ID A0A1Q3C8Z3_CEPFO Unreviewed; 715 AA.
AC A0A1Q3C8Z3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JUN-2023, entry version 23.
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=CFOL_v3_20054 {ECO:0000313|EMBL:GAV76581.1};
OS Cephalotus follicularis (Albany pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV76581.1, ECO:0000313|Proteomes:UP000187406};
RN [1] {ECO:0000313|Proteomes:UP000187406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA Fukushima K., Hasebe M., Fang X.;
RT "Cephalotus genome sequencing.";
RL Submitted (APR-2016) 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:GAV76581.1}.
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DR EMBL; BDDD01001508; GAV76581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3C8Z3; -.
DR STRING; 3775.A0A1Q3C8Z3; -.
DR InParanoid; A0A1Q3C8Z3; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000187406; 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:UP000187406};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 60..147
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 676..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 82573 MW; F418C331A97B3915 CRC64;
MADTMVMKEV EATAARIGID LTQLDLDSIH LPPGENFDIV SDDDEVYDTH NLEFDSGFGN
IVVVDNLPVV PREKFEKLEG VVRKIYSQIG VIREDGLWMP VDPDSQKSLG YCFIEYNTPQ
EAELAREKTN GYKLDRAHIF AVNMFDDFER FMKVPDQWAP PESRPYAPGE NLQQWLTDEK
ARDQFVIRAG TDTEVFWNDA RHLKPEPVYK RAYWTESFVQ WSPLGTYLAT VHRQGAAVWG
GATTFNRLMR YAHPQVKLVD FSPGERYLVT YSSHEPSNPR DANRVVINIF DVRTGKVMRD
FKGSADEFAI GGTGGVSGVS WPVLRWGGGN EDRYFAKMGK NMISVYETET FALIDKKSLK
VENVMEFNWS PTDPIIALFV PELGGGNQPA RVSLIQIPSK EELRQKNLFS VSDCKMYWQS
SGDYLAVKVD RYTKTKKSTY TGFELFRIKE RDIPIEVLEL DNKNDKIIAF AWEPKGHRFA
VIHGDSPRPD VSFYSMHTAQ HTSRVSKLAT LKGKQANALF WSPTGRFVIL AGLKGFNGQL
EFFNVDELET MATAEHFMAT DIEWDPTGRY VATAVTSVHE MENGFNIWSF NGKLLYRIPK
DHFFQYLWRP RPPSFLSPEK EEEIAKNLKK YSKKYEAEDQ DVSLLLSEQD REKRRMLKDE
WERWVNEWKR LHEEEKFERQ KLRDGEASDE EEEYEAKEVE VEELLDVSEE ILIDN
//
