ID A0A1A9UP55_GLOAU Unreviewed; 686 AA.
AC A0A1A9UP55;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
DE Short=eIF3b {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000256|HAMAP-Rule:MF_03001};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT010944-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT010944-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT010944-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis and, together
CC with other initiation factors, stimulates binding of mRNA and
CC methionyl-tRNAi to the 40S ribosome. {ECO:0000256|PIRNR:PIRNR036424}.
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:0000256|HAMAP-Rule:MF_03001}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03001,
CC ECO:0000256|PIRNR:PIRNR036424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001,
CC ECO:0000256|PIRNR:PIRNR036424}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000256|HAMAP-
CC Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424}.
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DR AlphaFoldDB; A0A1A9UP55; -.
DR STRING; 7395.A0A1A9UP55; -.
DR EnsemblMetazoa; GAUT010944-RA; GAUT010944-PA; GAUT010944.
DR VEuPathDB; VectorBase:GAUT010944; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000078200; 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; IEA:UniProtKB-UniRule.
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; 3.30.70.330; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03001};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03001}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 53..137
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 613..640
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..32
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 79918 MW; 9DEAC92C1EC893C9 CRC64;
MAKKKSEEPP AEGDVEEEPN FEDPEGYVDD ISDEELLADK LAQRPSEADG VESVVVVDNI
PKVEPSRLEK LKAVISKIFA NVGEIVNAVY PTDEEGKTKG YAFMEFKNAA QAEDIVEKFN
NHRLDKCHTL AVNLFTDFQK YKNIPDKWEP PTPQPFKIQN DLYSFLMDPD AYDQYCVAAE
TAPNSVQVAF WQNTLPEPTE LETRESFTDT FVKWSPLGTY VVTFHKQGVA IWGGSKFTRI
QRFPHPGTQF VEFSPCENYL VTYGPTPTGQ KVIIWDIRSG AEKRSFVADG MSMLSMFRWS
HDDKYVARLG DNSIHIYETP LFYLLDLKSI KIPGIRGFSW SPTDNVIAYW VEEQNQIPAR
VTLMEIPKKR EIRNKNLFHV ADSKLHWQKS GDYLCVKVDR YMKLKKDKKD CDVKFLGMFY
NFEIFHMREK EIPVDSVEIR ELILSFAWEP IGNKFAIIHG EANNSNVSFY EVSDGVKPTL
VKKLEKKSCT HLFWSPRGKF IVMANLTMGT FEFVDTSNNF LITASPDHFR ASEVEWDPTG
RYVVTGVSSW KVKEDTGFNM YTFQGRIIRR NILKNFVQFL WRPRPTTLLS EEEQKDIYKS
LKKYYAIFEQ KDRLRLTRAS KELLEKRAQL REQFLEYRNK RVVEWKDQKQ RRLQLRNLID
TDNLETEEVD EEVVEFLVKE EITLLE
//
