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Database: UniProt
Entry: G0WH29_NAUDC
LinkDB: G0WH29_NAUDC
Original site: G0WH29_NAUDC 
ID   G0WH29_NAUDC            Unreviewed;       450 AA.
AC   G0WH29;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN   Name=NDAI0J02150 {ECO:0000313|EMBL:CCD27107.1};
GN   OrderedLocusNames=NDAI_0J02150 {ECO:0000313|EMBL:CCD27107.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD27107.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD27107.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR   EMBL; HE580276; CCD27107.1; -; Genomic_DNA.
DR   RefSeq; XP_003672350.1; XM_003672302.1.
DR   AlphaFoldDB; G0WH29; -.
DR   STRING; 1071378.G0WH29; -.
DR   GeneID; 11494445; -.
DR   KEGG; ndi:NDAI_0J02150; -.
DR   eggNOG; KOG1470; Eukaryota.
DR   HOGENOM; CLU_016665_3_0_1; -.
DR   OMA; WRLIKGW; -.
DR   OrthoDB; 1539at2759; -.
DR   Proteomes; UP000000689; Chromosome 10.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 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; PTHR46590:SF1; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN CSR1; 1.
DR   PANTHER; PTHR46590; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN CSR1-RELATED; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
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:UP000000689}.
FT   DOMAIN          201..360
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          51..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  52244 MW;  B2713F9C42F48960 CRC64;
     MATEKEPKPL TTTMSLQDIT TDQETTLKQI WTYLFHLWGI PVDGTNAFKK DPSLHSLSPQ
     TSIKSVEKEP KKKSLFGKMY SMTGSSSSSS SSSFPPDSTQ QHSQHHHHHK LNERLPYTLN
     MIHPEFKQLT VPPKDTRKLF WEMLRLDPVD NHILRFARAR KWNTDNTIKM LSKTFQFRLT
     KKPINEILNK GEATIIKENK QQGLIKNLEL QKAVIYNHPT ENSACPLIVV RPKFHYSSDQ
     TEEELEHYAL LIIELARLFM REHSISILFD LTDFSLSNMD YTPVKFLIAC FEAHYPESLS
     HLFVHKAPWL FSPIWSIVKN WLDPVVASKI VFTKNTSELE RFLKPEQIPS YLGGKNDSID
     LDHYVKPDGS HDDKLKDKEG LQLVQNQRIE LIDKFVKLTV DWIQSETDEQ SKELFAERCN
     VSDDICNNYI ELDPFIRSRS SYDINGLLKL
//
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