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Database: UniProt
Entry: A0A0F8XBU3_9EURO
LinkDB: A0A0F8XBU3_9EURO
Original site: A0A0F8XBU3_9EURO 
ID   A0A0F8XBU3_9EURO        Unreviewed;       329 AA.
AC   A0A0F8XBU3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   SubName: Full=Phosphatidylinositol transporter {ECO:0000313|EMBL:KKK27010.1};
GN   ORFNames=ARAM_006352 {ECO:0000313|EMBL:KKK27010.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK27010.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK27010.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK27010.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KKK27010.1}.
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DR   EMBL; JZBS01000158; KKK27010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8XBU3; -.
DR   STRING; 308745.A0A0F8XBU3; -.
DR   OrthoDB; 6048at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   PANTHER; PTHR45657; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1.
DR   PANTHER; PTHR45657:SF1; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   PRINTS; PR00180; CRETINALDHBP.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          105..278
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  36970 MW;  97B4459712298B37 CRC64;
     MAAAVGNQST PASKYDNYDF PTTAPQAHPG HPGHTTPEQD AKVVQLRSEL EQLGYTERLD
     TLTLLRFLRA RKFDVAASKT MFVESEKWRK EFGTDYLAAS FKYDEKPQVF KYYPQYYHKT
     DKDGRPVYIE KLGGIDLNAM YKITTSDRML KNLVTEYEKL ADPRLPACSR KAGKLLETCC
     TIMDLKGVGI TKVSSVYTYV SQASAISQNY YPERLGKLYL INAPWGFSGA FSMVKSFLDP
     VTVEKIHILG SNYQSELLKQ VPAENLPKEF GGTCECAGGC ELSDMGPWQE SEWAKPPNWK
     IPEHEKDVIK NEASGPEKID TQEASQPTA
//
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