ID A0A365H887_9ACTN Unreviewed; 189 AA.
AC A0A365H887;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 10-JUN-2026, entry version 26.
DE RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000256|ARBA:ARBA00035202, ECO:0000256|HAMAP-Rule:MF_00362};
GN Name=rplJ {ECO:0000256|HAMAP-Rule:MF_00362};
GN ORFNames=DPM19_10645 {ECO:0000313|EMBL:RAY15176.1};
OS Actinomadura craniellae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2231787 {ECO:0000313|EMBL:RAY15176.1, ECO:0000313|Proteomes:UP000251891};
RN [1] {ECO:0000313|EMBL:RAY15176.1, ECO:0000313|Proteomes:UP000251891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW63021 {ECO:0000313|EMBL:RAY15176.1,
RC ECO:0000313|Proteomes:UP000251891};
RA Li L., Xu Q.H., Lin H.W., Lu Y.H.;
RT "Actinomadura craniellae sp. nov. isolated from marine sponge Craniella
RT sp.";
RL Submitted (JUN-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|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:RAY15176.1}.
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DR EMBL; QLYX01000004; RAY15176.1; -; Genomic_DNA.
DR RefSeq; WP_111865620.1; NZ_QLYX01000004.1.
DR AlphaFoldDB; A0A365H887; -.
DR OrthoDB; 3186107at2; -.
DR Proteomes; UP000251891; 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_uL10; 1.
DR InterPro; IPR001790; Ribosomal_uL10.
DR InterPro; IPR043141; Ribosomal_uL10-like_sf.
DR InterPro; IPR022973; Ribosomal_uL10_bact.
DR InterPro; IPR047865; Ribosomal_uL10_bact_orga.
DR InterPro; IPR002363; Ribosomal_uL10_CS_bac.
DR NCBIfam; NF000955; PRK00099.1-1; 1.
DR PANTHER; PTHR11560; 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:UP000251891};
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}.
FT REGION 168..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 189 AA; 19744 MW; 76B40E52EE01CC4A CRC64;
MAKAEKAAAV AELTDEFNNS SGAVLTEYRG LTVAQLGELR RNLGDNARFA VVKNTLTKIA
ASEAGVDEQF RQLLEGPSAI AFVKGDVVEA AKGLRDFAKA NPLLVIKGGV VDGKSMDATE
ITKLADLESR EVLLAKLAGA MKASMGNAAA TFNALPTQLA LLADALRTKR EEAGETSEAP
AEETQPAEG
//
