ID   CAF20_CANGA             Reviewed;         154 AA.
AC   Q6FKJ9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Cap-associated protein CAF20;
GN   Name=CAF20; OrderedLocusNames=CAGL0L10978g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
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DR   EMBL; CR380958; CAG62219.1; -; Genomic_DNA.
DR   RefSeq; XP_449245.1; XM_449245.1.
DR   AlphaFoldDB; Q6FKJ9; -.
DR   SMR; Q6FKJ9; -.
DR   STRING; 5478.XP_449245.1; -.
DR   EnsemblFungi; CAG62219; CAG62219; CAGL0L10978g.
DR   GeneID; 2891020; -.
DR   KEGG; cgr:CAGL0L10978g; -.
DR   CGD; CAL0135778; CAGL0L10978g.
DR   VEuPathDB; FungiDB:CAGL0L10978g; -.
DR   eggNOG; ENOG502S2E7; Eukaryota.
DR   HOGENOM; CLU_128343_0_0_1; -.
DR   InParanoid; Q6FKJ9; -.
DR   OMA; GHFNRRR; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005845; C:mRNA cap binding complex; IEA:InterPro.
DR   GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IEA:EnsemblFungi.
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   GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:EnsemblFungi.
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..154
FT                   /note="Cap-associated protein CAF20"
FT                   /id="PRO_0000330085"
FT   REGION          45..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..68
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   154 AA;  17274 MW;  199C5821ADBAE764 CRC64;
     MIKYSIDELI QLKPSETLKV SFDHVEFRNI IEKVVELQKL KEEEFHSHHG NRRRSSHHHM
     KPKIKHNKPK VKTDADGWST LEPATAGHEE ESSSSATPAA AATTKTGAPQ ETIRVKPNNK
     NISSSRPADN SDIIADKQTH GFNAFAALED EEDE