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Database: UniProt
Entry: A0A0J7AXD6_COCIT
LinkDB: A0A0J7AXD6_COCIT
Original site: A0A0J7AXD6_COCIT 
ID   A0A0J7AXD6_COCIT        Unreviewed;       967 AA.
AC   A0A0J7AXD6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Oxysterol-binding protein 1 {ECO:0000313|EMBL:KMP02042.1};
GN   ORFNames=CIRG_02181 {ECO:0000313|EMBL:KMP02042.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP02042.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
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).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC       {ECO:0000256|ARBA:ARBA00008842}.
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DR   EMBL; DS028093; KMP02042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J7AXD6; -.
DR   STRING; 404692.A0A0J7AXD6; -.
DR   Proteomes; UP000054565; Unassembled WGS sequence.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   CDD; cd13289; PH_Osh3p_yeast; 1.
DR   Gene3D; 2.40.160.120; -; 1.
DR   Gene3D; 3.30.70.3490; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   InterPro; IPR037239; OSBP_sf.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041680; PH_8.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR10972:SF216; OXYSTEROL-BINDING PROTEIN HOMOLOG 3; 1.
DR   PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF15409; PH_8; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50866; GOLD; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..145
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   DOMAIN          215..309
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          59..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   967 AA;  107624 MW;  4CA01C6BD179EB0E CRC64;
     MAGMEEIEIH SKSYLVRWIN VSGEHTISWS IQPHKKSLNF GIFKHPGTTG TLTATSASIH
     SSSDFGDGRE NGRPGNASSS VVTEKLKGIG LKPIRWVGKC EADKISQGTY DVGSGEGGNY
     ALVFDNTFSK QISKTATFVL LTYPTHCPPR SGHQIHHSQA GLGYAAVTSA LTRSNPNIAS
     GASDSTESLR NSRGLANSQS KTGSRGSDSP FPFHAQLHTG ILQKRRRKRH QGFARRFFSL
     DFNTSTLSYY HDRNSSALRG AIPLTLAAIA TNSDTREISI DSGAEIWHLR ALNEQDFNVW
     KRALEKASKI SEDVVQPEPK GKVRTHSIPT RRQSMITQDT KSWTEVGWLA EKVAMARDTV
     RQLAKDTDPK YLPYSSDRPH VNTRQMPQQT DGTNEMADRE KRSFWKLKYR NDNQSAQRAV
     SHGEPFGSYK PPMEMPNRGR DPVHDRLMAL LQELDSVVSD FSSLLEKKRP RPSRPPSIRT
     RPSIESDVSE EFFDANDGHC SPLLTMHRDS EDEDEKSVAA ETAVGDESSL SGSDIEERDD
     FLKFRHDNSS SLFPTKPKSL IPLPVENVVR RKTVLAPTVM PPSLIGFLRK NVGKDLSTIS
     MPVSANEPIS LLQRAAEQFE YSRLLDKAAS ATDALERLIY VTAFAISPFS NMRVKERSIR
     KPFNPMLGET YELVRGDLGF RFIAEKVSHR PVQLAYQADS KDWSYAQSPK PTQKFWGKSA
     EIITEGKVRL TLHSSGEHFS WSPGTSFLRN IIAGEKYVEP VGEMCIVNET TGQKTVVTFK
     AGGMFSGRSE EVTVKAFDTH GDELPLGLQG SWTTSLQLTE HGRETNHTIW AAGSLVDKAP
     KHYGFTVFAA SLNEITAVEK AKLPPTDSRL RPDQRALENG DVDQAENLKA LLEEKQRHRR
     KEMEAVGEVW RSRWFTKVGG TVDGANGTGT GDDDDDGVMW KLNTGKDGYW EERARGQWPG
     TVPVFKL
//
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