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Database: UniProt
Entry: Q0CN46
LinkDB: Q0CN46
Original site: Q0CN46 
ID   EIF3B_ASPTN             Reviewed;         742 AA.
AC   Q0CN46;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=ATEG_04888;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476599; EAU35335.1; -; Genomic_DNA.
DR   RefSeq; XP_001214066.1; XM_001214066.1.
DR   AlphaFoldDB; Q0CN46; -.
DR   SMR; Q0CN46; -.
DR   STRING; 341663.Q0CN46; -.
DR   EnsemblFungi; EAU35335; EAU35335; ATEG_04888.
DR   GeneID; 4320016; -.
DR   VEuPathDB; FungiDB:ATEG_04888; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   OMA; LWGGPQF; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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..742
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000363812"
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..290
FT                   /note="WD 2"
FT   REPEAT          304..345
FT                   /note="WD 3"
FT   REPEAT          515..558
FT                   /note="WD 4"
FT   REPEAT          573..611
FT                   /note="WD 5"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  84189 MW;  2341EC202449E3AE CRC64;
     MAPSFDTLSE QDLHEEEEEE IDFSDLKAQY EVKLDEGLDT FVVIDGLPIV PEESRQKLIK
     FLLRKLSAAG KTSEDAVFMP LNEKNMSEGF AFVEYETPEQ AVAAVKQLHG TPLDKKHTLA
     VNKLMDIDRY GREGRIDEEY KPPTIEPFKE KEHLRSWLAD PNARDQFALY RGDKVGVFWN
     NKNNPPENVV DRAHWTQLFV QWSPKGTYLA SVHPQGIQLW GGPAFSKLKQ FPHPFVSLVE
     FSPAENYVTT WSARPIQVEE GGSGPLSYEE DGKNIIIWDI VTGKPLRSFV SHDLAAGPAE
     AEAQPKKKVQ WPAFKWSADE KYVARMLQGQ SISIYEAPRM NLLGKTSVKI DGVMDFEWSP
     ATVNRDGVKQ YEQLLCFWTP EIGSNPARVG MMSVPSKEIV RTRNLFNVSD VKLHWQSQGT
     YVCVKVDRHS KSKKSMATNL EIFRVREKGV PVEVVDSLKD TVINFAWEPN GGRFVLITTG
     ETPTGAAVPP KTAVSFFAPE KKGGSAGNFK LVRTIEKKTS NAIYWSPKGR FVVVATVHSQ
     SSFDLDFWDM DFEGEKPEGE KDLAANLQLM KTVEHYGVTD VDWDPTGRYV VSSASVWTHS
     MENGWNLHTF AGQTLSENPT DKFKQFIWRP RPPTLLSKEE QKQVRKNLRE YSKEFDEEDK
     YAVDIANTAV VEKRKRVLSE WLAWIRREKE LLAEDKDAYG LPENVDDAKM AKDAPQVSED
     QGETVVEEIV EEIIEENEEV IG
//
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