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Database: UniProt
Entry: J9RGI7_9ACTN
LinkDB: J9RGI7_9ACTN
Original site: J9RGI7_9ACTN 
ID   J9RGI7_9ACTN            Unreviewed;       176 AA.
AC   J9RGI7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=KTR9_0997 {ECO:0000313|EMBL:AFR47642.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR47642.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR47642.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR47642.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
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}.
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DR   EMBL; CP002907; AFR47642.1; -; Genomic_DNA.
DR   RefSeq; WP_010844579.1; NC_018581.1.
DR   AlphaFoldDB; J9RGI7; -.
DR   STRING; 337191.KTR9_0997; -.
DR   KEGG; gor:KTR9_0997; -.
DR   PATRIC; fig|337191.3.peg.1217; -.
DR   eggNOG; COG0244; Bacteria.
DR   HOGENOM; CLU_092227_1_0_11; -.
DR   Proteomes; UP000003281; Chromosome.
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;  18395 MW;  9A0ADD2785FF18C7 CRC64;
     MAKSEKVAAV AEIAEQFKGS TATVVTEYRG LSVTQISQLR RSLGEGATYS VAKNTLVKRA
     AAEAGVEGLD ELFTGPTAIA FIEGEPVVAA KAIKTFAKDN KALVIKGGYM DGRALSIAEI
     EQIADLETRE VLLAKLAGAM KGNLAKAAGL FNQPASQVAR LAAALQEKKN EAGETE
//
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