ID C4XY16_CLAL4 Unreviewed; 298 AA.
AC C4XY16;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 03-MAY-2023, entry version 56.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN ORFNames=CLUG_00839 {ECO:0000313|EMBL:EEQ36716.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ36716.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ36716.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ36716.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; CH408076; EEQ36716.1; -; Genomic_DNA.
DR RefSeq; XP_002619680.1; XM_002619634.1.
DR AlphaFoldDB; C4XY16; -.
DR STRING; 306902.C4XY16; -.
DR GeneID; 8500427; -.
DR KEGG; clu:CLUG_00839; -.
DR VEuPathDB; FungiDB:CLUG_00839; -.
DR HOGENOM; CLU_014001_0_1_1; -.
DR InParanoid; C4XY16; -.
DR OMA; WAFSTVW; -.
DR OrthoDB; 6048at2759; -.
DR Proteomes; UP000007703; 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:UP000007703}.
FT DOMAIN 97..270
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
SQ SEQUENCE 298 AA; 34441 MW; CE9F9DC2F72E94E4 CRC64;
MPTEAEILAS YPQISAPTTQ TGFTSNLTEE QRAIMLKLRE QLVAMGFEFR LDDASLLRFL
RARKFDLEKA KTMFVECEKW RKEFGTNTIL EDFHYTEKPL VAKMYPQYYH ETDKDGRPVY
FEELGKVYLP DMLKITTQER MLKNLVWEYE SFTRNRLPAC SRKQGHLVET SCTIMDLKGI
SISAAYQVVG YVREASKIGQ DYYPERMGKF YCINAPFGFS TAFKLFKPFL DPVTVSKIFI
LGSSYKKELL KQIPAENLPA KFGGTSKVTE EELYMNDYGP WRDPKYIGPE GEAPRAIS
//
