ID   CAF20_LODEL             Reviewed;         219 AA.
AC   A5DTJ3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Cap-associated protein CAF20;
GN   Name=CAF20; ORFNames=LELG_00679;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
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}.
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DR   EMBL; CH981524; EDK42501.1; -; Genomic_DNA.
DR   RefSeq; XP_001528159.1; XM_001528109.1.
DR   AlphaFoldDB; A5DTJ3; -.
DR   SMR; A5DTJ3; -.
DR   STRING; 379508.A5DTJ3; -.
DR   PRIDE; A5DTJ3; -.
DR   EnsemblFungi; EDK42501; EDK42501; LELG_00679.
DR   GeneID; 5235854; -.
DR   KEGG; lel:LELG_00679; -.
DR   eggNOG; ENOG502S2E7; Eukaryota.
DR   HOGENOM; CLU_128343_0_0_1; -.
DR   InParanoid; A5DTJ3; -.
DR   OMA; GHFNRRR; -.
DR   OrthoDB; 1474950at2759; -.
DR   Proteomes; UP000001996; 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..219
FT                   /note="Cap-associated protein CAF20"
FT                   /id="PRO_0000330088"
FT   REGION          37..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   219 AA;  24081 MW;  A3A92A3312A0B71F CRC64;
     MAKYTEEQLF AIKEETSYVP QPQILSAFNE LIEQVKEHAH QQQLQYQQQQ QQQQGFSGIG
     SGVSGPGAQK WRNGDTYIDE HGHERSYHHM NRRRPSRSNN GEKKPFFNKK KTEVVVDEDG
     WETFTPVQHA HRGSIGEDGS EEKSKFRDSV SGSSGSGAGA GAGAGAASGS AGGVRARPNN
     KNLGSSKQVD PRQIASTKQT RTFNAFEALE GNDDEDDDE