EIF3B_DROGR
ID EIF3B_DROGR Reviewed; 690 AA.
AC B4J6D5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=GH20755;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916367; EDW00908.1; -; Genomic_DNA.
DR RefSeq; XP_001986041.1; XM_001986005.1.
DR AlphaFoldDB; B4J6D5; -.
DR SMR; B4J6D5; -.
DR STRING; 7222.FBpp0154661; -.
DR EnsemblMetazoa; FBtr0156169; FBpp0154661; FBgn0128218.
DR GeneID; 6559447; -.
DR KEGG; dgr:6559447; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; B4J6D5; -.
DR OMA; NVADCKI; -.
DR OrthoDB; 1194797at2759; -.
DR PhylomeDB; B4J6D5; -.
DR Proteomes; UP000001070; 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_0000363796"
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 292..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 613..646
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; 80313 MW; ED9D151915358305 CRC64;
MAKKKSEDHS GADANDSDYN EEPNFDDPPN FVDNISDEDL LGDMLAQRPS EADGVESVVV
VDNMPKVEPS RLDKLKSVIN KLFSHCGEIV NVVYPVDEEG NTKGYAFMEY KTASQAEDAV
KKLNNHRLDK NYTFAVNLFT DFQKYENIPE KWEPPTVQPF KVQSDLYNFI NDPDTYDQYC
VAAETAPNCV QVGFWQNTLP EPNELETRER FTDTFVKWSP LGTYVVTFHK PGVAIWGGSS
FQKIQKFPHP GTQFVEFSPC ENYLVTYGPT PTGQKIIIWD IRTGGEKRSF VGDGMSVLSM
FRWSHDDKYV ARMGESSIHI YETPSFYLLD LKSIKIPGIR GFSWSPTDNV IAYWVEEQNQ
IPARVTLMKI PKKREIRNKN LFHVADCKLH WQKSGDYLCV KVDRYSKLKK DKKELDVKFL
GMFYNFEIFH MREKEIPVDS IEIRELILAF AWEPIGNKFS IIHGEQNSAN VSFYEVNKGV
KPSLVKRLEK KSCTHLFWSP RGQFIVMANL TMGTFEFVDT TNDYIISASP DHFRASEVEW
DPTGRYVVTG VSSWKVKEDT GFNMYTLQGR IIKRTILKNF VQFLWRPRPP TLLSEEKQKE
IKKNLKKYYP TFEQKDRLRL TRASKELLEK RAQLRETFME YRNKRIAEWK DQKSRRQMLR
GHVDTDNLET DEVDEEVVEF LVKEEITLLE
