ID   A0A0J8S5C4_COCIT        Unreviewed;       812 AA.
AC   A0A0J8S5C4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Fatty acid synthase S-acetyltransferase {ECO:0000313|EMBL:KMU92041.1};
GN   ORFNames=CIHG_09849 {ECO:0000313|EMBL:KMU92041.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU92041.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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DR   EMBL; DS017051; KMU92041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8S5C4; -.
DR   STRING; 396776.A0A0J8S5C4; -.
DR   VEuPathDB; FungiDB:CIHG_09849; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   Proteomes; UP000054563; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW   Transferase {ECO:0000313|EMBL:KMU92041.1}.
FT   DOMAIN          42..467
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   812 AA;  87930 MW;  A67453B9365BCC28 CRC64;
     MTIDETHGMN GHSVAIGSDI NGPITNGHAH RTNGLRTNGT STNAAHMNGN SNTMNGANGS
     RPPISIPMVK FRSQFVQDGR CRVPESRYNI ETYYSDMKKP GTVSTQYGYF LDESVDVGAL
     DMSFFTMARS EVERADPQQR LMLEVAHEAL EDAGVTDWRG KTIGTYIGNF GEDWLEMLGR
     ETQPWGIHRI SGSGDFVVAN RLSYEFDLRG PSMTIRTACS SALVALNEAC AAISRGDCES
     ALVGGVNLIL APGMSVAMQE QGVLSSDGSC KTFSADANGY ARGEAVTAIF IKPLADAIRD
     GNPVQAVVRA TSHNVDGKTP TLSQPSTDVQ EALMRRAYEL GGITDFSETA MVECHRTGTP
     TGDPIETRAV ARVFGEKGVY ISSVKPNLGH TKAASGLVSL LKMVKALQHH IIPPNIKFSI
     PNPSIPFEEG KLTVPTEATP WPKDRLERVS VNSFGIGGAN AHVILESAAT YNIPTAVSGF
     PESPQLLLFT ANSSKSITRL VDNYKVWIEQ NPDKICDLAY TLARKRTHLP YRAFAIVNNG
     VIESVSQPIN SKSAGPPSIV MVFTGQGAQW PQMGRELLQS DEVFKSSIQS LNQQLQTIAG
     KKPHYSIKEE LKKAGKQSRL SSAKFSQPLC TAIQIALVDT LKTAGIVPHA VVGHSSGEIA
     AAYATRALTA KEAITVAHHH GAVAVKQERP GTMAAIEMGW REIENYLIPN ITIACDNSPK
     RITISANIDA VKSVVAAIKK EQPQILARLL QVDKAYHSYH MEEIGDHYQS LIEQVIGKAP
     SMLFFSSVSG NILDSEHKTG SKYWRDNLES PV
//