ID   RL10_METM6              Reviewed;         335 AA.
AC   A9A838;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=MmarC6_0694;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX01511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A838; -.
DR   SMR; A9A838; -.
DR   STRING; 444158.MmarC6_0694; -.
DR   EnsemblBacteria; ABX01511; ABX01511; MmarC6_0694.
DR   KEGG; mmx:MmarC6_0694; -.
DR   eggNOG; arCOG04288; Archaea.
DR   HOGENOM; CLU_053173_0_0_2; -.
DR   OMA; MAHVAEW; -.
DR   PhylomeDB; A9A838; -.
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_1000114837"
FT   REGION          304..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..326
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   335 AA;  35818 MW;  7C4AC6EB5976D57B CRC64;
     MIDAKSEHKI APWKIEEVNA LKELLKSTSI IALIDMMEVP AVQLQEIRDK IRDQMTLKMS
     RNTLMKRAIE EVAEETGNPE FAKLADYLDK GAAIIATEMN PFKLFKTLDE SKSPAPVKGG
     ATAPCDIEVK AGSTGMPPGP FLSELKAVGI PAAIDKGKIG IKEDKVVIKE GEVVSQKLAV
     VLSALGIKPV TVGLNVLGVY EDGVIYTESE LRIDEEEFIG KIQKAYTSAF NLSVNAVIPT
     SATVETIVQK AFNDAKAVSV ESAFVTDKTA DAILGKAYAQ MIAVAGLASD DALDEELKEK
     ISSGAAAPVE EAPVEEKKEE KKEEAAPAAG LGMLF