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Database: UniProt
Entry: A0A2B7XKI0_9EURO
LinkDB: A0A2B7XKI0_9EURO
Original site: A0A2B7XKI0_9EURO 
ID   A0A2B7XKI0_9EURO        Unreviewed;       971 AA.
AC   A0A2B7XKI0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN   ORFNames=AJ80_06768 {ECO:0000313|EMBL:PGH12254.1};
OS   Polytolypa hystricis UAMH7299.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX   NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH12254.1, ECO:0000313|Proteomes:UP000224634};
RN   [1] {ECO:0000313|EMBL:PGH12254.1, ECO:0000313|Proteomes:UP000224634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH12254.1,
RC   ECO:0000313|Proteomes:UP000224634};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC       {ECO:0000256|ARBA:ARBA00008842}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PGH12254.1}.
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DR   EMBL; PDNA01000120; PGH12254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XKI0; -.
DR   STRING; 1447883.A0A2B7XKI0; -.
DR   OrthoDB; 960at2759; -.
DR   Proteomes; UP000224634; Unassembled WGS sequence.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224634};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          213..307
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          42..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          897..924
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        395..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  108130 MW;  DE0048EFB5EC6CF5 CRC64;
     MAGMEELEIH SKSYLVRWVN VKSNHTISWS IQPHKKSLNF GIFKHPGHGP TAPPTSSNHE
     VKEDLNKENQ KAANSSSAVT EKLKNIGLKP IQWIGKCEAD KISQGTYDVE LNEGGNYALV
     IDNTFSKQIS KTATFVLLTY PSHAPPQSGH QVHHSQVLAG LTGVQAANRS TTNIAAGPSD
     STESLRQNRP WAWSISGARP PPRSSDSSRS FPLTVHTGVL QKRRRKRHQG YARRFFSLDF
     TSSTLSYYHD RNSSALRGAI PLALAAIATN DNTREISIDS GVEIWHLRAL TENDFRAWKH
     ALEKASKPQD AAPSTSEPRL RIQTEALQRV PSFATESRDW TEVEALVEKV TRSRDMVRRL
     AQDTDPKYLS TPIERRGRSR SPGAKSTRNA VEANGDENGE TKERRSFWKL KPKDNNIISS
     SALKRNVSSQ HLPSPASTDS HSIGKGLVES PARVEHIHDD LMALLRDLNT VVTEFSTLLT
     DRKHNRLSVP PSAKPRASFE SDMSQEFFDA VDGKLSPLLT IQGDSDDEGK SVMEDRTDEE
     ESLSGSDVDE SDTFITSGLR LDTSSSLFPA KPRSLVPLPL SSVSRRMKIP PPTVMPPSLI
     GFLRKNVGKD FSTISMPVSA NEPLSLLQKA AEQFEYSQLL DKATSATEGL ERLLYVTAFA
     ISILSNNRVK ERIIRKPFNP MLGETYELVR EDKGFRFIAE KVSHRPVQLA FHADAKDWSF
     AQSPKPSQKF WGKSAEIITE GKARLTLHSS GEHFSWSNAA SFLRNIIAGE KYVEPVGEMC
     VLNETTGQKT ITTFKAGGMF SGRSEEVSVK AFDTHGEELP LGLEGTWTGA LQLTQHGNQT
     NKTIWSAGSL VDKAAKHYGL TTFAACLNEI TPIEDAKLPA TDTRLRPDQR ALEQGDVDGA
     EDLKAQLEER QRERRREMEE AGDSWRPRWF TKVDPDNGCE EEVWKIRTGK DGYWEERAKG
     TWTGTLNVFQ L
//
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