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Database: UniProt
Entry: A0A010QMP7_9PEZI
LinkDB: A0A010QMP7_9PEZI
Original site: A0A010QMP7_9PEZI 
ID   A0A010QMP7_9PEZI        Unreviewed;      2635 AA.
AC   A0A010QMP7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:EXF77955.1};
GN   ORFNames=CFIO01_08862 {ECO:0000313|EMBL:EXF77955.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF77955.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF77955.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF77955.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXF77955.1}.
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DR   EMBL; JARH01000672; EXF77955.1; -; Genomic_DNA.
DR   RefSeq; XP_007598391.1; XM_007598329.1.
DR   STRING; 1445577.A0A010QMP7; -.
DR   KEGG; cfj:CFIO01_08862; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   eggNOG; KOG3717; Eukaryota.
DR   HOGENOM; CLU_000022_31_2_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; 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; cd05195; enoyl_red; 1.
DR   CDD; cd05274; KR_FAS_SDR_x; 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; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
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; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF08659; KR; 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; 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   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1972..2049
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          48..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2392
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   2635 AA;  290783 MW;  E580D0CD8F2766D4 CRC64;
     MKIATEMVPL PESTGPRRVS VNSFGYGGTN AHVILEAPAS YEKADRVPAP AKSNGTNGHT
     NGHTNGHANG HTNGHDTKEN GTNGYTEVQE ITSPDHGING PDGTNGTHGT NGHNGLNGKT
     RDHAEEVVSG TPKLFVLSAR SETSLQAMVA NLQGWVSSHD DASSLSNLAY TLSSRRSELQ
     FRFSVAAASH DELINLLGQK PRITKAASNF RSVFVFTGQG AQWHAMGREL TRKNLVFRKS
     MLQSEKILKD LGADWSLIEE LSRDEENSRV GQAEISQPST TAIQIALVDL LKSYQILPNL
     VLGHSSGEIA AGYAAEALDH ETALEISYRR GFMSQACARV ISARGAMMAV GLGEVDVKKY
     VEQTKTGLIC VACVNSPVST TISGDETAID ELKQILDEES IFNRKLKVDT AYHSHHMKKV
     AAEYLESIAH IKAHTPNPAI KFYSSVAVAH KTSEFDAKYW VDNLVSPVRF GNALELLCRT
     ELVGLEPAPL TLFTEVGPHG ALAGPVRQTI KGLNLTSFKS SYLSTLSRGR DAAITLLETA
     GKLFEFGYPV SLQATLGNNQ SATLVDDLDP YPWDHSTSFL YESKLSKEHR FRAHPPHDLL
     GLRVPGTTNH EPTWRNLLGV GSLPWLSDHV VDGFAIFPAS GYLSMAVEAV RQISVDRKIQ
     GVISQIHLKN VSFTKSIMIP ERRTDGLTSD VEVLLTLRPA KSLTDRTWET FRIMALSPED
     VWHEHCTGHI MVEWAAKEDE VEGFREEKMA NLIGLEHLRE VIDACSTTIS GEDLYKNFTE
     NGNVYGPTFA GIESAQIGSR GGIAEIKIPD VKSMMPRKHQ QEHVIHPASL DTVFQLGLPL
     YRRDVGNGPV MPTSIDDLII NCKLSSTPGT KWTVCSTMGQ KGFRFASIDI MVFEEVTQGA
     PLVPVLDIRG GALRGIGEAP VDENTLPFSR KMSYALEWQP DVDLLASLQQ GDEPNQLVSY
     LQLLAFKQPR MKILDLSAGS KADIALPFLK AIDRPEGLLL DRYTYCSAET HIESLDQAKA
     SLRQWIDRVD FKTLDNSNDF TQQGFQEGSY DLIIVSQAEH GSANEPLSNW RKLLKPRGRL
     VLCASSVEGE YDDSPALPEV DWHALLEHHN FEEVNSDQQN SIARPGMIVA TTVEEQSSPT
     GDFPSIRIIS QSQSDQIGSL ADAFVAHMTA LGFSCSLDGL SSEPVNVDAI HLVLDDSAGP
     ILAAPSAEKF AQIVSLVTKA KSVLWLSCQE SGAETHNPAK GMITGLARVV RRENSAMRFV
     TVDVQDDVLL TPEVLVCQIS DIIKTSFATP VSISRSDEDE YKFSNGQLLI PRVHADAKFD
     DWVKRAIYAQ GMETGPFQQA DRPLKLEVET PGLLSSLRFA DDETPSKPLQ PFEIELEARA
     YGVNFKDVFI AMGQMIPGVT MAGECAGVVR KVGSAIEGKF RIGDRVCGIF AEPFSSHPRI
     DGNFSCHLPE SMTYSVGASI PVIFCTAYHC IVEVARLERG DTILIHAASG GVGQAAIQLA
     QNIGAEIFCT VGSSAKRQLL IDTFNIPPDH IFSSRLRTFK QGILRLTQGK GVSCVLNSLS
     GESLHDSFAV IAPLGTFVEI GKSDIYRKNE ISMVPFDNSV TFAAVDLTVL ARLKPTKMRE
     TLDKVLTLFA EGTLKPVAPI TAMPMTDIED AFRLIQSRKH TGKVVLICDE QTQVKLTLAR
     PQPLRLDKNG TYVISGGLGD LGRRIAKFLA THGAGHVATL SRRKLEEKDQ LAFEEELRAI
     GSELHIIRCD VTDEESVQSA ATECAERLPP VRGVIHAGMV LRDHPFEIMS HDDYMTSIKP
     KVQGTQNLDN AFGASDSLDF FIMLSSITAI LGKSGQSNYA VGNAYQDAFA QSKKGSSCRY
     IALNLGAVDG SLAITSLPPA QQDAMRRGSV LMSFDEVFAV LTYAMSAQAN EDDLHQLILG
     FDRKSMEAVH DEMALANPIF SQIPYLEKEG EPTKEAATDV GKLLQQASSP EEVKSLVVNG
     ICQRFAMFTA VPVEEISPDV SMESFGLDSL VAIELKNFLS RTFQATLQTS EVLDAVNILS
     LAKVIILRSK LVPKDTDPAV VEKEDIATPT AVKVSDLAIE TAAPDTNHNF HCCRAIKTLQ
     KMPLVDFDVM FDDYLEKSRM FFSVEDFKTI EDDVAEFRKP DSIGRKFYGR LHEQAHDPAI
     ENWQEKYFLQ SMYLQRRMPL APFNNFMAFH PLGDMGHTQA ERAAMIASIA FQAKQDLESD
     RWEPMAYMFT ANCTDLWQYI FNTARLPGVP LDRMAKFPGN DYMAVLYRGH IYKVELVDGD
     HNVSIETLTK TFNALLAQQD LNDDWTSILG TDDRTSWAES RQALIELDDA NKETIDMVEA
     AAFLVCLDDT EPAHAEERIN NMMMLNGFNR WVDKSIAFVV CKNATSGTYV EHTMIDAMTL
     FAMQTAIVEG IRTYKPPREA NGHTNGVVSS PREFTLKTTP ALDARIQHVR QRFENDISKF
     GYRDIVLSDF GKDILLDRHL PIKGVFDLMG LLANYYYYGY NAQSWEAISM SHYHKGRPDI
     VQVNTPITAD FCTIADDDSV PARKRFELMV EAANARNQII KEAFTGRCYQ RTLRALELCA
     EEGEDLPALF KNPLYEQTVE PNQMFSNTDG LSPESCFIMQ NPKRFWMTYY VTDGG
//
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