RL10_PICTO
ID RL10_PICTO Reviewed; 315 AA.
AC Q6L1X8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=PTO0439;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43024.1; -; Genomic_DNA.
DR RefSeq; WP_011177240.1; NC_005877.1.
DR AlphaFoldDB; Q6L1X8; -.
DR SMR; Q6L1X8; -.
DR STRING; 263820.PTO0439; -.
DR EnsemblBacteria; AAT43024; AAT43024; PTO0439.
DR GeneID; 2845217; -.
DR KEGG; pto:PTO0439; -.
DR PATRIC; fig|263820.9.peg.464; -.
DR eggNOG; arCOG04288; Archaea.
DR HOGENOM; CLU_053173_0_0_2; -.
DR OMA; MAHVAEW; -.
DR OrthoDB; 73593at2157; -.
DR Proteomes; UP000000438; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..315
FT /note="50S ribosomal protein L10"
FT /id="PRO_0000154800"
FT REGION 287..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 315 AA; 34758 MW; 1570DE57AE2771A2 CRC64;
MTEPAQWKID FVKNLENEIN SRKVAAIVSI KGLRNNEFQK IRNSIRDKAR IKVSRARLLR
LAIENTGKNN IVKLKDYAHG QVALITTDES PKKIYDILEK SKTKAPAKGG EIAEEDIVIE
PKETNFPPGP KISEFQKAGL PAAIEKGKIV IKSEVTFVKK GDVITREKAL VLKDLEIYPI
TAGLDLIAAY EDGLIFNKDV LSISDEKIMS DLASAFLGAK SLAIEANFIV PEIVPDMISK
AYLEAQSLAI EANFVDEKNI DIFIRKAFIN ASAIEALINK DLNNEDITDK KEEKAEEKET
SSDEDAASGL GALFG