EIF3B_DROSI
ID EIF3B_DROSI Reviewed; 690 AA.
AC B4QB88;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=GD11284;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CM000362; EDX07512.1; -; Genomic_DNA.
DR RefSeq; XP_002081927.1; XM_002081891.2.
DR AlphaFoldDB; B4QB88; -.
DR SMR; B4QB88; -.
DR STRING; 7240.B4QB88; -.
DR EnsemblMetazoa; FBtr0211194; FBpp0209686; FBgn0183033.
DR GeneID; 6734930; -.
DR HOGENOM; CLU_011152_1_0_1; -.
DR OMA; NVADCKI; -.
DR PhylomeDB; B4QB88; -.
DR Proteomes; UP000000304; Chromosome 2r.
DR Bgee; FBgn0183033; Expressed in embryo and 3 other tissues.
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_0000363802"
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..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 595..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; 80332 MW; C1DF2393FAC06D80 CRC64;
MAKKKSEEHS GADANDSDYQ EEPNFEDPPG FVDNISDEDL LGDMLAQRPS EADGVESVVV
VDNIPKVEPV RLEKLKSVIN KLFSNYGDIV NVVYPVDEEG KTKGYAFMEY KQASQAEEAV
KKLNNHRLDK NHTFAVNLFT DFQKYENIPE KWEPPTVQTF KVQSDLYNFI NDPDTYDQYC
VAAETAPNCV QVGFWQNVLP EPFELETRER FTDTFVKWSP LGTYVVTFHK PGVAIWGGSS
FQKIQKFPHP GTQFVEFSPC ENYLVTYGPT PTGQKIIIWD IRTGAEKRSF VADGMSVLSM
FRWSHDDKFV ARMGENSIHI YETPSFYLLD LKSIKIPGIR GFSWSPTDNV IAYWVEEQNQ
IPARVTLMEI PKKREIRNKN LFHVADCKLH WQKSGDYLCV KVDRYSKLKK DKKDLDVKFL
GMFYNFEIFH MREKEIPVDS VEIRELILAF AWEPIGNKFS IIHGETNSSN VSFYEVNKGV
KPSLVKRLEK KSCTHLFWSP RGQFIVMANL TMGTFEFVDS TNDYIITSSP DHFRASEVEW
DPTGRYVVTG VSSWKVKEDT GFNMYTFQGR IIKRTILKNF VQFLWRPRPP TLLSEEKQKE
IKKNLKKYYA AFEQKDRLRL TRASKELLEK RSQLRETFME YRNKRIAEWA DQKSRRIMLR
GHVDTDNLET DEVDEEIVEF LVKEEVTLLE
