RL22_CALMQ
ID RL22_CALMQ Reviewed; 185 AA.
AC A8MBL4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=Cmaq_1930;
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein binds specifically to 23S rRNA. It makes
CC multiple contacts with different domains of the 23S rRNA in the
CC assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
CC -!- FUNCTION: The globular domain of the protein is located near the
CC polypeptide exit tunnel on the outside of the subunit, while an
CC extended beta-hairpin is found that lines the wall of the exit tunnel
CC in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01331}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000255|HAMAP-Rule:MF_01331}.
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DR EMBL; CP000852; ABW02747.1; -; Genomic_DNA.
DR RefSeq; WP_012186966.1; NC_009954.1.
DR AlphaFoldDB; A8MBL4; -.
DR SMR; A8MBL4; -.
DR STRING; 397948.Cmaq_1930; -.
DR EnsemblBacteria; ABW02747; ABW02747; Cmaq_1930.
DR GeneID; 5709557; -.
DR KEGG; cma:Cmaq_1930; -.
DR eggNOG; arCOG04098; Archaea.
DR HOGENOM; CLU_083987_0_2_2; -.
DR OMA; ANAEYKG; -.
DR OrthoDB; 103467at2157; -.
DR Proteomes; UP000001137; 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 CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_A; Ribosomal_L22_A; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR005721; Ribosomal_L22/L17_euk/arc.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR PANTHER; PTHR11593; PTHR11593; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01038; uL22_arch_euk; 1.
PE 3: Inferred from homology;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..185
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000354538"
SQ SEQUENCE 185 AA; 21519 MW; 137F1A0CA3F8F0B3 CRC64;
MRYWSIRDED VIDLVKRRYN VTISADQIAK ARGFEFRISW KKAIETARAI RFLTIKQAED
YMEKVKDLKA PIPIKEFTRK QAHHNVPWDG WPVAKWPVKV ADSFLQVLRN LESNASYRGL
NIDNTVIVHA SASRGMRIRN YMPRALGRAT PWFQDTVNIE LVAVELPAEL VPKKFSWARV
LKAIK