|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
93-1122 |
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: 1142.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 93 NEPVAVIGVGCRFPGdIDGPERLWDFLTEKKCAITAYPD-----------RGFTNAGTFAESGGFLKDVAGFDNRFFDIP 161
Cdd:COG3321 3 DEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPAdrwdadayydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 162 PDEALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVSASAQQkSTIWDNTGGSSSIIANRISYF 241
Cdd:COG3321 82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEA-IDAYALTGNAKSVLAGRISYK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 242 LDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEG 321
Cdd:COG3321 161 LDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 322 CGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIE 401
Cdd:COG3321 241 VGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 402 AHALGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEW 481
Cdd:COG3321 321 AAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRPW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 482 PvVAGRPRRAGVSSFGFGGTNAHVIVEEAGSVgadtvsgRADVGGSGGGVVAWVISGKTASALAAQAGRLGRYVRARPAL 561
Cdd:COG3321 401 P-AGGGPRRAGVSSFGFGGTNAHVVLEEAPAA-------APAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 562 DVVDVGYSLVSTRSVFDHRAVVVGQTRDELLAGLAGVVAGRPEAGVVCGVGKPAGKTAFVFAGQGSQWLGMGSELYAAYP 641
Cdd:COG3321 473 DLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEP 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 642 VFAEALDAVVDELDRHLRYPLRDVIWGHD-QDLLNTTEFAQPALFAVEVALYRLLMSWGVRPGLVLGHSVGELAAAHVAG 720
Cdd:COG3321 553 VFRAALDECDALLRPHLGWSLREVLFPDEeESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAG 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 721 ALCLPDAAMLVAARGRLMQALPAGGAMFAVQAREDEVAPMLG--HDVSIAAVNGPASVVISGAHDAVSAIADRLRGQGRR 798
Cdd:COG3321 633 VLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAgyDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIR 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 799 VHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVADDFASADYWARHIRAVVRFGDSVRSAHCAGAS 878
Cdd:COG3321 713 ARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALDADYWVRHLRQPVRFADAVEALLADGVR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 879 RFIEVGPGGGLTSLIEASLADAQ-IVSVPTLRKDRPEPVSVMTAAAQGFVSGMGLDWASVFSGYRPKRVELPTYAFQHQk 957
Cdd:COG3321 793 VFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQRE- 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 958 FWLAPAPSVSDPTAAGQIGASDGGAELLASSGFAARLAGRSADEQLAAAIEVVCEHAAAVLGRDGAAGLDAGQAFADSGF 1037
Cdd:COG3321 872 DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAA 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1038 NSLSAVELRNRLTAVTAVTLPATAIFDHPTPTELAQYLITQIDGHGSSAAAAANPAERIDALTDLFLQACDAGRDADGWK 1117
Cdd:COG3321 952 AAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAA 1031
|
....*
gi 624288879 1118 MVALA 1122
Cdd:COG3321 1032 AAALA 1036
|
|
| mycolic_Pks13 |
NF040607 |
polyketide synthase Pks13; |
16-971 |
0e+00 |
|
polyketide synthase Pks13;
Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 709.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 16 EVSLDVPIRDLGLKSIDVLAIPGDLGDRFGFCIPDLAVWDNPSANDLIDSLLNQRsaDSLRESHGHADRNTQGRGSINEP 95
Cdd:NF040607 24 QITDDRPMEEFGLSSRDAVALSGDIEDLTGVTLTATVAYQHPTIASLATRIIEGE--PEVAADDDDDADWSRRPRSDAHD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 96 VAVIGVGCRFPGDIDGPERLWDFLTEKKCAITAYP-DR--GFTNAGTFAES-------GGFLKDVAGFDNRFFDIPPDEA 165
Cdd:NF040607 102 IAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPeGRwsEFAADPRIAERvakantrGGYLDDIKGFDAEFFALSPLEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 166 LRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYvRLVSASAQQKSTIWDNTGGSSSIIANRISYFLDIQ 245
Cdd:NF040607 182 ENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDY-QMLAVADPAEAHPYALTGTSSSIIANRVSYFFDFR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 246 GPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFRE-AGILSQTGCCHAFDKSADGMVRGEGCGV 324
Cdd:NF040607 261 GPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 325 IVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHA 404
Cdd:NF040607 341 VVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 405 LGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEWPVV 484
Cdd:NF040607 421 LGRVVGRGRDADKPALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRY 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 485 AGRPrRAGVSSFGFGGTNAHVIVEE----------------------AGSVGADTVSGRADVGGSGGGVVA------WVI 536
Cdd:NF040607 501 SGHA-VAGVSGFGFGGTNAHVVVREvlpadlvepeaqpdedteaelaGLTAEAKRLLAEAELAAEFAPAAPegpvvpLPV 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 537 SGKTASALAAQAGRLGRYVRARP--ALDVVDVGYSLvSTRSVFDHRAVVVGQTRDELLAGLAGVVAGRPEAGVVCGVGkP 614
Cdd:NF040607 580 SGFLPSRRRAAAADLADWLESEEgrATPLADVARAL-ARRNHGRSRAVVLAHTHEEAIKGLRAVAEGKPGPGVFSADA-P 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 615 AGKTA-FVFAGQGSQWLGMGSELYAAYPVFAEALDAvVDEL-DRHLRYPLRDVIWGHDQDLlnTTEFAQPALFAVEVALY 692
Cdd:NF040607 658 AANGPvWVLSGFGSQHRKMAKQLYLENPVFAARIDE-VDELvQDESGYSIVELILDDEQTY--DIETAQVGIFAIQIALA 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 693 RLLMSWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLM----QALPAG--GAMFAVQAREDEVAPMLGH--D 764
Cdd:NF040607 735 DLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgegeAMLPGDdiRLMALVEYSAEEIETVLADfpD 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 765 VSIAAVNGPASVVISGAHDAVSAIADRLRGQGRRVHRLAVSHAFHSALMEPMIAEFtavAAELSvGL----PTIPVISNV 840
Cdd:NF040607 815 LEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHTSQMDPLLGEL---AAELA-GIepqpLTVGLYSSV 890
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 841 -------TGQLVADDfasADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGP------GGGLTSLiEASLADAQIvsVPT 907
Cdd:NF040607 891 drgtfyrPGHEPIHD---VDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPnpvalmSVAATTF-AAGLHDAQL--IPT 964
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624288879 908 LRKDRPEPVSVMTAAAQGFVSGMGLDWASVFSgyRPKRVELPTYAFQHQKFWLAPAPSVSDPTA 971
Cdd:NF040607 965 LKRKEDESESVLNALAQLYVHGHDVDLRSLFG--AGDYADIPRTRFKRKPYWLDARPSSGGGSG 1026
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
94-507 |
0e+00 |
|
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: 616.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 94 EPVAVIGVGCRFPGDIDgPERLWDFLTEKKCAITAYPDRGFTNAGTFAES----------GGFLKDVAGFDNRFFDIPPD 163
Cdd:cd00833 1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPgkpgktytrrGGFLDDVDAFDAAFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 164 EALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVSASAQQKSTiWDNTGGSSSIIANRISYFLD 243
Cdd:cd00833 80 EAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDA-YAATGTSRAFLANRISYFFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 244 IQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEGCG 323
Cdd:cd00833 159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 324 VIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAH 403
Cdd:cd00833 239 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 404 ALGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEWPv 483
Cdd:cd00833 319 ALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWP- 397
|
410 420
....*....|....*....|....
gi 624288879 484 VAGRPRRAGVSSFGFGGTNAHVIV 507
Cdd:cd00833 398 APAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
96-509 |
3.62e-154 |
|
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: 467.19 E-value: 3.62e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 96 VAVIGVGCRFPGdIDGPERLWDFLTEKkcaitaypdrgftnagtfaesggfLKDVAGFDNRFFDIPPDEALRMDPQQRLL 175
Cdd:smart00825 1 IAIVGMSCRFPG-ADDPEEFWDLLLAG------------------------LDDVDLFDAAFFGISPREAEAMDPQQRLL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 176 LEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYvrlvsasaqqkstiwdntggsssiianrisyfldiqgpSIVIDTAC 255
Cdd:smart00825 56 LEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY--------------------------------------SVTVDTAC 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 256 SSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEGCGVIVLQRLSDARL 335
Cdd:smart00825 98 SSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 336 EGRRILAILTGSAVNQDGKSNGIMAPNPSAQigvlenacksarvdpleigyveahgtgtslgdrieahalgmvfgrkrpg 415
Cdd:smart00825 178 DGDPILAVIRGSAVNQDGRSNGITAPSGPAQ------------------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 416 sgpLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEWPvVAGRPRRAGVSS 495
Cdd:smart00825 209 ---LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWP-PPGRPRRAGVSS 284
|
410
....*....|....
gi 624288879 496 FGFGGTNAHVIVEE 509
Cdd:smart00825 285 FGFGGTNAHVILEE 298
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
95-933 |
2.41e-100 |
|
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: 355.85 E-value: 2.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 95 PVAVIGVGCRFpGDIDGPERLWDFLTEKKCAITAYPDRGF-----------TNAGTFAESGGFLKDVaGFDNRFFDIPPD 163
Cdd:TIGR02813 8 PIAIVGMASIF-ANSRYLNKFWDLIFEKIDAITDVPSDHWakddyydsdksEADKSYCKRGGFLPEV-DFNPMEFGLPPN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 164 EALRMDPQQRLLLEVSWEALEHAGIiPESLRLSRTGVFVGV------SSTDYVRL--------VSASA------------ 217
Cdd:TIGR02813 86 ILELTDISQLLSLVVAKEVLNDAGL-PDGYDRDKIGITLGVgggqkqSSSLNARLqypvlkkvFKASGvededsemlikk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 218 -QQKSTIWDNT---GGSSSIIANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGG 293
Cdd:TIGR02813 165 fQDQYIHWEENsfpGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 294 FREAGILSQTGCCHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENA 373
Cdd:TIGR02813 245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 374 CKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLL 453
Cdd:TIGR02813 325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 454 PSGGFTEPNPAIPFTELGLRVVDELQEW-PVVAGRPRRAGVSSFGFGGTNAHVIVEEAGSVGAdtvsgRADVGGSGGGVV 532
Cdd:TIGR02813 405 PTINVDQPNPKLDIENSPFYLNTETRPWmQREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQ-----RDDQYRQRAVAQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 533 AWVISGKTASALAAQAGRLGRYVRARPALDVVD-----VGYSLvSTRSVFDHRAVVVGQTRDELLAGLAGVVA------- 600
Cdd:TIGR02813 480 TLLFTAANEKALVSSLKDWKNKLSAKADDQPYAfnalaVENTL-RTIAVALARLGFVAKNADELITMLEQAITqleaksc 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 601 ---------GRPEAGVVCGvgkpAGKTAFVFAGQGSQWLGMGSELYAAYPVFAEALDAVVDELDRH-------LRYPL-- 662
Cdd:TIGR02813 559 eewqlpsgiSYRKSALVVE----SGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAgkgalspVLYPIpv 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 663 --RDVIWGHDQDLLNtTEFAQPALFAVEVALYRLLMSWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLMQA 740
Cdd:TIGR02813 635 fnDESRKAQEEALTN-TQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 741 LPA---GGAMFAVQAREDEVAPMLGH------DVSIAAVNGPASVVISGAHDAVSAIADRLRGQGRRVHRLAVSHAFHSA 811
Cdd:TIGR02813 714 PTGeadIGFMYAVILAVVGSPTVIANcikdfeGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTP 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 812 LMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVADDFAS-ADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGPGGGLT 890
Cdd:TIGR02813 794 LVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAiKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQ 873
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 624288879 891 SLIEASLADAQ----IVSV-PTLRKDRPEpvSVMTAAAQGFVSGMGLD 933
Cdd:TIGR02813 874 KLVENTLKDKEnelcAISInPNPKGDSDM--QLRQAAVQLAVLGLELT 919
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
94-333 |
4.23e-91 |
|
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: 294.93 E-value: 4.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 94 EPVAVIGVGCRFPGDIDgPERLWDFLTEKKCAITAYPDRGF----------TNAGTFAESGGFLKDVAGFDNRFFDIPPD 163
Cdd:pfam00109 1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADRWdpdklydppsRIAGKIYTKWGGLDDIFDFDPLFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 164 EALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVSAS-AQQKSTIW-DNTGGSSSIIANRISYF 241
Cdd:pfam00109 80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDeDGGPRRGSpFAVGTMPSVIAGRISYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 242 LDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEG 321
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239
|
250
....*....|..
gi 624288879 322 CGVIVLQRLSDA 333
Cdd:pfam00109 240 VGAVVLKRLSDA 251
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1154-1380 |
3.42e-51 |
|
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: 179.73 E-value: 3.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1154 ICIPTLTVLSDQREYRDIANAMTGRHSVYSLTLPGFDSSDALPQNADMIVETVSNAIIDVVGGScRFVLSGYSSGGVLAY 1233
Cdd:smart00824 1 ICFPSTAAPSGPHEYARLAAALRGRRDVSALPLPGFGPGEPLPASADALVEAQAEAVLRAAGGR-PFVLVGHSSGGLLAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1234 ALCSHLSvKHQRNPLGVALIDTYLPSQIAnpsmNEGFSPndtgkGLSREVIRVARMLNRLTATRLTAAATYAAIFQAWEP 1313
Cdd:smart00824 80 AVAARLE-ARGIPPAAVVLLDTYPPGDPA----PEGWLP-----ELLRGVFEREDSFVPMDDARLTAMGAYLRLFGGWTP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 624288879 1314 GRSMAPVLNIVAKDRIAtveNLREERINRWRTaAAEAAYSVAEVPGDHFGMMSTSSEAIATEIHDWI 1380
Cdd:smart00824 150 GPVAAPTLLVRASEPLA---EWPDEDPDGWRA-HWPLPHTVVDVPGDHFTMMEEHAAATARAVHDWL 212
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
97-503 |
2.23e-39 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 152.54 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 97 AVIGVGCrfpgdidGPERLWDFLTEKKCAITAYPDRGFTNAGTFAESGGFLKDVAGFDNRF--FDIPPDE-------ALR 167
Cdd:PTZ00050 1 VVTPLGV-------GAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMPCQIaaEVDQSEFdpsdfapTKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 168 MDPQQRLLLEVSWEALEHAGIIPESLRL-SRTGVFVGVSSTDYVRLVSASaqqKSTIWDNTGGSS-----SIIANR---- 237
Cdd:PTZ00050 74 ESRATHFAMAAAREALADAKLDILSEKDqERIGVNIGSGIGSLADLTDEM---KTLYEKGHSRVSpyfipKILGNMaagl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 238 ISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQ------TGCCHAFDK 311
Cdd:PTZ00050 151 VAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkynddpQRASRPFDK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 312 SADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSngIMAPNPS--AQIGVLENACK-SARVDPLEIGYVE 388
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHH--ITAPHPDgrGARRCMENALKdGANININDVDYVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 389 AHGTGTSLGDRIEAHALGMVFGRKrpGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPaipft 468
Cdd:PTZ00050 309 AHATSTPIGDKIELKAIKKVFGDS--GAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDA----- 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 624288879 469 ELGLRVVDELQEWPVvagRPRRAGVS-SFGFGGTNA 503
Cdd:PTZ00050 382 ECDLNLVQGKTAHPL---QSIDAVLStSFGFGGVNT 414
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1167-1380 |
3.12e-05 |
|
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: 47.00 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1167 EYRDIANAMTGRHSVYSLTLPGFDSSDALPQNADMIVETVSNAIIDVVGgSCRFVLSGYSSGGVLAYALCSHL-SVKHQr 1245
Cdd:pfam00975 15 SFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQP-EGPYALFGHSMGGMLAFEVARRLeRQGEA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1246 nPLGVALIDTYLPSQIANPsmnegfSPNDTGKGLSREVIRVARMLNRLTATRLTAAATYAAIFQA-------WEPGRSMA 1318
Cdd:pfam00975 93 -VRSLFLSDASAPHTVRYE------ASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRAdyralesYSCPPLDA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624288879 1319 PVLNIVAKDRiaTVENLREERINRWRTAAAEAAySVAEVPGDHFGMMStSSEAIATEIHDWI 1380
Cdd:pfam00975 166 QSATLFYGSD--DPLHDADDLAEWVRDHTPGEF-DVHVFDGDHFYLIE-HLEAVLEIIEAKL 223
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1168-1252 |
4.27e-05 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 46.38 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1168 YRDIANAMTGRHSVYSLTLPGFDS--SDALPQNADMIVETVSNAIIDVVGGscRFVLSGYSSGGVLAYALCSHLSVKHQR 1245
Cdd:COG3208 22 YRPWAAALPPDIEVLAVQLPGRGDrlGEPPLTSLEELADDLAEELAPLLDR--PFALFGHSMGALLAFELARRLERRGRP 99
|
....*..
gi 624288879 1246 NPLGVAL 1252
Cdd:COG3208 100 LPAHLFV 106
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1-71 |
3.38e-04 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 40.61 E-value: 3.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624288879 1 MVSRVLVHAYRVSSNEVSLDVP-IRDLGLKSIDVLAIPGDLGDRFGFCIPDLAVWDNPSANDLIDSLLNQRS 71
Cdd:COG0236 9 RLAEIIAEVLGVDPEEITPDDSfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1-61 |
1.19e-03 |
|
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: 38.31 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 624288879 1 MVSRVLvhayRVSSNEVSLDVPIRDLGLKSIDVLAIPGDLGDRFGFCIPDLAVWDNPSAND 61
Cdd:pfam00550 6 LLAEVL----GVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
93-1122 |
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: 1142.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 93 NEPVAVIGVGCRFPGdIDGPERLWDFLTEKKCAITAYPD-----------RGFTNAGTFAESGGFLKDVAGFDNRFFDIP 161
Cdd:COG3321 3 DEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPAdrwdadayydpDPDAPGKTYVRWGGFLDDVDEFDALFFGIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 162 PDEALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVSASAQQkSTIWDNTGGSSSIIANRISYF 241
Cdd:COG3321 82 PREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEA-IDAYALTGNAKSVLAGRISYK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 242 LDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEG 321
Cdd:COG3321 161 LDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 322 CGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIE 401
Cdd:COG3321 241 VGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 402 AHALGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEW 481
Cdd:COG3321 321 AAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRPW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 482 PvVAGRPRRAGVSSFGFGGTNAHVIVEEAGSVgadtvsgRADVGGSGGGVVAWVISGKTASALAAQAGRLGRYVRARPAL 561
Cdd:COG3321 401 P-AGGGPRRAGVSSFGFGGTNAHVVLEEAPAA-------APAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 562 DVVDVGYSLVSTRSVFDHRAVVVGQTRDELLAGLAGVVAGRPEAGVVCGVGKPAGKTAFVFAGQGSQWLGMGSELYAAYP 641
Cdd:COG3321 473 DLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEP 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 642 VFAEALDAVVDELDRHLRYPLRDVIWGHD-QDLLNTTEFAQPALFAVEVALYRLLMSWGVRPGLVLGHSVGELAAAHVAG 720
Cdd:COG3321 553 VFRAALDECDALLRPHLGWSLREVLFPDEeESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAG 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 721 ALCLPDAAMLVAARGRLMQALPAGGAMFAVQAREDEVAPMLG--HDVSIAAVNGPASVVISGAHDAVSAIADRLRGQGRR 798
Cdd:COG3321 633 VLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAgyDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIR 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 799 VHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVADDFASADYWARHIRAVVRFGDSVRSAHCAGAS 878
Cdd:COG3321 713 ARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEALDADYWVRHLRQPVRFADAVEALLADGVR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 879 RFIEVGPGGGLTSLIEASLADAQ-IVSVPTLRKDRPEPVSVMTAAAQGFVSGMGLDWASVFSGYRPKRVELPTYAFQHQk 957
Cdd:COG3321 793 VFLEVGPGPVLTGLVRQCLAAAGdAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQRE- 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 958 FWLAPAPSVSDPTAAGQIGASDGGAELLASSGFAARLAGRSADEQLAAAIEVVCEHAAAVLGRDGAAGLDAGQAFADSGF 1037
Cdd:COG3321 872 DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAA 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1038 NSLSAVELRNRLTAVTAVTLPATAIFDHPTPTELAQYLITQIDGHGSSAAAAANPAERIDALTDLFLQACDAGRDADGWK 1117
Cdd:COG3321 952 AAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAA 1031
|
....*
gi 624288879 1118 MVALA 1122
Cdd:COG3321 1032 AAALA 1036
|
|
| mycolic_Pks13 |
NF040607 |
polyketide synthase Pks13; |
16-971 |
0e+00 |
|
polyketide synthase Pks13;
Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 709.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 16 EVSLDVPIRDLGLKSIDVLAIPGDLGDRFGFCIPDLAVWDNPSANDLIDSLLNQRsaDSLRESHGHADRNTQGRGSINEP 95
Cdd:NF040607 24 QITDDRPMEEFGLSSRDAVALSGDIEDLTGVTLTATVAYQHPTIASLATRIIEGE--PEVAADDDDDADWSRRPRSDAHD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 96 VAVIGVGCRFPGDIDGPERLWDFLTEKKCAITAYP-DR--GFTNAGTFAES-------GGFLKDVAGFDNRFFDIPPDEA 165
Cdd:NF040607 102 IAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPeGRwsEFAADPRIAERvakantrGGYLDDIKGFDAEFFALSPLEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 166 LRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYvRLVSASAQQKSTIWDNTGGSSSIIANRISYFLDIQ 245
Cdd:NF040607 182 ENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDY-QMLAVADPAEAHPYALTGTSSSIIANRVSYFFDFR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 246 GPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFRE-AGILSQTGCCHAFDKSADGMVRGEGCGV 324
Cdd:NF040607 261 GPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGGV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 325 IVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHA 404
Cdd:NF040607 341 VVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 405 LGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEWPVV 484
Cdd:NF040607 421 LGRVVGRGRDADKPALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRY 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 485 AGRPrRAGVSSFGFGGTNAHVIVEE----------------------AGSVGADTVSGRADVGGSGGGVVA------WVI 536
Cdd:NF040607 501 SGHA-VAGVSGFGFGGTNAHVVVREvlpadlvepeaqpdedteaelaGLTAEAKRLLAEAELAAEFAPAAPegpvvpLPV 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 537 SGKTASALAAQAGRLGRYVRARP--ALDVVDVGYSLvSTRSVFDHRAVVVGQTRDELLAGLAGVVAGRPEAGVVCGVGkP 614
Cdd:NF040607 580 SGFLPSRRRAAAADLADWLESEEgrATPLADVARAL-ARRNHGRSRAVVLAHTHEEAIKGLRAVAEGKPGPGVFSADA-P 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 615 AGKTA-FVFAGQGSQWLGMGSELYAAYPVFAEALDAvVDEL-DRHLRYPLRDVIWGHDQDLlnTTEFAQPALFAVEVALY 692
Cdd:NF040607 658 AANGPvWVLSGFGSQHRKMAKQLYLENPVFAARIDE-VDELvQDESGYSIVELILDDEQTY--DIETAQVGIFAIQIALA 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 693 RLLMSWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLM----QALPAG--GAMFAVQAREDEVAPMLGH--D 764
Cdd:NF040607 735 DLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgegeAMLPGDdiRLMALVEYSAEEIETVLADfpD 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 765 VSIAAVNGPASVVISGAHDAVSAIADRLRGQGRRVHRLAVSHAFHSALMEPMIAEFtavAAELSvGL----PTIPVISNV 840
Cdd:NF040607 815 LEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHTSQMDPLLGEL---AAELA-GIepqpLTVGLYSSV 890
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 841 -------TGQLVADDfasADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGP------GGGLTSLiEASLADAQIvsVPT 907
Cdd:NF040607 891 drgtfyrPGHEPIHD---VDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPnpvalmSVAATTF-AAGLHDAQL--IPT 964
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624288879 908 LRKDRPEPVSVMTAAAQGFVSGMGLDWASVFSgyRPKRVELPTYAFQHQKFWLAPAPSVSDPTA 971
Cdd:NF040607 965 LKRKEDESESVLNALAQLYVHGHDVDLRSLFG--AGDYADIPRTRFKRKPYWLDARPSSGGGSG 1026
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
94-507 |
0e+00 |
|
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: 616.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 94 EPVAVIGVGCRFPGDIDgPERLWDFLTEKKCAITAYPDRGFTNAGTFAES----------GGFLKDVAGFDNRFFDIPPD 163
Cdd:cd00833 1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDRWDADGYYPDPgkpgktytrrGGFLDDVDAFDAAFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 164 EALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVSASAQQKSTiWDNTGGSSSIIANRISYFLD 243
Cdd:cd00833 80 EAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDA-YAATGTSRAFLANRISYFFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 244 IQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEGCG 323
Cdd:cd00833 159 LRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 324 VIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAH 403
Cdd:cd00833 239 VVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 404 ALGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEWPv 483
Cdd:cd00833 319 ALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWP- 397
|
410 420
....*....|....*....|....
gi 624288879 484 VAGRPRRAGVSSFGFGGTNAHVIV 507
Cdd:cd00833 398 APAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
96-509 |
3.62e-154 |
|
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: 467.19 E-value: 3.62e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 96 VAVIGVGCRFPGdIDGPERLWDFLTEKkcaitaypdrgftnagtfaesggfLKDVAGFDNRFFDIPPDEALRMDPQQRLL 175
Cdd:smart00825 1 IAIVGMSCRFPG-ADDPEEFWDLLLAG------------------------LDDVDLFDAAFFGISPREAEAMDPQQRLL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 176 LEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYvrlvsasaqqkstiwdntggsssiianrisyfldiqgpSIVIDTAC 255
Cdd:smart00825 56 LEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY--------------------------------------SVTVDTAC 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 256 SSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEGCGVIVLQRLSDARL 335
Cdd:smart00825 98 SSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALR 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 336 EGRRILAILTGSAVNQDGKSNGIMAPNPSAQigvlenacksarvdpleigyveahgtgtslgdrieahalgmvfgrkrpg 415
Cdd:smart00825 178 DGDPILAVIRGSAVNQDGRSNGITAPSGPAQ------------------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 416 sgpLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRVVDELQEWPvVAGRPRRAGVSS 495
Cdd:smart00825 209 ---LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWP-PPGRPRRAGVSS 284
|
410
....*....|....
gi 624288879 496 FGFGGTNAHVIVEE 509
Cdd:smart00825 285 FGFGGTNAHVILEE 298
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
621-911 |
1.70e-127 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 396.39 E-value: 1.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 621 VFAGQGSQWLGMGSELYAAYPVFAEALDAVVDELDRHLRYPLRDVIWGHDQD-LLNTTEFAQPALFAVEVALYRLLMSWG 699
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGEDGAaSLLDTEVAQPALFAVQVALARLLRSWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 700 VRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLMQALPAGGAMFAVQAREDEVAPML---GHDVSIAAVNGPASV 776
Cdd:smart00827 81 VRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLagvPDRVSVAAVNSPSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 777 VISGAHDAVSAIADRLRGQGRRVHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLV-ADDFASADYW 855
Cdd:smart00827 161 VLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIdGAELDDADYW 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 624288879 856 ARHIRAVVRFGDSVRSAHCA-GASRFIEVGPGGGLTSLIEASLADA-QIVSVPTLRKD 911
Cdd:smart00827 241 VRNLREPVRFADAVRALLAEgGVTVFLEVGPHPVLTGPIKQTLAAAgSAVVLPSLRRG 298
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
95-933 |
2.41e-100 |
|
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: 355.85 E-value: 2.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 95 PVAVIGVGCRFpGDIDGPERLWDFLTEKKCAITAYPDRGF-----------TNAGTFAESGGFLKDVaGFDNRFFDIPPD 163
Cdd:TIGR02813 8 PIAIVGMASIF-ANSRYLNKFWDLIFEKIDAITDVPSDHWakddyydsdksEADKSYCKRGGFLPEV-DFNPMEFGLPPN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 164 EALRMDPQQRLLLEVSWEALEHAGIiPESLRLSRTGVFVGV------SSTDYVRL--------VSASA------------ 217
Cdd:TIGR02813 86 ILELTDISQLLSLVVAKEVLNDAGL-PDGYDRDKIGITLGVgggqkqSSSLNARLqypvlkkvFKASGvededsemlikk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 218 -QQKSTIWDNT---GGSSSIIANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGG 293
Cdd:TIGR02813 165 fQDQYIHWEENsfpGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 294 FREAGILSQTGCCHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENA 373
Cdd:TIGR02813 245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 374 CKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMVFGRKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLL 453
Cdd:TIGR02813 325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 454 PSGGFTEPNPAIPFTELGLRVVDELQEW-PVVAGRPRRAGVSSFGFGGTNAHVIVEEAGSVGAdtvsgRADVGGSGGGVV 532
Cdd:TIGR02813 405 PTINVDQPNPKLDIENSPFYLNTETRPWmQREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQ-----RDDQYRQRAVAQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 533 AWVISGKTASALAAQAGRLGRYVRARPALDVVD-----VGYSLvSTRSVFDHRAVVVGQTRDELLAGLAGVVA------- 600
Cdd:TIGR02813 480 TLLFTAANEKALVSSLKDWKNKLSAKADDQPYAfnalaVENTL-RTIAVALARLGFVAKNADELITMLEQAITqleaksc 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 601 ---------GRPEAGVVCGvgkpAGKTAFVFAGQGSQWLGMGSELYAAYPVFAEALDAVVDELDRH-------LRYPL-- 662
Cdd:TIGR02813 559 eewqlpsgiSYRKSALVVE----SGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAgkgalspVLYPIpv 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 663 --RDVIWGHDQDLLNtTEFAQPALFAVEVALYRLLMSWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLMQA 740
Cdd:TIGR02813 635 fnDESRKAQEEALTN-TQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 741 LPA---GGAMFAVQAREDEVAPMLGH------DVSIAAVNGPASVVISGAHDAVSAIADRLRGQGRRVHRLAVSHAFHSA 811
Cdd:TIGR02813 714 PTGeadIGFMYAVILAVVGSPTVIANcikdfeGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTP 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 812 LMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVADDFAS-ADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGPGGGLT 890
Cdd:TIGR02813 794 LVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAiKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQ 873
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 624288879 891 SLIEASLADAQ----IVSV-PTLRKDRPEpvSVMTAAAQGFVSGMGLD 933
Cdd:TIGR02813 874 KLVENTLKDKEnelcAISInPNPKGDSDM--QLRQAAVQLAVLGLELT 919
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
94-333 |
4.23e-91 |
|
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: 294.93 E-value: 4.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 94 EPVAVIGVGCRFPGDIDgPERLWDFLTEKKCAITAYPDRGF----------TNAGTFAESGGFLKDVAGFDNRFFDIPPD 163
Cdd:pfam00109 1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADRWdpdklydppsRIAGKIYTKWGGLDDIFDFDPLFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 164 EALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVSAS-AQQKSTIW-DNTGGSSSIIANRISYF 241
Cdd:pfam00109 80 EAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDeDGGPRRGSpFAVGTMPSVIAGRISYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 242 LDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEG 321
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEG 239
|
250
....*....|..
gi 624288879 322 CGVIVLQRLSDA 333
Cdd:pfam00109 240 VGAVVLKRLSDA 251
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
616-905 |
4.53e-83 |
|
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: 274.70 E-value: 4.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 616 GKTAFVFAGQGSQWLGMGSELYAAYPVFAEaldaVVDELDRHLRYPLRDVIWGHDQDLLNTTEFAQPALFAVEVALYRLL 695
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVARE----VFEEASEALGYDLSALCFEGPEEELNLTENTQPAILAASVAAYRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 696 MSWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLMQ-ALPAG-GAMFAVQ-AREDEVAPML-----GHDVSI 767
Cdd:COG0331 77 EEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQeAVPAGpGGMAAVLgLDDEEVEALCaeaaqGEVVEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 768 AAVNGPASVVISGAHDAVSAIADRLRGQG-RRVHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVA 846
Cdd:COG0331 157 ANYNSPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 624288879 847 DDFASADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGPGGGLTSLIEASLADAQIVSV 905
Cdd:COG0331 237 DPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPGVEVLAV 295
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
95-507 |
6.85e-67 |
|
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: 232.04 E-value: 6.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 95 PVAVIGVGCRFP-GDidGPERLWDFLTEKKCAITAYPDRGFTNAGTFAesGGFLKDVAGFDnrffDIPPDEALRMDPQQR 173
Cdd:cd00834 2 RVVITGLGAVTPlGN--GVEEFWEALLAGRSGIRPITRFDASGFPSRI--AGEVPDFDPED----YLDRKELRRMDRFAQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 174 LLLEVSWEALEHAGIIPESLRLSRTGVFVGVSS---TDYVRLVSASAQQKSTIW---DNTGGSSSIIANRISYFLDIQGP 247
Cdd:cd00834 74 FALAAAEEALADAGLDPEELDPERIGVVIGSGIgglATIEEAYRALLEKGPRRVspfFVPMALPNMAAGQVAIRLGLRGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 248 SIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILS------QTGCChAFDKSADGMVRGEG 321
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALStrnddpEKASR-PFDKDRDGFVLGEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 322 CGVIVLQRLSDARLEGRRILAILTGSAVNQDGksNGIMAPNPSA--QIGVLENACKSARVDPLEIGYVEAHGTGTSLGDR 399
Cdd:cd00834 233 AGVLVLESLEHAKARGAKIYAEILGYGASSDA--YHITAPDPDGegAARAMRAALADAGLSPEDIDYINAHGTSTPLNDA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 400 IEAHALGMVFGrkrPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTElglrVVDELQ 479
Cdd:cd00834 311 AESKAIKRVFG---EHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDY----VPNEAR 383
|
410 420
....*....|....*....|....*....
gi 624288879 480 EWPVvagrprRAGVS-SFGFGGTNAHVIV 507
Cdd:cd00834 384 EAPI------RYALSnSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
149-507 |
3.88e-64 |
|
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: 224.20 E-value: 3.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 149 DVAGFDNRF------FD----IPPDEALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVSASAq 218
Cdd:COG0304 39 DASGLPVRIagevkdFDpeeyLDRKELRRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYR- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 219 qkstIWDNTGGS-----------SSIIANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLIS 287
Cdd:COG0304 118 ----ALLEKGPRrvspffvpmmmPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 288 PEPWGGFREAGILSQ-----TGCCHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGksNGIMAPN 362
Cdd:COG0304 194 PLGLAGFDALGALSTrnddpEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDA--YHITAPA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 363 PSA--QIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMVFGRKRPGsgpLMIGSIKPNIGHLEGAAGIAGL 440
Cdd:COG0304 272 PDGegAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDHAYK---VPVSSTKSMTGHLLGAAGAIEA 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624288879 441 IKAVLMVERGSLLPSGGFTEPNPAIPFtelglrvvdelqewPVVAGRPRRAGVS-----SFGFGGTNAHVIV 507
Cdd:COG0304 349 IASVLALRDGVIPPTINLENPDPECDL--------------DYVPNEAREAKIDyalsnSFGFGGHNASLVF 406
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
620-929 |
1.32e-62 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 216.57 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 620 FVFAGQGSQWLGMGSELYAAYPVFAealdAVVDELDRHLR----YPLRDVIWGHDQDLLNTTEFAQPALFAVEVALYRLL 695
Cdd:pfam00698 2 FVFSGQGSQWAGMGMQLLKTSPAFA----AVIDRADEAFKpqygFSVSDVLRNNPEGTLDGTQFVQPALFAMQIALAALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 696 MSWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLMQALPAGGAMFAVQAREDEVAPMLGHDVSIAAVNGPAS 775
Cdd:pfam00698 78 QSYGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPDDVVGAVVNSPRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 776 VVISGAHDAVSAIADRLRGQGRRVHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVADDFASADYW 855
Cdd:pfam00698 158 VVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEYW 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624288879 856 ARHIRAVVRFGDSVRSAHCAGASRFIEVGPGGGLTSLIEASLADAQIVS----VPTLRKDRP-EPVSVMTAAAQGFVSG 929
Cdd:pfam00698 238 VRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGKvatlVGTLIRDQTdFLVTFLYILAVAHLTG 316
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
617-893 |
8.70e-60 |
|
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: 207.32 E-value: 8.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 617 KTAFVFAGQGSQWLGMGSELYAAYPVFAEaldaVVDELDRHLRYPLRDVIWGHDQDLLNTTEFAQPALFAVEVALYRLLM 696
Cdd:TIGR00128 2 KIAYVFPGQGSQTVGMGKDLYEQYPIAKE----LFDQASEALGYDLKKLCQEGPAEELNKTQYTQPALYVVSAILYLKLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 697 -SWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLMQ-ALPAG-GAMFAVQAREDE-VAPMLG----HDVSIA 768
Cdd:TIGR00128 78 eQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQeAVPEGgGAMAAVIGLDEEqLAQACEeateNDVDLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 769 AVNGPASVVISGAHDAVSAIADRLRGQG-RRVHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVAD 847
Cdd:TIGR00128 158 NFNSPGQVVISGTKDGVEAAAALFKEMGaKRAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYTN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 624288879 848 DFASADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGPGGGLTSLI 893
Cdd:TIGR00128 238 GDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLI 283
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1154-1380 |
3.42e-51 |
|
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: 179.73 E-value: 3.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1154 ICIPTLTVLSDQREYRDIANAMTGRHSVYSLTLPGFDSSDALPQNADMIVETVSNAIIDVVGGScRFVLSGYSSGGVLAY 1233
Cdd:smart00824 1 ICFPSTAAPSGPHEYARLAAALRGRRDVSALPLPGFGPGEPLPASADALVEAQAEAVLRAAGGR-PFVLVGHSSGGLLAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1234 ALCSHLSvKHQRNPLGVALIDTYLPSQIAnpsmNEGFSPndtgkGLSREVIRVARMLNRLTATRLTAAATYAAIFQAWEP 1313
Cdd:smart00824 80 AVAARLE-ARGIPPAAVVLLDTYPPGDPA----PEGWLP-----ELLRGVFEREDSFVPMDDARLTAMGAYLRLFGGWTP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 624288879 1314 GRSMAPVLNIVAKDRIAtveNLREERINRWRTaAAEAAYSVAEVPGDHFGMMSTSSEAIATEIHDWI 1380
Cdd:smart00824 150 GPVAAPTLLVRASEPLA---EWPDEDPDGWRA-HWPLPHTVVDVPGDHFTMMEEHAAATARAVHDWL 212
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
171-507 |
2.40e-48 |
|
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: 175.90 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 171 QQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDYVRLVS-ASAQQKSTIWDNTGGSSSIIANRISYFLDIQGPSI 249
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFgADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 250 VIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHAFDKSADGMVRGEGCGVIVLQR 329
Cdd:cd00825 91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 330 LSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMVF 409
Cdd:cd00825 171 LEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 410 GRKRPGsgplmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELGLRvvdelqewpvvAGRPR 489
Cdd:cd00825 251 GDKSPA-----VSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETT-----------PRELR 314
|
330
....*....|....*...
gi 624288879 490 RAGVSSFGFGGTNAHVIV 507
Cdd:cd00825 315 TALLNGFGLGGTNATLVL 332
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
94-507 |
1.78e-47 |
|
"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: 175.71 E-value: 1.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 94 EPVAVIGVGCRFP--GDIDGPERLWDFLTEKKCAITAYPDRGFTNAGTFAesgGFLKDvagfdnrfFDIPPDEALR---M 168
Cdd:cd00828 1 SRVVITGIGVVSPhgEGCDEVEEFWEALREGRSGIAPVARLKSRFDRGVA---GQIPT--------GDIPGWDAKRtgiV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 169 DPQQRLLLEVSWEALEHAGI-IPESLRLSRTGVFVGVSSTDYVRLVSASAQQKSTIWDNTG----GSSSIIANRISYFLD 243
Cdd:cd00828 70 DRTTLLALVATEEALADAGItDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSpkwmLSPNTVAGWVNILLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 244 I-QGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNvLISPEPWGGFREAGILSQT-----GCCHAFDKSADGMV 317
Cdd:cd00828 150 SsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALSTAeeepeEMSRPFDETRDGFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 318 RGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPsAQIGVLENACKSARVDPLEIGYVEAHGTGTSLG 397
Cdd:cd00828 229 EAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGK-GIARAIRTALAKAGLSLDDLDVISAHGTSTPAN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 398 DRIEAHALGMVFGrkrPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFtelgLRVVDE 477
Cdd:cd00828 308 DVAESRAIAEVAG---ALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEH----LSVVGL 380
|
410 420 430
....*....|....*....|....*....|
gi 624288879 478 LQEWPvvaGRPRRAGVSSFGFGGTNAHVIV 507
Cdd:cd00828 381 SRDLN---LKVRAALVNAFGFGGSNAALVL 407
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
341-459 |
1.14e-46 |
|
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: 163.12 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 341 LAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMVFGRKRPGSgPLM 420
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKQ-PLA 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 624288879 421 IGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFT 459
Cdd:pfam02801 80 IGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| malonate_mdcH |
TIGR03131 |
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ... |
619-905 |
4.78e-46 |
|
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group.
Pssm-ID: 132175 Cd Length: 295 Bit Score: 167.87 E-value: 4.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 619 AFVFAGQGSQWLGMGSELY---AAYPVFAEALDAV---VDELDrhlryplrdviwghDQDLLNTTEFAQPALFAVEVALY 692
Cdd:TIGR03131 2 ALLFPGQGSQRAGMLAELPdhpAVAAVLAEASDVLgidPRELD--------------DAEALASTRSAQLCILAAGVAAW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 693 RLLMSWGVRPGLVLGHSVGELAAAHVAGALCLPDAAMLVAARGRLM-QALPAGGAMFAVQ-AREDEVAPML-GHDVSIAA 769
Cdd:TIGR03131 68 RALLALLPRPSAVAGYSVGEYAAAVVAGVLTFDDALRLVALRAALMdQAVPGGYGMLAVLgLDLAAVEALIaKHGVYLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 770 VNGPASVVISGAHDAVSAIADRLRGQG-RRVHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVADD 848
Cdd:TIGR03131 148 INAPDQVVIAGSRAALRAVAELARAAGaSRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLVRDA 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 624288879 849 FASADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGPGGGLTSLIEASLADAQIVSV 905
Cdd:TIGR03131 228 AQIRDDLARQIATPVDWHDCMQAAYERGARLVIELGPGDVLTKLANEAFPELPARSA 284
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
97-503 |
2.23e-39 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 152.54 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 97 AVIGVGCrfpgdidGPERLWDFLTEKKCAITAYPDRGFTNAGTFAESGGFLKDVAGFDNRF--FDIPPDE-------ALR 167
Cdd:PTZ00050 1 VVTPLGV-------GAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMPCQIaaEVDQSEFdpsdfapTKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 168 MDPQQRLLLEVSWEALEHAGIIPESLRL-SRTGVFVGVSSTDYVRLVSASaqqKSTIWDNTGGSS-----SIIANR---- 237
Cdd:PTZ00050 74 ESRATHFAMAAAREALADAKLDILSEKDqERIGVNIGSGIGSLADLTDEM---KTLYEKGHSRVSpyfipKILGNMaagl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 238 ISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQ------TGCCHAFDK 311
Cdd:PTZ00050 151 VAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkynddpQRASRPFDK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 312 SADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSngIMAPNPS--AQIGVLENACK-SARVDPLEIGYVE 388
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHH--ITAPHPDgrGARRCMENALKdGANININDVDYVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 389 AHGTGTSLGDRIEAHALGMVFGRKrpGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPaipft 468
Cdd:PTZ00050 309 AHATSTPIGDKIELKAIKKVFGDS--GAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDA----- 381
|
410 420 430
....*....|....*....|....*....|....*.
gi 624288879 469 ELGLRVVDELQEWPVvagRPRRAGVS-SFGFGGTNA 503
Cdd:PTZ00050 382 ECDLNLVQGKTAHPL---QSIDAVLStSFGFGGVNT 414
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
160-506 |
1.69e-38 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 149.55 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 160 IPPDEALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVFVGvSSTDYVRLVsasAQQKSTIwdNTGGSS-------- 231
Cdd:PRK07314 61 MSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENADRIGVIIG-SGIGGLETI---EEQHITL--LEKGPRrvspffvp 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 232 SIIANRISYFLDI----QGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQ----- 302
Cdd:PRK07314 135 MAIINMAAGHVSIrygaKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrnddp 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 303 TGCCHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSngIMAPNPSAQIGV--LENACKSARVD 380
Cdd:PRK07314 215 ERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYH--MTAPAPDGEGAAraMKLALKDAGIN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 381 PLEIGYVEAHGTGTSLGDRIEAHALGMVFGRkrpGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTE 460
Cdd:PRK07314 293 PEDIDYINAHGTSTPAGDKAETQAIKRVFGE---HAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDN 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 624288879 461 PNPAIPftelglrvVDelqewpVVAGRPRRAGV-----SSFGFGGTNAHVI 506
Cdd:PRK07314 370 PDEECD--------LD------YVPNEARERKIdyalsNSFGFGGTNASLV 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
110-506 |
8.22e-36 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 142.06 E-value: 8.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 110 DGPERLWDFLTEKKCAITAYPDrgFTNAGTFAESGGFLKDVAGFDNRFFD----IPPDEALRMDPQQRLLLEVSWEALEH 185
Cdd:PRK06333 19 CGVETFWQRLLAGQSGIRTLTD--FPVGDLATKIGGQVPDLAEDAEAGFDpdryLDPKDQRKMDRFILFAMAAAKEALAQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 186 AGIIPESLR-LSRTGVFVGV------SSTDYVRLVSASAQQKS---TIwdntggsSSIIAN----RISYFLDIQGPSIVI 251
Cdd:PRK06333 97 AGWDPDTLEdRERTATIIGSgvggfpAIAEAVRTLDSRGPRRLspfTI-------PSFLTNmaagHVSIRYGFKGPLGAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 252 DTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTG------CCHAFDKSADGMVRGEGCGVI 325
Cdd:PRK06333 170 VTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFndapeqASRPFDRDRDGFVMGEGAGIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 326 VLQRLSDARLEGRRILAILTGSAVNQDGKSngiMAPNPSAQIGV---LENACKSARVDPLEIGYVEAHGTGTSLGDRIEA 402
Cdd:PRK06333 250 VIETLEHALARGAPPLAELVGYGTSADAYH---MTAGPEDGEGArraMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 403 HALGMVFGRkrpgSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPFTELglrVVDELQEWP 482
Cdd:PRK06333 327 AAIKKVFGH----VSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDV---VANKARPMD 399
|
410 420
....*....|....*....|....
gi 624288879 483 VvagrpRRAGVSSFGFGGTNAHVI 506
Cdd:PRK06333 400 M-----DYALSNGFGFGGVNASIL 418
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
614-886 |
6.40e-33 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 131.42 E-value: 6.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 614 PAGKTAFVFAGQGSQWLGMGSELyAAYPVFAEALDAVVDELDrhlrYPLRDVIWGHDQDLLNTTEFAQPALFAVEVALYR 693
Cdd:PLN02752 36 YKPTTAFLFPGQGAQAVGMGKEA-AEVPAAKALFDKASEILG----YDLLDVCVNGPKEKLDSTVVSQPAIYVASLAAVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 694 LLMSWGVRPGLV------LGHSVGELAAAHVAGALCLPDAAMLVAARGRLMQAL--PAGGAMFAVQAREDEVAPML---- 761
Cdd:PLN02752 111 KLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAadAGPSGMVSVIGLDSDKVQELcaaa 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 762 ------GHDVSIAAVNGPASVVISGAHDAVSAIADRLRGQG-RRVHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTI 834
Cdd:PLN02752 191 neevgeDDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRI 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 624288879 835 PVISNVTGQLVADDFASADYWARHIRAVVRFGDSVRSAHCAGASRFIEVGPG 886
Cdd:PLN02752 271 PVISNVDAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPG 322
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
157-506 |
4.29e-32 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 130.91 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 157 FFDIPPDEAlrMDPQQRLLLEVSWEALEHAGII-------------------PESLRLSRTGVFVGVSstDYVRLVSASA 217
Cdd:PRK06501 63 FLPESPFGA--SALSEALARLAAEEALAQAGIGkgdfpgplflaappvelewPARFALAAAVGDNDAP--SYDRLLRAAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 218 QQKSTIWDNTGGSSSIiANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREA 297
Cdd:PRK06501 139 GGRFDALHERFQFGSI-ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 298 GILSQ-----TGCCHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLEN 372
Cdd:PRK06501 218 SALSTqndppEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 373 ACKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMVFGrKRPGSGPlmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSL 452
Cdd:PRK06501 298 ALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFG-ERLASIP--VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRL 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 624288879 453 LPSGGFTEPNPAIPFTelglrvvdelqewpVVAGRPRRAGVS-----SFGFGGTNAHVI 506
Cdd:PRK06501 375 PPTINYDNPDPAIPLD--------------VVPNVARDARVTavlsnSFGFGGQNASLV 419
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
235-503 |
3.43e-30 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 125.67 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 235 ANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQ------TGCCHA 308
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfnscpTEASRP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 309 FDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSngIMAPNPSAQIGVL--ENACKSARVDPLEIGY 386
Cdd:PLN02836 244 FDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHH--ITQPHEDGRGAVLamTRALQQSGLHPNQVDY 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 387 VEAHGTGTSLGDRIEAHALGMVFGRKRPgSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIp 466
Cdd:PLN02836 322 VNAHATSTPLGDAVEARAIKTVFSEHAT-SGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIF- 399
|
250 260 270
....*....|....*....|....*....|....*..
gi 624288879 467 ftELGLRVVDELQEWPVVAgrprrAGVSSFGFGGTNA 503
Cdd:PLN02836 400 --DDGFVPLTASKAMLIRA-----ALSNSFGFGGTNA 429
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
238-508 |
2.33e-29 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 122.45 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 238 ISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQ-------TGCCHAFD 310
Cdd:PRK07103 150 CSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSdrfadepEAACRPFD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 311 KSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGimAPNPSAQIGVLENACKSARVDPLEIGYVEAH 390
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGP--DPSLEGEMRVIRAALRRAGLGPEDIDYVNPH 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 391 GTGTSLGDRIEAHALgmvfgrKRPGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPnpaipfTEL 470
Cdd:PRK07103 308 GTGSPLGDETELAAL------FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEP------IDE 375
|
250 260 270
....*....|....*....|....*....|....*...
gi 624288879 471 GLRVVDElqewPVVAGRPRRAGVSSFGFGGTNAHVIVE 508
Cdd:PRK07103 376 RFRWVGS----TAESARIRYALSLSFGFGGINTALVLE 409
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
181-507 |
1.01e-28 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 119.77 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 181 EALEHAGIIPEslrLSRTGVFVGVS-----------STDYVRLVSASAQQKSTIWDNT-GGSSSIIANRIsyfLDIQGPS 248
Cdd:PRK05952 66 AALKDAGLTPP---LTDCGVVIGSSrgcqgqweklaRQMYQGDDSPDEELDLENWLDTlPHQAAIAAARQ---IGTQGPV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 249 IVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTGCcHAFDKSADGMVRGEGCGVIVLQ 328
Cdd:PRK05952 140 LAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTGA-YPFDRQREGLVLGEGGAILVLE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 329 RLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMV 408
Cdd:PRK05952 219 SAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQAL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 409 FGRKRPgsgplmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPnpaipftELGLRVVDELQEWPVvagrp 488
Cdd:PRK05952 299 FPHRVA------VSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEP-------EFDLNFVRQAQQSPL----- 360
|
330
....*....|....*....
gi 624288879 489 RRAGVSSFGFGGTNAHVIV 507
Cdd:PRK05952 361 QNVLCLSFGFGGQNAAIAL 379
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
994-1079 |
1.75e-28 |
|
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: 110.03 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 994 LAGRSADEQLAAAIEVVCEHAAAVLGRDGAAGLDAGQAFADSGFNSLSAVELRNRLTAVTAVTLPATAIFDHPTPTELAQ 1073
Cdd:smart00823 1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
|
....*.
gi 624288879 1074 YLITQI 1079
Cdd:smart00823 81 HLAAEL 86
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
162-506 |
2.33e-28 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 119.45 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 162 PDEALRMDPQQRLLLEVSWEALEHAGIIPESLRLSRTGVfvgvsstdyvrlVSASA-------QQKSTIWDNTGGSS--- 231
Cdd:PRK08439 63 PKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAERFGV------------SSASGigglpniEKNSIICFEKGPRKisp 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 232 ----SIIANRISYFLDI----QGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQT 303
Cdd:PRK08439 131 ffipSALVNMLGGFISIehglKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 304 G-----CCHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGsaVNQDGKSNGIMAPNPSAQIGVLENACKSAR 378
Cdd:PRK08439 211 NddpkkASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPAPEGPLRAMKAALEMAG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 379 VDplEIGYVEAHGTGTSLGDRIEAHALGMVFGRKRpgSGPLmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGF 458
Cdd:PRK08439 289 NP--KIDYINAHGTSTPYNDKNETAALKELFGSKE--KVPP-VSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQ 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 624288879 459 TEPNPaipftELGLRVVdelqewPVVAgrpRRAGV-----SSFGFGGTNAHVI 506
Cdd:PRK08439 364 ETPDP-----ECDLDYI------PNVA---RKAELnvvmsNSFGFGGTNGVVI 402
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
171-507 |
1.65e-26 |
|
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: 110.23 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 171 QQRLLLEVSWEALEHAGIIPESlrlsRTGVFVGVSSTDYvrLVSASAQQkstiwdntggsssiianrISYFLDIQ-GPSI 249
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGP----IVGVIVGTTGGSG--EFSGAAGQ------------------LAYHLGISgGPAY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 250 VIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLispepwggfreagilsqtgcchafdksadgmVRGEGCGVIVLQR 329
Cdd:cd00327 63 SVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-------------------------------VFGDGAAAAVVES 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 330 LSDARLEGRRILAILTGSAVNQDGKSnGIMAPNPSAQIGVLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHALGMVF 409
Cdd:cd00327 112 EEHALRRGAHPQAEIVSTAATFDGAS-MVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 410 GRKRPGsgplmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGgftepnpaipftelglrvvdelqewpvvaGRPR 489
Cdd:cd00327 191 GVRSPA-----VSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTP-----------------------------REPR 236
|
330
....*....|....*...
gi 624288879 490 RAGVSSFGFGGTNAHVIV 507
Cdd:cd00327 237 TVLLLGFGLGGTNAAVVL 254
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
253-502 |
2.05e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 113.67 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 253 TACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQT------GCCHAFDKSADGMVRGEGCGVIV 326
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMSTnnddpaGACRPFDKDRDGFVFGEGGALMV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 327 LQRLSDARLEGRRILAILTGSAVNQDGKSngIMAPNPSAQIG--VLENACKSARVDPLEIGYVEAHGTGTSLGDRIEAHA 404
Cdd:PRK07910 249 IETEEHAKARGANILARIMGASITSDGFH--MVAPDPNGERAghAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 405 LGMVFGRKRPGsgplmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIpftelglrvvdelqEWPVV 484
Cdd:PRK07910 327 INNALGGHRPA-----VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEI--------------DLDVV 387
|
250 260
....*....|....*....|...
gi 624288879 485 AGRPRR-----AGVSSFGFGGTN 502
Cdd:PRK07910 388 AGEPRPgnyryAINNSFGFGGHN 410
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
232-506 |
2.59e-26 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 113.56 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 232 SIIANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQTG-----CC 306
Cdd:PRK08722 141 NMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNdepqkAS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 307 HAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNqdGKSNGIMAPNPSAQIGVL--ENACKSARVDPLEI 384
Cdd:PRK08722 221 RPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMS--GDAYHMTSPSEDGSGGALamEAAMRDAGVTGEQI 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 385 GYVEAHGTGTSLGDRIEAHALGMVFGRKrpGSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPnpa 464
Cdd:PRK08722 299 GYVNAHGTSTPAGDVAEIKGIKRALGEA--GSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDP--- 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 624288879 465 ipftELGLRVvdelqewPVVAGRPRR------AGVSSFGFGGTNAHVI 506
Cdd:PRK08722 374 ----EEGLDI-------DLVPHTARKvesmeyAICNSFGFGGTNGSLI 410
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
160-506 |
8.63e-26 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 113.53 E-value: 8.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 160 IPPDEALRMDPQQRLLLEVSWEALEHAGIIPE---SLRLSRTGVFVGVSS------TDYVRLVSASAQQKSTI---WDNT 227
Cdd:PLN02787 188 VAPKLSKRMDKFMLYLLTAGKKALADGGITEDvmkELDKTKCGVLIGSAMggmkvfNDAIEALRISYRKMNPFcvpFATT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 228 GGSSSIIANRISYFldiqGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQ----- 302
Cdd:PLN02787 268 NMGSAMLAMDLGWM----GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrnddp 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 303 TGCCHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPL 382
Cdd:PLN02787 344 TKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 383 EIGYVEAHGTGTSLGDRIEAHALGMVFGRKrPGsgpLMIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPN 462
Cdd:PLN02787 424 DVNYINAHATSTKAGDLKEYQALMRCFGQN-PE---LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPE 499
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 624288879 463 PAIpftELGLRVVDELQEWPVVAgrprrAGVSSFGFGGTNAHVI 506
Cdd:PLN02787 500 SGV---DTKVLVGPKKERLDIKV-----ALSNSFGFGGHNSSIL 535
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
235-506 |
1.47e-25 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 110.70 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 235 ANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLiSPEPWGGFREAGILSqTGCCHAFDKSAD 314
Cdd:PRK09185 140 ADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSL-CRLTLNGFNSLESLS-PQPCRPFSANRD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 315 GMVRGEGCGVIVLQRLSDARLegrrilaILTGSAVNQDGKSngIMAPNPSAQ--IGVLENACKSARVDPLEIGYVEAHGT 392
Cdd:PRK09185 218 GINIGEAAAFFLLEREDDAAV-------ALLGVGESSDAHH--MSAPHPEGLgaILAMQQALADAGLAPADIGYINLHGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 393 GTSLGDRIEAHALGMVFGRKRPGSgplmigSIKPNIGHLEGAAGIAGLIKAVLMVERGslLPSGGF--TEPNPAIPftel 470
Cdd:PRK09185 289 ATPLNDAMESRAVAAVFGDGVPCS------STKGLTGHTLGAAGAVEAAICWLALRHG--LPPHGWntGQPDPALP---- 356
|
250 260 270
....*....|....*....|....*....|....*.
gi 624288879 471 GLRVVDELQewpvvAGRPRRAGVSSFGFGGTNAHVI 506
Cdd:PRK09185 357 PLYLVENAQ-----ALAIRYVLSNSFAFGGNNCSLI 387
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
182-506 |
6.09e-25 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 109.31 E-value: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 182 ALEHAGII-PESLRLSRTGVFVGVS--STDYVRLVSASAQQKSTiwDNTGGSSSI------IANRISYFLDIQGPSIVID 252
Cdd:PRK09116 84 ALEDAGLLgDPILTDGRMGIAYGSStgSTDPIGAFGTMLLEGSM--SGITATTYVrmmphtTAVNVGLFFGLKGRVIPTS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 253 TACSSSLVAVHLACRSLSTWDCDIALVGGTNVL----------------------ISPEPwggfreagilsqtgcchaFD 310
Cdd:PRK09116 162 SACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELcpteaavfdtlfatstrndapeLTPRP------------------FD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 311 KSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSngIMAPNPSAQIGVLENACKSARVDPLEIGYVEAH 390
Cdd:PRK09116 224 ANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH--VTQPQAETMQIAMELALKDAGLAPEDIGYVNAH 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 391 GTGTSLGDRIEAHALGMVFGRKRPgsgplmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPftEL 470
Cdd:PRK09116 302 GTATDRGDIAESQATAAVFGARMP------ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACG--AL 373
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 624288879 471 GLrvvdelqewpvVAGRPRRAGV-----SSFGFGGTNAHVI 506
Cdd:PRK09116 374 DY-----------IMGEAREIDTeyvmsNNFAFGGINTSLI 403
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
232-508 |
1.40e-21 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 97.88 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 232 SIIANRISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTWDCDIALVGGTNVLISPEPWGGFREAGILSQ------TGC 305
Cdd:PRK14691 68 NLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfnstpEKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 306 CHAFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNGIMAPNPSAQIGVLENACKSARVDPLEIG 385
Cdd:PRK14691 148 SRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 386 YVEAHGTGTSLGDRIEAHALGMVFGRkrpgSGPLMIGSIKPNIGHLEGAAGIAGLIKAVLMVeRGSLLPSG-GFTEPNPA 464
Cdd:PRK14691 228 HLNAHATSTPVGDLGEINAIKHLFGE----SNALAITSTKSATGHLLGAAGGLETIFTVLAL-RDQIVPATlNLENPDPA 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 624288879 465 IPftelGLRvvdelqewpVVAGRPR-----RAGVSSFGFGGTNAHVIVE 508
Cdd:PRK14691 303 AK----GLN---------IIAGNAQphdmtYALSNGFGFAGVNASILLK 338
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
308-503 |
1.44e-17 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 86.65 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 308 AFDKSADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSngIMAPNPSAQIGVLENACksARVDpLEIGYV 387
Cdd:PRK07967 220 AYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYD--MVAPSGEGAVRCMQMAL--ATVD-TPIDYI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 388 EAHGTGTSLGDRIEAHALGMVFGRKRPGsgplmIGSIKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPaipf 467
Cdd:PRK07967 295 NTHGTSTPVGDVKELGAIREVFGDKSPA-----ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP---- 365
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 624288879 468 telglrvvdELQEWPVVAGRPRRAGV-----SSFGFGGTNA 503
Cdd:PRK07967 366 ---------QAAGMPIVTETTDNAELttvmsNSFGFGGTNA 397
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
461-584 |
2.67e-17 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 78.74 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 461 PNPAIP-FTELGLRVVDELQEWPvvagrPRRAGVSSFGFGGTNAHVIVEEAGSVgadtvsgRADVGGSGGGVVAWVISGK 539
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPWP-----GGIVGVNSFGFGGANAHVILKSNPKP-------KIPPESPDNLPRLVLLSGR 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 624288879 540 TASALAAQAGRLGRYVRARPALDVVDVGYSLVSTRsvFDHRAVVV 584
Cdd:pfam16197 69 TEEAVKALLEKLENHLDDAEFLSLLNDIHSLPISG--HPYRGYAI 111
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
95-507 |
8.79e-16 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 81.25 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 95 PVAVIGVGCRFPGDIdGPERLWDFLTEKKCAITayPDRGFTNAGTFAESGGflkDVAGFDNRffDIPPDEAL-RMDPQQR 173
Cdd:cd00832 2 RAVVTGIGVVAPNGL-GVEEYWKAVLDGRSGLG--PITRFDPSGYPARLAG---EVPDFDAA--EHLPGRLLpQTDRMTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 174 LLLEVSWEALEHAGIIPESLRLSRTGVFVGVSSTDY--------------VRLVSAsaqQKSTIW---DNTGgsssiian 236
Cdd:cd00832 74 LALAAADWALADAGVDPAALPPYDMGVVTASAAGGFefgqrelqklwskgPRHVSA---YQSFAWfyaVNTG-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 237 RISYFLDIQGPSIVIDTACSSSLVAVHLACRSLSTwDCDIALVGGTNVLISPEPWGGFREAGILSQTGCCHA----FDKS 312
Cdd:cd00832 143 QISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRR-GTPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARaylpFDAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 313 ADGMVRGEGCGVIVLQRLSDARLEGRRILAILTGSAVNQDGKSNgimAPNPSAQIGVLENACKSARVDPLEIGYVEAHGT 392
Cdd:cd00832 222 AAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG---SGRPPGLARAIRLALADAGLTPEDVDVVFADAA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 393 GTSLGDRIEAHALGMVFGRKR-PGSGPlmigsiKPNIGHLEGAAGIAGLIKAVLMVERGSLLPSGGFTEPNPAIPftelg 471
Cdd:cd00832 299 GVPELDRAEAAALAAVFGPRGvPVTAP------KTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG----- 367
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 624288879 472 lrvVDelqewpVVAGRPRRAGVS-----SFGFGGTNAHVIV 507
Cdd:cd00832 368 ---LD------LVTGRPRPAALRtalvlARGRGGFNSALVV 399
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
555-1382 |
2.91e-13 |
|
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: 74.74 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 555 VRARPALDVVDVGYSLVSTRSVFDHRAVVVGQTRDELLAGLAGVVAGRPEAGVVCGVGKPAGKTAFVFAGQGSQWLGMGS 634
Cdd:COG3319 3 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 635 ELYAAYPVFAEALDAVVDELDRHLRYPLRDVIWGHDQDLLNTTEFAQPALFAVEVALYRLLMSWGVRPGLVLGHSVGELA 714
Cdd:COG3319 83 ALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 715 AAHVAGALCLPDAAMLVAARGRLMQALPAGGAMFAVQAREDEVAPMLGHDVSIAAVNGPASVVISGAHDAVSAIADRLRG 794
Cdd:COG3319 163 VLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 795 QGRRVHRLAVSHAFHSALMEPMIAEFTAVAAELSVGLPTIPVISNVTGQLVADDFASADYWARHIRAVVRFGDSVRSAHC 874
Cdd:COG3319 243 LLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 875 AGASRFIEVGPGGGLTSLIEASLADAQIVSVPTLRKDRPEPVSVMTAAAQGFVSGMGLDWASVFSGYRPKRVELPTYAFQ 954
Cdd:COG3319 323 GLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 955 HQKFWLAPAPsVSDPTAAGQIGASDGGAELLASSGFAARLAGRSADEQLAAAIEVVCEHAAAVLGRDGAAGLDAGQAFAD 1034
Cdd:COG3319 403 LQRLRRGLRE-ELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1035 SGFNSLSAVELRNRLTAVTAVTLPATAIFDHPTPTELAQyLITQIDGHGSSAAAAANPAERIDALTDLFLQACDAGRDAD 1114
Cdd:COG3319 482 LLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALAL-LLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1115 GWKMVALASNTRERM-----SSPVRNNVSKNVALLADGISDVVVICIPTLTVLSdqREYRDIANAMTGRHSVYSLTLPGF 1189
Cdd:COG3319 561 LLLLLALLLAPTLAAlaaalAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNV--LCYRPLARALGPDRPVYGLQAPGL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1190 DSSDALPQNADMIVETVSNAIIDVVGGScRFVLSGYSSGGVLAYALCSHLSVKHQRNPLgVALIDTYLPSQIANPS---- 1265
Cdd:COG3319 639 DGGEPPPASVEEMAARYVEAIRAVQPEG-PYHLLGWSFGGLVAYEMARQLEAQGEEVAL-LVLLDSYAPGALARLDeael 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1266 -------MNEGFSPNDTGKGLS--------REVIRVARMLNRLTATRLTAAATYAAIFQA-------WEPGRSMAPVLNI 1323
Cdd:COG3319 717 laallrdLARGVDLPLDAEELRaldpeerlARLLERLREAGLPAGLDAERLRRLLRVFRAnlralrrYRPRPYDGPVLLF 796
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1324 VAKDRIATvenLREERINRWRTaAAEAAYSVAEVPGDHFGMMSTSS-EAIATEIHDWISG 1382
Cdd:COG3319 797 RAEEDPPG---RADDPALGWRP-LVAGGLEVHDVPGDHFSMLREPHvAELAAALRAALAA 852
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1007-1079 |
2.70e-09 |
|
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: 54.86 E-value: 2.70e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624288879 1007 IEVVCEHAAAVLGRDgAAGLDAGQAFADS-GFNSLSAVELRNRLTAVTAVTLPATAIFDHPTPTELAQYLITQI 1079
Cdd:COG0236 7 EERLAEIIAEVLGVD-PEEITPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
945-1081 |
5.77e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 60.82 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 945 RVELPTyafqhQKFW-LAPAPSVSDptAAGQIGASDGGAELLASSGfaarLAGRSADEQLAA--------AIEVVCEHAA 1015
Cdd:PRK06060 487 RKQSPT-----KPIWeLSLTEPGSG--VRAQRDDLSASNMTIAGGN----DGGATLRERLVAlrqerqrlVVDAVCAEAA 555
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 624288879 1016 AVLGRDGAAGLDAGQAFADSGFNSLSAVELRNRLTAVTAVTLPATAIFDHPTPTELAQYLITQIDG 1081
Cdd:PRK06060 556 KMLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAG 621
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1008-1070 |
5.29e-08 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 50.64 E-value: 5.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 624288879 1008 EVVCEHAAAVLGRDgAAGLDAGQAFADSGFNSLSAVELRNRLTAVTAVTLPATAIFDHPTPTE 1070
Cdd:pfam00550 1 ERLRELLAEVLGVP-AEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1167-1380 |
3.12e-05 |
|
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: 47.00 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1167 EYRDIANAMTGRHSVYSLTLPGFDSSDALPQNADMIVETVSNAIIDVVGgSCRFVLSGYSSGGVLAYALCSHL-SVKHQr 1245
Cdd:pfam00975 15 SFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQP-EGPYALFGHSMGGMLAFEVARRLeRQGEA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1246 nPLGVALIDTYLPSQIANPsmnegfSPNDTGKGLSREVIRVARMLNRLTATRLTAAATYAAIFQA-------WEPGRSMA 1318
Cdd:pfam00975 93 -VRSLFLSDASAPHTVRYE------ASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRAdyralesYSCPPLDA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624288879 1319 PVLNIVAKDRiaTVENLREERINRWRTAAAEAAySVAEVPGDHFGMMStSSEAIATEIHDWI 1380
Cdd:pfam00975 166 QSATLFYGSD--DPLHDADDLAEWVRDHTPGEF-DVHVFDGDHFYLIE-HLEAVLEIIEAKL 223
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1168-1252 |
4.27e-05 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 46.38 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 1168 YRDIANAMTGRHSVYSLTLPGFDS--SDALPQNADMIVETVSNAIIDVVGGscRFVLSGYSSGGVLAYALCSHLSVKHQR 1245
Cdd:COG3208 22 YRPWAAALPPDIEVLAVQLPGRGDrlGEPPLTSLEELADDLAEELAPLLDR--PFALFGHSMGALLAFELARRLERRGRP 99
|
....*..
gi 624288879 1246 NPLGVAL 1252
Cdd:COG3208 100 LPAHLFV 106
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1-71 |
3.38e-04 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 40.61 E-value: 3.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624288879 1 MVSRVLVHAYRVSSNEVSLDVP-IRDLGLKSIDVLAIPGDLGDRFGFCIPDLAVWDNPSANDLIDSLLNQRS 71
Cdd:COG0236 9 RLAEIIAEVLGVDPEEITPDDSfFEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
174-281 |
7.13e-04 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 43.06 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624288879 174 LLLEVSWEALEHAGIIPESLrlsrtgvfvgvsstDYVrlvsasaqqkstIWDN--TGGSSSIIANRISYFLDIQ--GPSI 249
Cdd:pfam00108 26 LGAEAIKAALERAGVDPEDV--------------DEV------------IVGNvlQAGEGQNPARQAALKAGIPdsAPAV 79
|
90 100 110
....*....|....*....|....*....|..
gi 624288879 250 VIDTACSSSLVAVHLACRSLSTWDCDIALVGG 281
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGG 111
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1-61 |
1.19e-03 |
|
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: 38.31 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 624288879 1 MVSRVLvhayRVSSNEVSLDVPIRDLGLKSIDVLAIPGDLGDRFGFCIPDLAVWDNPSAND 61
Cdd:pfam00550 6 LLAEVL----GVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| |
