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Database: UniProt
Entry: A0A3G8YBX7_9DEIO
LinkDB: A0A3G8YBX7_9DEIO
Original site: A0A3G8YBX7_9DEIO 
ID   A0A3G8YBX7_9DEIO        Unreviewed;       111 AA.
AC   A0A3G8YBX7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN   Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN   ORFNames=EHF33_08655 {ECO:0000313|EMBL:AZI42808.1};
OS   Deinococcus psychrotolerans.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2489213 {ECO:0000313|EMBL:AZI42808.1, ECO:0000313|Proteomes:UP000276417};
RN   [1] {ECO:0000313|EMBL:AZI42808.1, ECO:0000313|Proteomes:UP000276417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S14-83T {ECO:0000313|EMBL:AZI42808.1,
RC   ECO:0000313|Proteomes:UP000276417};
RA   Tian J.;
RT   "Deinococcus shelandsis sp. nov., isolated from South Shetland Islands soil
RT   of Antarctica.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; its binding is
CC       stimulated by other ribosomal proteins, e.g., L4, L17, and L20. It is
CC       important during the early stages of 50S assembly. It makes multiple
CC       contacts with different domains of the 23S rRNA in the assembled 50S
CC       subunit and ribosome. {ECO:0000256|HAMAP-Rule:MF_01331,
CC       ECO:0000256|RuleBase:RU004008}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01331, ECO:0000256|RuleBase:RU004006}.
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; CP034183; AZI42808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G8YBX7; -.
DR   KEGG; dph:EHF33_08655; -.
DR   OrthoDB; 9805969at2; -.
DR   Proteomes; UP000276417; Chromosome 1.
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_B; Ribosomal_L22_B; 1.
DR   InterPro; IPR001063; Ribosomal_uL22.
DR   InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR   InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR   InterPro; IPR036394; Ribosomal_uL22_sf.
DR   NCBIfam; TIGR01044; rplV_bact; 1.
DR   PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 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|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01331};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01331}.
SQ   SEQUENCE   111 AA;  12498 MW;  4766EA21C0C8787D CRC64;
     MQAKAIARYI RISPRKVRLV VDVIRGKNVR DAEDLLRFVP KAASTPVDKV LKSAKANAVN
     NHDMIEDRLY VSQIFVDAGP TLKRLIPRAR GTANIIKKRT SHITVILEER A
//
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