ID R4W0T7_9EURY Unreviewed; 158 AA.
AC R4W0T7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=L593_11130 {ECO:0000313|EMBL:AGN02171.1};
OS Salinarchaeum sp. Harcht-Bsk1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Natronoarchaeaceae; Salinarchaeum.
OX NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN02171.1, ECO:0000313|Proteomes:UP000014072};
RN [1] {ECO:0000313|EMBL:AGN02171.1, ECO:0000313|Proteomes:UP000014072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN02171.1};
RX PubMed=23868130;
RA Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA Toshchakov S.V.;
RT "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT Isolated from Hypersaline Lake Baskunchak, Russia.";
RL Genome Announc. 1:E00505-13(2013).
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; CP005962; AGN02171.1; -; Genomic_DNA.
DR RefSeq; WP_020447065.1; NC_021313.1.
DR AlphaFoldDB; R4W0T7; -.
DR STRING; 1333523.L593_11130; -.
DR GeneID; 16180794; -.
DR KEGG; sali:L593_11130; -.
DR PATRIC; fig|1333523.5.peg.2296; -.
DR eggNOG; arCOG04098; Archaea.
DR HOGENOM; CLU_083987_0_2_2; -.
DR OrthoDB; 314984at2157; -.
DR Proteomes; UP000014072; 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:UP000014072};
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}.
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 158 AA; 17051 MW; 144CE0F10A2983E8 CRC64;
MGISYSVDAD PDTTAKAMLR ERQMSQKHSK AIAREIKGQT AEDAVAYLED VVAGEQSVPF
REHNSGVGHR SDIDGWDAGR YPEKASEGFL DLLENAIANA EHQGFDGETM EIVHVASHKV
GETQGRKPRA MGRAGAWNSP EVDVEIVLAE STDDGGDA
//
