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Database: UniProt
Entry: F2I1J4_PELSM
LinkDB: F2I1J4_PELSM
Original site: F2I1J4_PELSM 
ID   F2I1J4_PELSM            Unreviewed;       170 AA.
AC   F2I1J4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Large ribosomal subunit protein uL10 {ECO:0000256|HAMAP-Rule:MF_00362};
GN   Name=rplJ {ECO:0000256|HAMAP-Rule:MF_00362};
GN   OrderedLocusNames=SAR11G3_01233 {ECO:0000313|EMBL:AEA81708.1};
OS   Pelagibacter sp. (strain IMCC9063).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae; Pelagibacter.
OX   NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA81708.1, ECO:0000313|Proteomes:UP000009181};
RN   [1] {ECO:0000313|EMBL:AEA81708.1, ECO:0000313|Proteomes:UP000009181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA81708.1,
RC   ECO:0000313|Proteomes:UP000009181};
RX   PubMed=21515764; DOI=10.1128/JB.05033-11;
RA   Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.;
RT   "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup
RT   3, isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3379-3380(2011).
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}.
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DR   EMBL; CP002511; AEA81708.1; -; Genomic_DNA.
DR   RefSeq; WP_013695873.1; NC_015380.1.
DR   AlphaFoldDB; F2I1J4; -.
DR   STRING; 1002672.SAR11G3_01233; -.
DR   KEGG; pel:SAR11G3_01233; -.
DR   eggNOG; COG0244; Bacteria.
DR   HOGENOM; CLU_092227_0_0_5; -.
DR   OrthoDB; 9791972at2; -.
DR   Proteomes; UP000009181; 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   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:UP000009181};
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   170 AA;  18617 MW;  96A7CE1B36D96772 CRC64;
     MNREQKSSYV SSLKESLNNN EAMMIYHYHG LNVNQLDDLR NQMREAGALL KVTKNRITKI
     ALKDTQHEEA ISLFSGQTGV ALSKDPITLA KTLVNFQKKN DMLKIVGGVM DSKVLAPEDV
     AKIATLPTLD EARAKIAAIL QTPAQQLISI LLAPGAKIAN LAHAKSLKKD
//
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