RL2_HALSA
ID RL2_HALSA Reviewed; 240 AA.
AC Q9HPD1; Q06843;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=VNG_1692G;
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].
RA Itoh T.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-211.
RX PubMed=8241282; DOI=10.1016/0167-4781(93)90169-e;
RA Yuki Y., Kanechika R., Itoh T.;
RT "Nucleotide sequence of the genes encoding the L3, L4, and L23 equivalent
RT ribosomal proteins from the archaebacterium Halobacterium halobium.";
RL Biochim. Biophys. Acta 1216:335-338(1993).
CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the 30S
CC subunit in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; AB006961; BAA22273.1; -; Genomic_DNA.
DR EMBL; AE004437; AAG19939.1; -; Genomic_DNA.
DR PIR; G84321; G84321.
DR PIR; T43819; T43819.
DR RefSeq; WP_010903237.1; NC_002607.1.
DR AlphaFoldDB; Q9HPD1; -.
DR SMR; Q9HPD1; -.
DR STRING; 64091.VNG_1692G; -.
DR PaxDb; Q9HPD1; -.
DR EnsemblBacteria; AAG19939; AAG19939; VNG_1692G.
DR GeneID; 5954225; -.
DR GeneID; 62887089; -.
DR KEGG; hal:VNG_1692G; -.
DR PATRIC; fig|64091.14.peg.1291; -.
DR HOGENOM; CLU_036235_0_3_2; -.
DR InParanoid; Q9HPD1; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 74812at2157; -.
DR PhylomeDB; Q9HPD1; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_A; Ribosomal_L2_A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR023672; Ribosomal_L2_arc.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..240
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129713"
FT REGION 199..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 53..55
FT /note="SAP -> TA (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..85
FT /note="GI -> ES (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..124
FT /note="FARAGG -> LPRGR (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="P -> A (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..209
FT /note="GGGRQH -> AVAAR (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 25449 MW; 51861CD27B304CAC CRC64;
MGRRIQGQRR GRGTSTFRAP SHRYKAELSH KRTEDTDVLA GEVIDVEHDP ARSAPVARVA
FEDDDQRLVL ASEGVGVGDT IEIGISATIE EGNTLPLAEI PEGVPVCNVE SHPGDGGKFA
RAGGVNADLV THERDATIVE LPSGETKRLS PDCRATIGVV AGGGRTEKPF VKAGNKHHKM
KARGTKWPRV RGVAMNAVDH PFGGGGRQHP GRPKSVSRDA APGRKVGDIA SKRTGRGGNE
