ID A0A1Q9JY03_9FIRM Unreviewed; 163 AA.
AC A0A1Q9JY03;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BHF69_12450 {ECO:0000313|EMBL:OLR61034.1};
OS Anaerostipes sp. 992a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=1261637 {ECO:0000313|EMBL:OLR61034.1, ECO:0000313|Proteomes:UP000187371};
RN [1] {ECO:0000313|EMBL:OLR61034.1, ECO:0000313|Proteomes:UP000187371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=992a {ECO:0000313|EMBL:OLR61034.1,
RC ECO:0000313|Proteomes:UP000187371};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR61034.1}.
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DR EMBL; MJIG01000005; OLR61034.1; -; Genomic_DNA.
DR RefSeq; WP_075672201.1; NZ_MJIG01000005.1.
DR AlphaFoldDB; A0A1Q9JY03; -.
DR STRING; 1261637.BHF69_12450; -.
DR OrthoDB; 9808307at2; -.
DR Proteomes; UP000187371; 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:UP000187371};
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 163 AA; 17958 MW; A42710769FD9874A CRC64;
MAKVELKQPI VEEIKELLDG AASAVLVEYR GITVEDDTKL RKELREADVI YKVYKNTMIR
FAVQGTEFEP LTADLEGPTA IAVSKDDATA PARILAKYAK AVKPFELKSG VVEGTYYDRD
GIKVIATIPS REELLSKLLG SLQSPMANFA RVINQIAEAK EEA
//
