQLQQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2027 ELWRAVSHD----GDI--TGGLAATRTAGGYPVVFTSTLGLTHQDASGLTNVRTLTQTPGVWLDCQTEDEVAGIRMSWDI 2100
Cdd:cd19542 292 QYLRSLPHQhlslREIqrALGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSL 371
|
410 420
....*....|....*....|...
gi 2181016861 2101 A--TNVVAAESISVAFSRFEEAV 2121
Cdd:cd19542 372 AysTSVLSEEQAEELLEQFDDIL 394
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1769-1956 |
3.10e-04 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 45.03 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1769 IDLDRFARVVTRCVDEFAMLRCALDADTTQRVQV--DAGPVPVHDLDIQDDPDL--------LLRRMAAAPFDPHSVPVI 1838
Cdd:COG4908 30 LDVEALERALRELVRRHPALRTRFVEEDGEPVQRidPDADLPLEVVDLSALPEPereaeleeLVAEEASRPFDLARGPLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1839 QCFAPSRSPRHVGLLISY--LGLDARSLSTVVTTIIAEYQ--SQPRPRQVDPTAAVFARFAsesAWGENDVD-------- 1906
Cdd:COG4908 110 RAALIRLGEDEHVLLLTIhhIISDGWSLGILLRELAALYAalLEGEPPPLPELPIQYADYA---AWQRAWLQsealekql 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 1907 ----NSVAG-PPLLPLHDQRRDPFERV-TFARRSFTIEEQAAATLREHAAHLGVTP 1956
Cdd:COG4908 187 eywrQQLAGaPPVLELPTDRPRPAVQTfRGATLSFTLPAELTEALKALAKAHGATV 242
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1786-1965 |
3.48e-04 |
|
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: 46.10 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1786 AMLRCAL---DADTTQRVQVDAG-PVPVHDLDIQDDPDLLL----RRMAAAPFDPHSVPVIQC-FAPSRSPRHVGLLIS- 1855
Cdd:cd20483 53 EVLRTAYfegDDFGEQQVLDDPSfHLIVIDLSEAADPEAALdqlvRNLRRQELDIEEGEVIRGwLVKLPDEEFALVLASh 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1856 YLGLDARSLSTVVTTIIAEYQS--QPRPRQ-VDPTAAVFARFAS------ESAWGENDVD---NSVAGPP----LLPLHD 1919
Cdd:cd20483 133 HIAWDRGSSKSIFEQFTALYDAlrAGRDLAtVPPPPVQYIDFTLwhnallQSPLVQPLLDfwkEKLEGIPdaskLLPFAK 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2181016861 1920 QRRDP---FERVTFarrSFTIEEQAAATLREHAAHLGVTPTALVFEAFA 1965
Cdd:cd20483 213 AERPPvkdYERSTV---EATLDKELLARMKRICAQHAVTPFMFLLAAFR 258
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
172-224 |
4.33e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.86 E-value: 4.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAA-FAANVWNGDDDMHmVSWLPLYH 224
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAgSSLSTKFYPSDVH-ISYLPLAH 273
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
601-660 |
4.35e-04 |
|
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: 40.62 E-value: 4.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 601 ELAQHLAAMLGVEPYELAPDADLTTLGLTSMMTAQIVEWSSSQ-SRRLDFADLYAEPTLRS 660
Cdd:pfam00550 2 RLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1875-2389 |
4.95e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.02 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1875 YQSQPRPRQVDPTAAvFAR----FASESAWGENDVDNSVAGPPLLPLHDQRRDPFERVTFARRSFTIEEQAAATLREHAA 1950
Cdd:COG3321 853 YPGRGRRRVPLPTYP-FQRedaaAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLA 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1951 HLGVTPTALVFEAFAHALASIGAGQRFAVTVPksyrPDYAPADREVLGNFTRLALCEVDYGAVRPGSAEAVAAAQRELWR 2030
Cdd:COG3321 932 LVALAAAAAALLALAAAAAAAAAALAAAEAGA----LLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAA 1007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2031 AVSHDGDITGGLAATRTAGGYPVVFTSTLGLTHQDASGLTNVRTLTQTPGVWLDcQTEDEVAGIRMSWDIATNVVAAESI 2110
Cdd:COG3321 1008 AALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAAL-ALALAALLLLAALAELALAAAALAL 1086
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2111 SVAFSRFEEAVRRHAGQAEPPGTAVAPAVGGSPGPEWASAVIAAALRHCRPEQVLPQYTMLVRRWEALRYVPSGYAASDV 2190
Cdd:COG3321 1087 AAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAA 1166
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2191 ERAARRLAGIVTGAVSPQTLIGDPQLTPEALLLRDDRMRMALDDLAGAIFGHARTLGRRLRVVEVGSRTGLITERLTELV 2270
Cdd:COG3321 1167 LLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVA 1246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2271 GVVVEEYLCLEPNPTLAGIAAGRRFPAPTRHVDAPDAASGVDVVICCGSLHQLPDAEAVLEAITVSDDGWLWMVENSEAT 2350
Cdd:COG3321 1247 ALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALL 1326
|
490 500 510
....*....|....*....|....*....|....*....
gi 2181016861 2351 QATLISAAVLDPGLLASDSKTLRPADRWWRLIADHGWRP 2389
Cdd:COG3321 1327 AAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAA 1365
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
168-566 |
5.16e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 45.61 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 168 ADHGEHVAfLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHdmgifwgvfmplLNGGCTTlipp 247
Cdd:PLN02479 192 ADEWQSIA-LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFH------------CNGWCFT---- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 248 hdfvrnpriWleTVSRFRGNWIggpdfayrrCIEAFDGTALQSLdlsclrLATNG-----AEPVRGTTLRDFTAKFRAAG 322
Cdd:PLN02479 255 ---------W--TLAALCGTNI---------CLRQVTAKAIYSA------IANYGvthfcAAPVVLNTIVNAPKSETILP 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 323 LRD--DVM----APQ----YGLAEAGLGVT---------GSQTVRVWVEksfDADALergiavevaqpnPADGRSRALVS 383
Cdd:PLN02479 309 LPRvvHVMtagaAPPpsvlFAMSEKGFRVThtyglsetyGPSTVCAWKP---EWDSL------------PPEEQARLNAR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 384 CGDGAFGWD-IQIVDPDRHMTL-TDGE-VGEIWVGGPGLPDGYWRQPEQTATTFGartadglGPYLRTGDAGFRY-QGEL 459
Cdd:PLN02479 374 QGVRYIGLEgLDVVDTKTMKPVpADGKtMGEIVMRGNMVMKGYLKNPKANEEAFA-------NGWFHSGDLGVKHpDGYI 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 460 YVCGRYRDLIIVGGRNHFPNDIEKTVeEAHCGVAPGGACAvQPD-----APQAngewWLVLETGSPVED----LDDLSRI 530
Cdd:PLN02479 447 EIKDRSKDIIISGGENISSLEVENVV-YTHPAVLEASVVA-RPDerwgeSPCA----FVTLKPGVDKSDeaalAEDIMKF 520
|
410 420 430
....*....|....*....|....*....|....*.
gi 2181016861 531 LRRRILAHheTAPERVVWVPcrtLPTTTSGKIRRRE 566
Cdd:PLN02479 521 CRERLPAY--WVPKSVVFGP---LPKTATGKIQKHV 551
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
712-963 |
5.68e-04 |
|
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: 45.33 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 712 FELVGaRVDAGRLAAALDALTRRHPMLRATFPD----PGRCLITPEAVRLPLAVhdltdapVTTRDTHLAEIRRRLRTHR 787
Cdd:cd19538 30 IKLKG-KLDVQALQQALYDVVERHESLRTVFPEedgvPYQLILEEDEATPKLEI-------KEVDEEELESEINEAVRYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 788 FDIETGDTWTVELTRLPHGciVHFAVDL---IIADVTSIGTMLRDLAASYRG---------EKLPAPSATFA----DLIQ 851
Cdd:cd19538 102 FDLSEEPPFRATLFELGEN--EHVLLLLlhhIAADGWSLAPLTRDLSKAYRArckgeapelAPLPVQYADYAlwqqELLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 852 STSPPPQACADRL----------PEGPQLPR---------VQEADISF-----LrHQHtLSALAtkaiddacHNHGVTRA 907
Cdd:cd19538 180 DESDPDSLIARQLaywkkqlaglPDEIELPTdyprpaessYEGGTLTFeidseL-HQQ-LLQLA--------KDNNVTLF 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2181016861 908 AVLLAAYTLVLRRWASQDDFLVNVTTFGRSPE-VSDVVGDFTETHLYRAQLDGQISF 963
Cdd:cd19538 250 MVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDsLEDLVGFFVNTLVLRTDTSGNPSF 306
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1634-1703 |
6.26e-04 |
|
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: 40.99 E-value: 6.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2181016861 1634 TLTVVERLVAEVWSDVLGAPIT--GREDNFFAQ-GGDSLRATEAVARLTRR-GVAgAEVGQLLSHQTLGQFSAA 1703
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEeiTPDDSFFEDlGLDSLDAVELIAALEEEfGIE-LPDTELFEYPTVADLADY 74
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
172-245 |
6.35e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 45.52 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 172 EHVAFLQYSSGSTGKPKGVVNTHQSILRQAAfaanvwngdddMHMvSWLPLYHDMGIFW-------------GVFMPLLN 238
Cdd:PRK00174 245 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAA-----------MTM-KYVFDYKDGDVYWctadvgwvtghsyIVYGPLAN 312
|
....*..
gi 2181016861 239 GGcTTLI 245
Cdd:PRK00174 313 GA-TTLM 318
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1261-1339 |
6.59e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 45.47 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1261 PHDAAYVIYTSGSTGEPKGVLVSHAAAL------NTIVDVNRRNRIdthdrllaLSAL----DFDLSVyDTFGALGCGAQ 1330
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLanveqiKTIADFTPNDRF--------MSALplfhSFGLTV-GLFTPLLTGAE 434
|
90
....*....|.
gi 2181016861 1331 --LVTIPEHAR 1339
Cdd:PRK08043 435 vfLYPSPLHYR 445
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
616-1133 |
6.59e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 45.63 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 616 ELAPDADLTTLGLTSMMTAQIVEWSSSQSRRLD--------FADLYAEPTLRSWQRLFDAAPPVQTgtssvaasgPWPTT 687
Cdd:COG3321 796 EVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDelaqlltaLAQLWVAGVPVDWSALYPGRGRRRV---------PLPTY 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 688 PLQ------QAYWVGRGAEQPLGGVGCQTYFELVGARVDAGRLAAALDALTRRHPMLRATFPDPGRCLITPEAVRLPLAV 761
Cdd:COG3321 867 PFQredaaaALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 762 HDLTDAPVTTRDTHLAEIRRRLRTHRFDIETGDTWTVELTRLPHGCIVHFAVDLIIADVTSIGTMLRDLAASYRGEKLPA 841
Cdd:COG3321 947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 842 PSAT--------FADLIQSTSPPPQACADRLPEGPQLPRVQEADISFLRHQHTLSALATKAIDDACHNHGVTRAAVLLAA 913
Cdd:COG3321 1027 LLAAaaaalaaaAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 914 YTLVLRRWASQDDFLVNVTTFGRSPEVSDVVGDFTETHLYRAQLDGQISFVDQAQVTQKGLRTALRAAPAPDLLATQLRS 993
Cdd:COG3321 1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 994 GTGHSGIVPVVFTYAADSPLLSAEDANTLGAIDEVVSMTPQVLIDHQACRLGDDVVLSWDYRAGCFPPGVVDDMFEAYVT 1073
Cdd:COG3321 1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLA 1266
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1074 LLERLGGHDWSTPATPGLSAHSRLARAHRNATTTPAPAGLLYDAFRENAATHPARLALRW 1133
Cdd:COG3321 1267 AAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALL 1326
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
2962-3039 |
8.83e-04 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 40.70 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2962 LGEGASNDELLQRVSRICASALGQP---RVEPHDNFFQLGGDSVSATKVVEQIGRELSASATLRLLFANPVIGDFAAKIA 3038
Cdd:smart00823 4 LPPAERRRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLA 83
|
.
gi 2181016861 3039 D 3039
Cdd:smart00823 84 A 84
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
175-240 |
1.46e-03 |
|
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: 43.88 E-value: 1.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 175 AFLQYSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNGG 240
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGA 149
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2443-2505 |
1.52e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 2443 TLAEIWQRHLAIPTPGVDDDFFLLGGDSLVATRVYADLRAAGFGQLAFVDLFNHSTLGELAAH 2505
Cdd:PRK05691 4245 TLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEY 4307
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
115-241 |
1.56e-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: 44.20 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 115 QHILRDCEPSAVYTCGELVEVLErdPILgalpirtPASTADGL--------APHPG---------GTTAD---ADHGEHV 174
Cdd:cd05938 71 LHCFRCCGAKVLVVAPELQEAVE--EVL-------PALRADGVsvwylshtSNTEGvislldkvdAASDEpvpASLRAHV 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181016861 175 AFLQ-----YSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSwLPLYHDMGIFWGVfmpllnGGC 241
Cdd:cd05938 142 TIKSpalyiYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYIT-LPLYHSSGFLLGI------GGC 206
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
2251-2341 |
1.63e-03 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 40.19 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2251 RVVEVGSRTGLITERLTELVGVVveEYLCLEPNPTLAGIAAGRRFPAPTRHVDAPD--AASGVDVVICCGSLHQLPDAEA 2328
Cdd:COG4106 4 RVLDLGCGTGRLTALLAERFPGA--RVTGVDLSPEMLARARARLPNVRFVVADLRDldPPEPFDLVVSNAALHWLPDHAA 81
|
90
....*....|....*
gi 2181016861 2329 VLEAI--TVSDDGWL 2341
Cdd:COG4106 82 LLARLaaALAPGGVL 96
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1253-1285 |
1.66e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.93 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|...
gi 2181016861 1253 PTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHA 1285
Cdd:PLN02736 212 PQPFRPPKPEDVATICYTSGTTGTPKGVVLTHG 244
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1240-1522 |
2.62e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 43.43 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1240 VAVSDITAMIECAPTD-PIRI--DPHDAAYVIYTSGSTGEPKGVLVSH---AAALNTIVD-----VNRRNRIDTHDRLLA 1308
Cdd:PTZ00216 239 VAWTDVVAKGHSAGSHhPLNIpeNNDDLALIMYTSGTTGDPKGVMHTHgslTAGILALEDrlndlIGPPEEDETYCSYLP 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1309 LsALDFDLSVYDTFGALGC----GAQLVTIPEHAR-RDAFhwlsltTEFGITVWNSVPGLMDMLLIAAGDK---AGSLPt 1380
Cdd:PTZ00216 319 L-AHIMEFGVTNIFLARGAligfGSPRTLTDTFARpHGDL------TEFRPVFLIGVPRIFDTIKKAVEAKlppVGSLK- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1381 lRSVFLSGdwipldLPRRLR-------------------RAAPGVRLVAM---GGATEAAiwSNEFV------------- 1425
Cdd:PTZ00216 391 -RRVFDHA------YQSRLRalkegkdtpywnekvfsapRAVLGGRVRAMlsgGGPLSAA--TQEFVnvvfgmviqgwgl 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1426 -----------VDDVDPDWAsipyGYPLANQMFRVVDDNG---DDQPDyVAGELWIGGAGVALGYHNAPELTsdRFVHDP 1491
Cdd:PTZ00216 462 tetvccggiqrTGDLEPNAV----GQLLKGVEMKLLDTEEykhTDTPE-PRGEILLRGPFLFKGYYKQEELT--REVLDE 534
|
330 340 350
....*....|....*....|....*....|.
gi 2181016861 1492 TGsrWYRTGDMGCYWRDGTLQFLGRADSQVK 1522
Cdd:PTZ00216 535 DG--WFHTGDVGSIAANGTLRIIGRVKALAK 563
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
160-226 |
3.52e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 43.04 E-value: 3.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181016861 160 HPGGTTADADHgehVAFLQYSSGSTGKPKGVVNTHQSiLRQAAFAANVWNGD------DDMHMVSWLPLYHDM 226
Cdd:PTZ00216 255 HPLNIPENNDD---LALIMYTSGTTGDPKGVMHTHGS-LTAGILALEDRLNDligppeEDETYCSYLPLAHIM 323
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
179-239 |
3.64e-03 |
|
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: 42.80 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181016861 179 YSSGSTGKPKGVVNTHQSILRQAAFAANVWNGDDDMHMVSWLPLYHDMGIFWGVFMPLLNG 239
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHG 171
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
2407-2481 |
3.76e-03 |
|
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: 43.13 E-value: 3.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181016861 2407 DKPGMPTP-PAEQRRDGRWSRP-AVPASSLPTDATVvatlAEIWQRHLAIPTPGV--DDDFFLLGGDSLVATRVYADLR 2481
Cdd:TIGR03443 818 DKPALPFPdTAQLAAVAKNRSAsAADEEFTETEREI----RDLWLELLPNRPATIspDDSFFDLGGHSILATRMIFELR 892
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
174-224 |
3.97e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 42.80 E-value: 3.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181016861 174 VAFLQYSSGSTGKPKGVVNTHQSILrqaAFAANVWN-----GDDDMHMvSWLPLYH 224
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTHGNIV---ATVAGVMTvvpklGKNDVYL-AYLPLAH 303
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
392-562 |
4.05e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 42.63 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 392 DIQIVDPDrhmTLT----DGE-VGEIWVGGPGLPDGYWRQPEQTATTFgartADGlgpYLRTGDAGFRY-QGELYVCGRY 465
Cdd:PRK08162 369 GVTVLDPD---TMQpvpaDGEtIGEIMFRGNIVMKGYLKNPKATEEAF----AGG---WFHTGDLAVLHpDGYIKIKDRS 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 466 RDLIIVGGRNhfPNDIEktVEEA---HCGVApggACAV--QPDA-----PQANGEwwlvLETGSPVEDlDDLSRILRRRi 535
Cdd:PRK08162 439 KDIIISGGEN--ISSIE--VEDVlyrHPAVL---VAAVvaKPDPkwgevPCAFVE----LKDGASATE-EEIIAHCREH- 505
|
170 180
....*....|....*....|....*..
gi 2181016861 536 LAHHETaPERVVWVPcrtLPTTTSGKI 562
Cdd:PRK08162 506 LAGFKV-PKAVVFGE---LPKTSTGKI 528
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1253-1295 |
4.41e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 42.49 E-value: 4.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2181016861 1253 PTDPIRIDPHDAAYVIYTSGSTGEPKGVLVSHAAALNTIVDVN 1295
Cdd:PLN02430 211 PSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVD 253
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
2567-2828 |
5.63e-03 |
|
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: 41.87 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2567 DRPRFDSAARQLVARHAGLRtTVSPAgTDAASSGEVAVVHTAPIEPVVR--DHDDVRAAMRDQI---IDLTARPGIDFGV 2641
Cdd:cd19538 37 DVQALQQALYDVVERHESLR-TVFPE-EDGVPYQLILEEDEATPKLEIKevDEEELESEINEAVrypFDLSEEPPFRATL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2642 QTRGDGRTVVGISMDNTMLDGASMMIALSELDHLYRGETVDQLP---PLETSFAHYV-WNHPELLPDADEAvlPRLAASR 2717
Cdd:cd19538 115 FELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPelaPLPVQYADYAlWQQELLGDESDPD--SLIARQL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2718 DYWRARLPSLPpapklADMSLLFEIEEP-----RFERATATIPAVDWSQVTRSCRAEGVTVASFLLANYARVLSRW-SGT 2791
Cdd:cd19538 193 AYWKKQLAGLP-----DEIELPTDYPRPaessyEGGTLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLgAGT 267
|
250 260 270
....*....|....*....|....*....|....*...
gi 2181016861 2792 DhFCINVTLFDRDPDvvGIENVVGDF-TSLVLlecRVD 2828
Cdd:cd19538 268 D-IPIGSPVAGRNDD--SLEDLVGFFvNTLVL---RTD 299
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1496-1612 |
5.89e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 42.42 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 1496 WYRTGDMGCYWRDGTLQFLGRADSQVKIRGHRVECGEIEHALRGHPLVAAATVVPIHNCTALGAGI-VVTGSGAEQFDDS 1574
Cdd:PTZ00237 493 YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIgLLVLKQDQSNQSI 572
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2181016861 1575 TPGALRAHLAVRLPQYMIPKVFVS----CPELPLTANGKVDR 1612
Cdd:PTZ00237 573 DLNKLKNEINNIITQDIESLAVLRkiiiVNQLPKTKTGKIPR 614
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
2253-2333 |
6.46e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 38.41 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2253 VEVGSRTGLITERLTELVGVVVeeylCLEPNPTLAGIA--AGRRFPAPTRHVDA-----PDAAsgVDVVICCGSLHQLPD 2325
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVT----GVDISPEMLELAreKAPREGLTFVVGDAedlpfPDNS--FDLVLSSEVLHHVED 74
|
....*...
gi 2181016861 2326 AEAVLEAI 2333
Cdd:pfam08241 75 PERALREI 82
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
2252-2333 |
7.12e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 38.31 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 2252 VVEVGSRTGLITERLTELVGVvveEYLCLEPNPTLAGIA----AGRRFPAPTRHVDA---PDAASGVDVVICCGSLHQL- 2323
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGA---RVTGVDLSPEMLERAreraAEAGLNVEFVQGDAedlPFPDGSFDLVVSSGVLHHLp 77
|
90
....*....|.
gi 2181016861 2324 -PDAEAVLEAI 2333
Cdd:pfam13649 78 dPDLEAALREI 88
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1242-1284 |
7.25e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 41.89 E-value: 7.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2181016861 1242 VSDITAMIECAPTDPIRIDPH------DAAYVIYTSGSTGEPKGVLVSH 1284
Cdd:cd05938 118 VISLLDKVDAASDEPVPASLRahvtikSPALYIYTSGTTGLPKAARISH 166
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
167-566 |
8.91e-03 |
|
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: 41.40 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 167 DADHGEHVAFLQYSSGSTGKPKGVVNTHQSiLRQAAFAANVWNG--DDDMHMVSWLPLYHDMGifWGVFMPLLNGGCTTL 244
Cdd:cd05974 80 ENTHADDPMLLYFTSGTTSKPKLVEHTHRS-YPVGHLSTMYWIGlkPGDVHWNISSPGWAKHA--WSCFFAPWNAGATVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 245 IppHDFVR-NPRIWLETVSRFRGNWIGGPDFAYRRCIEAfdgtALQSLDLScLRLATNGAEPVRGTTLRDFTakfRAAGL 323
Cdd:cd05974 157 L--FNYARfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ----DLASFDVK-LREVVGAGEPLNPEVIEQVR---RAWGL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 324 --RDDvmapqYGLAE--AGLGVTGSQTVRVWveksfdadalergiavEVAQPNPadgrsralvscgdgafGWDIQIVDPD 399
Cdd:cd05974 227 tiRDG-----YGQTEttALVGNSPGQPVKAG----------------SMGRPLP----------------GYRVALLDPD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 400 RHmTLTDGEVG-EIWVGGP-GLPDGYWRQPEQTATTFGartadglGPYLRTGDAGFRYQ-GELYVCGRYRDLIIVGGRNH 476
Cdd:cd05974 270 GA-PATEGEVAlDLGDTRPvGLMKGYAGDPDKTAHAMR-------GGYYRTGDIAMRDEdGYLTYVGRADDVFKSSDYRI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 477 FPNDIEKTVEEaHCGVAPGgACAVQPDA-----PQAngewWLVLETGS-PVEDLD-DLSRILRRRILAHhetapERVVWV 549
Cdd:cd05974 342 SPFELESVLIE-HPAVAEA-AVVPSPDPvrlsvPKA----FIVLRAGYePSPETAlEIFRFSRERLAPY-----KRIRRL 410
|
410
....*....|....*..
gi 2181016861 550 PCRTLPTTTSGKIRRRE 566
Cdd:cd05974 411 EFAELPKTISGKIRRVE 427
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
373-568 |
9.24e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 41.62 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 373 PADGRSRALVSCGDGAFGWDIQIVDPDRHMTLTDGEV-GEIWVGGPGLPDGYWRQPeqtattfGARTADGLGPylrTGD- 450
Cdd:PRK07008 347 PLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKAfGDLQVRGPWVIDRYFRGD-------ASPLVDGWFP---TGDv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181016861 451 AGFRYQGELYVCGRYRDLIIVGGRNHFPNDIEkTVEEAHCGVAPGGACAVqpdapqANGEWW---LVLETGSPVEDLDdl 527
Cdd:PRK07008 417 ATIDADGFMQITDRSKDVIKSGGEWISSIDIE-NVAVAHPAVAEAACIAC------AHPKWDerpLLVVVKRPGAEVT-- 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2181016861 528 srilRRRILAHHE--TA----PERVVWVpcRTLPTTTSGKI---RRRETL 568
Cdd:PRK07008 488 ----REELLAFYEgkVAkwwiPDDVVFV--DAIPHTATGKLqklKLREQF 531
|
|
| |
