ID   A0A2T3BDA8_AMORE        Unreviewed;       978 AA.
AC   A0A2T3BDA8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   ORFNames=M430DRAFT_111964 {ECO:0000313|EMBL:PSS27323.1};
OS   Amorphotheca resinae ATCC 22711.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Amorphothecaceae; Amorphotheca.
OX   NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS27323.1, ECO:0000313|Proteomes:UP000241818};
RN   [1] {ECO:0000313|EMBL:PSS27323.1, ECO:0000313|Proteomes:UP000241818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS27323.1,
RC   ECO:0000313|Proteomes:UP000241818};
RX   PubMed=29315638; DOI=10.1111/nph.14974;
RA   Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA   Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA   LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA   Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA   Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT   "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT   as versatile saprotrophs and plant mutualists.";
RL   New Phytol. 217:1213-1229(2018).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC       {ECO:0000256|ARBA:ARBA00008842}.
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DR   EMBL; KZ679006; PSS27323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3BDA8; -.
DR   STRING; 857342.A0A2T3BDA8; -.
DR   InParanoid; A0A2T3BDA8; -.
DR   OrthoDB; 960at2759; -.
DR   Proteomes; UP000241818; 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:UP000241818};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          217..311
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          154..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   978 AA;  107125 MW;  E746889D2C429445 CRC64;
     MALEQLEIHS KSYIVRWVKV EEGHTISWSI QPHKKSLNFG IVKHPGTGNA ANAQHVVVED
     TLLQPETAPE KQRRPSTAKN DASTAQIQLK AKGFIPIQWY GKCEADKVSR GTYSVAKGHG
     GMYGLVLDNT FSMAFSKTAT FVLLTYPSNS PPQSALHLHA GQGGLTGPSA TSLGKNQSPR
     LGATSSESVD SIPSHYANSG NKGSHARGPS DSQNTVATHH VGVLQKRRRK RGQGYARRFF
     SLDFASCTLS YYHNRNSSAL RGAIPLGLAA IAADERMREI NIDSGAEVWH LKTSSAKDFE
     EWTRALERAS AIARGVEIDD APSPERVQSR TSGLQITASH EDQEWEQAEA ILSRIAGTRD
     AMRRLYNDMA PEAKKNSNPG LGLPTNSSPM LDDNNDLLGA PSEKKSFWKR RSGLPPTAQS
     QLVGRSIPSQ LAVPAPTTVT TITANGSVTP SFRKSKNQEE IGVHDHVAAL LAELDTVVLD
     FSTLLASSKR RRAPAQIFPS RNSMDSTSTG EFYDAEGGDP DRPQVLMIGR QSEEDTPPSD
     DDFVSDASSV SSVDEDDVSP NIGHAASLFP QKPKNLDPLP VSKVLKRRKV IPPAKVMPPS
     LVATLRKNVG KDLSTISMPV SANEPISLLQ RVAEQLEYAQ ILDAAVAQKI PAQRLLHVAA
     FAISQLSSNR CKERAIRKPF NPMLGETFEL VRTEKEVPGG FRLLVEKVSH RPVRTACQAE
     SANWSFGQSS APTQKFWGKS AELITEGRIR IVLRLPDGTE ELYSWSVATV FLRNVVMGEK
     YVEPVGTMTV ANDSTGAKAT IEFKAKGMFG GRSEDVQVES YGPDGASTGF SLVGTWTTSL
     QLLENGKPVR EIWHVGDLVD NAPQTYGLTT FAASLNEITE IEKGKLPATD SRLRPDQRAA
     ERGDLDEAEE WKRRLEERQR AKRKEVEERG EVHKPRWFVK VDGGDEGEEV WKLKTGKEGY
     WEERSRGAFT GVEDIFAA
//