EIF3B_DROPE
ID EIF3B_DROPE Reviewed; 690 AA.
AC B4GAY7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GL11461;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479181; EDW32089.1; -; Genomic_DNA.
DR RefSeq; XP_002016199.1; XM_002016163.1.
DR AlphaFoldDB; B4GAY7; -.
DR SMR; B4GAY7; -.
DR STRING; 7234.FBpp0175568; -.
DR EnsemblMetazoa; FBtr0177076; FBpp0175568; FBgn0149070.
DR GeneID; 6591209; -.
DR KEGG; dpe:6591209; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_1_0_1; -.
DR OMA; NVADCKI; -.
DR PhylomeDB; B4GAY7; -.
DR Proteomes; UP000008744; 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_0000363799"
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 247..289
FT /note="WD 2"
FT REPEAT 293..331
FT /note="WD 3"
FT REPEAT 334..369
FT /note="WD 4"
FT REPEAT 442..484
FT /note="WD 5"
FT REPEAT 530..575
FT /note="WD 6"
FT REGION 1..37
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; 80271 MW; 5E171EBEA7A293FE CRC64;
MAKKKSEDHS GGDANDSDYN EEPNFEDPPN FVDNISDDDL LGDMLAQRPS EADGVESVVV
VDNIPKVEPV RLEKLKSVIN KLFSHCGDIV NVVYPVDEEG KTKGYAFMEY KHAGQAEEAV
KKLNNHRLDK NHTFAVNLFT DFQKYENIPE KWEPPTVQSF KVQNDLYNFI NDPDAYDQYC
VAAETSQNCV QVGFWQNVLP EPNELETRER FTDTFVKWSP LGTYVVTFHK PGVAIWGGSS
FQKIQKFPHT GTQFVEFSPC ENYLVTYGPT PTGQKIIIWD IRTGAEKRSF VADGMSVLSM
FRWSHDDKYV ARMGDNSIHI YETPSFYLLD LKSIKIPGIR GFSWSPTDNV IAYWVEEQNQ
IPARVTLMEI PKKRETRNKN LFHVADCKLH WQKSGDYLCV KVDRYSKLKK DKKELDVKFL
GMFYNFEIFH MREKEVPVDS VEIRELILAF AWEPIGNKFS IIHGEPNSAN VSFYEVNKGV
KPSLVKRLEK KSCTHLFWSP RGQFIVMANL TMGTFEFVDS TNDYIISASP DHFRASEVEW
DPTGRYVVTG VSSWKVKEDT GFNMYTFQGR IIKRTILKNF VQFLWRPRPP TLLSEDKQKD
IKKNLKKYYP AFEQKDRLRL TRASKELLEK RSQLRETFME YRNKRIGEWK EQKSRRVMLR
GHVDTDNLET EEVDEEVVEF LVKEEITLLE
