RL10_METS3
ID RL10_METS3 Reviewed; 335 AA.
AC A5UKU8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00280};
DE AltName: Full=Acidic ribosomal protein P0 homolog {ECO:0000255|HAMAP-Rule:MF_00280};
GN Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280};
GN Synonyms=rplP0 {ECO:0000255|HAMAP-Rule:MF_00280};
GN OrderedLocusNames=Msm_0621;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in
CC the interaction of the ribosome with GTP-bound translation factors.
CC {ECO:0000255|HAMAP-Rule:MF_00280}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms part of the ribosomal
CC stalk which helps the ribosome interact with GTP-bound translation
CC factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10
CC forms an elongated spine to which the L12 dimers bind in a sequential
CC fashion. {ECO:0000255|HAMAP-Rule:MF_00280}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000255|HAMAP-Rule:MF_00280}.
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DR EMBL; CP000678; ABQ86826.1; -; Genomic_DNA.
DR RefSeq; WP_004036529.1; NC_009515.1.
DR AlphaFoldDB; A5UKU8; -.
DR SMR; A5UKU8; -.
DR STRING; 420247.Msm_0621; -.
DR EnsemblBacteria; ABQ86826; ABQ86826; Msm_0621.
DR GeneID; 5217346; -.
DR KEGG; msi:Msm_0621; -.
DR PATRIC; fig|420247.28.peg.618; -.
DR eggNOG; arCOG04288; Archaea.
DR HOGENOM; CLU_053173_0_0_2; -.
DR OMA; MAHVAEW; -.
DR Proteomes; UP000001992; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR HAMAP; MF_00280; Ribosomal_L10_arch; 1.
DR InterPro; IPR022909; 50S_L10_arch.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..335
FT /note="50S ribosomal protein L10"
FT /id="PRO_1000006791"
FT REGION 306..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..326
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 35996 MW; 6DEEFFF7F65D9EB6 CRC64;
MAHVAEWKKE EVNELKSLID KYDVIGIVDL LNIPAKQLQE MRKSLHNKAV IRMSKKNLID
LALEDCNASK NNIVDLSEHM EGQVAVIATE MNPFKLYKIL EDSKTSAPAK PGAIATDDIV
IPEGDTGFEP GPFLGELQQV GIPAKIDKGK IVVSKETVLV EAGEEVSAAV ASTLSRMDIN
PMEVGIDLRA VYEEEAIYTS EVLAIDEEQT LADVQNAFRN AFNLSVNAAI PTEETISTII
TLAYTRAINV GVDAAIMTSE TSEPIIGLAQ AKMLALASEV SGTEGALDDE LAEKLSNVAV
AAAPVVEETV EEEEEEEEEE DAEEEAAAGL GALFG
