ID   RL10_SULIL              Reviewed;         338 AA.
AC   C3MR85;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
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=LS215_1903;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001399; ACP35898.1; -; Genomic_DNA.
DR   RefSeq; WP_012713970.1; NC_012589.1.
DR   AlphaFoldDB; C3MR85; -.
DR   SMR; C3MR85; -.
DR   EnsemblBacteria; ACP35898; ACP35898; LS215_1903.
DR   GeneID; 7809659; -.
DR   KEGG; sis:LS215_1903; -.
DR   HOGENOM; CLU_053173_0_0_2; -.
DR   OMA; MAHVAEW; -.
DR   OrthoDB; 73593at2157; -.
DR   Proteomes; UP000001747; 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..338
FT                   /note="50S ribosomal protein L10"
FT                   /id="PRO_1000204814"
FT   REGION          297..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  37109 MW;  3B446B9CB051E9AA CRC64;
     MKRLALALKQ KKVASWKLEE VKELTELIKN SNTILIGSLE GFPADKLHEI RKKLRGKAII
     KVTKNTLFKI AAKNAGISTE KLEQYLTGPN VFIFTKDNPF LTNMFFENYK LRRYAMPGDK
     AEEEVIIPAG DTGMPAGPIL SVFGKLKVQT KVQDGKVHVV KDTVVAKPGD VIPTEALPIL
     QKLGIMPVYV KLKIKVAYHE GLVIPAENLK LNLEGYRSNI AEAYRNAFTL AVEIAYPVPD
     VLKFTINKIF KNAITLASEI GYLTPESAQA VISKAVAKAY ALATAISGKV DLGVKLPSAQ
     QTQTQQSTAE EKKEEKKEEE KKGPSEEEIG SGLASLFG