ID A0A0P8A479_9EURY Unreviewed; 148 AA.
AC A0A0P8A479;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rpl22p {ECO:0000313|EMBL:KPQ42967.1};
GN Synonyms=rpl22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN ORFNames=MPEBLZ_02474 {ECO:0000313|EMBL:KPQ42967.1};
OS Candidatus Methanoperedens sp. BLZ1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ42967.1, ECO:0000313|Proteomes:UP000050360};
RN [1] {ECO:0000313|EMBL:KPQ42967.1, ECO:0000313|Proteomes:UP000050360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA Welte C.U.;
RT "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT oxidation of methane by Methanoperedens-like archaea.";
RL Submitted (SEP-2015) 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. 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:KPQ42967.1}.
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DR EMBL; LKCM01000191; KPQ42967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8A479; -.
DR Proteomes; UP000050360; 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 148 AA; 16753 MW; C1D306023467636E CRC64;
MKLNFSIEPA PEKTSKAMGK ELHISRKQAH EIATAIKGMK LDIAQKFLEN VAALKQAVPY
KRFTRNIPHR KGMCSGRYPQ KAAREFLCII KNAQSNATYK GLDPESMRII HVETKKGHSY
MGQFPRAQGR ATPKRQETVT VEMIAEVQ
//
