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Database: UniProt
Entry: Q2URB7
LinkDB: Q2URB7
Original site: Q2URB7 
ID   EIF3B_ASPOR             Reviewed;         741 AA.
AC   Q2URB7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=AO090005000892;
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: 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; AP007151; BAE55898.1; -; Genomic_DNA.
DR   RefSeq; XP_001817900.1; XM_001817848.2.
DR   AlphaFoldDB; Q2URB7; -.
DR   SMR; Q2URB7; -.
DR   STRING; 510516.Q2URB7; -.
DR   EnsemblFungi; BAE55898; BAE55898; AO090005000892.
DR   GeneID; 5989845; -.
DR   KEGG; aor:AO090005000892; -.
DR   VEuPathDB; FungiDB:AO090005000892; -.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   OMA; LWGGPQF; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
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; 3.30.70.330; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR   PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 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; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 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..741
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000363811"
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          303..344
FT                   /note="WD 3"
FT   REPEAT          514..557
FT                   /note="WD 4"
FT   REPEAT          572..610
FT                   /note="WD 5"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..715
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   741 AA;  84291 MW;  9FCCEAE02E0AD7A0 CRC64;
     MAPSFDTLSE QDLHEEEEEE IDFSDLKEQF EVKLEEGLDT FIVIDGLPIV PEESRQKLIK
     FLLRKLNAVG HTSEDAVFMP TNDKNMSEGF AFVEYETPEQ AIAAVKQLHG TPLDKKHTLA
     VNKLMDIDRY GREGRIDEEY KPPTVEPFKE KEHLRSWLSD PNARDQFALY RNDKVGVFWN
     NKNNPPENVV DRAHWTQLFV QWSPKGTYLA SVHPQGVQLW GGPAFSKQKQ FPHPFVQLVE
     FSPGESYLTT WSSRPIQVEE GHPVLSFEED GKNIIVWDIV SGKPLRSFVS HDLAGGPVEG
     DAAPKKKVQW PAFKWSADEK YVARMLQGQS ISIYELPRMN LLGKTSVKID GVMDFEWSPA
     TVTRDGVKQY EQLLSFWTPE IGSNPARVAL MSVPSKEIVR TRNLFNVSDV KLHWQSQGTY
     VCVKVDRHSK SKKSMATNLE IFRVREKGVP VEVVDSLKDT VINFAWEPNG GRFVLITTGE
     APSGAAVLPK TSVSFFAPEK KGPQAGNFKL VRTIEKKTSN AIYWSPKGRF VVVATVHSQS
     NFDLDFWDMD FEGEKAEGEK DLAANLQLMK TVEHYGVTDI DWDPTGRYVV SSASVWTHSM
     ENGWNIHTFA GQTLAEHPTD KFKQFVWRPR PPTLLSKEEQ KQVRKNLREY SKEFDEEDKY
     AVDIANTAVV ETRKRVLNEW VAWLRREKEL MAEEKDAYGI PEDADDAKVA KDAPPVSEDQ
     GEAVVEEIVE EIVEENEEVI G
//
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