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Q8VVE3

- RL10_THET8

UniProt

Q8VVE3 - RL10_THET8

Protein

50S ribosomal protein L10

Gene

rplJ

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.Curated

    GO - Molecular functioni

    1. large ribosomal subunit rRNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. ribosome biogenesis Source: InterPro
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-218-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L10
    Gene namesi
    Name:rplJ
    Ordered Locus Names:TTHA0209
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. ribosome Source: UniProtKB-KW

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 17317250S ribosomal protein L10PRO_0000154736Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which 3 L12 dimers bind in a sequential fashion.1 Publication

    Protein-protein interaction databases

    STRINGi300852.TTHA0209.

    Structurei

    Secondary structure

    1
    173
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 125
    Turni13 – 186
    Beta strandi22 – 243
    Beta strandi35 – 373
    Beta strandi43 – 464
    Helixi57 – 626
    Turni63 – 653
    Beta strandi66 – 705
    Beta strandi76 – 805
    Helixi88 – 936
    Turni94 – 985
    Beta strandi99 – 1013
    Beta strandi103 – 1053
    Beta strandi113 – 1164
    Beta strandi118 – 1214
    Helixi122 – 1254
    Beta strandi126 – 1283
    Turni136 – 1383

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J01X-ray2.80J2-173[»]
    2J03X-ray2.80J2-173[»]
    3I8IX-ray3.10Y1-173[»]
    3KIRX-ray3.30J1-173[»]
    3KITX-ray3.30J1-173[»]
    3KIWX-ray3.60J1-173[»]
    3KIYX-ray3.60J1-173[»]
    ProteinModelPortaliQ8VVE3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8VVE3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L10P family.Curated

    Phylogenomic databases

    eggNOGiCOG0244.
    HOGENOMiHOG000004852.
    KOiK02864.
    OMAiFERMSSA.
    OrthoDBiEOG6DNTDR.
    PhylomeDBiQ8VVE3.

    Family and domain databases

    HAMAPiMF_00362. Ribosomal_L10.
    InterProiIPR022973. Ribosomal_L10.
    IPR001790. Ribosomal_L10/acidic_P0.
    [Graphical view]
    PfamiPF00466. Ribosomal_L10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8VVE3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNKRNVELL ATLKENLERA QGSFFLVNYQ GLPAKETHAL RQALKQNGAR    50
    LFVAKNTLIR LALKELGLPE LDGLQGPSAV VFYEDPVAAA KTLVQFAKSN 100
    PKGIPQVKSG LLQGQILTAK DVEALAELPT MDELRAELVG VLQAPMAELV 150
    GVLGGVAREL VGILEAYAEK KAA 173
    Length:173
    Mass (Da):18,566
    Last modified:January 23, 2007 - v4
    Checksum:i266CF72B036C6D5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1282EL → DV in CAD11986. 1 PublicationCurated
    Sequence conflicti137 – 1382EL → DV in CAD11986. 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 96075±13 Da from positions 2 - 173. Determined by ESI. Isolated L10(L12)6.1 Publication
    Molecular mass is 18434±1 Da from positions 2 - 173. Determined by ESI. 1 Publication
    Molecular mass is 18436 Da from positions 2 - 173. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ419825 Genomic DNA. Translation: CAD11986.1.
    AP008226 Genomic DNA. Translation: BAD70032.1.
    RefSeqiYP_143475.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD70032; BAD70032; BAD70032.
    GeneIDi3168578.
    KEGGittj:TTHA0209.
    PATRICi23955359. VBITheThe93045_0207.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ419825 Genomic DNA. Translation: CAD11986.1 .
    AP008226 Genomic DNA. Translation: BAD70032.1 .
    RefSeqi YP_143475.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J01 X-ray 2.80 J 2-173 [» ]
    2J03 X-ray 2.80 J 2-173 [» ]
    3I8I X-ray 3.10 Y 1-173 [» ]
    3KIR X-ray 3.30 J 1-173 [» ]
    3KIT X-ray 3.30 J 1-173 [» ]
    3KIW X-ray 3.60 J 1-173 [» ]
    3KIY X-ray 3.60 J 1-173 [» ]
    ProteinModelPortali Q8VVE3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA0209.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD70032 ; BAD70032 ; BAD70032 .
    GeneIDi 3168578.
    KEGGi ttj:TTHA0209.
    PATRICi 23955359. VBITheThe93045_0207.

    Phylogenomic databases

    eggNOGi COG0244.
    HOGENOMi HOG000004852.
    KOi K02864.
    OMAi FERMSSA.
    OrthoDBi EOG6DNTDR.
    PhylomeDBi Q8VVE3.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-218-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q8VVE3.

    Family and domain databases

    HAMAPi MF_00362. Ribosomal_L10.
    InterProi IPR022973. Ribosomal_L10.
    IPR001790. Ribosomal_L10/acidic_P0.
    [Graphical view ]
    Pfami PF00466. Ribosomal_L10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Ribosomal protein L12 and L10 from Thermus thermophilus, dissertation."
      Huang Y., Sprinzl M.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    3. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
      Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
      Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11, BLOCKAGE OF N-TERMINUS.
    4. "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria."
      Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H., Robinson C.V.
      Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, STOICHIOMETRY, MASS SPECTROMETRY.
    5. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
      Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
      Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.

    Entry informationi

    Entry nameiRL10_THET8
    AccessioniPrimary (citable) accession number: Q8VVE3
    Secondary accession number(s): Q5SLT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 85 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Note that in PubMed:11154066 it was found that the N-terminus is blocked, whereas the mass determined in PubMed:16287167 suggests that the initiator methionine is removed. No extra mass for a blocking group was found.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3