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EIF3G_ASHGO
ID   EIF3G_ASHGO             Reviewed;         269 AA.
AC   Q759T4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
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}; OrderedLocusNames=ADR189W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52109.1; -; Genomic_DNA.
DR   RefSeq; NP_984285.1; NM_209638.1.
DR   AlphaFoldDB; Q759T4; -.
DR   SMR; Q759T4; -.
DR   STRING; 33169.AAS52109; -.
DR   EnsemblFungi; AAS52109; AAS52109; AGOS_ADR189W.
DR   GeneID; 4620447; -.
DR   KEGG; ago:AGOS_ADR189W; -.
DR   eggNOG; KOG0122; Eukaryota.
DR   HOGENOM; CLU_034595_0_0_1; -.
DR   InParanoid; Q759T4; -.
DR   OMA; TTKCPFK; -.
DR   Proteomes; UP000000591; Chromosome IV.
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: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:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0043614; C:multi-eIF complex; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0032781; P:positive regulation of ATP-dependent activity; IEA:EnsemblFungi.
DR   GO; GO:0002188; P:translation reinitiation; IEA:EnsemblFungi.
DR   GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
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   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
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   SUPFAM; SSF57756; SSF57756; 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..269
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   G"
FT                   /id="PRO_0000365431"
FT   DOMAIN          188..267
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT   REGION          155..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
SQ   SEQUENCE   269 AA;  29767 MW;  CDC7FA0164F3BF9B CRC64;
     MSEVPEPRII ENPDGSKTII SFKIDGGKKL KITQRVKEIK ITEKVNKSIA ERRKWAKYGA
     EAGSGPGPNL STTKLAEELQ LRLAPSLKEV REQDSKEKEK EKQEGEKSLY VCRTCGIPGH
     FTTKCPFRDI LGEMSGPAEG EGGLDAAVDT AMPAASAPGK YVPPSRRAGG RDPSSDVYKD
     QRERDDAMTL KIMQLNENAD EMTIKQKLLS PFPNVPRVAV VRNKETGRSR GIAYVTFASE
     KDAETALRLL HGRGFMNLIL QVDWSKPKK
 
 
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