ID A0A2U2RPN8_9MICO Unreviewed; 171 AA.
AC A0A2U2RPN8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000256|HAMAP-Rule:MF_00362};
GN Name=rplJ {ECO:0000256|HAMAP-Rule:MF_00362};
GN ORFNames=DEO23_03975 {ECO:0000313|EMBL:PWH07775.1};
OS Brachybacterium endophyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=2182385 {ECO:0000313|EMBL:PWH07775.1, ECO:0000313|Proteomes:UP000245590};
RN [1] {ECO:0000313|EMBL:PWH07775.1, ECO:0000313|Proteomes:UP000245590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1HQ-2 {ECO:0000313|EMBL:PWH07775.1,
RC ECO:0000313|Proteomes:UP000245590};
RA Tuo L.;
RT "Brachybacterium sp. M1HQ-2T, whole genome shotgun sequence.";
RL Submitted (MAY-2018) 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|ARBA:ARBA00002633, 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|ARBA:ARBA00026025, 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:PWH07775.1}.
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DR EMBL; QFKX01000001; PWH07775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2RPN8; -.
DR OrthoDB; 3186107at2; -.
DR Proteomes; UP000245590; 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 Reference proteome {ECO:0000313|Proteomes:UP000245590};
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 171 AA; 18197 MW; C1675703C38A7AE9 CRC64;
MAKPEKVDAV AELTQLFRES DAAVLTEYRG LSVTQLQQLR RSLGADTTYA VVKNTLTEIA
AREAGIDAFE GKLAGPTAIA FIKGEPVGPA KTLRDFAKGN ESLVLKSGYF EGKPLSEDDV
KTLADLESRE VLLAKAAGAF KANLSKAAAV FQAPLSKTAR TVDALRAKQE A
//