EIF3B_ASPOR
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 03-AUG-2022, entry version 106.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; NVADCKI; -.
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; 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..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