ID   A0A2J6T1L2_9HELO        Unreviewed;       991 AA.
AC   A0A2J6T1L2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Oxysterol-binding protein {ECO:0000313|EMBL:PMD56906.1};
GN   ORFNames=K444DRAFT_654069 {ECO:0000313|EMBL:PMD56906.1};
OS   Hyaloscypha bicolor E.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX   NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD56906.1, ECO:0000313|Proteomes:UP000235371};
RN   [1] {ECO:0000313|EMBL:PMD56906.1, ECO:0000313|Proteomes:UP000235371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E {ECO:0000313|EMBL:PMD56906.1,
RC   ECO:0000313|Proteomes:UP000235371};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC       {ECO:0000256|ARBA:ARBA00008842}.
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DR   EMBL; KZ613847; PMD56906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6T1L2; -.
DR   STRING; 1095630.A0A2J6T1L2; -.
DR   InParanoid; A0A2J6T1L2; -.
DR   OrthoDB; 960at2759; -.
DR   Proteomes; UP000235371; 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; 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; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          222..316
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          175..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  108453 MW;  574E27B5A7F0B574 CRC64;
     MAGLEQLEIH SKSYIVRWVK IEEGHTISWN VQPHKKSINF GIFKHPGGSS TGTAQHLDDA
     TASLIHLDAG VDKLRRPSNA TKNDESTAQE QLRAKGFISI QWYGKYDADK VSTGTFSVTK
     GQGGMYGLVF DNTFSKQFSK SATFVLLTYP SNAPPHTTHQ LSNLASSMST TGIGNASKGV
     SPHLGPSASD SVDSLQSHLG LGTGGSRGGS VLGRNGSDNG LATYHVGILS KRRRKRGQGY
     ARRFFSLDFA SCTLSYYYSR NSSALRGAIP LSLAAIAADE RRREISIDSG AEVWHLKAGN
     AKDFDEWTRA LEKASKSARG LEPESAPDSP EQRLRVRTTG LQAPSSTREE EREWEQVESL
     VSRIVGTRDA VRRLSKDTAP GATKRLALAG LGLSTGSSPS IDEGSDYFAT PPEKRPFWKR
     KVSTPSTPQL VQRGISSQLA VPAPATVTTI TANGSVTPSS RRGRHSSQLD EPSMHEHCAA
     LLKDLDDVLN DFSTLLSNSK RRRMPAPVSA TRNSMDSTST GEFYDAEAGD GERSQVFVID
     RQSEEDTQLS EADDEFVTDA SSISSHEEDS SAHLQGSAAL FPLKPKSLDP LPITTSIKRR
     KIVPPATTMP PSLIGHLRKN VGKDLSTLSM PVSANEPTSL LQRIAEQCEY SQLLDTAASH
     KVPTQRILHV AAFAVSQFSI NRAKERAIRK PFNPMLGETF ELVRTEKEVP GGFRLLVEKV
     SHRPVRMAIQ ADSARWSLSQ SPAPTQKFWG KSVELITEGR VRLNLRLLDG SDEFYSWNLA
     TVFLRNVVMG EKYVEPVGSM TITNETTGAK ATIEFKQKGM FSGRSEDVQI ESYNPDGVHT
     GVGLTGTWTT NLRSLEAGKA AGAEIWHVGD LVENAAQTYG LTTFAAGLNE ITELEKGKLP
     PTDCRLRPDQ RAAEMGDLDT AETWKATLEA SQRVRRKEAE ERGQPHMPRW FVRVEGGDDG
     EEVWKLKGGR DGYWEERQRG KWTGVENILA G
//