EIF3B_ASPCL
ID EIF3B_ASPCL Reviewed; 741 AA.
AC A1CS92;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=ACLA_032480;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW08513.1; -; Genomic_DNA.
DR RefSeq; XP_001269939.1; XM_001269938.1.
DR AlphaFoldDB; A1CS92; -.
DR SMR; A1CS92; -.
DR STRING; 5057.CADACLAP00002466; -.
DR EnsemblFungi; EAW08513; EAW08513; ACLA_032480.
DR GeneID; 4701103; -.
DR KEGG; act:ACLA_032480; -.
DR VEuPathDB; FungiDB:ACLA_032480; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_4_0_1; -.
DR OMA; NVADCKI; -.
DR OrthoDB; 1194797at2759; -.
DR Proteomes; UP000006701; 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; 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_0000363807"
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..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 84481 MW; 3631C778AD42BBF9 CRC64;
MAPSFDTLSE QDLHEEEEEE IDVSDLKAQY EVKLEEGLDT FVVIDGLPVV PEESRQKLVK
FLMRKLNTVG HTSEDAVFMP VNDKNMSEGY AFVEYETPEQ AVAAVKQLHG TPLDKKHTLL
VNKLMDIERY GREGRIDEEY KPPTIEPFKE KEHLRSWLSD PNARDQFALY RGDKVGVFWN
NKNNPPENVV DRAHWTQLFV QWSPKGTFLA SVHPQGVQLW GGPAFSKQKQ FPHPFVQLIE
FSPGESYLTT WSARPIQVEE GQPILSYEED GKNIIVWDIE TGKPLRSFVS HDLSAPGGES
DAQPKKKVQW PAFKWSADEK YVARMLQGQS ISIYELPRMN LLGKTSVKVD GVMDFEWSPA
TVNREGVKQY EQLLCFWTPE IGSNPARVAM MSVPSKEIVR TRNLFNVSDV KLHWQSQGSF
VCVKVDRHSK SKKSMATNLE IFRVREKGVP VEVVDSLKDT VINFAWEPNG SRFVLITNGE
TVAGAAVAPK TAVSFFAREK KGGAAGNFKL VRTIEKKNSN AIYWSPKGRF VVVATVHSQT
SFDMDFWDMD FEGEKPEAEK DLTANVQLMK TLEHYGVTDI DWDPTGRYVV SSASAWTHSL
ENGWNMHTFS GNTLSENPTE KFKQFLWRPR PPTFLSKEEQ KQVRKNLREY SKEFDEEDRY
AVDIANTAVV EKRKRVLSEW IAWIRREKEL LSEDKDAYGL PEDVDDPKKA KDAPAVTSEQ
GEAVVEEIVE EIVEESEEVI G
