ID A0A4D6H7Y3_9EURY Unreviewed; 153 AA.
AC A0A4D6H7Y3;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rpl22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN ORFNames=DV733_00120 {ECO:0000313|EMBL:QCC49725.1};
OS Halapricum salinum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halapricum.
OX NCBI_TaxID=1457250 {ECO:0000313|EMBL:QCC49725.1, ECO:0000313|Proteomes:UP000296706};
RN [1] {ECO:0000313|EMBL:QCC49725.1, ECO:0000313|Proteomes:UP000296706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1105 {ECO:0000313|EMBL:QCC49725.1,
RC ECO:0000313|Proteomes:UP000296706};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
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:0000256|HAMAP-Rule:MF_01331}.
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:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004007}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01331, ECO:0000256|RuleBase:RU004007}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004005}.
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DR EMBL; CP031310; QCC49725.1; -; Genomic_DNA.
DR RefSeq; WP_049993172.1; NZ_CP031310.1.
DR AlphaFoldDB; A0A4D6H7Y3; -.
DR STRING; 1457250.GCA_000755225_02313; -.
DR GeneID; 39846229; -.
DR KEGG; hsn:DV733_00120; -.
DR OrthoDB; 314984at2157; -.
DR Proteomes; UP000296706; 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; Ribosomal protein L22/L17; 1.
DR HAMAP; MF_01331_A; Ribosomal_L22_A; 1.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR018260; Ribosomal_uL22_CS.
DR InterPro; IPR005721; Ribosomal_uL22_euk/arc.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
DR NCBIfam; TIGR01038; uL22_arch_euk; 1.
DR PANTHER; PTHR11593; 60S RIBOSOMAL PROTEIN L17; 1.
DR PANTHER; PTHR11593:SF10; 60S RIBOSOMAL PROTEIN L17; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000296706};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01331,
KW ECO:0000256|RuleBase:RU004007};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01331,
KW ECO:0000256|RuleBase:RU004007}.
SQ SEQUENCE 153 AA; 16799 MW; E7F1011FD50DDEE2 CRC64;
MGISYSVDAD PDTTAKAMLR ERQMSHKHSK AIAREIKGKT AGEAVTYLEA VVEGDQPVPF
RQHNSGVGHR KNIDGWDAGR FPNKASKAFL DLLENAIGNA DHQGFDGESM EIMHVAAHKV
GETQGRQPRA MGRASPFNSM EVDVELILEE VEE
//