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RL23_MYCCT
ID   RL23_MYCCT              Reviewed;          94 AA.
AC   P10140; Q2SRF5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; OrderedLocusNames=MCAP_0694;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3481422; DOI=10.1007/bf00325700;
RA   Ohkubo S., Muto A., Kawauchi Y., Yamao F., Osawa S.;
RT   "The ribosomal protein gene cluster of Mycoplasma capricolum.";
RL   Mol. Gen. Genet. 210:314-322(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of
CC       the proteins that surrounds the polypeptide exit tunnel on the outside
CC       of the ribosome. Forms the main docking site for trigger factor binding
CC       to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, and
CC       trigger factor when it is bound to the ribosome. {ECO:0000255|HAMAP-
CC       Rule:MF_01369}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR   EMBL; X06414; CAA29706.1; -; Genomic_DNA.
DR   EMBL; CP000123; ABC01471.1; -; Genomic_DNA.
DR   PIR; S02833; R5YM23.
DR   RefSeq; WP_011166911.1; NC_007633.1.
DR   AlphaFoldDB; P10140; -.
DR   SMR; P10140; -.
DR   EnsemblBacteria; ABC01471; ABC01471; MCAP_0694.
DR   GeneID; 23778352; -.
DR   KEGG; mcp:MCAP_0694; -.
DR   HOGENOM; CLU_037562_3_2_14; -.
DR   OMA; FEVDHRA; -.
DR   OrthoDB; 1978865at2; -.
DR   PhylomeDB; P10140; -.
DR   Proteomes; UP000001928; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR   InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   PANTHER; PTHR11620; PTHR11620; 1.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..94
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_0000129416"
SQ   SEQUENCE   94 AA;  10857 MW;  7D2507D2F1A7FC31 CRC64;
     MHITEVLKKP VLTEKSFAGH KDNVYTFLVD KKANKVQIKK TFEEIFEVKV ESVRTINYDA
     KEKRLGKYVG KKPSYKKAII TLKEGQKLDV LSDL
 
 
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