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Database: UniProt
Entry: G0HIU4_THES4
LinkDB: G0HIU4_THES4
Original site: G0HIU4_THES4 
ID   G0HIU4_THES4            Unreviewed;       156 AA.
AC   G0HIU4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN   OrderedLocusNames=GQS_04860 {ECO:0000313|EMBL:AEK72873.1};
OS   Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK72873.1, ECO:0000313|Proteomes:UP000000874};
RN   [1] {ECO:0000313|EMBL:AEK72873.1, ECO:0000313|Proteomes:UP000000874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX   PubMed=21914870; DOI=10.1128/JB.05851-11;
RA   Wang X., Gao Z., Xu X., Ruan L.;
RT   "Complete genome sequence of Thermococcus sp. strain 4557, a
RT   hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT   area.";
RL   J. Bacteriol. 193:5544-5545(2011).
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; CP002920; AEK72873.1; -; Genomic_DNA.
DR   RefSeq; WP_014012556.1; NC_015865.1.
DR   AlphaFoldDB; G0HIU4; -.
DR   STRING; 1042877.GQS_04860; -.
DR   GeneID; 40474094; -.
DR   KEGG; the:GQS_04860; -.
DR   PATRIC; fig|1042877.9.peg.952; -.
DR   eggNOG; arCOG04098; Archaea.
DR   HOGENOM; CLU_083987_0_2_2; -.
DR   OrthoDB; 314984at2157; -.
DR   Proteomes; UP000000874; 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   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   156 AA;  17747 MW;  35ACB0F0B6EB0CE8 CRC64;
     MSRGRFSYSF QNFDPEKMAR ASGRDLRISP KHSVELLREI RGMMVNDALR YLDDVIALKR
     PVPMKRHNDS QGHKPGRGFG PGRYPVKVAK AVKKVLLNAK NNAEQKGLDP DRLKIIHAAA
     HRGPVLRGYI PRAFGRATPF NEQTTHIEIV VEEIRR
//
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