EIF3J_ASPOR
ID EIF3J_ASPOR Reviewed; 265 AA.
AC Q2UMC5;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
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;
DE Short=eIF-3 30 kDa;
GN Name=hcr1; ORFNames=AO090003000054;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
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DR EMBL; AP007155; BAE57290.1; -; Genomic_DNA.
DR RefSeq; XP_001819292.1; XM_001819240.2.
DR AlphaFoldDB; Q2UMC5; -.
DR SMR; Q2UMC5; -.
DR STRING; 510516.Q2UMC5; -.
DR EnsemblFungi; BAE57290; BAE57290; AO090003000054.
DR GeneID; 5991275; -.
DR KEGG; aor:AO090003000054; -.
DR VEuPathDB; FungiDB:AO090003000054; -.
DR HOGENOM; CLU_087988_0_0_1; -.
DR OMA; HYGLFLE; -.
DR Proteomes; UP000006564; Chromosome 2.
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..265
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000365149"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 29689 MW; DB19734AB269D46B CRC64;
MAPERWDDEE DSVSPPPVAP RRRFDDEEED EVLDSWDAAE DSEVEREKAA KAAEAKAKAD
AEAAAKKKSK SQRIQEHKEE RKKKAEEEDS DSEEEDDADK RARLRRAQKD ADLKHAEDLF
GDIDLNRNRG APKAIVISDS ADPTQAVDLS AMPLFKPTTK EQFARLTSTL IPLLTPHSKK
PHYSLWAQEF AKQLVKELNS ADVKKIASAM TTMSNEKMRE ERAADKGSKK SKAAKTKVSL
VTSRDNKLDA DYDNGDDGLG DDDFM
