EIF3J_ASPNC
ID EIF3J_ASPNC Reviewed; 266 AA.
AC A2RBC7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=An18g06260;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270411; CAK43351.1; -; Genomic_DNA.
DR RefSeq; XP_001399079.1; XM_001399042.2.
DR AlphaFoldDB; A2RBC7; -.
DR SMR; A2RBC7; -.
DR PaxDb; A2RBC7; -.
DR EnsemblFungi; CAK43351; CAK43351; An18g06260.
DR GeneID; 4990194; -.
DR KEGG; ang:ANI_1_830164; -.
DR VEuPathDB; FungiDB:An18g06260; -.
DR HOGENOM; CLU_087988_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
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..266
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000365148"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..82
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..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 29678 MW; B579915979B0384D CRC64;
MAPSKWDDEE ESVSPPPVVA RRKFDDEEEE DVLDSWDAAE DSEVEREKAA KAAEAKAKAE
AEAAANKKSK AQRIQEKKAQ RKADADAEDS DDSDEDEAER RARLRKTEKD ADLKHAEDLF
GDIDLNRMRN RSAPKAVVIS DGTDPTQAVD LSAMPLFKPA TKDQFTRVTT TLIPLLTTQS
KKPQYALWAQ DFIKQLVKDL PSGDVKKIAS SLTTLSNEKM KEERAADKGN KKTKAAKTKV
SLVTSRENKI ETNSYDDDGL DDDDFM
