EIF3B_YARLI
ID EIF3B_YARLI Reviewed; 717 AA.
AC Q6C1H8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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;
GN Name=PRT1 {ECO:0000255|HAMAP-Rule:MF_03001};
GN OrderedLocusNames=YALI0F16115g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382132; CAG78293.1; -; Genomic_DNA.
DR RefSeq; XP_505484.1; XM_505484.1.
DR AlphaFoldDB; Q6C1H8; -.
DR SMR; Q6C1H8; -.
DR STRING; 4952.CAG78293; -.
DR EnsemblFungi; CAG78293; CAG78293; YALI0_F16115g.
DR GeneID; 2908586; -.
DR KEGG; yli:YALI0F16115g; -.
DR VEuPathDB; FungiDB:YALI0_F16115g; -.
DR HOGENOM; CLU_011152_4_0_1; -.
DR InParanoid; Q6C1H8; -.
DR OMA; NVADCKI; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
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; 2.130.10.10; -; 2.
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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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 Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..717
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000363827"
FT DOMAIN 28..115
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 183..221
FT /note="WD 1"
FT REPEAT 223..284
FT /note="WD 2"
FT REPEAT 293..332
FT /note="WD 3"
FT REPEAT 445..484
FT /note="WD 4"
FT REPEAT 506..549
FT /note="WD 5"
FT REPEAT 564..609
FT /note="WD 6"
FT REGION 1..216
FT /note="Sufficient for interaction with PIC8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REGION 1..89
FT /note="Sufficient for interaction with HCR1 and TIF32"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
SQ SEQUENCE 717 AA; 82678 MW; 490B976F1E4BC45E CRC64;
MTVEDNLDID FSDLEEKYAV NADEGFESFI VVDGAPVIPQ AKQAALANVM KKFFGAVGKI
KEDGIFIPFD EATGKSTGFV FIEYETGEMA AAAVKSFHNK QFDKNHKLLV NKLSEVEKYG
MQYDTLKTEE FVEPETEPFV EQGHLRSWLM DPQGRDQFVL HRGDTVGVFW NKKGDTLEAD
VDRERWTETQ VYWSPTGTYL VSTHTQGVQL WGGPDWAPPI CKFQHPNVKM VQFSPCEKFL
VTWSNVPLVL PDDEEKRKSI PFGPADEGKQ IIVWNLETRL PVRTFAMPPE KKGASMSWPI
LKFSPDDKYA ARMIPGEQLS IYETETMSLL DKKSVKAPGI VDFEWAPALV NLEGRQKSAT
ESVLCYWTPE IGNQTARVVL MKASNKEVLR TRNLFNVADC KIHWQDQGRF LCVKVDRHTK
SKKSTFTNLE FFRLCERGVP VEVMELKDTV TNMAWEPHGD RFVTISNSDS TTNYDGPLPA
NRHTLSFYAL ERHKGTQGTW KLIKAFDKKN CNSLFWSPNG RFLITVMIEG SNSIDLDFWD
MDYEGDRKHG DKDLPANLHF LGSSEHYGIS ALEWDPSGRF VATWSSYWRH HTENGYKIWD
FRGQLQREES IDRFKHFSWR PRPPTLLSKQ QKKDIRNNLE EYSRKFEEID AMEASEASRE
LIMLRKRLLE EWTAWRAQTD KKLEELGLVE PEPAESEYTT IEEIKEVVVE DKEEVCE
