EIF3B_DROWI
ID EIF3B_DROWI Reviewed; 690 AA.
AC B4MQL8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
GN Name=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
GN Synonyms=eIF3-S9 {ECO:0000255|HAMAP-Rule:MF_03001}; ORFNames=GK21404;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(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. The eIF-3 complex interacts with pix. Interacts with
CC mxt (By similarity). {ECO:0000250|UniProtKB:Q0E940, ECO:0000255|HAMAP-
CC 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; CH963849; EDW74407.1; -; Genomic_DNA.
DR RefSeq; XP_002063421.1; XM_002063385.2.
DR AlphaFoldDB; B4MQL8; -.
DR SMR; B4MQL8; -.
DR STRING; 7260.FBpp0250547; -.
DR PRIDE; B4MQL8; -.
DR EnsemblMetazoa; FBtr0252055; FBpp0250547; FBgn0223396.
DR GeneID; 6640577; -.
DR KEGG; dwi:6640577; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; B4MQL8; -.
DR OMA; NVADCKI; -.
DR OrthoDB; 1194797at2759; -.
DR PhylomeDB; B4MQL8; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
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:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
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 GO; GO:0030707; P:ovarian follicle cell development; IEA:EnsemblMetazoa.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 1.
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 Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..690
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000363804"
FT DOMAIN 57..141
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 207..246
FT /note="WD 1"
FT REPEAT 293..331
FT /note="WD 2"
FT REPEAT 334..369
FT /note="WD 3"
FT REPEAT 442..484
FT /note="WD 4"
FT REPEAT 530..575
FT /note="WD 5"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 614..645
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 80480 MW; B4B7E5D93DAFD5E5 CRC64;
MAKKKSEEHS SADANDSDYQ EEPNFDDPPN FVDNINDEDL LGDMLAQRPS EADGVESVVV
VDNIPKVEPS RLEKLKSVIL KVFSHCGEIV NVVYPVDDEG TTKGYAFMEY RHASQAEDAV
KKLNNHRLDK NHTFAVNLFT DFQKYENIPE KWEPPTVQPF KIQNDLYNFI NDPDAYDQYC
VAAETAPNCV QVGFWQNTLP EPNELETRER FTDTFVKWSP LGTYVVTFHK PGVAIWGGSN
FQKIQKFPHT GTQFVEFSPC ENYLVTYGPT PTGQKIIIWD IRTGSEKRSF VADGMSVLSM
FRWSHDDKFV ARMGENSIHI YETPSFYLLD LKSIKIPGIR GFSWSPTDNV IAYWVEEQNQ
IPARVTLMEI PKKREIRNKN LFHVADCKLH WQKSGDYLCV KVDRYSKLKK DKKELDVKFL
GMFYNFEIFH MREKEIPVDS VEIRELILAF AWEPIGNKFS IIHGELNSSN VSFYEVNKGV
KPSLVKRLEK KSCTHLFWSP RGQFIVMANL TMGTFEFVDT TNDYIISASP DHFRASEVEW
DPTGRYVVTG VSSWKVKEDT GFNMYTFQGR IIKRTILKNF VQFLWRPRPP TLLSEEKQKD
IKKNLKKYYP AFEQKDRLRL TRASKELLEK RSQLRETFME YRNKRIAEWK DQKSRRVMLR
GHVDTDNLET EEVDEEIVEF LVKEEITLLE
