EIF3G_PICST
ID EIF3G_PICST Reviewed; 271 AA.
AC A3GGU2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF3g {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF-3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Translation initiation factor eIF3 p33 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF3 p33 homolog {ECO:0000255|HAMAP-Rule:MF_03006};
GN Name=TIF35 {ECO:0000255|HAMAP-Rule:MF_03006}; ORFNames=PICST_80765;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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. This
CC subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000255|HAMAP-
CC Rule:MF_03006}.
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DR EMBL; AAVQ01000001; EAZ63981.2; -; Genomic_DNA.
DR RefSeq; XP_001388004.2; XM_001387967.1.
DR AlphaFoldDB; A3GGU2; -.
DR SMR; A3GGU2; -.
DR STRING; 4924.XP_001388004.2; -.
DR EnsemblFungi; EAZ63981; EAZ63981; PICST_80765.
DR GeneID; 4851491; -.
DR KEGG; pic:PICST_80765; -.
DR eggNOG; KOG0122; Eukaryota.
DR HOGENOM; CLU_034595_0_0_1; -.
DR InParanoid; A3GGU2; -.
DR OMA; TTKCPFK; -.
DR OrthoDB; 1226059at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR CDD; cd12933; eIF3G; 1.
DR CDD; cd12408; RRM_eIF3G_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03006; eIF3g; 1.
DR InterPro; IPR017334; eIF3_g.
DR InterPro; IPR024675; eIF3g_N.
DR InterPro; IPR034240; eIF3G_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF12353; eIF3g; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037949; Transl_init_eIF-3_RNA-bind; 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 Reference proteome; RNA-binding.
FT CHAIN 1..271
FT /note="Eukaryotic translation initiation factor 3 subunit
FT G"
FT /id="PRO_0000366894"
FT DOMAIN 188..267
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
SQ SEQUENCE 271 AA; 30134 MW; 575D7C12E82CC337 CRC64;
MSTTVIGSWA DAGDEFSAPD ITTNPDGTKT VITYRTNQDG KKVKITQKIK EVKVQERVHP
LIAQRKNWKK YGKESKSPPG PDTSTTQLGE KVELKLGTSW KQQEKEEEEE KAENRAQKLS
VQTIRCRTCG GDHYTSKCPF KDTLGATTSS PAAESGAGDN GPGKYVPRHL RADANGNLPS
KEGRDDSTTL KVSQLNSFVD EDMLRNELFA RFGPLQRVTL VRNRETGDSR GFAYVSFITE
DMAQRALDAL NGKGYHSLIL HLEWSKKKKT V
