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Database: UniProt
Entry: C4XLY4
LinkDB: C4XLY4
Original site: C4XLY4 
ID   RL24_DESMR              Reviewed;         107 AA.
AC   C4XLY4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   26-NOV-2014, entry version 32.
DE   RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326};
GN   OrderedLocusNames=DMR_12310;
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 two assembly initiator proteins, it binds
CC       directly to the 5'-end of the 23S rRNA, where it nucleates
CC       assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L24P family.
CC       {ECO:0000255|HAMAP-Rule:MF_01326}.
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DR   EMBL; AP010904; BAH74722.1; -; Genomic_DNA.
DR   RefSeq; WP_006920478.1; NC_012796.1.
DR   RefSeq; YP_002952608.1; NC_012796.1.
DR   STRING; 573370.DMR_12310; -.
DR   EnsemblBacteria; BAH74722; BAH74722; DMR_12310.
DR   GeneID; 7982342; -.
DR   KEGG; dma:DMR_12310; -.
DR   PATRIC; 21748701; VBIDesMag26496_1135.
DR   eggNOG; COG0198; -.
DR   HOGENOM; HOG000039892; -.
DR   KO; K02895; -.
DR   OMA; DKGCSGE; -.
DR   OrthoDB; EOG6FFSDM; -.
DR   BioCyc; DMAG573370:GHJL-1242-MONOMER; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR003256; Ribosomal_L24.
DR   InterPro; IPR005825; Ribosomal_L24/26_CS.
DR   InterPro; IPR008991; Translation_prot_SH3-like.
DR   PANTHER; PTHR12903; PTHR12903; 1.
DR   Pfam; PF00467; KOW; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01079; rplX_bact; 1.
DR   PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN         1    107       50S ribosomal protein L24.
FT                                /FTId=PRO_1000214539.
SQ   SEQUENCE   107 AA;  11879 MW;  374C0C1495B7FC25 CRC64;
     MKTYRIRKDD KVMVIAGKDK GKVGKILKIL PKRNAVLVEK VNQVKRHTKA NPYAKTPGGI
     IEKEAPLDIS NVALLCEGCA KPAKVGYKYT ADGKKVRFCK KCNHEIA
//
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