EIF3J_PICGU
ID EIF3J_PICGU Reviewed; 279 AA.
AC A5DI69;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009};
DE Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=Eukaryotic translation initiation factor 3 30 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03009};
DE Short=eIF-3 30 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03009};
GN Name=HCR1 {ECO:0000255|HAMAP-Rule:MF_03009}; ORFNames=PGUG_02970;
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: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit J family. {ECO:0000255|HAMAP-
CC Rule:MF_03009}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK38872.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408157; EDK38872.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001485241.1; XM_001485191.1.
DR AlphaFoldDB; A5DI69; -.
DR SMR; A5DI69; -.
DR STRING; 4929.XP_001485241.1; -.
DR EnsemblFungi; EDK38872; EDK38872; PGUG_02970.
DR GeneID; 5127223; -.
DR KEGG; pgu:PGUG_02970; -.
DR eggNOG; KOG4813; Eukaryota.
DR HOGENOM; CLU_085412_0_0_1; -.
DR InParanoid; A5DI69; -.
DR OrthoDB; 1484669at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.246.60; -; 1.
DR HAMAP; MF_03009; eIF3j; 1.
DR InterPro; IPR023194; eIF3-like_dom_sf.
DR InterPro; IPR013906; eIF3j.
DR PANTHER; PTHR21681; PTHR21681; 1.
DR Pfam; PF08597; eIF3_subunit; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..279
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000366907"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..74
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COMPBIAS 35..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 31099 MW; 710B97ED18527F02 CRC64;
MSWDDDDFDV PATKTAGVSW EDEDNDDPLL ESWDIDEEEV ARKKKEEEAK KKAEKEALKQ
KQQEAKNKKL SQKSGERKLL DIDLIDEETR QELLRKAQVT SDLNNAADLF GGLGVANDDD
FDVNEHPRER AAKLAAAKQA AKPAAPRLTR DSPLEMHPLF QPTDKAEYEK LRKALATSLQ
QLAEDSPLNY SSALGIDLIR DAAQPLSLEN VRKVISTLNV IVKDKERAER QARLKKAGGT
ATGGAGKKKA KPAVKTNVSD MYKKDAGDDF DDFDDDDFM
