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Database: UniProt
Entry: A0A0P6XIV6_9SPHN
LinkDB: A0A0P6XIV6_9SPHN
Original site: A0A0P6XIV6_9SPHN 
ID   A0A0P6XIV6_9SPHN        Unreviewed;       171 AA.
AC   A0A0P6XIV6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=SZ64_12625 {ECO:0000313|EMBL:KPL68867.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68867.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL68867.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68867.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
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|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:KPL68867.1}.
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DR   EMBL; JXQC01000003; KPL68867.1; -; Genomic_DNA.
DR   RefSeq; WP_054531142.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6XIV6; -.
DR   STRING; 1603897.SZ64_12625; -.
DR   PATRIC; fig|1603897.4.peg.2472; -.
DR   OrthoDB; 9791972at2; -.
DR   Proteomes; UP000049978; 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:UP000049978};
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;  17658 MW;  AC6054EBC205E988 CRC64;
     MDRSQKADSV AQLNANFNEV SVVVVTRNLG LTVAQSTALR TKMREVGASY KVAKNRLAKL
     ALKDTQFEGL EDYLSGPTAL ATSVDPVAAA KAAVDFAKAN PKLEIVGGSM GGTLLDEAGV
     KALASMPSLD ELRAKLVGLV QAPATKVAQL STAPAAKLAR VFGAYAAKDA A
//
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