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EF1B_PYRIL
ID   EF1B_PYRIL              Reviewed;          92 AA.
AC   A1RSD0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Elongation factor 1-beta {ECO:0000255|HAMAP-Rule:MF_00043};
DE            Short=EF-1-beta {ECO:0000255|HAMAP-Rule:MF_00043};
DE   AltName: Full=aEF-1beta {ECO:0000255|HAMAP-Rule:MF_00043};
GN   Name=ef1b {ECO:0000255|HAMAP-Rule:MF_00043}; OrderedLocusNames=Pisl_0684;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus
CC       allowing the regeneration of EF-1-alpha/GTP that could then be used to
CC       form the ternary complex EF-1-alpha/GTP/AAtRNA. {ECO:0000255|HAMAP-
CC       Rule:MF_00043}.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC       {ECO:0000255|HAMAP-Rule:MF_00043}.
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DR   EMBL; CP000504; ABL87862.1; -; Genomic_DNA.
DR   RefSeq; WP_011762438.1; NC_008701.1.
DR   AlphaFoldDB; A1RSD0; -.
DR   SMR; A1RSD0; -.
DR   STRING; 384616.Pisl_0684; -.
DR   EnsemblBacteria; ABL87862; ABL87862; Pisl_0684.
DR   GeneID; 4616379; -.
DR   KEGG; pis:Pisl_0684; -.
DR   eggNOG; arCOG01988; Archaea.
DR   HOGENOM; CLU_165896_1_0_2; -.
DR   OMA; YELEYFS; -.
DR   OrthoDB; 124073at2157; -.
DR   Proteomes; UP000002595; Chromosome.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00292; EF1B; 1.
DR   Gene3D; 3.30.70.60; -; 1.
DR   HAMAP; MF_00043; EF1_beta; 1.
DR   InterPro; IPR036219; eEF-1beta-like_sf.
DR   InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   InterPro; IPR004542; Transl_elong_EF1B_B_arc.
DR   PANTHER; PTHR39647; PTHR39647; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   PIRSF; PIRSF006521; Transl_elong_EF1B_B_arc; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF54984; SSF54984; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Protein biosynthesis.
FT   CHAIN           1..92
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_1000006622"
SQ   SEQUENCE   92 AA;  10526 MW;  D2E0E52B0C9DC26E CRC64;
     MSAEVALVYR VLPESVEVDI EKLKNAVVNK LAPKYKVDKV EVEDVGFGIK ALRFFIRMPE
     SDEYSSDEVE ELLRSVEGVG SYELEYFSRL SF
 
 
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