|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
367-1243 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 787.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 367 TQTDKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGKNKSHTPFGCFIDEPGLFDPRFFNM 446
Cdd:COG3321 1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 447 SPREAAQTDPMGRLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDDW--REINAAENVDTYYITGGVRAFAPGRI 524
Cdd:COG3321 81 SPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGS---RTGVFVGASSNDYalLLLADPEAIDAYALTGNAKSVLAGRI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 525 NYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCR 604
Cdd:COG3321 158 SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 605 GDACGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGD 684
Cdd:COG3321 238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 685 GIEMTSVTNVFaprRRQRKPEQTVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgELNktfPA-DLKDRN 763
Cdd:COG3321 318 PIEAAALTAAF---GQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFE-TPN---PHiDFENSP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 764 VHISLKQVDWPRkTEAPRKVFLNNFSAAGGNTALLIEDGPVHKMPNGVDPRSTLPITVTARSIGSLKRNLMNLQKYVAEN 843
Cdd:COG3321 391 FYVNTELRPWPA-GGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 844 GSTTLPSFSYTLTARRIQHNYRVAFPLADISKVADALEAQAKDSYSP-----VPMVTTKTAFCFTGQGSQYTGLGQKLYQ 918
Cdd:COG3321 470 PDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGMGRELYE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 919 DLKSFRDDIDQLDQMARIQGLPSFLELLDGTDVQTL--SPVKVQLGMACIQVALSRMWASWGVTPTAVIGHSLGEYAALH 996
Cdd:COG3321 550 TEPVFRAALDECDALLRPHLGWSLREVLFPDEEESRldRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAAC 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 997 VAGVISASDMVLLVGRRAELLVRecTPHTHGMLAVKGGVEAIRNAL-GINMTEIACINGPEETVLCGSSDVVAAANDTLG 1075
Cdd:COG3321 630 VAGVLSLEDALRLVAARGRLMQA--LPGGGAMLAVGLSEEEVEALLaGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1076 KNGFKATKLNVPFAFHSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIrDGGIITADYLARHARETVNFSSAL--L 1153
Cdd:COG3321 708 ARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWL-TGEALDADYWVRHLRQPVRFADAVeaL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1154 SGQKEAVFdektawLEVGAHPVCSGMVKASI---GTTITAPSLRRGEDAWKTISTSICHLFTAGVNFNFDEFHREFndAQ 1230
Cdd:COG3321 787 LADGVRVF------LEVGPGPVLTGLVRQCLaaaGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGR--GR 858
|
890
....*....|...
gi 1915400804 1231 ELLTLPTYSFDNK 1243
Cdd:COG3321 859 RRVPLPTYPFQRE 871
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
370-799 |
4.70e-174 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 537.91 E-value: 4.70e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 370 DKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGkNKSHTPFGCFIDEPGLFDPRFFNMSPR 449
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKP-GKTYTRRGGFLDDVDAFDAAFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 450 EAAQTDPMGRLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDDWREINA--AENVDTYYITGGVRAFAPGRINYY 527
Cdd:cd00833 80 EAEAMDPQQRLLLEVAWEALEDAGYSPESLAGS---RTGVFVGASSSDYLELLArdPDEIDAYAATGTSRAFLANRISYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 528 FKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCRGDA 607
Cdd:cd00833 157 FDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 608 CGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGDGIE 687
Cdd:cd00833 237 VGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 688 MTSVTNVFAPRRRQRKPeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgELNktfPA-DLKDRNVHI 766
Cdd:cd00833 317 VEALAKVFGGSRSADQP---LLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFE-TPN---PKiDFEESPLRV 389
|
410 420 430
....*....|....*....|....*....|...
gi 1915400804 767 SLKQVDWPRKTeAPRKVFLNNFSAAGGNTALLI 799
Cdd:cd00833 390 PTEARPWPAPA-GPRRAGVSSFGFGGTNAHVIL 421
|
|
| PT_fungal_PKS |
TIGR04532 |
iterative type I PKS product template domain; Sequences found by this model are the so-called ... |
1285-1604 |
2.73e-137 |
|
iterative type I PKS product template domain; Sequences found by this model are the so-called product template (PT) domain of various fungal iterative type I polyketide synthases. This domain resembles pfam14765, designated polyketide synthase dehydratase by Pfam, but members of that family are primarily bacterial, where type I PKS are predominantly modular, not iterative. The dehydratase active site residues well-conserved in pfam14765 (His in the first hot dog domain, Asp in the second hot dog domain) seem well conserved in this family also.
Pssm-ID: 275325 Cd Length: 324 Bit Score: 431.66 E-value: 2.73e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1285 STSCQNVISEEFDGNRATVVIRSNLADSKLYPVVCGHMVNNAALCPSSLYADMALTVGDYIYKELQP--GVETPGMNVCN 1362
Cdd:TIGR04532 1 TTSVHRVVEETSDGSKATVVFESDLSDPDLLAAIQGHRVNGVPLCPSSVYADMALTAAKYLLKRLRGskDAADVGLDVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1363 MEVPKPFIANiPQPAEGQHLEMEATADLDLGT-VSLKFRSVHPDGKKIQDHAFCTIRYED-KAVWASEWTRYNYMVKAQI 1440
Cdd:TIGR04532 81 MEVDKPLVAD-PSDSDPQLLRVTATADASTSSrVSISFSSSSSSGKKTEEHATCTVRFGDpAAAWLAEWSRTAYLVKSRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1441 DMLTARTMTGGAHKVQRGMAYKLFKALVNYDDKYRAMAEVVLDGANTEASAAIDFPTKPDDGDFYCPPYHIDGACHISGF 1520
Cdd:TIGR04532 160 DALRQSAKEGSAHRLSRRMAYKLFSSLVDYSPKYRGMQEVVLDSDGLEATATVKLPTDPPDGGFTVSPYWIDSLLHLAGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1521 IVNASDLLDSEQNVYVSHGWGAMKFSRPLVAGMKLRNYVRMVPQPNNISKGDVYIMEGDE-IVAVCEGIKFQQIPRKVLN 1599
Cdd:TIGR04532 240 IMNANDAVDSKDEVYINHGWGSLRFAEPLSPGKTYRSYVRMQPVEGGLYAGDVYVFDGDRkIVAVCGGIKFQRVPRRLLN 319
|
....*
gi 1915400804 1600 VFLPP 1604
Cdd:TIGR04532 320 RLLPP 324
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
372-801 |
5.58e-119 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 378.21 E-value: 5.58e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 372 IAIVGMAGRFPNSANHEALWDLLMKGLDvhrkvpadrfdadahcdpsgkgknkshtpfgcfidEPGLFDPRFFNMSPREA 451
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLD-----------------------------------DVDLFDAAFFGISPREA 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 452 AQTDPMGRLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDDWreinaaenvdtyyitggvrafapgrinyyfkfs 531
Cdd:smart00825 46 EAMDPQQRLLLEVAWEALEDAGIDPESLRGS---RTGVFVGVSSSDY--------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 532 gpSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCRGDACGTV 611
Cdd:smart00825 90 --SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 612 ILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQeflykqvlanagidaheisyvemhgtgtqagdgiemtsv 691
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 692 tnvfaprrrqrkpeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgELNktFPADLKDRNVHISLKQV 771
Cdd:smart00825 209 ----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFE-TPN--PHIDLEESPLRVPTELT 269
|
410 420 430
....*....|....*....|....*....|
gi 1915400804 772 DWPRkTEAPRKVFLNNFSAAGGNTALLIED 801
Cdd:smart00825 270 PWPP-PGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| SAT |
pfam16073 |
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit: ... |
5-242 |
2.85e-99 |
|
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit:ACP transacylase of the aflatoxin biosynthesis pathway. SAT selects the hexanoyl starter unit from a pair of specialized fungal fatty acid synthase subunits (HexA/HexB) and transfers it onto the polyketide synthase A acyl-carrier protein to prime polyketide chain elongation. The family is found in association with pfam02801, pfam00109, pfam00550, pfam00975, pfam00698.
Pssm-ID: 465005 Cd Length: 239 Bit Score: 319.16 E-value: 2.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 5 LLFGDQTAEQYPLLHRIVLRKDNVLLLSFVERCALALREETRTLSRSQREVMPDFLTLSNLIEAYYQKGEKVLMLESAFL 84
Cdd:pfam16073 1 LLFGDQTLDFLPGLRQLLRAKDNPLLASFLERAADALRAEISRLPRAERDSLPRFTSLQELLERYYASGDKNPALESALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 85 TIAQLGHYIGYFSENPSELPAVSDTRVLGLCTGLLAASAVVSAKTVEELAIVGVDFVRIAFRSGAVVDNVRSMLGQSSQD 164
Cdd:pfam16073 81 CIAQLGHFIDYLEENGEDYPSPSSTYLVGLCTGLLAAAAVSCSRSLSELVPLAVEAVRIAFRLGLLVQRVADRLEGSSSS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915400804 165 KSTWSTIISGPSEVDVKDALTSFHEASGIPRSNQAYVSAVSTMALTVSGPPITVERFFQESSLI-INHRVSIPIYGPYH 242
Cdd:pfam16073 161 PGSWSLVVPGLSEEEAEKALEQFNESKGIPPASRPYISAVSPSSVTISGPPSTLELLLSSSPAKkSLPKTPLPIYAPYH 239
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
370-619 |
5.34e-81 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 267.58 E-value: 5.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 370 DKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGKNKSHTPFGCfIDEPGLFDPRFFNMSPR 449
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 450 EAAQTDPMGRLALVTAYEALEMSGYVPNRSTSTKL-NRIGTFYGQTSDDWREINAAENVDTY-YITGGVRAFAPGRINYY 527
Cdd:pfam00109 80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTgVFIGSGIGDYAALLLLDEDGGPRRGSpFAVGTMPSVIAGRISYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 528 FKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCRGDA 607
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239
|
250
....*....|..
gi 1915400804 608 CGTVILKRYQDA 619
Cdd:pfam00109 240 VGAVVLKRLSDA 251
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
366-1280 |
3.95e-73 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 273.03 E-value: 3.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 366 RTQTDKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGKNKSHTPFGCFIDEPGlFDPRFFN 445
Cdd:TIGR02813 3 RLKDMPIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKSYCKRGGFLPEVD-FNPMEFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 446 MSPREAAQTDPMGRLALVTAYEALEMSGyVPNRSTSTKLN-RIGTFYGQ-----------------------TSDDWREI 501
Cdd:TIGR02813 82 LPPNILELTDISQLLSLVVAKEVLNDAG-LPDGYDRDKIGiTLGVGGGQkqssslnarlqypvlkkvfkasgVEDEDSEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 502 NAAENVDTYY------ITGGVRAFAPGRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPD 575
Cdd:TIGR02813 161 LIKKFQDQYIhweensFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 576 IFSGLSKGQFLSKTGGCKTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFL 655
Cdd:TIGR02813 241 MYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 656 YKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVFAPRRRQRkpeQTVHLGAIKANVGHAEAASGINSLVKVLMM 735
Cdd:TIGR02813 321 LKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQK---QHIALGSVKSQIGHTKSTAGTAGMIKAVLA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 736 MKNNKIPANVGVKGELNKTfpaDLKDRNVHISLKQVDW-PRKTEAPRKVFLNNFSAAGGNTALLIED-GPVHKMPNGVDP 813
Cdd:TIGR02813 398 LHHKVLPPTINVDQPNPKL---DIENSPFYLNTETRPWmQREDGTPRRAGISSFGFGGTNFHMVLEEySPKHQRDDQYRQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 814 RS---TLPITVTARS--IGSLKRNLMNLQKYvAENGSTTLPSF--SYTLTARRIQHNyRVAFPLAD----ISKVADA--- 879
Cdd:TIGR02813 475 RAvaqTLLFTAANEKalVSSLKDWKNKLSAK-ADDQPYAFNALavENTLRTIAVALA-RLGFVAKNadelITMLEQAitq 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 880 LEAQAKDSYSpVP-----------MVTTKTAFCFTGQGSQYTGLGQKLYQDLKSFRDDIDQLDQMARIQGLPSFLELL-- 946
Cdd:TIGR02813 553 LEAKSCEEWQ-LPsgisyrksalvVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLyp 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 947 ------DGTDVQ----TLSpVKVQLGMACIQVALSRMWASWGVTPTAVIGHSLGEYAALHVAGVISASDMVLLVGRRAEL 1016
Cdd:TIGR02813 632 ipvfndESRKAQeealTNT-QHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQA 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1017 LVRECTPHTHG-----MLAVKGGVEAIRNALG-INMTEIACINGPEETVLCGSSDVVAAANDTLGKNGFKATKLNVPFAF 1090
Cdd:TIGR02813 711 MAAPTGEADIGfmyavILAVVGSPTVIANCIKdFEGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAF 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1091 HSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIRDGGIITADYLARHARETVNFSSALlsgqkEAVFDEKT-AWLE 1169
Cdd:TIGR02813 791 HTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQL-----EAMYAAGArVFVE 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1170 VGAHPVCSGMV------KASIGTTITAPSLRRGeDAWKTISTSICHLFTAGVNF-NFDEFHREFNDAQEL------LTLP 1236
Cdd:TIGR02813 866 FGPKNILQKLVentlkdKENELCAISINPNPKG-DSDMQLRQAAVQLAVLGLELtEIDPYQAEKRPPAATspmnikLNAA 944
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 1915400804 1237 TY-SFDNKKYWLDYHNN-WTLTKGE-VQKTKEVIVEKEIVAPVI-EVP 1280
Cdd:TIGR02813 945 NYiSPATRKKMDDSLNDgWTIKQATsVPQVVEKIVEKIVEKERIvEVE 992
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1915-2172 |
4.60e-31 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 133.29 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1915 PSATSVLLQGNPKTATKKVFFLPDGSGSATSYVSI-PNIGPHVAAFGLNCPFMKDPEQWQCGIEvsSLI--YLAEIRRRQ 1991
Cdd:COG3319 586 AAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLaRALGPDRPVYGLQAPGLDGGEPPPASVE--EMAarYVEAIRAVQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1992 PKGPYIIGGWSAGGVIAYAVAQALLAAGEKVEKLLLLDSPCPVNLAPL--PTRLHVFFNEIG------------------ 2051
Cdd:COG3319 664 PEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPGALARLdeAELLAALLRDLArgvdlpldaeelraldpe 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 2052 ---------LLGTGDPAKTPKWLLPH----FSAAIRSLSAYDPKPTIAelPTYAVWCKDGVAGNPGDPrpppaeeedpap 2118
Cdd:COG3319 744 erlarllerLREAGLPAGLDAERLRRllrvFRANLRALRRYRPRPYDG--PVLLFRAEEDPPGRADDP------------ 809
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1915400804 2119 mkwllnhrtdfsDNGWAQLCGQNMKFGVMGGHHFSMMKDPHASELGQLIKEGIE 2172
Cdd:COG3319 810 ------------ALGWRPLVAGGLEVHDVPGDHFSMLREPHVAELAAALRAALA 851
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
388-798 |
4.00e-29 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 122.88 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 388 EALWDLLMKGLDVHRKVPadRFDAD-AHCDPSGKGKNKSHTPFGCFIDEP---GLFDPRFFNMSPREaaqtDPMGRLALV 463
Cdd:PTZ00050 10 ESTWEALIAGKSGIRKLT--EFPKFlPDCIPEQKALENLVAAMPCQIAAEvdqSEFDPSDFAPTKRE----SRATHFAMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 464 TAYEALEMSGYVPNRSTSTklNRIGTFYGQTSDDWREI-----NAAE----NVDTYYITGGVRAFAPGRINYYFKFSGPS 534
Cdd:PTZ00050 84 AAREALADAKLDILSEKDQ--ERIGVNIGSGIGSLADLtdemkTLYEkghsRVSPYFIPKILGNMAAGLVAIKHKLKGPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 535 YSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK------TGGCKTYDNDADGYCRGDAC 608
Cdd:PTZ00050 162 GSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkynddpQRASRPFDKDRAGFVMGEGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 609 GTVILKRYQDAVADKDNILGCILGAATnhSAEAVSITHPHA---GAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGDG 685
Cdd:PTZ00050 242 GILVLEELEHALRRGAKIYAEIRGYGS--SSDAHHITAPHPdgrGARRCMENALKDGANININDVDYVNAHATSTPIGDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 686 IEMTSVTNVFAPrrrqrKPEQTVHLGAIKANVGHA-EAASGINSLVKVlMMMKNNKIPANvgvkgeLNKTFPADLKDRNv 764
Cdd:PTZ00050 320 IELKAIKKVFGD-----SGAPKLYVSSTKGGLGHLlGAAGAVESIVTI-LSLYEQIIPPT------INLENPDAECDLN- 386
|
410 420 430
....*....|....*....|....*....|....
gi 1915400804 765 hisLKQVDWPRKTEAPRKVFLNNFSAAGGNTALL 798
Cdd:PTZ00050 387 ---LVQGKTAHPLQSIDAVLSTSFGFGGVNTALL 417
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1932-2075 |
2.18e-14 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 74.73 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1932 KVFFLPDGSGSATSYVSIPNIGPHVAAFgLNCPFMKD--PEQWQCGIEVSSLIYLAEIRRRQPKGPYIIGGWSAGGVIAY 2009
Cdd:pfam00975 2 PLFCFPPAGGSASSFRSLARRLPPPAEV-LAVQYPGRgrGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 2010 AVAQALLAAGEKVEKLLLLDSPCPVNLAPLPTR-------LHVFfneIGLLGTGDPAKTPKWLLPHFSAAIRS 2075
Cdd:pfam00975 81 EVARRLERQGEAVRSLFLSDASAPHTVRYEASRapdddevVAEF---TDEGGTPEELLEDEELLSMLLPALRA 150
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1811-1869 |
1.89e-13 |
|
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: 66.82 E-value: 1.89e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915400804 1811 RHIIAQEMGVDISEVTDDAELAEMGMDSLMSLTILGELREKTGIDLPGTFLMTNPTLVD 1869
Cdd:pfam00550 4 RELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1673-1734 |
5.94e-12 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 62.58 E-value: 5.94e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915400804 1673 DKVLTILSKETEVDVAELVDDAHFENLGVDSLLSLTISAIFREDLSMEISPSLFTDYPTVGE 1734
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1815-2032 |
1.86e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 70.07 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1815 AQEMGVDISEVtdDAELAEMGMDSLMSLTILGELREKTGIDL-PGTfLMTNPTLvdienalgmrpkpKAVGPKLSKPSTK 1893
Cdd:PRK10252 988 SSLLGCDVVDA--DADFFALGGHSLLAMKLAAQLSRQFARQVtPGQ-VMVASTV-------------AKLATLLDAEEDE 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1894 TDMNEVSSRLTainktdisqypsatsvLLQGNPKTatkkVFFLPDGSGSATSY-VSIPNIGPHVAAFGLNCPFMKDPEQW 1972
Cdd:PRK10252 1052 SRRLGFGTILP----------------LREGDGPT----LFCFHPASGFAWQFsVLSRYLDPQWSIYGIQSPRPDGPMQT 1111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915400804 1973 QCGIEVSSLIYLAEIRRRQPKGPYIIGGWSAGGVIAYAVAQALLAAGEKVEKLLLLDS-PC 2032
Cdd:PRK10252 1112 ATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTwPP 1172
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1667-1741 |
2.02e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 58.71 E-value: 2.02e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915400804 1667 PAGSMVDKVLTILSKETEVDVAELVDDAHFEN-LGVDSLLSLTISAIFREDLSMEISPSLFTDYPTVGEMKKYFSQ 1741
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1745-1882 |
5.14e-10 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 62.85 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1745 VESTTESEDDSDTDSLATTDVATPFDEMSTPASSAPSVPQSDAGKPSPDSPTGD-----SLSDDVGDVSIARHIIAQEMG 1819
Cdd:COG3433 154 DGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAaaspaPALETALTEEELRADVAELLG 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 1820 VDISEVTDDAELAEMGMDSLMSLTILGELReKTGIDLPGTFLMTNPTLVDIENALGMRPKPKA 1882
Cdd:COG3433 234 VDPEEIDPDDNLFDLGLDSIRLMQLVERWR-KAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1813-1874 |
5.92e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 57.56 E-value: 5.92e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 1813 IIAQEMGVDISEVTDDAEL-AEMGMDSLMSLTILGELREKTGIDLPGTFLMTNPTLVDIENAL 1874
Cdd:COG0236 13 IIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1811-1867 |
9.06e-09 |
|
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: 54.18 E-value: 9.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915400804 1811 RHIIAQEMGVDISEVTD-DAELAEMGMDSLMSLTILGELREKTGIDLPGTFLMTNPTL 1867
Cdd:smart00823 18 REQVAAVLGHAAAEAIDpDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTP 75
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1671-1735 |
6.62e-06 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.09 E-value: 6.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915400804 1671 MVDKVLTILSKETEVDVAELVD-DAHFENLGVDSLLSLTISAIFREDLSMEISPSLFTDYPTVGEM 1735
Cdd:smart00823 13 LLDLVREQVAAVLGHAAAEAIDpDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAAL 78
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
1321-1598 |
1.06e-05 |
|
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.
Pssm-ID: 434191 Cd Length: 296 Bit Score: 49.68 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1321 HMVNNAALCPSSLYADMALTVGDYIYKElQPGVEtpgmnVCNMEVPKPFIANipqpaEGQHLEM--EATADLDLGTVSLK 1398
Cdd:pfam14765 33 HRVGGTVVLPGAGYLEMALEAARQLFGG-SGAVA-----LRDVSILKALVLP-----EDDPVEVqtSLTPEEDGADSWWE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1399 FR--SVHPDGKKIQDHAFCTIRYEDKAVWASEWTRYnymVKAQIDMLTARTMTGGAHKVQRGMAYKLFkalvnYDDKYRA 1476
Cdd:pfam14765 102 FEifSRAGGGWEWTLHATGTVRLAPGEPAAPVDLES---LPARCAQPADPRSVSSAEFYERLAARGLF-----YGPAFQG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1477 MAEVVLDGANTEASAAIDFPTKPDDGDFYCPPYHIDGACHIsgFIVNASDLLDSEQNVYVSHGWGAMKFSRPLVAGMKLR 1556
Cdd:pfam14765 174 LRRIWRGDGEALAEARLPEAAAGGESPYLLHPALLDAALQL--LGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLW 251
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1915400804 1557 NYVRMVPQPNNISKGDVYIMEGD-EIVAVCEGIKFQQIPRKVL 1598
Cdd:pfam14765 252 VHARLERRGGRTIVGDLTLVDEDgRVVARIEGLRLRRVEREAL 294
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1983-2030 |
6.10e-04 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 43.37 E-value: 6.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1915400804 1983 YLAE-IRRRQPKGPYIIGGWSAGGVIAYAVAQALLAAGEKVEKLLLLDS 2030
Cdd:smart00824 52 AQAEaVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDT 100
|
|
| acpP |
PRK00982 |
acyl carrier protein; Provisional |
1813-1857 |
7.52e-03 |
|
acyl carrier protein; Provisional
Pssm-ID: 179197 [Multi-domain] Cd Length: 78 Bit Score: 37.46 E-value: 7.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1915400804 1813 IIAQEMGVDISEVTDDAELAE-MGMDSLMSLTILGELREKTGIDLP 1857
Cdd:PRK00982 11 IIVEQLGVDEEEVTPEASFVDdLGADSLDTVELVMALEEEFGIEIP 56
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
367-1243 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 787.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 367 TQTDKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGKNKSHTPFGCFIDEPGLFDPRFFNM 446
Cdd:COG3321 1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 447 SPREAAQTDPMGRLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDDW--REINAAENVDTYYITGGVRAFAPGRI 524
Cdd:COG3321 81 SPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGS---RTGVFVGASSNDYalLLLADPEAIDAYALTGNAKSVLAGRI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 525 NYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCR 604
Cdd:COG3321 158 SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 605 GDACGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGD 684
Cdd:COG3321 238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 685 GIEMTSVTNVFaprRRQRKPEQTVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgELNktfPA-DLKDRN 763
Cdd:COG3321 318 PIEAAALTAAF---GQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFE-TPN---PHiDFENSP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 764 VHISLKQVDWPRkTEAPRKVFLNNFSAAGGNTALLIEDGPVHKMPNGVDPRSTLPITVTARSIGSLKRNLMNLQKYVAEN 843
Cdd:COG3321 391 FYVNTELRPWPA-GGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 844 GSTTLPSFSYTLTARRIQHNYRVAFPLADISKVADALEAQAKDSYSP-----VPMVTTKTAFCFTGQGSQYTGLGQKLYQ 918
Cdd:COG3321 470 PDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPgvvtgAAAAAPKVAFLFPGQGSQYVGMGRELYE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 919 DLKSFRDDIDQLDQMARIQGLPSFLELLDGTDVQTL--SPVKVQLGMACIQVALSRMWASWGVTPTAVIGHSLGEYAALH 996
Cdd:COG3321 550 TEPVFRAALDECDALLRPHLGWSLREVLFPDEEESRldRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAAC 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 997 VAGVISASDMVLLVGRRAELLVRecTPHTHGMLAVKGGVEAIRNAL-GINMTEIACINGPEETVLCGSSDVVAAANDTLG 1075
Cdd:COG3321 630 VAGVLSLEDALRLVAARGRLMQA--LPGGGAMLAVGLSEEEVEALLaGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1076 KNGFKATKLNVPFAFHSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIrDGGIITADYLARHARETVNFSSAL--L 1153
Cdd:COG3321 708 ARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWL-TGEALDADYWVRHLRQPVRFADAVeaL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1154 SGQKEAVFdektawLEVGAHPVCSGMVKASI---GTTITAPSLRRGEDAWKTISTSICHLFTAGVNFNFDEFHREFndAQ 1230
Cdd:COG3321 787 LADGVRVF------LEVGPGPVLTGLVRQCLaaaGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGR--GR 858
|
890
....*....|...
gi 1915400804 1231 ELLTLPTYSFDNK 1243
Cdd:COG3321 859 RRVPLPTYPFQRE 871
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
370-799 |
4.70e-174 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 537.91 E-value: 4.70e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 370 DKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGkNKSHTPFGCFIDEPGLFDPRFFNMSPR 449
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKP-GKTYTRRGGFLDDVDAFDAAFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 450 EAAQTDPMGRLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDDWREINA--AENVDTYYITGGVRAFAPGRINYY 527
Cdd:cd00833 80 EAEAMDPQQRLLLEVAWEALEDAGYSPESLAGS---RTGVFVGASSSDYLELLArdPDEIDAYAATGTSRAFLANRISYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 528 FKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCRGDA 607
Cdd:cd00833 157 FDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 608 CGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGDGIE 687
Cdd:cd00833 237 VGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 688 MTSVTNVFAPRRRQRKPeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgELNktfPA-DLKDRNVHI 766
Cdd:cd00833 317 VEALAKVFGGSRSADQP---LLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFE-TPN---PKiDFEESPLRV 389
|
410 420 430
....*....|....*....|....*....|...
gi 1915400804 767 SLKQVDWPRKTeAPRKVFLNNFSAAGGNTALLI 799
Cdd:cd00833 390 PTEARPWPAPA-GPRRAGVSSFGFGGTNAHVIL 421
|
|
| PT_fungal_PKS |
TIGR04532 |
iterative type I PKS product template domain; Sequences found by this model are the so-called ... |
1285-1604 |
2.73e-137 |
|
iterative type I PKS product template domain; Sequences found by this model are the so-called product template (PT) domain of various fungal iterative type I polyketide synthases. This domain resembles pfam14765, designated polyketide synthase dehydratase by Pfam, but members of that family are primarily bacterial, where type I PKS are predominantly modular, not iterative. The dehydratase active site residues well-conserved in pfam14765 (His in the first hot dog domain, Asp in the second hot dog domain) seem well conserved in this family also.
Pssm-ID: 275325 Cd Length: 324 Bit Score: 431.66 E-value: 2.73e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1285 STSCQNVISEEFDGNRATVVIRSNLADSKLYPVVCGHMVNNAALCPSSLYADMALTVGDYIYKELQP--GVETPGMNVCN 1362
Cdd:TIGR04532 1 TTSVHRVVEETSDGSKATVVFESDLSDPDLLAAIQGHRVNGVPLCPSSVYADMALTAAKYLLKRLRGskDAADVGLDVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1363 MEVPKPFIANiPQPAEGQHLEMEATADLDLGT-VSLKFRSVHPDGKKIQDHAFCTIRYED-KAVWASEWTRYNYMVKAQI 1440
Cdd:TIGR04532 81 MEVDKPLVAD-PSDSDPQLLRVTATADASTSSrVSISFSSSSSSGKKTEEHATCTVRFGDpAAAWLAEWSRTAYLVKSRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1441 DMLTARTMTGGAHKVQRGMAYKLFKALVNYDDKYRAMAEVVLDGANTEASAAIDFPTKPDDGDFYCPPYHIDGACHISGF 1520
Cdd:TIGR04532 160 DALRQSAKEGSAHRLSRRMAYKLFSSLVDYSPKYRGMQEVVLDSDGLEATATVKLPTDPPDGGFTVSPYWIDSLLHLAGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1521 IVNASDLLDSEQNVYVSHGWGAMKFSRPLVAGMKLRNYVRMVPQPNNISKGDVYIMEGDE-IVAVCEGIKFQQIPRKVLN 1599
Cdd:TIGR04532 240 IMNANDAVDSKDEVYINHGWGSLRFAEPLSPGKTYRSYVRMQPVEGGLYAGDVYVFDGDRkIVAVCGGIKFQRVPRRLLN 319
|
....*
gi 1915400804 1600 VFLPP 1604
Cdd:TIGR04532 320 RLLPP 324
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
372-801 |
5.58e-119 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 378.21 E-value: 5.58e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 372 IAIVGMAGRFPNSANHEALWDLLMKGLDvhrkvpadrfdadahcdpsgkgknkshtpfgcfidEPGLFDPRFFNMSPREA 451
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLD-----------------------------------DVDLFDAAFFGISPREA 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 452 AQTDPMGRLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDDWreinaaenvdtyyitggvrafapgrinyyfkfs 531
Cdd:smart00825 46 EAMDPQQRLLLEVAWEALEDAGIDPESLRGS---RTGVFVGVSSSDY--------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 532 gpSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCRGDACGTV 611
Cdd:smart00825 90 --SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 612 ILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQeflykqvlanagidaheisyvemhgtgtqagdgiemtsv 691
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ--------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 692 tnvfaprrrqrkpeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgELNktFPADLKDRNVHISLKQV 771
Cdd:smart00825 209 ----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFE-TPN--PHIDLEESPLRVPTELT 269
|
410 420 430
....*....|....*....|....*....|
gi 1915400804 772 DWPRkTEAPRKVFLNNFSAAGGNTALLIED 801
Cdd:smart00825 270 PWPP-PGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| SAT |
pfam16073 |
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit: ... |
5-242 |
2.85e-99 |
|
Starter unit:ACP transacylase in aflatoxin biosynthesis; SAT is the N-terminal starter unit:ACP transacylase of the aflatoxin biosynthesis pathway. SAT selects the hexanoyl starter unit from a pair of specialized fungal fatty acid synthase subunits (HexA/HexB) and transfers it onto the polyketide synthase A acyl-carrier protein to prime polyketide chain elongation. The family is found in association with pfam02801, pfam00109, pfam00550, pfam00975, pfam00698.
Pssm-ID: 465005 Cd Length: 239 Bit Score: 319.16 E-value: 2.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 5 LLFGDQTAEQYPLLHRIVLRKDNVLLLSFVERCALALREETRTLSRSQREVMPDFLTLSNLIEAYYQKGEKVLMLESAFL 84
Cdd:pfam16073 1 LLFGDQTLDFLPGLRQLLRAKDNPLLASFLERAADALRAEISRLPRAERDSLPRFTSLQELLERYYASGDKNPALESALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 85 TIAQLGHYIGYFSENPSELPAVSDTRVLGLCTGLLAASAVVSAKTVEELAIVGVDFVRIAFRSGAVVDNVRSMLGQSSQD 164
Cdd:pfam16073 81 CIAQLGHFIDYLEENGEDYPSPSSTYLVGLCTGLLAAAAVSCSRSLSELVPLAVEAVRIAFRLGLLVQRVADRLEGSSSS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915400804 165 KSTWSTIISGPSEVDVKDALTSFHEASGIPRSNQAYVSAVSTMALTVSGPPITVERFFQESSLI-INHRVSIPIYGPYH 242
Cdd:pfam16073 161 PGSWSLVVPGLSEEEAEKALEQFNESKGIPPASRPYISAVSPSSVTISGPPSTLELLLSSSPAKkSLPKTPLPIYAPYH 239
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
901-1196 |
4.92e-97 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 315.50 E-value: 4.92e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 901 CFTGQGSQYTGLGQKLYQDLKSFRDDIDQLDQMARIQGLPSFLELLDGTDVQT--LSPVKVQLGMACIQVALSRMWASWG 978
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAAslLDTEVAQPALFAVQVALARLLRSWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 979 VTPTAVIGHSLGEYAALHVAGVISASDMVLLVGRRAELLVRecTPHTHGMLAVKGGVEAIRNALG--INMTEIACINGPE 1056
Cdd:smart00827 81 VRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQA--LPGGGAMLAVGLSEEEVEPLLAgvPDRVSVAAVNSPS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1057 ETVLCGSSDVVAAANDTLGKNGFKATKLNVPFAFHSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIRDGGIITAD 1136
Cdd:smart00827 159 SVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELDDAD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915400804 1137 YLARHARETVNFSSALlsgqkEAVFDEK--TAWLEVGAHPVCSGMVKASI---GTTITAPSLRRG 1196
Cdd:smart00827 239 YWVRNLREPVRFADAV-----RALLAEGgvTVFLEVGPHPVLTGPIKQTLaaaGSAVVLPSLRRG 298
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
370-619 |
5.34e-81 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 267.58 E-value: 5.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 370 DKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGKNKSHTPFGCfIDEPGLFDPRFFNMSPR 449
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 450 EAAQTDPMGRLALVTAYEALEMSGYVPNRSTSTKL-NRIGTFYGQTSDDWREINAAENVDTY-YITGGVRAFAPGRINYY 527
Cdd:pfam00109 80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTgVFIGSGIGDYAALLLLDEDGGPRRGSpFAVGTMPSVIAGRISYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 528 FKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCRGDA 607
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239
|
250
....*....|..
gi 1915400804 608 CGTVILKRYQDA 619
Cdd:pfam00109 240 VGAVVLKRLSDA 251
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
366-1280 |
3.95e-73 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 273.03 E-value: 3.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 366 RTQTDKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPADRFDADAHCDPSGKGKNKSHTPFGCFIDEPGlFDPRFFN 445
Cdd:TIGR02813 3 RLKDMPIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDDYYDSDKSEADKSYCKRGGFLPEVD-FNPMEFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 446 MSPREAAQTDPMGRLALVTAYEALEMSGyVPNRSTSTKLN-RIGTFYGQ-----------------------TSDDWREI 501
Cdd:TIGR02813 82 LPPNILELTDISQLLSLVVAKEVLNDAG-LPDGYDRDKIGiTLGVGGGQkqssslnarlqypvlkkvfkasgVEDEDSEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 502 NAAENVDTYY------ITGGVRAFAPGRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPD 575
Cdd:TIGR02813 161 LIKKFQDQYIhweensFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 576 IFSGLSKGQFLSKTGGCKTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFL 655
Cdd:TIGR02813 241 MYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 656 YKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVFAPRRRQRkpeQTVHLGAIKANVGHAEAASGINSLVKVLMM 735
Cdd:TIGR02813 321 LKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQK---QHIALGSVKSQIGHTKSTAGTAGMIKAVLA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 736 MKNNKIPANVGVKGELNKTfpaDLKDRNVHISLKQVDW-PRKTEAPRKVFLNNFSAAGGNTALLIED-GPVHKMPNGVDP 813
Cdd:TIGR02813 398 LHHKVLPPTINVDQPNPKL---DIENSPFYLNTETRPWmQREDGTPRRAGISSFGFGGTNFHMVLEEySPKHQRDDQYRQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 814 RS---TLPITVTARS--IGSLKRNLMNLQKYvAENGSTTLPSF--SYTLTARRIQHNyRVAFPLAD----ISKVADA--- 879
Cdd:TIGR02813 475 RAvaqTLLFTAANEKalVSSLKDWKNKLSAK-ADDQPYAFNALavENTLRTIAVALA-RLGFVAKNadelITMLEQAitq 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 880 LEAQAKDSYSpVP-----------MVTTKTAFCFTGQGSQYTGLGQKLYQDLKSFRDDIDQLDQMARIQGLPSFLELL-- 946
Cdd:TIGR02813 553 LEAKSCEEWQ-LPsgisyrksalvVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLyp 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 947 ------DGTDVQ----TLSpVKVQLGMACIQVALSRMWASWGVTPTAVIGHSLGEYAALHVAGVISASDMVLLVGRRAEL 1016
Cdd:TIGR02813 632 ipvfndESRKAQeealTNT-QHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQA 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1017 LVRECTPHTHG-----MLAVKGGVEAIRNALG-INMTEIACINGPEETVLCGSSDVVAAANDTLGKNGFKATKLNVPFAF 1090
Cdd:TIGR02813 711 MAAPTGEADIGfmyavILAVVGSPTVIANCIKdFEGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAF 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1091 HSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIRDGGIITADYLARHARETVNFSSALlsgqkEAVFDEKT-AWLE 1169
Cdd:TIGR02813 791 HTPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQL-----EAMYAAGArVFVE 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1170 VGAHPVCSGMV------KASIGTTITAPSLRRGeDAWKTISTSICHLFTAGVNF-NFDEFHREFNDAQEL------LTLP 1236
Cdd:TIGR02813 866 FGPKNILQKLVentlkdKENELCAISINPNPKG-DSDMQLRQAAVQLAVLGLELtEIDPYQAEKRPPAATspmnikLNAA 944
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 1915400804 1237 TY-SFDNKKYWLDYHNN-WTLTKGE-VQKTKEVIVEKEIVAPVI-EVP 1280
Cdd:TIGR02813 945 NYiSPATRKKMDDSLNDgWTIKQATsVPQVVEKIVEKIVEKERIvEVE 992
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
896-1181 |
1.81e-48 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 176.09 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 896 TKTAFCFTGQGSQYTGLGQKLYQDLKSFRDDIDQLDQMAriqGLPsFLELLDGTDVQTLS-PVKVQLGMACIQVALSRMW 974
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEAL---GYD-LSALCFEGPEEELNlTENTQPAILAASVAAYRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 975 ASWGVTPTAVIGHSLGEYAALHVAGVISASDMVLLVGRRAELLVRECTPHTHGMLAVKGG----VEAIRNALGINMT-EI 1049
Cdd:COG0331 77 EEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGPGGMAAVLGLddeeVEALCAEAAQGEVvEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1050 ACINGPEETVLCGSSDVVAAANDTLGKNGFK-ATKLNVPFAFHSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIR 1128
Cdd:COG0331 157 ANYNSPGQIVISGEKEAVEAAAELAKEAGAKrAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 1129 DGGIItADYLARHARETVNFSSALLSGQKEAVfdekTAWLEVGAHPVCSGMVK 1181
Cdd:COG0331 237 DPEEI-RELLVRQLTSPVRWDESVEALAEAGV----TTFVELGPGKVLSGLVK 284
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
372-799 |
6.06e-46 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 171.95 E-value: 6.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 372 IAIVGMAGRFPNSANHEALWDLLMKGldVHRKVPADRFDADAhcdpsgkgknkshtpFGCFIDEPGLFDPRFFNMSPREA 451
Cdd:cd00834 3 VVITGLGAVTPLGNGVEEFWEALLAG--RSGIRPITRFDASG---------------FPSRIAGEVPDFDPEDYLDRKEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 452 AQTDPMGRLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDDWREInaaENVDTYYITGGVRAFAPGRINY----- 526
Cdd:cd00834 66 RRMDRFAQFALAAAEEALADAGLDPEELDPE---RIGVVIGSGIGGLATI---EEAYRALLEKGPRRVSPFFVPMalpnm 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 527 -------YFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK-----TGGCKT 594
Cdd:cd00834 140 aagqvaiRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrnddpEKASRP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 595 YDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATnhSAEAVSITHPH---AGAQEFLyKQVLANAGIDAHEIS 671
Cdd:cd00834 220 FDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGA--SSDAYHITAPDpdgEGAARAM-RAALADAGLSPEDID 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 672 YVEMHGTGTQAGDGIEMTSVTNVFAPRRRQrkpeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgEL 751
Cdd:cd00834 297 YINAHGTSTPLNDAAESKAIKRVFGEHAKK------VPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLE-EP 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1915400804 752 NKTFPADLkdrnVHIslkqvdwpRKTEAPRKVFLNNFSAAGG-NTALLI 799
Cdd:cd00834 370 DPECDLDY----VPN--------EAREAPIRYALSNSFGFGGhNASLVF 406
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
900-1216 |
1.80e-44 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 164.95 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 900 FCFTGQGSQYTGLGQKLYQDLKSFRDDIDQLDQ-MARIQGLpSFLELLDGTDVQTLSPV-KVQLGMACIQVALSRMWASW 977
Cdd:pfam00698 2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEaFKPQYGF-SVSDVLRNNPEGTLDGTqFVQPALFAMQIALAALLQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 978 GVTPTAVIGHSLGEYAALHVAGVISASDMVLLVGRRAELLVRECTPhtHGMLAVKGGVEAIRNALGINMTeIACINGPEE 1057
Cdd:pfam00698 81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGP--GGMAAVELSAEEVEQRWPDDVV-GAVVNSPRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1058 TVLCGSSDVVAAANDTLGKNGFKATKLNVPFAFHSAQVDPILDEFRKVASSVTFNKPSVPILSpLVGIVIRDGGIITADY 1137
Cdd:pfam00698 158 VVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFIS-STSIDPSDQRTLSAEY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1138 LARHARETVNFSSALLSgqkeAVFDEKTAWLEVGAHPVCSGMV------KASIGTTITAPSLRRGEDAW-KTISTSICHL 1210
Cdd:pfam00698 237 WVRNLRSPVRFAEAILS----AAEPGPLVFIEISPHPLLLAALidtlksASDGKVATLVGTLIRDQTDFlVTFLYILAVA 312
|
....*.
gi 1915400804 1211 FTAGVN 1216
Cdd:pfam00698 313 HLTGSA 318
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
372-799 |
9.26e-43 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 162.57 E-value: 9.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 372 IAIVGMAGRFPNSANHEALWDLLMKGldVHRKVPADRFDADAHcdpsgkgknksHTPFGCFIDEpglFDPRFFnMSPREA 451
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAG--RSGIRPITRFDASGL-----------PVRIAGEVKD---FDPEEY-LDRKEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 452 AQTDPMGRLALVTAYEALEMSGYVPNRSTStklNRIGTFYGQTSDDWREInaAENVDTYYiTGGVRAFAP---------- 521
Cdd:COG0304 66 RRMDRFTQYALAAAREALADAGLDLDEVDP---DRTGVIIGSGIGGLDTL--EEAYRALL-EKGPRRVSPffvpmmmpnm 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 522 --GRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK-----TGGCKT 594
Cdd:COG0304 140 aaGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrnddpEKASRP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 595 YDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATnhSAEAVSITHPH---AGAQEFLyKQVLANAGIDAHEIS 671
Cdd:COG0304 220 FDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGA--SSDAYHITAPApdgEGAARAM-RAALKDAGLSPEDID 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 672 YVEMHGTGTQAGDGIEMTSVTNVFAPRRRQrkpeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGvkgel 751
Cdd:COG0304 297 YINAHGTSTPLGDAAETKAIKRVFGDHAYK------VPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTIN----- 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1915400804 752 nktfpadLKDRNVHISLKQVdwPRKT-EAPRKVFLNNFSAAGG-NTALLI 799
Cdd:COG0304 366 -------LENPDPECDLDYV--PNEArEAKIDYALSNSFGFGGhNASLVF 406
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
627-748 |
2.51e-37 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 136.93 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 627 LGCILGAATNHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVFAPRRRqrkpEQ 706
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGAR----KQ 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1915400804 707 TVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVK 748
Cdd:pfam02801 77 PLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
459-799 |
5.44e-36 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 140.85 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 459 RLALVTAYEALEMSGYVPNRSTSTklnRIGTFYGQTSDD----WREINAAENVDTYYITGGVRAFAPGRINYYFKFSGPS 534
Cdd:cd00825 13 ILGFEAAERAIADAGLSREYQKNP---IVGVVVGTGGGSprfqVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 535 YSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGGCKTYDNDADGYCRGDACGTVILK 614
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 615 RYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNV 694
Cdd:cd00825 170 ELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 695 FAPRRRQrkpeqtvhLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVkgelnktfpADLKDRNVHISLKQVDwp 774
Cdd:cd00825 250 FGDKSPA--------VSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHI---------EELDEAGLNIVTETTP-- 310
|
330 340
....*....|....*....|....*
gi 1915400804 775 rktEAPRKVFLNNFSAAGGNTALLI 799
Cdd:cd00825 311 ---RELRTALLNGFGLGGTNATLVL 332
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1915-2172 |
4.60e-31 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 133.29 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1915 PSATSVLLQGNPKTATKKVFFLPDGSGSATSYVSI-PNIGPHVAAFGLNCPFMKDPEQWQCGIEvsSLI--YLAEIRRRQ 1991
Cdd:COG3319 586 AAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLaRALGPDRPVYGLQAPGLDGGEPPPASVE--EMAarYVEAIRAVQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1992 PKGPYIIGGWSAGGVIAYAVAQALLAAGEKVEKLLLLDSPCPVNLAPL--PTRLHVFFNEIG------------------ 2051
Cdd:COG3319 664 PEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPGALARLdeAELLAALLRDLArgvdlpldaeelraldpe 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 2052 ---------LLGTGDPAKTPKWLLPH----FSAAIRSLSAYDPKPTIAelPTYAVWCKDGVAGNPGDPrpppaeeedpap 2118
Cdd:COG3319 744 erlarllerLREAGLPAGLDAERLRRllrvFRANLRALRRYRPRPYDG--PVLLFRAEEDPPGRADDP------------ 809
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1915400804 2119 mkwllnhrtdfsDNGWAQLCGQNMKFGVMGGHHFSMMKDPHASELGQLIKEGIE 2172
Cdd:COG3319 810 ------------ALGWRPLVAGGLEVHDVPGDHFSMLREPHVAELAAALRAALA 851
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
429-799 |
1.77e-30 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 126.40 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 429 FGCFIDEPGLFDPRF------FNMSPREAAQT---DPMGRLALVTAYEALEMSGYvpNRSTSTKLNRIGTFYGQTSDDWR 499
Cdd:cd00828 35 IAPVARLKSRFDRGVagqiptGDIPGWDAKRTgivDRTTLLALVATEEALADAGI--TDPYEVHPSEVGVVVGSGMGGLR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 500 EI-----NAAENVDTYYITGG--VRAFAPGRINYYFKFS-GPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVL 571
Cdd:cd00828 113 FLrrggkLDARAVNPYVSPKWmlSPNTVAGWVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 572 TnPDIFSGLSKGQFLSKT-----GGCKTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITH 646
Cdd:cd00828 193 L-EEGLSGFANMGALSTAeeepeEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 647 PHAGAQEFLyKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVFAPRRRQrkpeqtVHLGAIKANVGHAEAASGI 726
Cdd:cd00828 272 GGKGIARAI-RTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAGALGAP------LPVTAQKALFGHSKGAAGA 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 727 NSLVKVLMMMKNNKIPANVGVKGelnktFPADLKDRNVHISLKqvDWPRKTEAprkVFLNNFSAAGGNTALLI 799
Cdd:cd00828 345 LQLIGALQSLEHGLIPPTANLDD-----VDPDVEHLSVVGLSR--DLNLKVRA---ALVNAFGFGGSNAALVL 407
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
896-1181 |
8.39e-30 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 121.42 E-value: 8.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 896 TKTAFCFTGQGSQYTGLGQKLYQDLKSFRDDIDQLDQmarIQGLpSFLELLDGTDVQTLSPVK-VQLGMACIQVALSRMW 974
Cdd:TIGR00128 1 MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASE---ALGY-DLKKLCQEGPAEELNKTQyTQPALYVVSAILYLKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 975 A-SWGVTPTAVIGHSLGEYAALHVAGVISASDMVLLVGRRAELLVRECTPHTHGMLAVKG-GVEAIRNAL---GINMTEI 1049
Cdd:TIGR00128 77 KeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPEGGGAMAAVIGlDEEQLAQACeeaTENDVDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1050 ACINGPEETVLCGSSDVVAAANDTLGKNGFK-ATKLNVPFAFHSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIR 1128
Cdd:TIGR00128 157 ANFNSPGQVVISGTKDGVEAAAALFKEMGAKrAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 1129 DGGIITaDYLARHARETVNFSSALLSGQKEAVfdekTAWLEVGAHPVCSGMVK 1181
Cdd:TIGR00128 237 NGDRIK-EKLSEQLTSPVRWTDSVEKLMARGV----TEFAEVGPGKVLTGLIK 284
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
388-798 |
4.00e-29 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 122.88 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 388 EALWDLLMKGLDVHRKVPadRFDAD-AHCDPSGKGKNKSHTPFGCFIDEP---GLFDPRFFNMSPREaaqtDPMGRLALV 463
Cdd:PTZ00050 10 ESTWEALIAGKSGIRKLT--EFPKFlPDCIPEQKALENLVAAMPCQIAAEvdqSEFDPSDFAPTKRE----SRATHFAMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 464 TAYEALEMSGYVPNRSTSTklNRIGTFYGQTSDDWREI-----NAAE----NVDTYYITGGVRAFAPGRINYYFKFSGPS 534
Cdd:PTZ00050 84 AAREALADAKLDILSEKDQ--ERIGVNIGSGIGSLADLtdemkTLYEkghsRVSPYFIPKILGNMAAGLVAIKHKLKGPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 535 YSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK------TGGCKTYDNDADGYCRGDAC 608
Cdd:PTZ00050 162 GSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkynddpQRASRPFDKDRAGFVMGEGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 609 GTVILKRYQDAVADKDNILGCILGAATnhSAEAVSITHPHA---GAQEFLYKQVLANAGIDAHEISYVEMHGTGTQAGDG 685
Cdd:PTZ00050 242 GILVLEELEHALRRGAKIYAEIRGYGS--SSDAHHITAPHPdgrGARRCMENALKDGANININDVDYVNAHATSTPIGDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 686 IEMTSVTNVFAPrrrqrKPEQTVHLGAIKANVGHA-EAASGINSLVKVlMMMKNNKIPANvgvkgeLNKTFPADLKDRNv 764
Cdd:PTZ00050 320 IELKAIKKVFGD-----SGAPKLYVSSTKGGLGHLlGAAGAVESIVTI-LSLYEQIIPPT------INLENPDAECDLN- 386
|
410 420 430
....*....|....*....|....*....|....
gi 1915400804 765 hisLKQVDWPRKTEAPRKVFLNNFSAAGGNTALL 798
Cdd:PTZ00050 387 ---LVQGKTAHPLQSIDAVLSTSFGFGGVNTALL 417
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
367-745 |
1.21e-23 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 106.24 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 367 TQTDKIAIVGMAGRFPNSANHEALWDLLMKGLDVHRKVPAdrFDADAHCDPSGkGKNKSHTPfgcfiDEPGLFDPRFFnM 446
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTD--FPVGDLATKIG-GQVPDLAE-----DAEAGFDPDRY-L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 447 SPREAAQTDPMGRLALVTAYEALEMSGYVPNrsTSTKLNRIGTFYGQTSDDWREInaAENVDTYYITGGVRA-------- 518
Cdd:PRK06333 72 DPKDQRKMDRFILFAMAAAKEALAQAGWDPD--TLEDRERTATIIGSGVGGFPAI--AEAVRTLDSRGPRRLspftipsf 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 519 ---FAPGRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSG------LSKGQFLSKT 589
Cdd:PRK06333 148 ltnMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGfaaaraLSTRFNDAPE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 590 GGCKTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATnhSAEAVSITHPH---AGAQEFLyKQVLANAGID 666
Cdd:PRK06333 228 QASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGT--SADAYHMTAGPedgEGARRAM-LIALRQAGIP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 667 AHEISYVEMHGTGTQAGDGIEMTSVTNVFAPRRrqrkpeqTVHLGAIKANVGHA-EAASGINSLVKVLmMMKNNKIPANV 745
Cdd:PRK06333 305 PEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVS-------GLAVSSTKSATGHLlGAAGGVEAIFTIL-ALRDQIAPPTL 376
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
405-742 |
6.02e-21 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 97.94 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 405 PADRFDADAHCdpsgkgknkshTPFGCFIDEpglFDPRFFnMSPREAAQTDPMGRLALVTAYEALEMSGYVPNRSTStkl 484
Cdd:PRK07314 35 PITHFDTSDLA-----------VKIAGEVKD---FNPDDY-MSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENA--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 485 NRIGTFYGQTSDDWREInaAENVDTYYiTGGVRA----FAPGRI--------NYYFKFSGPSYSIDTACSSSLAAIQLAC 552
Cdd:PRK07314 97 DRIGVIIGSGIGGLETI--EEQHITLL-EKGPRRvspfFVPMAIinmaaghvSIRYGAKGPNHSIVTACATGAHAIGDAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 553 TSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK-----TGGCKTYDNDADGYCRGDACGTVILKRYQDAVADKDNIL 627
Cdd:PRK07314 174 RLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrnddpERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 628 GCILGAAtnHSAEAVSITHPH---AGAQEFLyKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVF---APRrrq 701
Cdd:PRK07314 254 AEVVGYG--MTGDAYHMTAPApdgEGAARAM-KLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFgehAYK--- 327
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1915400804 702 rkpeqtVHLGAIKANVGHA-EAASGINSLVKVLmMMKNNKIP 742
Cdd:PRK07314 328 ------VAVSSTKSMTGHLlGAAGAVEAIFSVL-AIRDQVIP 362
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
436-800 |
4.64e-20 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 95.10 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 436 PGLFDP-RFFNMSPREAAQTdpmGRLALVTAYEALEMSGYVPNRStstklNRIGTFYGQTSddwreINAAENVDTYYITG 514
Cdd:PRK07103 61 DSLALPeRLDAKLLRRASLS---AQAALAAAREAWRDAALGPVDP-----DRIGLVVGGSN-----LQQREQALVHETYR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 515 GVRAFAP-------------GRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACA-GGLNVLTNPDIFSGL 580
Cdd:PRK07103 128 DRPAFLRpsyglsfmdtdlvGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAvGALMDLSYWECQALR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 581 SKGQFLSKTGG------CKTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATNHSAEavSITHPHAGAQEF 654
Cdd:PRK07103 208 SLGAMGSDRFAdepeaaCRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDAN--RGPDPSLEGEMR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 655 LYKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVFAPRRRqrkpeqtvhLGAIKANVGHAEAASGINSLVKVLM 734
Cdd:PRK07103 286 VIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGLAHAW---------INATKSLTGHGLSAAGIVELIATLL 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915400804 735 MMKNNKIPANvgvkgeLNKTFPADLkdrnvhislkQVDWPRKTEAPR--KVFLNNFSAAGG-NTALLIE 800
Cdd:PRK07103 357 QMRAGFLHPS------RNLDEPIDE----------RFRWVGSTAESAriRYALSLSFGFGGiNTALVLE 409
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
520-725 |
9.90e-19 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 91.39 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 520 APGRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK------TGGCK 593
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfnscpTEASR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 594 TYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATnhSAEAVSITHPHA-GAQEFL-YKQVLANAGIDAHEIS 671
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGM--SGDAHHITQPHEdGRGAVLaMTRALQQSGLHPNQVD 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1915400804 672 YVEMHGTGTQAGDGIEMTSVTNVFAprrrQRKPEQTVHLGAIKANVGHAEAASG 725
Cdd:PLN02836 321 YVNAHATSTPLGDAVEARAIKTVFS----EHATSGGLAFSSTKGATGHLLGAAG 370
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
527-799 |
1.17e-18 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 90.67 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 527 YFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDI--FSGLskgQFLSKtGGCKTYDNDADGYCR 604
Cdd:PRK09185 146 YLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLngFNSL---ESLSP-QPCRPFSANRDGINI 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 605 GDACGTVILKRyqdavADKDNILgcILGAATNHSAEAVSITHPH-AGAQEFLyKQVLANAGIDAHEISYVEMHGTGTQAG 683
Cdd:PRK09185 222 GEAAAFFLLER-----EDDAAVA--LLGVGESSDAHHMSAPHPEgLGAILAM-QQALADAGLAPADIGYINLHGTATPLN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 684 DGIEMTSVTNVFAPrrrqrkpeqTVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVkGELNKTFPADLKDRN 763
Cdd:PRK09185 294 DAMESRAVAAVFGD---------GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNT-GQPDPALPPLYLVEN 363
|
250 260 270
....*....|....*....|....*....|....*.
gi 1915400804 764 VHislkqvdwprkTEAPRKVFLNNFsAAGGNTALLI 799
Cdd:PRK09185 364 AQ-----------ALAIRYVLSNSF-AFGGNNCSLI 387
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
514-743 |
3.56e-18 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 86.34 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 514 GGVRAFAPGRINYYFKFS-GPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTnpdifsglskgqflsktggc 592
Cdd:cd00327 40 SGEFSGAAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFV-------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 593 ktydndadgycRGDACGTVILKRYQDAVADKDNILGCILGAATnHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISY 672
Cdd:cd00327 100 -----------FGDGAAAAVVESEEHALRRGAHPQAEIVSTAA-TFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDY 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915400804 673 VEMHGTGTQAGDGIEMTSVTNVFAPRrrqrkpeqTVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPA 743
Cdd:cd00327 168 VEAHGTGTPIGDAVELALGLDPDGVR--------SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP 230
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
371-800 |
1.37e-17 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 87.75 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 371 KIAIVGMAGRFPNSANHEALWDLLMKGLDvhRKVPADRFDAdahcdpsgkgkNKSHTPFGCFIDEpglFDPRFFnMSPRE 450
Cdd:PRK08722 5 RVVVTGMGMLSPVGNTVESSWKALLAGQS--GIVNIEHFDT-----------TNFSTRFAGLVKD---FNCEEY-MSKKD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 451 AAQTDPMGRLALVTAYEALEMSGYvpnRSTSTKLNRIGTFYGQTSDDWREINAAEN---------VDTYYITGGVRAFAP 521
Cdd:PRK08722 68 ARKMDLFIQYGIAAGIQALDDSGL---EVTEENAHRIGVAIGSGIGGLGLIEAGHQalvekgprkVSPFFVPSTIVNMIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 522 GRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTG-----GCKTYD 596
Cdd:PRK08722 145 GNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNdepqkASRPWD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 597 NDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVEMH 676
Cdd:PRK08722 225 KDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 677 GTGTQAGDGIEMTSVTnvfapRRRQRKPEQTVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVkgelnktfp 756
Cdd:PRK08722 305 GTSTPAGDVAEIKGIK-----RALGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINL--------- 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1915400804 757 aDLKDRNVHISLKQVDwPRKTEAPRKVFLNNFSAAGGNTALLIE 800
Cdd:PRK08722 371 -DDPEEGLDIDLVPHT-ARKVESMEYAICNSFGFGGTNGSLIFK 412
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
453-799 |
1.38e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 84.27 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 453 QTDPMGRLAL--VTAYE-ALEMSGYVPNRSTSTklNRIGTFYGQTSDDWREINAAENVDTYYITGGVRA---------FA 520
Cdd:PRK09116 66 KIRSMGRVSLmaTRASElALEDAGLLGDPILTD--GRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITAttyvrmmphTT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 521 PGRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPD--IFSGL----SKGQFLSKTGgcKT 594
Cdd:PRK09116 144 AVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEaaVFDTLfatsTRNDAPELTP--RP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 595 YDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATNhsAEAVSITHPHAGAQEFLYKQVLANAGIDAHEISYVE 674
Cdd:PRK09116 222 FDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTN--SDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 675 MHGTGTQAGDGIEMTSVTNVFAPRrrqrkpeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKipanvgvkgelnkt 754
Cdd:PRK09116 300 AHGTATDRGDIAESQATAAVFGAR---------MPISSLKSYFGHTLGACGALEAWMSIEMMNEGW-------------- 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1915400804 755 FPADLKDRNVHISLKQVDW----PRKTEApRKVFLNNFSAAGGNTALLI 799
Cdd:PRK09116 357 FAPTLNLTQVDPACGALDYimgeAREIDT-EYVMSNNFAFGGINTSLIF 404
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
532-798 |
1.05e-15 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 82.72 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 532 GPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK-----TGGCKTYDNDADGYCRGD 606
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrnddpTKASRPWDMNRDGFVMGE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 607 ACGTVILKRYQDAVADKDNILGCILGAAtnHSAEAVSITHPHA-GAQEFL-YKQVLANAGIDAHEISYVEMHGTGTQAGD 684
Cdd:PLN02787 362 GAGVLLLEELEHAKKRGANIYAEFLGGS--FTCDAYHMTEPHPeGAGVILcIEKALAQSGVSKEDVNYINAHATSTKAGD 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 685 GIEMTSVTNVFAprrrqRKPEQTVHlgAIKANVGHAEAASGINSLVKVLMMMKNNKIPANvgvkgeLNKTFPADLKDRNV 764
Cdd:PLN02787 440 LKEYQALMRCFG-----QNPELRVN--STKSMIGHLLGAAGAVEAIATVQAIRTGWVHPN------INLENPESGVDTKV 506
|
250 260 270
....*....|....*....|....*....|....*
gi 1915400804 765 HISlkqvdwPRKTEAPRKVFL-NNFSAAGGNTALL 798
Cdd:PLN02787 507 LVG------PKKERLDIKVALsNSFGFGGHNSSIL 535
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
536-742 |
4.01e-15 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 80.06 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 536 SIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDI---FSGLSKgqfLSK-----TGGCKTYDNDADGYCRGDA 607
Cdd:PRK06501 170 SLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEAlirFSLLSA---LSTqndppEKASKPFSKDRDGFVMAEG 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 608 CGTVILKRYQDAVADKDNILGCILGAA--------TNHSAEAVSIThphaGAqeflYKQVLANAGIDAHEISYVEMHGTG 679
Cdd:PRK06501 247 AGALVLESLESAVARGAKILGIVAGCGekadsfhrTRSSPDGSPAI----GA----IRAALADAGLTPEQIDYINAHGTS 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 680 TQAGDGIEMTSVTNVFAPRRRQrkpeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIP 742
Cdd:PRK06501 319 TPENDKMEYLGLSAVFGERLAS------IPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLP 375
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
865-1181 |
2.02e-14 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 77.11 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 865 RVAFPLADISKVADALEAQAKDsYSPvpmvttKTAFCFTGQGSQYTGLGQklyqDLKSFRDDIDQLDQMARIQGLpSFLE 944
Cdd:PLN02752 14 SRVSMSVSVGSQATAADALFAD-YKP------TTAFLFPGQGAQAVGMGK----EAAEVPAAKALFDKASEILGY-DLLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 945 L--------LDGTDVQtlSPVKVQLGMACIQVALSRMWASWGVTPTAV-IGHSLGEYAALHVAGVISASDMVLLVGRRAE 1015
Cdd:PLN02752 82 VcvngpkekLDSTVVS--QPAIYVASLAAVEKLRARDGGQAVIDSVDVcAGLSLGEYTALVFAGALSFEDGLKLVKLRGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1016 LLVRECTPHTHGMLAVKG--------GVEAIRNALG-INMTEIACINGPEETVLCGSSDVVAAANdTLGKNgFKA---TK 1083
Cdd:PLN02752 160 AMQAAADAGPSGMVSVIGldsdkvqeLCAAANEEVGeDDVVQIANYLCPGNYAVSGGKKGIDAVE-AKAKS-FKArmtVR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1084 LNVPFAFHSAQVDPILDEFRKVASSVTFNKPSVPILSPLVGIVIRDGGIITaDYLARHARETVNFSS---ALLSGQKEAV 1160
Cdd:PLN02752 238 LAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVDAQPHSDPATIK-KILARQVTSPVQWETtvkTLLEKGLEKS 316
|
330 340
....*....|....*....|.
gi 1915400804 1161 FdektawlEVGAHPVCSGMVK 1181
Cdd:PLN02752 317 Y-------ELGPGKVIAGIVK 330
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1932-2075 |
2.18e-14 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 74.73 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1932 KVFFLPDGSGSATSYVSIPNIGPHVAAFgLNCPFMKD--PEQWQCGIEVSSLIYLAEIRRRQPKGPYIIGGWSAGGVIAY 2009
Cdd:pfam00975 2 PLFCFPPAGGSASSFRSLARRLPPPAEV-LAVQYPGRgrGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 2010 AVAQALLAAGEKVEKLLLLDSPCPVNLAPLPTR-------LHVFfneIGLLGTGDPAKTPKWLLPHFSAAIRS 2075
Cdd:pfam00975 81 EVARRLERQGEAVRSLFLSDASAPHTVRYEASRapdddevVAEF---TDEGGTPEELLEDEELLSMLLPALRA 150
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
439-742 |
2.82e-14 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 77.47 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 439 FDPRFFnMSPREAAQTDPMGRLALVTAYEALEMSGYVPNRSTStklNRIGTFYGQTsddwreINAAENVDTYYI---TGG 515
Cdd:PRK08439 55 FDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDA---ERFGVSSASG------IGGLPNIEKNSIicfEKG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 516 VRAFAP------------GRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKG 583
Cdd:PRK08439 125 PRKISPffipsalvnmlgGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 584 QFLSKTG-----GCKTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAAtnHSAEAVSITHPHAGAQEFLYKQ 658
Cdd:PRK08439 205 KALSTRNddpkkASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFG--ESGDANHITSPAPEGPLRAMKA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 659 VLANAGIDahEISYVEMHGTGTQAGDGIEMTSVTNVFAPRrrqrkpEQTVHLGAIKANVGHAEAASGINSLVKVLMMMKN 738
Cdd:PRK08439 283 ALEMAGNP--KIDYINAHGTSTPYNDKNETAALKELFGSK------EKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRD 354
|
....
gi 1915400804 739 NKIP 742
Cdd:PRK08439 355 GILP 358
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1811-1869 |
1.89e-13 |
|
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: 66.82 E-value: 1.89e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1915400804 1811 RHIIAQEMGVDISEVTDDAELAEMGMDSLMSLTILGELREKTGIDLPGTFLMTNPTLVD 1869
Cdd:pfam00550 4 RELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
540-771 |
2.03e-13 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 74.32 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 540 ACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSKTGgCKTYDNDADGYCRGDACGTVILKRYQDA 619
Cdd:PRK05952 145 ACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAELA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 620 VADKDNILGCILGAATNHSAEAVSITHP-HAGAQEFLyKQVLANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVFAPR 698
Cdd:PRK05952 224 QKRGAKIYGQILGFGLTCDAYHMSAPEPdGKSAIAAI-QQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFPHR 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 699 rrqrkpeqtVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGVKgelNKTFPADLKDRNVHISLKQV 771
Cdd:PRK05952 303 ---------VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ---EPEFDLNFVRQAQQSPLQNV 363
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
528-741 |
5.26e-13 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 73.55 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 528 FKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVL--TNPDIFSGLskGQFLSK-----TGGCKTYDNDAD 600
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELdwEMSCLFDAM--GALSTKyndtpEKASRAYDANRD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 601 GYCRGDACGTVILKRYQDAVADKDNILGCILG-AATNHSAEAVSithPHAGAQEFLYKQVLAnaGIDaHEISYVEMHGTG 679
Cdd:PRK07967 227 GFVIAGGGGVVVVEELEHALARGAKIYAEIVGyGATSDGYDMVA---PSGEGAVRCMQMALA--TVD-TPIDYINTHGTS 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915400804 680 TQAGDGIEMTSVTNVFAprrrqrkpEQTVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKI 741
Cdd:PRK07967 301 TPVGDVKELGAIREVFG--------DKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFI 354
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1673-1734 |
5.94e-12 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 62.58 E-value: 5.94e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1915400804 1673 DKVLTILSKETEVDVAELVDDAHFENLGVDSLLSLTISAIFREDLSMEISPSLFTDYPTVGE 1734
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
519-748 |
1.18e-11 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 68.60 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 519 FAPGRINYYFKFSGPSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFLSK------TGGC 592
Cdd:PRK14691 69 LAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfnstpEKAS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 593 KTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATnhSAEAVSIThphAGAQE-----FLYKQVLANAGIDA 667
Cdd:PRK14691 149 RPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGT--SADAYHMT---SGAEDgdgayRAMKIALRQAGITP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 668 HEISYVEMHGTGTQAGDGIEMTSVTNVFAprrrqrkPEQTVHLGAIKANVGHAEAASGINSLVKVLMMMKNNKIPANVGV 747
Cdd:PRK14691 224 EQVQHLNAHATSTPVGDLGEINAIKHLFG-------ESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNL 296
|
.
gi 1915400804 748 K 748
Cdd:PRK14691 297 E 297
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1815-2032 |
1.86e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 70.07 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1815 AQEMGVDISEVtdDAELAEMGMDSLMSLTILGELREKTGIDL-PGTfLMTNPTLvdienalgmrpkpKAVGPKLSKPSTK 1893
Cdd:PRK10252 988 SSLLGCDVVDA--DADFFALGGHSLLAMKLAAQLSRQFARQVtPGQ-VMVASTV-------------AKLATLLDAEEDE 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1894 TDMNEVSSRLTainktdisqypsatsvLLQGNPKTatkkVFFLPDGSGSATSY-VSIPNIGPHVAAFGLNCPFMKDPEQW 1972
Cdd:PRK10252 1052 SRRLGFGTILP----------------LREGDGPT----LFCFHPASGFAWQFsVLSRYLDPQWSIYGIQSPRPDGPMQT 1111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915400804 1973 QCGIEVSSLIYLAEIRRRQPKGPYIIGGWSAGGVIAYAVAQALLAAGEKVEKLLLLDS-PC 2032
Cdd:PRK10252 1112 ATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTwPP 1172
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
446-797 |
1.22e-10 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 65.91 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 446 MSPREAAQTDPMGRLALVTAYEALEMSGyVPNRSTSTKLNRIGTFYGQTS------DDWREinaaenvdtyyitGGVRAF 519
Cdd:PRK07910 72 LTRVELRRMSYLQRMSTVLGRRVWENAG-SPEVDTNRLMVSIGTGLGSAEelvfayDDMRA-------------RGLRAV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 520 APGRINYYFKfSGPSYSID-------------TACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTNPDIFSGLSKGQFL 586
Cdd:PRK07910 138 SPLAVQMYMP-NGPAAAVGlerhakagvitpvSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 587 SKT------GGCKTYDNDADGYCRGDACGTVILKRYQDAVADKDNILGCILGAATNHSAEAVSITHPHAGAQEFLYKQVL 660
Cdd:PRK07910 217 MSTnnddpaGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 661 ANAGIDAHEISYVEMHGTGTQAGDGIEMTSVTNVFAPRRrqrkpeQTVHlgAIKANVGHAEAASGINSLVKVLMMMKNNK 740
Cdd:PRK07910 297 ELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGGHR------PAVY--APKSALGHSVGAVGAVESILTVLALRDGV 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915400804 741 IPANvgvkgeLNktfpadLKDRNVHISLKQV-DWPRKTEApRKVFLNNFSAAGGNTAL 797
Cdd:PRK07910 369 IPPT------LN------LENLDPEIDLDVVaGEPRPGNY-RYAINNSFGFGGHNVAL 413
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1667-1741 |
2.02e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 58.71 E-value: 2.02e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915400804 1667 PAGSMVDKVLTILSKETEVDVAELVDDAHFEN-LGVDSLLSLTISAIFREDLSMEISPSLFTDYPTVGEMKKYFSQ 1741
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1745-1882 |
5.14e-10 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 62.85 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1745 VESTTESEDDSDTDSLATTDVATPFDEMSTPASSAPSVPQSDAGKPSPDSPTGD-----SLSDDVGDVSIARHIIAQEMG 1819
Cdd:COG3433 154 DGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAaaspaPALETALTEEELRADVAELLG 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 1820 VDISEVTDDAELAEMGMDSLMSLTILGELReKTGIDLPGTFLMTNPTLVDIENALGMRPKPKA 1882
Cdd:COG3433 234 VDPEEIDPDDNLFDLGLDSIRLMQLVERWR-KAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1813-1874 |
5.92e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 57.56 E-value: 5.92e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915400804 1813 IIAQEMGVDISEVTDDAEL-AEMGMDSLMSLTILGELREKTGIDLPGTFLMTNPTLVDIENAL 1874
Cdd:COG0236 13 IIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1780-2040 |
1.86e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1780 PSVPQSDAGK------PSPDSPTGDSLSDDVGDVSIARHIIAQE-MGVDISEVTDDaeLAEMGMDSLMSLTILGELREKT 1852
Cdd:PRK12467 3573 AAMPLGPNGKvdrkalPDPDAKGSREYVAPRSEVEQQLAAIWADvLGVEQVGVTDN--FFELGGDSLLALQVLSRIRQSL 3650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1853 GIDLPGTFLMTNPTLVDIENALGmrpkpkavgpklskpstktDMNEVSSRLTAINKTdisqypsatsvllqgnpKTATKK 1932
Cdd:PRK12467 3651 GLKLSLRDLMSAPTIAELAGYSP-------------------LGDVPVNLLLDLNRL-----------------ETGFPA 3694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1933 VFFLPDGSGSATSYVSIPNIGP-HVAAFGLNCPFMKDpEQWQ-CGIEVSSLIYLAEIRRRQPKGPYIIGGWSAGGVIAYA 2010
Cdd:PRK12467 3695 LFCRHEGLGTVFDYEPLAVILEgDRHVLGLTCRHLLD-DGWQdTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARL 3773
|
250 260 270
....*....|....*....|....*....|
gi 1915400804 2011 VAQALLAAGEKVEKLLLLDSPCPVNLAPLP 2040
Cdd:PRK12467 3774 VAELLEREGESEAFLGLFDNTLPLPDEFVP 3803
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1811-1867 |
9.06e-09 |
|
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: 54.18 E-value: 9.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915400804 1811 RHIIAQEMGVDISEVTD-DAELAEMGMDSLMSLTILGELREKTGIDLPGTFLMTNPTL 1867
Cdd:smart00823 18 REQVAAVLGHAAAEAIDpDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTP 75
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1671-1735 |
6.62e-06 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 46.09 E-value: 6.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915400804 1671 MVDKVLTILSKETEVDVAELVD-DAHFENLGVDSLLSLTISAIFREDLSMEISPSLFTDYPTVGEM 1735
Cdd:smart00823 13 LLDLVREQVAAVLGHAAAEAIDpDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAAL 78
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
1321-1598 |
1.06e-05 |
|
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.
Pssm-ID: 434191 Cd Length: 296 Bit Score: 49.68 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1321 HMVNNAALCPSSLYADMALTVGDYIYKElQPGVEtpgmnVCNMEVPKPFIANipqpaEGQHLEM--EATADLDLGTVSLK 1398
Cdd:pfam14765 33 HRVGGTVVLPGAGYLEMALEAARQLFGG-SGAVA-----LRDVSILKALVLP-----EDDPVEVqtSLTPEEDGADSWWE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1399 FR--SVHPDGKKIQDHAFCTIRYEDKAVWASEWTRYnymVKAQIDMLTARTMTGGAHKVQRGMAYKLFkalvnYDDKYRA 1476
Cdd:pfam14765 102 FEifSRAGGGWEWTLHATGTVRLAPGEPAAPVDLES---LPARCAQPADPRSVSSAEFYERLAARGLF-----YGPAFQG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1477 MAEVVLDGANTEASAAIDFPTKPDDGDFYCPPYHIDGACHIsgFIVNASDLLDSEQNVYVSHGWGAMKFSRPLVAGMKLR 1556
Cdd:pfam14765 174 LRRIWRGDGEALAEARLPEAAAGGESPYLLHPALLDAALQL--LGAALPAEAEHADQAYLPVGIERLRIYRSLPPGEPLW 251
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1915400804 1557 NYVRMVPQPNNISKGDVYIMEGD-EIVAVCEGIKFQQIPRKVL 1598
Cdd:pfam14765 252 VHARLERRGGRTIVGDLTLVDEDgRVVARIEGLRLRRVEREAL 294
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
533-567 |
3.94e-04 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 45.16 E-value: 3.94e-04
10 20 30
....*....|....*....|....*....|....*
gi 1915400804 533 PSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGG 567
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGG 110
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1983-2030 |
6.10e-04 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 43.37 E-value: 6.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1915400804 1983 YLAE-IRRRQPKGPYIIGGWSAGGVIAYAVAQALLAAGEKVEKLLLLDS 2030
Cdd:smart00824 52 AQAEaVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGIPPAAVVLLDT 100
|
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| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
533-573 |
1.11e-03 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 43.76 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1915400804 533 PSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGGLNVLTN 573
Cdd:TIGR01930 75 PAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSR 115
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| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
533-567 |
2.50e-03 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 42.75 E-value: 2.50e-03
10 20 30
....*....|....*....|....*....|....*
gi 1915400804 533 PSYSIDTACSSSLAAIQLACTSLWAGDCDTACAGG 567
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGG 114
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| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1984-2107 |
3.21e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 41.14 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915400804 1984 LAEIRRRQPKGPYIIGGWSAGGVIAYAVAqalLAAGEKVEKLLLLDSpcpvnlapLPTRLHvffneigllgtgDPAKTPK 2063
Cdd:COG0596 79 LAALLDALGLERVVLVGHSMGGMVALELA---ARHPERVAGLVLVDE--------VLAALA------------EPLRRPG 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1915400804 2064 WLLPHFSAAIRSLSAYDPKPTIAEL--PTYAVWCKDGVAGNPGDPR 2107
Cdd:COG0596 136 LAPEALAALLRALARTDLRERLARItvPTLVIWGEKDPIVPPALAR 181
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|
| acpP |
PRK00982 |
acyl carrier protein; Provisional |
1813-1857 |
7.52e-03 |
|
acyl carrier protein; Provisional
Pssm-ID: 179197 [Multi-domain] Cd Length: 78 Bit Score: 37.46 E-value: 7.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1915400804 1813 IIAQEMGVDISEVTDDAELAE-MGMDSLMSLTILGELREKTGIDLP 1857
Cdd:PRK00982 11 IIVEQLGVDEEEVTPEASFVDdLGADSLDTVELVMALEEEFGIEIP 56
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