ID A5DWV6_LODEL Unreviewed; 394 AA.
AC A5DWV6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 22-FEB-2023, entry version 75.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN ORFNames=LELG_01843 {ECO:0000313|EMBL:EDK43664.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43664.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK43664.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
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; CH981525; EDK43664.1; -; Genomic_DNA.
DR RefSeq; XP_001527014.1; XM_001526964.1.
DR AlphaFoldDB; A5DWV6; -.
DR STRING; 379508.A5DWV6; -.
DR GeneID; 5233689; -.
DR KEGG; lel:LELG_01843; -.
DR VEuPathDB; FungiDB:LELG_01843; -.
DR eggNOG; KOG1470; Eukaryota.
DR HOGENOM; CLU_014001_1_1_1; -.
DR InParanoid; A5DWV6; -.
DR OMA; DIHARPC; -.
DR OrthoDB; 878418at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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; PTHR45824; GH16843P; 1.
DR PANTHER; PTHR45824:SF6; GH16843P; 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:UP000001996}.
FT DOMAIN 185..342
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 44677 MW; 22C536F7B203C077 CRC64;
MFGKLKNKIT ASSSKTPPPS GDSSETSSLN EKIKNGLSTT HEGDDQQSLS SGASSSKNGL
SASTPRYIPF DAPSTESHIP SEPKLTEEQK GMYLKVLKYF QNPDLCISTS EENHKHKIRC
SPNDGGLLTA GEKSWLTREC FLRYLRATKW HVEEAIDRIE LTLAWRREFG ISEPFDKDNE
VDGKLTGPEN ETGKEVILGY DNDSRPCLYL KPGRQNTKTS QRQVQHLVYM LEKVIDYMPS
GQDSLALLID FKAHPVGTQG GKIPPVGTGR QVLHILQTHY PERLGKALLT NIPWLGWTFL
KIIHPFIDPL TREKLVFDQP FENYVPKVQL DKDFHGDVNF VYEHDKYWPK MIEISQEKKH
KYFTRFEKFG ACIGLSEVDL RGDNDELIHP VGTI
//
