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
//