EIF3B_ASPNC
ID EIF3B_ASPNC Reviewed; 740 AA.
AC A2Q908;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Translation initiation factor eIF3 p90 subunit homolog;
GN Name=prt1; ORFNames=An01g06230;
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: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S 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_03001}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; AM269969; CAK37098.1; -; Genomic_DNA.
DR RefSeq; XP_001389047.1; XM_001389010.2.
DR AlphaFoldDB; A2Q908; -.
DR SMR; A2Q908; -.
DR PaxDb; A2Q908; -.
DR EnsemblFungi; CAK37098; CAK37098; An01g06230.
DR GeneID; 4977446; -.
DR KEGG; ang:ANI_1_800014; -.
DR VEuPathDB; FungiDB:An01g06230; -.
DR HOGENOM; CLU_011152_4_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011400; EIF3B.
DR InterPro; IPR034363; eIF3B_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR14068; PTHR14068; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW Repeat; RNA-binding; WD repeat.
FT CHAIN 1..740
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000363810"
FT DOMAIN 40..126
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 193..230
FT /note="WD 1"
FT REPEAT 232..289
FT /note="WD 2"
FT REPEAT 302..343
FT /note="WD 3"
FT REPEAT 513..556
FT /note="WD 4"
FT REPEAT 571..609
FT /note="WD 5"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 84246 MW; 0B204A1AF5D92644 CRC64;
MAPSFDTLTE QDLHEEEEEE IDFSDLKEQY EVKLEEGLDT FVVIDGLPVV PEESRQKLIK
FLLRKLNTVG HTSEDAVFMP LNDKNMSEGF AFVEYETPEQ AIAAVKQLHG VPLDKKHTLA
VNKLMDIDRY GREGRIDEEY KPPTIEPFKE KEHLRSWLGD ANARDQFALY RGDKVGVFWN
NKSNPPENVV DRAHWTQLFV QWSPKGTYLA SVHPQGVQLW GGPAFSKQKQ FPHPFVQLVE
FSPGESYLTT WSARPIQVEE GHPVLTYEED GKNIIIWDIV TGKPLRSFVS HDLTAGPGGD
GEPKKKVQWP AFKWSADEKY VARMQQHQSI SIYELPRMNL LGKTSVKIDG VMDFEWSPAT
VVREGVKQYE QLLCFWTPEI GSNPARVALM SVPSKEIVRT RNLFNVSDVK LHWQSQGTYV
CVKVDRHSKS KKSMATNLEI FRVREKGVPV EVVDSLKDTV INFAWEPNGG RFVAITTGEA
PSGAAVLPKT SVSFFAPEKK GVSAGNFKVV RTIEKKTSNA IYWSPKGRFV VVATVHSQTN
FDIDFWDMDF EGEKPEGEKD LAANLQLMKT VEHYGVTDID WDPTGRYVVS SASVWTHSME
NGYNIHTFAG QTLAEHPTDK FKQFIWRPRP PTLLSKEEQK QVRKNLREYS KEFDEEDKYA
VDIANTAVVE TRKRVLNEWA AWIRREKEML AEEKDAYGVP EDVDSSKQAK DAPAVSEDQG
ETVVEEIVEE IIEENEEVIG
