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Database: UniProt
Entry: C4XLX5
LinkDB: C4XLX5
Original site: C4XLX5 
ID   RL23_DESMR              Reviewed;          96 AA.
AC   C4XLX5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   01-OCT-2014, entry version 31.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369};
GN   OrderedLocusNames=DMR_12220;
OS   Desulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=573370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX   PubMed=19675025; DOI=10.1101/gr.088906.108;
RA   Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K.,
RA   Aoki N., Tsuruyama A., Okamura Y., Tanikawa S., Fujita N.,
RA   Takeyama H., Matsunaga T.;
RT   "Whole genome sequence of Desulfovibrio magneticus strain RS-1
RT   revealed common gene clusters in magnetotactic bacteria.";
RL   Genome Res. 19:1801-1808(2009).
CC   -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA.
CC       One of the proteins that surrounds the polypeptide exit tunnel on
CC       the outside of the ribosome. Forms the main docking site for
CC       trigger factor binding to the ribosome. {ECO:0000255|HAMAP-
CC       Rule:MF_01369}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29,
CC       and trigger factor when it is bound to the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR   EMBL; AP010904; BAH74713.1; -; Genomic_DNA.
DR   RefSeq; WP_006920469.1; NC_012796.1.
DR   RefSeq; YP_002952599.1; NC_012796.1.
DR   STRING; 573370.DMR_12220; -.
DR   EnsemblBacteria; BAH74713; BAH74713; DMR_12220.
DR   GeneID; 7982334; -.
DR   KEGG; dma:DMR_12220; -.
DR   PATRIC; 21748683; VBIDesMag26496_1126.
DR   eggNOG; COG0089; -.
DR   HOGENOM; HOG000231364; -.
DR   KO; K02892; -.
DR   OMA; QHGKTNA; -.
DR   OrthoDB; EOG6HTP4P; -.
DR   BioCyc; DMAG573370:GHJL-1233-MONOMER; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR   InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN         1     96       50S ribosomal protein L23.
FT                                /FTId=PRO_1000215031.
SQ   SEQUENCE   96 AA;  10593 MW;  C88CA00E56F7E4C9 CRC64;
     MEYANILLKP VISEKATMVK DAANQVVFFV HPAANKIEIA KAVEKAFSVT VKGVRVVKHK
     SLARSRMGRV TGRIPGYKKA YVTLAQGDKI EFFEGV
//
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