RL11_HALSA
ID RL11_HALSA Reviewed; 163 AA.
AC P05969; Q9HQL2;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
GN Name=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=VNG_1108G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33170 / DSM 669 / NCCB 81095 / NRC 34001;
RX PubMed=2743981; DOI=10.1002/j.1460-2075.1989.tb03496.x;
RA Shimmin L.C., Dennis P.P.;
RT "Characterization of the L11, L1, L10 and L12 equivalent ribosomal protein
RT gene cluster of the halophilic archaebacterium Halobacterium cutirubrum.";
RL EMBO J. 8:1225-1235(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [3]
RP PROTEIN SEQUENCE OF 2-35.
RX PubMed=6467081; DOI=10.1139/o84-058;
RA Matheson A.T., Yaguchi M., Christensen P., Rollin C.F., Hasnain S.;
RT "Purification, properties, and N-terminal amino acid sequence of certain
RT 50S ribosomal subunit proteins from the archaebacterium Halobacterium
RT cutirubrum.";
RL Can. J. Biochem. Cell Biol. 62:426-433(1984).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit.
CC Interacts with L10 and the large rRNA to form the base of the stalk.
CC L10 forms an elongated spine to which L12 dimers bind in a sequential
CC fashion forming a multimeric L10(L12)X complex. {ECO:0000255|HAMAP-
CC Rule:MF_00736}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15078; CAA33178.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19501.1; -; Genomic_DNA.
DR PIR; A84267; A84267.
DR PIR; S04118; R5HSC1.
DR RefSeq; WP_010902796.1; NC_002607.1.
DR AlphaFoldDB; P05969; -.
DR SMR; P05969; -.
DR STRING; 64091.VNG_1108G; -.
DR PaxDb; P05969; -.
DR EnsemblBacteria; AAG19501; AAG19501; VNG_1108G.
DR GeneID; 5954210; -.
DR GeneID; 62886623; -.
DR KEGG; hal:VNG_1108G; -.
DR PATRIC; fig|64091.14.peg.847; -.
DR HOGENOM; CLU_074237_4_0_2; -.
DR InParanoid; P05969; -.
DR OMA; CKQFNAK; -.
DR OrthoDB; 98187at2157; -.
DR PhylomeDB; P05969; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6467081"
FT CHAIN 2..163
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104432"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 17039 MW; 648835B1EC9D7B53 CRC64;
MAETIEVLVA GGQADPGPPL GPELGPTPVD VQAVVQEIND QTEAFDGTEV PVTIEYEDDG
SFSIEVGVPP TAALVKDEAG FDTGSGEPQE NFVADLSIEQ LKTIAEQKKP DLLAYDARNA
AKEVAGTCAS LGVTIEGEDA RTFNERVDDG DYDDVLGDEL AAA