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Q8VVE3

- RL10_THET8

UniProt

Q8VVE3 - RL10_THET8

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Protein

50S ribosomal protein L10

Gene
rplJ, TTHA0209
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 17317250S ribosomal protein L10UniRule annotationPRO_0000154736Add
BLAST

Post-translational modificationi

The N-terminus is blocked.UniRule annotation

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.

Miscellaneous databases

EvolutionaryTraceiQ8VVE3.

Family & Domainsi

Sequence similaritiesi

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

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 conflict

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 84 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 1 Publication it was found that the N-terminus is blocked, whereas the mass determined in 1 Publication suggests that the initiator methionine is removed. No extra mass for a blocking group was found.

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

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