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Database: UniProt
Entry: A0A1J4UIG1_9ARCH
LinkDB: A0A1J4UIG1_9ARCH
Original site: A0A1J4UIG1_9ARCH 
ID   A0A1J4UIG1_9ARCH        Unreviewed;       233 AA.
AC   A0A1J4UIG1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000256|ARBA:ARBA00035480, ECO:0000256|RuleBase:RU004007};
GN   ORFNames=AUJ14_05965 {ECO:0000313|EMBL:OIO24522.1};
OS   Candidatus Micrarchaeota archaeon CG1_02_55_22.
OC   Archaea; Candidatus Micrarchaeota.
OX   NCBI_TaxID=1805250 {ECO:0000313|EMBL:OIO24522.1, ECO:0000313|Proteomes:UP000182370};
RN   [1] {ECO:0000313|EMBL:OIO24522.1, ECO:0000313|Proteomes:UP000182370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_55_22 {ECO:0000313|EMBL:OIO24522.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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|RuleBase:RU004007}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC       {ECO:0000256|RuleBase:RU004007}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000256|ARBA:ARBA00009451, 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:OIO24522.1}.
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DR   EMBL; MNVH01000070; OIO24522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4UIG1; -.
DR   Proteomes; UP000182370; Unassembled WGS sequence.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.90.470.10; Ribosomal protein L22/L17; 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,
KW   ECO:0000256|RuleBase:RU004005};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000256|RuleBase:RU004005};
KW   RNA-binding {ECO:0000256|RuleBase:RU004007};
KW   rRNA-binding {ECO:0000256|RuleBase:RU004007}.
FT   REGION          175..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   233 AA;  25646 MW;  E4226818926D9FB3 CRC64;
     MGLYKYSVTY DAEKSAPAQA FDINASYKDL TQVLRAIRGK SVKDAKKILD EAITLKRAIR
     FSKFNKGMGH RSELGGKKGK YPAKECRIAL HMLNNAFANA QSKGLDENAV VLHAAAYKQN
     VFPRYRTFFV GGNTLGYGKQ AIFSRYVTAR AEIVVGEKGL KPLARKTKVQ VRAEAKLKSK
     TPVEKVEKKA DAKAKPSEAK VDAKAKPEVT EKPAKPAPVK VVEKPVEKPA VKQ
//
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