ID A0A0B0MWZ8_GOSAR Unreviewed; 715 AA.
AC A0A0B0MWZ8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=eIF-3-eta {ECO:0000256|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03001};
GN ORFNames=F383_33732 {ECO:0000313|EMBL:KHG06633.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG06633.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHG06633.1}.
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DR EMBL; JRRC01456922; KHG06633.1; -; Genomic_DNA.
DR RefSeq; XP_017637737.1; XM_017782248.1.
DR AlphaFoldDB; A0A0B0MWZ8; -.
DR SMR; A0A0B0MWZ8; -.
DR GeneID; 108479568; -.
DR KEGG; gab:108479568; -.
DR OMA; HLFWAPR; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000032142; 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; 2.
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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03001,
KW ECO:0000256|PIRNR:PIRNR036424};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03001,
KW ECO:0000256|PIRNR:PIRNR036424};
KW Reference proteome {ECO:0000313|Proteomes:UP000032142};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03001,
KW ECO:0000256|PIRNR:PIRNR036424}.
SQ SEQUENCE 715 AA; 82502 MW; 117092141A195064 CRC64;
MAAEVMLMNE IEAKAASMGI DLNIDFNSIQ LPRGEDCGIV SDDEDVYHDD QLEFDSGFGN
VIVVDNLPVV PREKFEKLEG VIRKIYSQIG VIKEDGLWMP VDPETKKTLG YCFIEYNTPQ
EAELAKEKTN GYKLDRAHIF AVNMFDDFDK YMRVPDEWAP PEIKPYTPGE NLQKWLTDEK
ARDQFVIRAG TDTEVLWNDA RQSKTELVYK RTYWTESFVQ WSPLGTYLAT VHRQGAAVWG
GANTFNRLMR YAHPQVKLID FSPGEKFLVT YSSHEPSNPR DANRVVINIF DVRTGKVMRD
FKGSADEFTI GGAGGVAGVS WPVFRWGGGK EDKYFAKLGK NMISVYETET FSLIDKKSLK
VENVVDFSWS PTDLILALFV PELGGGNQPA RVSLVQIPSK VELRQKNLFS VSDCKMYWQS
NGEYLAVKAD RYTKTKKSTY TGFELFRIKE RDIPIEVLEL DNKNDKIIAF AWEPKGHRFA
VIHGDNPRPD ISFYSMKSSH NLGRVSKLTT LKGKQANALF WSPGGRFIVL AGLKGFNGQL
EFFNVDELET MATAEHFMAT DIEWDPTGRY VATAVTSVHE MENGFNIWSF HGKLLYRILK
DHFFQFLWRP RPPSFLSAEK EEEILKYLKK YSKKYDAEDQ DVSMLLSEQD REKRRMLKEE
WEKWISEWRR ASEEEKLERQ KLRDGEASDE EEEYEAKEVE VEEILDFSEE VLFEE
//
