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Database: UniProt
Entry: D1Y5S2_9BACT
LinkDB: D1Y5S2_9BACT
Original site: D1Y5S2_9BACT 
ID   D1Y5S2_9BACT            Unreviewed;       176 AA.
AC   D1Y5S2;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000256|HAMAP-Rule:MF_00362};
GN   Name=rplJ {ECO:0000256|HAMAP-Rule:MF_00362,
GN   ECO:0000313|EMBL:EFB90345.1};
GN   ORFNames=HMPREF7215_2228 {ECO:0000313|EMBL:EFB90345.1};
OS   Pyramidobacter piscolens W5455.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Pyramidobacter.
OX   NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB90345.1, ECO:0000313|Proteomes:UP000006462};
RN   [1] {ECO:0000313|EMBL:EFB90345.1, ECO:0000313|Proteomes:UP000006462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5455 {ECO:0000313|EMBL:EFB90345.1,
RC   ECO:0000313|Proteomes:UP000006462};
RA   Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (DEC-2009) 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:0000256|HAMAP-Rule:MF_00362}.
CC   -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. The
CC       N-terminus interacts with L11 and the large rRNA to form the base of
CC       the stalk. The C-terminus forms an elongated spine to which L12 dimers
CC       bind in a sequential fashion forming a multimeric L10(L12)X complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00362}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC       {ECO:0000256|ARBA:ARBA00008889, ECO:0000256|HAMAP-Rule:MF_00362}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFB90345.1}.
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DR   EMBL; ADFP01000084; EFB90345.1; -; Genomic_DNA.
DR   RefSeq; WP_009165159.1; NZ_ADFP01000084.1.
DR   AlphaFoldDB; D1Y5S2; -.
DR   STRING; 352165.HMPREF7215_2228; -.
DR   eggNOG; COG0244; Bacteria.
DR   OrthoDB; 9808307at2; -.
DR   Proteomes; UP000006462; Unassembled WGS sequence.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd05797; Ribosomal_L10; 1.
DR   Gene3D; 3.30.70.1730; -; 1.
DR   Gene3D; 6.10.250.290; -; 1.
DR   HAMAP; MF_00362; Ribosomal_L10; 1.
DR   InterPro; IPR001790; Ribosomal_uL10.
DR   InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR   InterPro; IPR022973; Ribosomal_uL10_bac.
DR   InterPro; IPR047865; Ribosomal_uL10_bac_type.
DR   InterPro; IPR002363; Ribosomal_uL10_CS_bac.
DR   PANTHER; PTHR11560; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11560:SF8; 39S RIBOSOMAL PROTEIN L10, MITOCHONDRIAL; 1.
DR   Pfam; PF00466; Ribosomal_L10; 1.
DR   SUPFAM; SSF160369; Ribosomal protein L10-like; 1.
DR   PROSITE; PS01109; RIBOSOMAL_L10; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00362};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00362}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_00362};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00362}.
SQ   SEQUENCE   176 AA;  18299 MW;  F32ABE3497234A5D CRC64;
     MPAQYKVDQV AELKELFNGA EAVFVAEYRG LTVAQASALR KAIRAAGGQA KVARNRLAEI
     ALDEVGLAKD VKMMKGPNLY VVAAANSPAV AKAIKDFSEV KENAAFVIKG GVMGKNLLGL
     DNVKALASMP SREELVAKAV GSIASPLRGL VTVLSGLPRG LVTALSAIAD KKKEAA
//
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