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Database: UniProt
Entry: F0XK23_GROCL
LinkDB: F0XK23_GROCL
Original site: F0XK23_GROCL 
ID   F0XK23_GROCL            Unreviewed;      2210 AA.
AC   F0XK23;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EFX01892.1};
GN   ORFNames=CMQ_4963 {ECO:0000313|EMBL:EFX01892.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX01892.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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DR   EMBL; GL629787; EFX01892.1; -; Genomic_DNA.
DR   RefSeq; XP_014171374.1; XM_014315899.1.
DR   STRING; 655863.F0XK23; -.
DR   GeneID; 25978232; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; F0XK23; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT   DOMAIN          13..376
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   2210 AA;  241438 MW;  54A2489702F105FF CRC64;
     MDVQEAAPNN GTSNAIAVVG MACRFPGAAT DIESFWEMLR NGKDAWSEIP EDRFNTKGWY
     HPDPNRPGSF HIRGAHFLKE DIAAFDAPFF SISTAEAISM DPQQRILLEV VYEALDSDYE
     QPCMRDPDTT PPYAATGNGV AILANRISHV FDFSGTSQTI DTGCSASLIA VHQACKSLLG
     GESSLAIAAG VGLIFSPNTL VPMANLNILS PDGRCFTFDE RANGYGRGEG VGVVILKRLE
     DAIAANDTIR AIIRATASNQ DGHTQGDIKE AQAVSEVFCQ QRTSDRPLII GSVKPNIGHL
     EGSAGVAGII KGILVAERGY IPKHLNFTSP NPNIDFNNMK LQIASQLSPW PVDGLRRVSV
     NSFGFGGTNA HVVLDDVPHF LAENDIAGGQ HNTFIYPSDK FPFSLWDELH RDKDTSRIDE
     PQIAQPATTA IQVALVDLLI ASGIQPAAVV GHSSGEIAAA YALGAIHRED AWKIAYYRGQ
     CVRNISTLAP DVHGRMLAAE LSEDDARRMV SDAGTQSVCI ACINGPASAT LSGDAEEISH
     LYTCFQKKGI RTVMVNVDVA YHSPHMHIVE SIYLNAIKDV TPLQQKSNGV FFSSVYGRRI
     LASDLGAEYW VKNMVLPVQF FKAVTEVMSQ MSPAVFLEVS PHRVWKSTLR QIHSSATASG
     TSPVYLSLLS RESDACDTAL DALGGLWAQG LSFKLEWASS SYGEKPRHLA DTPSYPWDHS
     RRYWHESHLS KANRFRSHGR EDIIGAPLEN STPQAPSWRG FFRVQENPWL EDHVIQKSIF
     YPAGGMVAMA IEAAKQLSES SRTLKGFEVK EISIIKPMLI PRSPQGLENM FSARLLDKDD
     ALSSKNLTCY EFSILSKPED SLWIVHAKGR VSIVYGEECP DPDDYIDPGQ TTKVQRQAFY
     RAREACDIEH SPRQFYEDLD VIGMTYGPQF RNLTEIRTDN TAAYTVIEIP DTKACMPFQF
     EFDHVIHPTT LDTMIQTVLV LSDGVGEAML PCSIGRIYVS ASLPKGAGSQ FRGYTTAHKT
     HMHTARADIS MFDYQLCAPV VTIENLMLKS VPSSGNDGFL PSHRNLCSEI VWKMDIGANC
     SLGIDLPESF QDMIDAASHK NPALSILCHV HPLYESVEAP PSFAKQHVAA SYFSGLIFDV
     LTVGHETPRF SQLVISGSEL LWRQLCESKR SYPGVERVHS SEMPSANSQF DVVVVSVGVA
     GPRDIDSQLF RCVAPDGWII VVPEETGIFS TEQRTELANA VHAAGFQGSK AQNDTFRFFA
     AQKNSTTASQ TTSENTILLV LPDQMSELTK ALRDTIRPII KNSLSLEILE VPFSTISSLS
     NEELAFSCMC LVELDASTIF CMREDEYESI RRLLMVTKGL LWLTRGAQLG AKDPSRSPFL
     GLARAIRSED AKKNIISLDI DVQPAENRIH NMEQLAEKTV LLLKRACSDL PPEPFVEDVE
     FVFSEGHLMI PRLMPLPTLN RLIEHGPTMP QSVARIPLTL KDKALKLDNT SVEKPSGLLF
     VEDQEGLHRP LHPDEVRIAV VGTNLLPEDI ALASLGAPNA KVGTDAFGHV VEVGINVKDV
     WPYCRVVARM RDTIKTHVIA HKSRVRRILH QGEWPGSCPT AFATALYALR TRRRSLEGEV
     VLVYGASSAY GQAAIWIALA LGNKVLVACK SSMERKLMLE SFKLPASHVI DAQCSDVEFE
     LRILSATFNR GVDVVFDPTS KFIEQAFCCA SEGGCVIRVA WAGCDGSAVR LPLKNVSLET
     VDLGLLEARN PLEVERLFFE VDQILQLAPK LGAINGTLEY RMSQVQDALK AATADPFAGS
     YVVTTHSDSI HPNTVNIPVP LTQTPRLSQS STYLLIGGLG GLGRAIAEHL VTNGARCIAF
     FSRSGGSAPP AQAFIAKLNA KGVYARAFAV DICNEAQLGT AIRELYGSMP PIQGAIQCAA
     VVTDAAFPNM DYGCWKQCFG PKTIGSYNLH QLLPRAMDFF VFLSSLSGII GNRGQANYAA
     GNSFQDALAR HRSSQGMHSV SLDLGLVLGA GMVAEDESLL DAMRARGFLG TRLQDVLFIL
     DRAMARPGTE NIDIPPQIVT SVGTGGLTIQ NQPSDPFWTR AALFRYLNQV DAPPRGFNKI
     TGGSSHSGGS ENLRTAIQRT ASMEDAAYLI CTALIASLAR RKSMVPSDFD PLQSLDSYGI
     DSLDSLFILG WISRETGVTM QTVDGLTITQ LSQAVAQRSF EALEQDAVRG
//
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