CAF20_PICGU
ID CAF20_PICGU Reviewed; 173 AA.
AC A5DEY7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Cap-associated protein CAF20;
GN Name=CAF20; ORFNames=PGUG_01838;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., 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.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Acts as an inhibitor of cap-dependent translation. Competes
CC with eIF4G1 and EAP1 for binding to eIF4E and interferes with the
CC formation of the eIF4F complex, inhibiting translation and stabilizing
CC mRNA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAF20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK37740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408156; EDK37740.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001486167.1; XM_001486117.1.
DR AlphaFoldDB; A5DEY7; -.
DR SMR; A5DEY7; -.
DR STRING; 4929.XP_001486167.1; -.
DR EnsemblFungi; EDK37740; EDK37740; PGUG_01838.
DR GeneID; 5127580; -.
DR KEGG; pgu:PGUG_01838; -.
DR eggNOG; ENOG502S2E7; Eukaryota.
DR HOGENOM; CLU_128343_0_0_1; -.
DR InParanoid; A5DEY7; -.
DR OrthoDB; 1474950at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005845; C:mRNA cap binding complex; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR031456; Caf20.
DR Pfam; PF17052; CAF20; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Protein synthesis inhibitor; Reference proteome; Translation regulation.
FT CHAIN 1..173
FT /note="Cap-associated protein CAF20"
FT /id="PRO_0000330089"
FT REGION 49..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 173 AA; 19539 MW; 42A835A91D1A655E CRC64;
MVKYTEDELL EFQEIAYNPQ PQVLDAFNQM VDEVREHANA EIERQKHLKW SNGDTYIDEN
GNERPYHHLN RRRGSRSGAK PNLKRKGAES VTVDDDGWAT LAKPKKSFGA EEAGEERTKF
RDSLKDGSVK ARPNNKNLGS SKAVDPRDAI ADKNTISFNA FEALGDDSDD DDE
