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Database: UniProt
Entry: Q5LMQ0
LinkDB: Q5LMQ0
Original site: Q5LMQ0 
ID   RL1_RUEPO               Reviewed;         232 AA.
AC   Q5LMQ0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   14-MAY-2014, entry version 61.
DE   RecName: Full=50S ribosomal protein L1;
GN   Name=rplA; OrderedLocusNames=SPO3513;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile
CC       in the ribosome, and is involved in E site tRNA release (By
CC       similarity).
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA
CC       (By similarity).
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L1P family.
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DR   EMBL; CP000031; AAV96738.1; -; Genomic_DNA.
DR   RefSeq; YP_168708.1; NC_003911.12.
DR   ProteinModelPortal; Q5LMQ0; -.
DR   SMR; Q5LMQ0; 6-227.
DR   STRING; 246200.SPO3513; -.
DR   EnsemblBacteria; AAV96738; AAV96738; SPO3513.
DR   GeneID; 3194818; -.
DR   KEGG; sil:SPO3513; -.
DR   PATRIC; 23380497; VBIRuePom114501_3584.
DR   eggNOG; COG0081; -.
DR   HOGENOM; HOG000207015; -.
DR   KO; K02863; -.
DR   OMA; AKITPIA; -.
DR   OrthoDB; EOG6FBX2G; -.
DR   GO; GO:0015934; C:large ribosomal subunit; 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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.190.20; -; 2.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR   InterPro; IPR005878; Ribosom_L1_bac-type.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR023674; Ribosomal_L1-like.
DR   InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR   InterPro; IPR016094; Ribosomal_L1_2-a/b-sand.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_L1_CS.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; SSF56808; 1.
DR   TIGRFAMs; TIGR01169; rplA_bact; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT   CHAIN         1    232       50S ribosomal protein L1.
FT                                /FTId=PRO_0000230640.
SQ   SEQUENCE   232 AA;  24039 MW;  541D9CCE3976754B CRC64;
     MAKLGKRTRA AREAFAGKEE LSVEQAVALI KSAASAKFDE TVEIAMNLGV DPRHADQMVR
     GVVGLPNGTG KTVRVAVFAR GPKAEEAQAA GADIVGAEDL METIQSGKIE FDRCIATPDM
     MPVVGRLGKI LGPRNLMPNP KVGTVTMDVA QAVQNAKGGE VQFKVEKAGV IHAGVGKVSF
     DEAKLVENVR AFVDAVAKAK PAGAKGTYLK KIALSSTMGP GVSVDVASAS GN
//
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