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RL5_CALMQ
ID   RL5_CALMQ               Reviewed;         197 AA.
AC   A8MB19;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=Cmaq_1831;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is 1 of the proteins that binds and probably mediates
CC       the attachment of the 5S RNA into the large ribosomal subunit, where it
CC       forms part of the central protuberance. In the 70S ribosome it contacts
CC       protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits;
CC       this bridge is implicated in subunit movement. May contact the P site
CC       tRNA; the 5S rRNA and some of its associated proteins might help
CC       stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_01333}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; contacts the 5S rRNA and
CC       probably tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
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DR   EMBL; CP000852; ABW02648.1; -; Genomic_DNA.
DR   RefSeq; WP_012186867.1; NC_009954.1.
DR   AlphaFoldDB; A8MB19; -.
DR   SMR; A8MB19; -.
DR   STRING; 397948.Cmaq_1831; -.
DR   EnsemblBacteria; ABW02648; ABW02648; Cmaq_1831.
DR   GeneID; 5710083; -.
DR   KEGG; cma:Cmaq_1831; -.
DR   eggNOG; arCOG04092; Archaea.
DR   HOGENOM; CLU_061015_3_0_2; -.
DR   OMA; ERMYAFL; -.
DR   OrthoDB; 97230at2157; -.
DR   Proteomes; UP000001137; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   HAMAP; MF_01333_A; Ribosomal_L5_A; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR022804; Ribosomal_L5_arc.
DR   InterPro; IPR031309; Ribosomal_L5_C.
DR   InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR   InterPro; IPR031310; Ribosomal_L5_N.
DR   PANTHER; PTHR11994; PTHR11994; 1.
DR   Pfam; PF00281; Ribosomal_L5; 1.
DR   Pfam; PF00673; Ribosomal_L5_C; 1.
DR   PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR   SUPFAM; SSF55282; SSF55282; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..197
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000365639"
SQ   SEQUENCE   197 AA;  22421 MW;  072BF741B8EC82FA CRC64;
     MPAIDLSTID LRAIKPSDLD WRKFTLDTGH PMRRIFIWSV AVNMGIGQSG ERLEKAAKVM
     SELTGRTPSY RLAHKSIKDF GIRRGEPIGL LVTLRRNEAV WFLLRALAAV DFTLREESFN
     AGNVSFGIRE HILVPGSRYD PALGIFGFDV AVTLARPGFR VQYRRRARAD VGKDHRVSRE
     ETIRFFQDVL GVRILKR
 
 
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