EIF3B_YEAS7
ID EIF3B_YEAS7 Reviewed; 765 AA.
AC A6ZPJ1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 90 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Translation initiation factor eIF3, p90 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
GN Name=PRT1 {ECO:0000255|HAMAP-Rule:MF_03001}; ORFNames=SCY_5406;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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. {ECO:0000255|HAMAP-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; AAFW02000032; EDN63681.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZPJ1; -.
DR SMR; A6ZPJ1; -.
DR IntAct; A6ZPJ1; 2.
DR MINT; A6ZPJ1; -.
DR PRIDE; A6ZPJ1; -.
DR EnsemblFungi; EDN63681; EDN63681; SCY_5406.
DR HOGENOM; CLU_011152_4_0_1; -.
DR Proteomes; UP000007060; 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 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 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 Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW RNA-binding.
FT CHAIN 1..765
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000366878"
FT DOMAIN 77..162
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REGION 1..136
FT /note="Sufficient for interaction with HCR1 and TIF32"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REGION 28..261
FT /note="Sufficient for interaction with PIC8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06103, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06103"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06103, ECO:0000255|HAMAP-
FT Rule:MF_03001"
SQ SEQUENCE 765 AA; 88329 MW; C4A667003DAA92A8 CRC64;
MKNFLPRTLK NIYELYFNNI SVHSIVSRNT QLKRSKIIQM TTETFEDIKL EDIPVDDIDF
SDLEEQYKVT EEFNFDQYIV VNGAPVIPSA KVPVLKKALT SLFSKAGKVV NMEFPIDEAT
GKTKGFLFVE CGSMNDAKKI IKSFHGKRLD LKHRLFLYTM KDVERYNSDD FDTEFREPDM
PTFVPSSSLK SWLMDDKVRD QFVLQDDVKT SVFWNSMFNE EDSLVESREN WSTNYVRFSP
KGTYLFSYHQ QGVTAWGGPN FDRLRRFYHP DVRNSSVSPN EKYLVTFSTE PIIVEEDNEF
SPFTKKNEGH QLCIWDIASG LLMATFPVIK SPYLKWPLVR WSYNDKYCAR MVGDSLIVHD
ATKNFMPLEA KALKPSGIRD FSFAPEGVKL QPFRNGDEPS VLLAYWTPET NNSACTATIA
EVPRGRVLKT VNLVQVSNVT LHWQNQAEFL CFNVERHTKS GKTQFSNLQI CRLTERDIPV
EKVELKDSVF EFGWEPHGNR FVTISVHEVA DMNYAIPANT IRFYAPETKE KTAKDVIKRW
SLVKEIPKTF ANTVSWSPAG RFVVVGALVG PNMRRSDLQF YDMDYPGEKN INDNNDVSAS
LKDVAHPTYS AATNITWDPS GRYVTAWSSS LKHKVEHGYK IFNIAGNLVK EDIIAGFKNF
AWRPRPASIL SNAERKKVRK NLREWSAQFE EQDAMEADTA MRDLILHQRE LLKQWTEYRE
KIGQEMEKSM NFKIFDVQPE DASDDFTTIE EIVEEVLEET KEKVE
