RL10_SULIY
ID RL10_SULIY Reviewed; 338 AA.
AC C3N7E1;
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=YG5714_1879;
OS Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=439386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.G.57.14 / Yellowstone #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; CP001403; ACP46135.1; -; Genomic_DNA.
DR RefSeq; WP_012713970.1; NC_012622.1.
DR AlphaFoldDB; C3N7E1; -.
DR SMR; C3N7E1; -.
DR EnsemblBacteria; ACP46135; ACP46135; YG5714_1879.
DR GeneID; 7809659; -.
DR KEGG; siy:YG5714_1879; -.
DR HOGENOM; CLU_053173_0_0_2; -.
DR OMA; MAHVAEW; -.
DR Proteomes; UP000002308; 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_1000204817"
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