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EIF3B_KLULA
ID   EIF3B_KLULA             Reviewed;         732 AA.
AC   Q6CY34;
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=KLLA0A03531g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382121; CAH02743.1; -; Genomic_DNA.
DR   RefSeq; XP_451155.1; XM_451155.1.
DR   AlphaFoldDB; Q6CY34; -.
DR   SMR; Q6CY34; -.
DR   STRING; 28985.XP_451155.1; -.
DR   EnsemblFungi; CAH02743; CAH02743; KLLA0_A03531g.
DR   GeneID; 2896595; -.
DR   KEGG; kla:KLLA0_A03531g; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; Q6CY34; -.
DR   OMA; NVADCKI; -.
DR   Proteomes; UP000000598; Chromosome A.
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: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   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..732
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000363820"
FT   DOMAIN          37..120
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REPEAT          185..224
FT                   /note="WD 1"
FT   REPEAT          237..280
FT                   /note="WD 2"
FT   REPEAT          439..481
FT                   /note="WD 3"
FT   REPEAT          507..554
FT                   /note="WD 4"
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   732 AA;  84187 MW;  D7BC192F71D0EBC1 CRC64;
     MTTLESLKIE DIPVDDIDFS DLEREFQIQD GGVNFDNFLV VDGAPVAPEA KVPVLEKVLT
     KLFSQAGKVL DMQIPVEDGK TKGHLFIEME SVSAAKEAIQ LFNGKKLDAK HRLLVNSLND
     MEKYGSDDFE SQSHEPVVPD FAPTDFLRSW LQNQDGRDQF VLQKGDMTRV FWNRLAHQPD
     GVGEARKNWS NDVVKFSPKG TYLLSFHDQG VTSWGGPNFD RLKRFFHPDV SRLDVSPTEK
     FLITFSMNPI KPGEDTPFGP ESEGHQICVW DLATGFLMKT FGIPPNAKLQ WPLIRFSYDD
     KYCGRLGPNA LAIYDIENNF QLLDGKLHKV EGIQDFSFAP KGVQLTYNRR KSDPTTLLAY
     WTPETNNQSC KAFLMTLPNK RIVKTVNLVQ VSNVSIHWHE QADFVCFQVD RHTKSKKTFF
     TNLEICKLNE SEIPVEKIEM KDRVLELAWE PKGTRFVTIS KMDNGGEENP MYPKNFVKFF
     APEKKDNKDK DLAVLPDQLK WKLVKTVDQQ FANCISWSPA GRFVAVCTIV NGKEIKKASL
     DFYDFDFTGE KTLNEVQDVK ASLQAVAHID NQFFTDLEWD SSGRFLTAWS SYSKHKLENG
     YTIYNCCGEA VRKEIVDQFR NFVWRPRPES LLSNAEKKKA RKNLKQWSVK FEEQDAMESD
     SALRDLILKR RAELSAWVSY REQSKERLES EDSYTIFDNF ESDKADETQY VTVEEVKEEI
     LEETQEEVES FE
 
 
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