RL2_IGNH4
ID RL2_IGNH4 Reviewed; 251 AA.
AC A8AC70;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
GN Name=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=Igni_1346;
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU82522.1; -; Genomic_DNA.
DR RefSeq; WP_012123486.1; NC_009776.1.
DR AlphaFoldDB; A8AC70; -.
DR SMR; A8AC70; -.
DR STRING; 453591.Igni_1346; -.
DR EnsemblBacteria; ABU82522; ABU82522; Igni_1346.
DR GeneID; 5563163; -.
DR KEGG; iho:Igni_1346; -.
DR eggNOG; arCOG04067; Archaea.
DR HOGENOM; CLU_036235_0_3_2; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 74812at2157; -.
DR PhylomeDB; A8AC70; -.
DR Proteomes; UP000000262; Chromosome.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
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; 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.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..251
FT /note="50S ribosomal protein L2"
FT /id="PRO_1000051936"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 26864 MW; 990E35B8663DC7E8 CRC64;
MGKRLRVQRH GRGTPQWRNR GHLRVAPGRY PSPEVLKLDE TYEGYVVELK HDPGRWVPLA
HIVIPNVADF WIPAAEGMYT GQKVQIGPNA APVNGNILPL YAIPEGTQIF NVEIRPGDGG
KLARSGGAYA ILVGKSGNSA IIQLPSGKVK QVNAKARATI GIAAGAGRDE KPLLKAGNAY
YKWKAKAKKW PVVRGVAMNA VNHPHGGGNH QSPGYPTTVA RNAPPGQKVG HIAARCTGRG
CKQAKARLGL K