UniProt: A0A010SK08

Database: UniProt
Entry: A0A010SK08_9PEZI

LinkDB:  A0A010SK08_9PEZI 
Original site:  A0A010SK08_9PEZI

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Ontology (7)   
   GO (7)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (42)   
   InterPro (23)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
All databases (52)   

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ID   A0A010SK08_9PEZI        Unreviewed;      2383 AA.
AC   A0A010SK08;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:EXF85213.1};
GN   ORFNames=CFIO01_03284 {ECO:0000313|EMBL:EXF85213.1};
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:EXF85213.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF85213.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF85213.1,
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   -!- 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:EXF85213.1}.
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DR   EMBL; JARH01000118; EXF85213.1; -; Genomic_DNA.
DR   RefSeq; XP_007591209.1; XM_007591147.1.
DR   STRING; 1445577.A0A010SK08; -.
DR   KEGG; cfj:CFIO01_03284; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_1_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 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; 3.
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; 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; 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; 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; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 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; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 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; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
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          57..460
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2299..2379
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          88..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2383 AA;  256923 MW;  4D22CC9A3014FB9A CRC64;
     MTINDGRNSA YTIPTNGYPS NGTTGATYND GTNGIHGTNG YNGIGVNGPT TGAPQAHEPI
     AVIGMGCRLP GEVDNPHALT QLLKRGGVAR NEPPESRFSL DGHHDGSKKP KTMRSPGGMF
     LENIDPREFD AGFFQVPRLD AVAMDPQQRQ LLEVVYECLE NSGVTLQELQ GAQVGCFVGS
     YAVDYADMQA RDPEDRAPSV TIGVGRAILS NRISHFLNIK GPREMDGAIV AGCNLYLSPE
     HNMDVGPMKG ASSLSGKCHT FDVKADGYIK GEAVNAVMVK RLSDALRDGD PIRAVILGTA
     TNSDGNTPGI ASPSSEAQAA AIRSAYANAG ITNFNDTTYL ECHGTGTQAG DPTEVSGIAS
     VFAPSRSPDQ PLIIGSIKSN IGHSEPAAGI SGLIKAILSL ENGTIFGNPT FVTPNPKIDF
     KGQKVFATRT SMPWPTGARK RASVNSFGYG GSNAHVVLES ADQYLQDNQI STHVSSHLAE
     EADLFGEDDD ASSTTAVAKQ PQLLVFSANN ESSLRGYVKL LRKHLLNPSV KVDLRDLSFT
     LSSKRSAHFN RGFLLADKAV IAEDSLVLGK KSPEAPKIGF VFTGQGAQWS QMGKALVDAF
     PTARDLLKHL DTVLRTALVP PTWSLLDELV EPRSPGLLRQ PEFSQPLCTA LQLAILSVLE
     DWGVAPRSVV GHSSGEIAAA YAAGYLSKED AIKVAYYRGL AAKQLANVVD GTKNVGMLAV
     GLGAEAVMPF LEPYAGLVHI ACFNSPSSVT LSGKVDKLEA VMAALVAESH FARLLQVNLA
     YHSPFMLEVS SLYEALLRQD FGTCKKDGKK DSVRMFSSVS GKEMRHAADA SYWKSNMSSA
     VRFEQATKGM LADDNRPDFL VEIGPSGALS GPVAQVKKAV LGGGADVQYV ASWSRGPAAL
     KSLYEVAGKL FIRGGEVNLA NVNKTETWNP RTIIDLPNYA WDHSTQYWYE SDASKDWRYR
     LFPHHDLLGS KILGTSWQAP SFKKSLKLAD LPWLRDHKMG PEIVFPAAGF IAMAIEAVRQ
     NTEALRILDS KVPPTEYHYK LRDINFIRAL VLDDSDEATK IMLALHPRTG AKDSWHEFKI
     SSQVGDSWLE NCRGLVRIQE STPENSTAVE GSVKPLIDPV SGALWYKAMH DTGYNFGPVF
     QKHLEIESIV DSRESRSLVD LSPPASEHPQ SWYPMHPAAI DGSFQSCAPS LWAGDRPGIS
     AVLVPAIIDE LAIFPVESIS GKGISTTSSE YVGLGLPEST KSYKSNAVVL DSETGDLRFK
     LTGLRYHQLD TQEDPYSSHT YSRVSWKPDV THLTEETVAA IAAADDPLNE IIDLAAHKFP
     NLSVLEASTI PSEASSVWLE GSKADPAVRS ACRSFQFSSC DASAVVNAEE TYGSKSGVAY
     TMLDVAADPE KLQAPEKTFN LVIIRAADGI LESQNTVLRN ARTLVSDGGH VVIQAIGADI
     PAISSSFGFC SSFSISSKDG STIYILVASS GTVTNKQRIE LVHFSEPTDA TAQVVSGLSK
     FGWQLTDTEH TQEGHKTILV LSDLSAPVLP TMTEAQWQLL KNTLVSGNQV LWVTSGSQLN
     VTSPDRAMIH GLCRTVRNED PSISITTLDV ESATGTKTVS AINEVLERLG RAAYRKQTTG
     IENEFVERQG VIHISRVQPN EAVNVVEKAL AHGAELVEGE LHDFNTTVRL QCERVGTIDS
     LQYTEVAATE LPVPDGSVEV ELFAAGLNFK DVAVTMGIVP ENQHLLGLEG AGEIRRAGKN
     AVNIYKPGDR VLVFKKGAFG NRVIASVERT HHIPDWMSFE EASTLASVYL TALYSIFDLA
     NTQAGHKVLI HSASGGLGIA SIQICKFIGA EIYATVGTDE KVDFLVDSFG IPRENIFNSR
     TTTFAAQLKA VTKGHGVDVI LNSLTGDILD ESWRCIADGG TMVELGKRDM LDRNYLSMEP
     FGRNASYRCF DMSHEHVSDT VIARLMRQMM SLISQGAIKP IAPMTTFPFE DVAGAFRYMR
     AAKHMGKIVL SAKDKADKPT VMVRPAIRRF DLPQTTSILI VGGLKGLCGS LAVYLAQQGA
     KHLVILARGG YDDERSQAVL KNIHAQGAKV DLVRGDVSIL EDVRRAFKSS SVPVGGVIQG
     AMVLRDKIFT SMTTEEYHGA VACKVPGTWN LHNVAQEEGL DLSFFTMLSS VSGVVGQKGQ
     ANYAAANAFL DAFAVYRQGL GLSAVSVDLG AIDDVGYMHE HNDLRVALDR DAWTPINENL
     FRQIVRVSIQ QQQKSSSTGN SSQLITSIAV PQPDSSNLLA DARFVSLAFG TGEVAVGGDG
     KDDKSRAVQA LMLLLQSSAD ASLVLKAAVD VVNTQFQATL RLSEPMEPAK PLSSYGLDSL
     SAVELRNWVR LDLGVELTTL EITSATSLTA LCEKIVSKMK KKE
//

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