ID D7SV75_VITVI Unreviewed; 718 AA.
AC D7SV75;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 OrderedLocusNames=VIT_04s0008g07070 {ECO:0000313|EMBL:CBI21174.3};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI21174.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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 EMBL; FN595231; CBI21174.3; -; Genomic_DNA.
DR RefSeq; XP_002285591.1; XM_002285555.3.
DR AlphaFoldDB; D7SV75; -.
DR STRING; 29760.D7SV75; -.
DR PaxDb; 29760-VIT_04s0008g07070-t01; -.
DR EnsemblPlants; Vitvi04g00640_t001; Vitvi04g00640_P001; Vitvi04g00640.
DR GeneID; 100244090; -.
DR Gramene; Vitvi04g00640_t001; Vitvi04g00640_P001; Vitvi04g00640.
DR KEGG; vvi:100244090; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_2_0_1; -.
DR InParanoid; D7SV75; -.
DR OMA; LWGGPQF; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000009183; Chromosome 4.
DR ExpressionAtlas; D7SV75; baseline and differential.
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; IBA:GO_Central.
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 GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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:UP000009183};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 59..146
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 674..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 82761 MW; 05A1F770D59738ED CRC64;
MAEVISMEDI RATASTLGID VSNIDFDSIR LPPGEDFGIT SDDDLHEEDP LEYDSGFGNI
IVVDNLPVVP REKFEKLEGV VRKIYSQIGV IKEDGLWMPV DSDTQKTLGY CFIEYNTPQE
AELAREKTNG YKLDRAHIFA VNMFDDFDRF MKVPDEWAPP ETKPYTPGEN LQHWLTDEKA
RDQFVIRAGS DTEVLWNDAR HLKPEPVYKR AYWTESFVQW SPLGTYLATV HRQGAAVWGG
ATAFNRLMRY AHPQVKLIDF SPGEKYLVTY SSHEPSNPRD THRVVLNVFD VRTGKVMRDF
KGSMDEFSVG GAGGVSGVSW PVFRWGGGKE DKYFARIGKN VISVYETETF SLIDKKSLKV
ENVMDLSWSP ADPILALFVP ELGGGNQPAR VSLVQIPSKE ELRQKNLFSV SDCKMYWQSN
GDYLAVKVDR YTKTKKSTYT GFELFRIKER DIPIEVLELE NKNDKIIAFA WEPKGHRFAV
IHGDSPRPDV SFYTMRSGSN TGRVSKLTTL KGKQANALFW SPAGRYIILA GLKGFNGQLE
FYNVDELETM ATAEHFMATD IEWDPTGRYV ATSVTSVHEM ENGFNIWSFN GKLLYRILKD
HFFQFLWRPR PPSFLSPEKE EEIAKNLKKY SKKYEAEDQD VSMLLSEQDR EKRKMLKDEW
ERWVNDWKRW HEEEKAERQR LRDGEASDEE EEYEAKEVEV EELLDVSEEV LSFDLDQE
//
