ID E9DY99_METAQ Unreviewed; 982 AA.
AC E9DY99;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Oxysterol binding protein (Osh3), putative {ECO:0000313|EMBL:EFY91434.1};
GN ORFNames=MAC_02597 {ECO:0000313|EMBL:EFY91434.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY91434.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY91434.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|ARBA:ARBA00008842}.
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DR EMBL; GL698482; EFY91434.1; -; Genomic_DNA.
DR RefSeq; XP_007808937.1; XM_007810746.1.
DR AlphaFoldDB; E9DY99; -.
DR STRING; 655827.E9DY99; -.
DR GeneID; 19246908; -.
DR KEGG; maw:MAC_02597; -.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_007105_4_0_1; -.
DR InParanoid; E9DY99; -.
DR OMA; SYFVRWV; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000002499; 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; 2.60.120.680; GOLD domain; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..147
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT DOMAIN 213..307
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 151..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 902..929
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 151..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 107897 MW; 09BC7F5998ACCE4B CRC64;
MAGIEKLEVH SKSYIVRWVR VDEDHTLSWS VQPNKKSINF GIVKHPGSGA TTILSSNGDV
LDGAPVQGTT DGKGGRFPKK ETTAQDLLIS KGFIPISWHG KCEADKVSRG THDVHTGQGG
MYGLVFDNTF SKQTSKTATF VVLTYPTGAP PQTTNHLPNL QLPNAQNSQS SLGKHGSPHN
ENGPSTSVDS LPSHGRARAQ SSAGKSDVTG ASPNYHVGTL SKRRRKKGQG YARRFFSLDY
STCTLSYYYN RNSSALRGAI PLSLAAIAAD ERRREISIDS GAEVWHLRAP NDKEFQDWAR
ALERASRLAR GLETLTKPSK PSLKLDGHVP RRTQDPCHSE TVEWQQVETL VSRVVGTRDA
LRRLTKELAQ LPKPSPNGQL LSPGFGTPNE ENKDGYFPPT VEKKSFWKRK SSAPSLSTSP
IQQTTPSALA VPSLANATSG VETVTRQASK RRSRGVAQEE KSLYDHCQAL LSDLDSVVSE
FTALIANSKR RRLPQPPSAG GASRMSIETT STDEFFDAED AKSGVVKIDG SEDESAETEA
EEESIHESSS ISSIEDEEGV GTEGTGDVYP VRPKNLTPLP LDQAVTRRTG IPPALVQPPS
LIAFVRKNVG KDLSTISMPV SANEPISLLQ KVAEPLEYAQ LLDKACRQKS PTERLLFVTA
FAVSRFSGGR AKERAIRKPF NPLLGETFEL VRTNKDIPGG FRLLVEKVQH RPVRLAMQAD
SANWSFSHSP APGQKFWGKS AEITTEGRVR VVLRLTDGSD ELYSWNVATM FLRNVVMGEK
YVEPVGSMHV ANDTTGHKAS VEFKSKGMFG GRAEDVYVTT FSPDGNDTGS GLVGTWTGGL
KTIGPGKAAS EEIWEVGEMV DNPSQTYGMT LFAARLNEIT EIEKGKMAPT DTRLRPDQRL
AEKGELEEAE KWKHRLEEAQ RARRREMEDR GEVHRPRWFV KADDSPDGEE VWKIKTGKDG
YWEERAKGSW SGVQRLFDVP EL
//
