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Database: UniProt
Entry: A0A1L7X771_9HELO
LinkDB: A0A1L7X771_9HELO
Original site: A0A1L7X771_9HELO 
ID   A0A1L7X771_9HELO        Unreviewed;      3173 AA.
AC   A0A1L7X771;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Related to polyketide synthase {ECO:0000313|EMBL:CZR60866.1};
GN   ORFNames=PAC_10762 {ECO:0000313|EMBL:CZR60866.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR60866.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR60866.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR60866.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; FJOG01000017; CZR60866.1; -; Genomic_DNA.
DR   STRING; 576137.A0A1L7X771; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000184330; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
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; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF22; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 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   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..431
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2483..2561
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   ACT_SITE        2897
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   3173 AA;  349640 MW;  EA1C50CC5D0A45B8 CRC64;
     MTNQVPIPIA VVGIGCRFPG GANSPQKLWQ MLSEGRSGWS EVPHDRWNSN SFHHPSAEAK
     DGFDVHGGHF LDQDISVFEP SFFGISANEA ESMDPQQRIL LETTYEALEN AGIPQEKIRG
     SDTGVYVGYF ARDYDRMVFK DTSDLPKQHI TGGGDAIVSN RISYVFDLKG PSMTIDTGCS
     GSLVALHLAC QSLRAGESAM SIVGGVNLHL SPDYDVMMSF VNVLNKDGKC YAFDSRGSGY
     GRGEGSATIV LKRLDEALAN GDSIRGVIRN TGINQDGKTN GISLPNKEAQ KGLIRSVYQS
     SGLDPYDTGY VEAHGTGTVV GDQAEVDSIA ELFTGYGKQD DEIFVGSVKT NLGHLEAASG
     LAGLIKTLLV LEKGLIPPNL NLQKEKEGLH LETRKIKVPL KLERWSKSGI RRASVNSYGY
     GGTNCHAILE AVPTANVNGF KVEVASKSSN GTLSNGFHTE TVSVNGNGIL SNGFHKETVQ
     INSNKSLVPV RNNTLYKITD QTSKGAQLFV LTSKSQKSLP VIAENLRRVL ASYPGDNAYL
     KDLAYTLSCR RSLLQWRCCV IATNHQELVA ALDPTKLRIF KSNIDVRVFI FTGQGVQWPT
     MGRDLITRYS TFRESLDTSA NILRVLGADW DLIDELTKDT SSRVNESEIS QPVTTAIQVA
     LVDLLAAFNI KPQEVLGHSS GEIGAAYAAG VLSHEAALTV SYRRGFVATA CRRAVSGGGA
     MLAAGIGEDE INSYIERLRA GIVCVACMNS PSSTTISGDT AAIDELHAHL DEAGIFNRKL
     KVDVAYHSHH MRGFANQYLQ SIEGLVAKNP SPGVKFFSSV TGKQKVSGFG AEYWMENLVS
     QVKFSIALEE LSRSQHTGAT FIEIGPHSAL QGPIRQIMTQ PNLESYKYSY FPTLLRNNDG
     VRTLLDLSKH LFESGCLINL GVINSLNDSK HRYAVVKDLA PYAWDHSVKY WRESRLSKDH
     RLRPHPYHDL LGLRIVSSTV NEPIWRHIIN ADRLPWLRDH VVDDSVIFPG SGYLCMAIEA
     IRQITQDRRV AGTVLNYIFK DVSFRKALIV PDSPGSVEML LALTPSIKTV ADRNSTMREE
     FRISSLAADG SWREHCNGLV SVEFDATNVD EVEGQRETHL SVIGEQEQLR DTEDNTPTVV
     NTVAMYEDLA ANGNTYGPSF ALVKQLRLGQ HQGLATIEIP DVQAIMPSHF FQPHVIHPTT
     LDALMQIEVP LFNQHCGFGA VMPVFFEDLA ISADIVNTPG SNLTAMTKVF PAGSKSLTFD
     STVFQTRGDV QTAVVKLTHG ELQRIGRPAS TADQTSNLRM NYNIEWNQDV NFLTQETIQI
     TPRETPENEV SPQQRMESLD RAASLYISEC LNQIGAIDPA ISKLHLLALF DWMKRYTASE
     DSKLLIDNIS SSDKASLFAQ LAALGAEGEM LSRLGGNLQS ILQGKLDALS LMLDEDLLYR
     VYAENMSIQR CYLHMADYLK LLSVKEPFIR VLEIGAGTGS ATVHILDVLS HEQGVWLDRY
     DFTDISSGFF EKAKPKFEKY AGYMEYKTLD IENDPAKQGF EIGTYDLVIA SNVLHATSRI
     DATLSNVRKL LKPGGRLILV ELTKLRPYLN ITFGTLSGWW AGVEDGRKDC PLLSLDRWDK
     ALAKNSFNGV EVAVNDYKGS AQTGALIVSK ATSDLDSTIL APVEVICGSA STHLQAFAGE
     LVSAFEKVGY PATAKTWPSQ VQRDVIYIVI DDGAKPLLVH PSREQFYQII TLTTSADSVL
     WISAHEDAST KSNAETGLIT GLARVARTEN TEMKFVVVHI QQNIVEERDN VVSALSKLVR
     STFGATPEGE KSTETEFLYR DSQLHIPRVL PNTAFDQWMD AGKEKKDMGS FHQPSRFLKL
     HVETPGLLDS LVFLNDDLVQ EPIRPDEIEI ETKAHGVNFK DVYIALGQMK PAERMTGESS
     GFVTRVGSDF ETKFKVGDRV CGWGSLSPFA TRSRVLGNCA YPLPDYMSFT SAASIPVVFL
     TAYIGLVRIA KLQKGQVVLI HAASGGVGQA AIMIAQHIGA TIIATVGSIS KSELLSGKYG
     IPKSHIFSSR LRTFKQGILR LTQGRGVDVV LNSLSGDYLH DTWAGIAPCG TFVEIGKADI
     VKRNQLSMAP FDKMVIFASL DLGVMKDYRS LELASAFAEV MSLFEKGLLK PVEPINVFNI
     GNIEEAFRFI QARKHRGKVV LSSGDDAMVK IMSARPPLRL KSDATFVIAG GLGDLGRRIC
     HFLAQHGAKH IVTLSRRNLD AAVRRVFEEE IRAFGAEVHI LACDVNDSER VQEIASECAA
     TLPLVRGIIQ AAMVLRDRAL NKMEYDEFMT AFKPKFDGTR HLRQAFQNPN LENFIMLSSV
     AAILGNPGQG NYAAGCAYED ALANSQTESN THFISLNLGL VEGSDIDTPE RRAYLLAQGA
     APVRMNELFS LLEYSLSSQA REDKCNQIIS RLDRDSLSQR LGKLLKFPML NHLQRATNTK
     DSRATATVSM DVAGFIGAAK AAEEVNDIVS NAIVSKISSL VALEAEDISM DVTMAEFGLD
     SLVAIELKNW IARNLQAQIQ TIEILDMPSI RHLATTVIER SALVTKPVQA AAAEVQLEEV
     ETANTISPNT RHPLTCCRAA KEVRKLPLHG LEQILQSYLL GIRHLVTDEE YTNSVEATEE
     FQQPGSPGQL LYSQLMKMKD DPAVENWMED LYLQSMYLSR RSPTALYYDI MGTFGAVTVL
     HTQAERAAVI SVTAFKFKQD LGANAVSPVC LNEMPLCMDS QDWLFNATRV PLPGSDEVVK
     YKDPEYDYLI VLRLGHFFKV PLTEGNRNSS IEQLRASFQS ILDLELEDCW VGILTADERD
     SWATIRNKLV SLDPENEQAI RVIDGASFLI CLDHVSPATP EDRIRNFMMD RGINRWHDKS
     LQFLIASNAS TGFIGDHTKL DGGSVHQLLG SIKKAIFTYE PTGSACDNSP SLFEEVVFKT
     SPDIEFEIRR MRKTWLDQCA DIDYANLEYT GFGATYLKDR RCNPQSGFEV VAQLASRMIF
     GRFEACWQPV NMAHYHKGRT EIIQTMTSTM SSFITSALAS PPPRPDPALK TLFFAATREH
     STSMALAQKG HGYHRTLTAM EMLAKQQGGK IPSLYSDLAW CKTGPENIMT GPRDGLFTEV
     ASVWPKRESL FVNYEVGDDR ARFSVVGHGG RAHEYCKLLE KAAGIVKSIL DEE
//
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