ID M0AHZ3_9EURY Unreviewed; 165 AA.
AC M0AHZ3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rpl22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Synonyms=rpl22p {ECO:0000313|EMBL:ELY97502.1};
GN ORFNames=C482_12804 {ECO:0000313|EMBL:ELY97502.1};
OS Natrialba chahannaoensis JCM 10990.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1227492 {ECO:0000313|EMBL:ELY97502.1, ECO:0000313|Proteomes:UP000011693};
RN [1] {ECO:0000313|EMBL:ELY97502.1, ECO:0000313|Proteomes:UP000011693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10990 {ECO:0000313|EMBL:ELY97502.1,
RC ECO:0000313|Proteomes:UP000011693};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY97502.1}.
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DR EMBL; AOIN01000067; ELY97502.1; -; Genomic_DNA.
DR RefSeq; WP_006167985.1; NZ_AOIN01000067.1.
DR AlphaFoldDB; M0AHZ3; -.
DR STRING; 1227492.C482_12804; -.
DR PATRIC; fig|1227492.4.peg.2529; -.
DR OrthoDB; 314984at2157; -.
DR Proteomes; UP000011693; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
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 165 AA; 17976 MW; 184E11928193624E CRC64;
MGINYSVDAD PNTTAKAMLR ERHMSHKHSK EIARELKGRT VGNAQAYLQD VIDEKQSVPF
KSHNTGAGHR SDIEGWDAGK YPEKASEAFL DLLENVAANA DSQGFDGESM EIAHVAAHKV
GESVGRKPRA MGRASAWNTP QVDVEIVVED VDETAEDTED AEGDN
//