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RL5_METVA
ID   RL5_METVA               Reviewed;         181 AA.
AC   P14029;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, 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};
OS   Methanococcus vannielii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2530355; DOI=10.1016/0022-2836(89)90167-8;
RA   Auer J., Spicker G., Boeck A.;
RT   "Organization and structure of the Methanococcus transcriptional unit
RT   homologous to the Escherichia coli 'spectinomycin operon'. Implications for
RT   the evolutionary relationship of 70 S and 80 S ribosomes.";
RL   J. Mol. Biol. 209:21-36(1989).
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; X16720; CAA34693.1; -; Genomic_DNA.
DR   PIR; S05617; R5MX5.
DR   AlphaFoldDB; P14029; -.
DR   SMR; P14029; -.
DR   GeneID; 5326050; -.
DR   OMA; ERMYAFL; -.
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; IPR020929; Ribosomal_L5_CS.
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.
DR   PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..181
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000125060"
SQ   SEQUENCE   181 AA;  20293 MW;  982486779041892C CRC64;
     MSFQEVWEKE PMKKPRIQKV TVNFGVGEAG DRLTIGAKVI ETLTGQAPVR TLAKQTNPAF
     GIRKKLPIGL KVTLRGKNAE EFLENAFVAF KVSGKVLYAS SFDKVGNFSF GVPEHIDFPG
     QKYDPTVGIY GMDICVTFEK PGYRVKSRKL KRSHIPAKHL VKKEEAIEYI EKKFGAEVVM
     E
 
 
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