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EIF3B_ASHGO
ID   EIF3B_ASHGO             Reviewed;         736 AA.
AC   Q758X9;
DT   10-FEB-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 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}; OrderedLocusNames=ADR399C;
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.
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; AE016817; AAS52318.1; -; Genomic_DNA.
DR   RefSeq; NP_984494.1; NM_209847.1.
DR   AlphaFoldDB; Q758X9; -.
DR   SMR; Q758X9; -.
DR   STRING; 33169.AAS52318; -.
DR   EnsemblFungi; AAS52318; AAS52318; AGOS_ADR399C.
DR   GeneID; 4620659; -.
DR   KEGG; ago:AGOS_ADR399C; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; Q758X9; -.
DR   OMA; NVADCKI; -.
DR   Proteomes; UP000000591; Chromosome IV.
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; -; 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   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   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   Repeat; RNA-binding; WD repeat.
FT   CHAIN           1..736
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000363806"
FT   DOMAIN          37..120
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REPEAT          140..182
FT                   /note="WD 1"
FT   REPEAT          186..224
FT                   /note="WD 2"
FT   REPEAT          226..244
FT                   /note="WD 3"
FT   REPEAT          245..284
FT                   /note="WD 4"
FT   REPEAT          288..328
FT                   /note="WD 5"
FT   REPEAT          332..375
FT                   /note="WD 6"
FT   REPEAT          443..483
FT                   /note="WD 7"
FT   REPEAT          511..557
FT                   /note="WD 8"
FT   REPEAT          566..604
FT                   /note="WD 9"
FT   REPEAT          616..662
FT                   /note="WD 10"
FT   REGION          1..219
FT                   /note="Sufficient for interaction with PIC8"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REGION          1..94
FT                   /note="Sufficient for interaction with HCR1 and TIF32"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
SQ   SEQUENCE   736 AA;  84631 MW;  DA3B4FB13A16D9C2 CRC64;
     MAAVFDDIRL EDIPVDDVDM QDLEETYAVE RSIEFDRYVV VDGAPVAPEA KVGALQKVLT
     KLFSQAGSVV DMDVPVEEGR TKGHLFIEFE DAGAARRAIK MFNGKKLDVK HRLWVNGLDD
     MERYGRPDFS TEYREPVVPE FEATEYPRSW LQDETGRDQF VLQKGEMTAV FWNRNNLQPE
     NVVEPRRNWS NSILNFSPHG TYLFSFHDQG IASWGGPQFK RLRRFAHPDV KAISMSSTEK
     YLVTFSSEPL EVSDEPNEAC PFGPESRGHQ LCIWDVATGV CVKTFALPPQ QQLQWPMVKW
     SFDDKFCARL GPGAIAVYET EKNFQLLGGK VMKIEDVQDF SFAPKGIKLA SNRPNDPPST
     VMVYWTPESN NQSCKAVLIE LPNRRVLRTI NLVQVTDVSF HWQNQAEFLC VQVDRHTKSR
     KTIFTNMEIC SLTAREFPFE KVEIKDRCMR FAWEPNSDRF VIISRSENVN DNPAIAKNVV
     SFYAPEKKVD KKGVIIDKEL SIFKKWKLVR AIDGKFSNEI TWSPAGRFVC VAAIGKIGSR
     NENIDFYDMD YPNTEKIINT ATDVNATLRD VAHINYASAT DYEWDPSGRY LAFWSSAWKH
     KAENGYKVFN LAGAIVREEL ITDFNNFFWR PRPDSLLSNS EKKKVRKNLK EWSAHFEEQD
     AMEADSATRE LILKRRNWLD EWSKYREACK QTLSESGLSI CDCVELSTKD EDCELVEEIR
     ETVVEESTEE VPFFEE
 
 
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