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Protein

50S ribosomal protein L21

Gene

rplU

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This protein binds to 23S rRNA in the presence of protein L20 (By similarity). Found on the solvent side of the large subunit.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1825-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L21UniRule annotation
Gene namesi
Name:rplUUniRule annotation
Ordered Locus Names:TTHA1783
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10110150S ribosomal protein L21PRO_0000181018Add
BLAST

Interactioni

Subunit structurei

Contacts protein L20 (By similarity). Part of the 50S ribosomal subunit.By similarity

Protein-protein interaction databases

STRINGi300852.TTHA1783.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 134Combined sources
Beta strandi32 – 343Combined sources
Beta strandi48 – 514Combined sources
Beta strandi58 – 669Combined sources
Beta strandi70 – 767Combined sources
Turni77 – 804Combined sources
Beta strandi81 – 877Combined sources
Beta strandi90 – 989Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RV/YV1-101[»]
1VY4X-ray2.60BV/DV1-101[»]
1VY5X-ray2.55BV/DV1-101[»]
1VY6X-ray2.90BV/DV1-101[»]
1VY7X-ray2.80BV/DV1-101[»]
4L47X-ray3.22RV/YV1-101[»]
4L71X-ray3.90RV/YV1-101[»]
4LELX-ray3.90RV/YV1-101[»]
4LFZX-ray3.92RV/YV1-101[»]
4LNTX-ray2.94RV/YV1-101[»]
4LSKX-ray3.48RV/YV1-101[»]
4LT8X-ray3.14RV/YV1-101[»]
4P6FX-ray3.60RV/YV1-101[»]
4P70X-ray3.68RV/YV1-101[»]
4TUAX-ray3.60RV/YV1-101[»]
4TUBX-ray3.60RV/YV1-101[»]
4TUCX-ray3.60RV/YV1-101[»]
4TUDX-ray3.60RV/YV1-101[»]
4TUEX-ray3.50RV/YV1-101[»]
4V4PX-ray5.5021-101[»]
4V4XX-ray5.00BU1-101[»]
4V4YX-ray5.50BU1-101[»]
4V4ZX-ray4.51BU1-101[»]
4V51X-ray2.80BV/DV1-101[»]
4V5AX-ray3.50BV/DV1-101[»]
4V5CX-ray3.30BV/DV1-101[»]
4V5DX-ray3.50BV/DV1-101[»]
4V5EX-ray3.45BV/DV1-101[»]
4V5FX-ray3.60BV/DV1-101[»]
4V5GX-ray3.60BV/DV1-101[»]
4V5JX-ray3.10BV/DV1-101[»]
4V5KX-ray3.20BV/DV1-101[»]
4V5LX-ray3.10BV1-101[»]
4V5Melectron microscopy7.80BV1-101[»]
4V5Nelectron microscopy7.60BV1-101[»]
4V5PX-ray3.10BV/DV1-101[»]
4V5QX-ray3.10BV/DV1-101[»]
4V5RX-ray3.10BV/DV1-101[»]
4V5SX-ray3.10BV/DV1-101[»]
4V68electron microscopy6.40BV1-101[»]
4V6AX-ray3.10BV/DV1-101[»]
4V6FX-ray3.10A2/D21-101[»]
4V6GX-ray3.50B2/D21-101[»]
4V7JX-ray3.30AV/BV1-101[»]
4V7KX-ray3.60AV/BV1-101[»]
4V7LX-ray3.00BV/DV1-101[»]
4V7MX-ray3.45BV/DV1-101[»]
4V7WX-ray3.00BV/DV1-101[»]
4V7XX-ray3.00BV/DV1-101[»]
4V7YX-ray3.00BV/DV1-101[»]
4V7ZX-ray3.10BV/DV1-101[»]
4V87X-ray3.10A2/D21-101[»]
4V8AX-ray3.20AV/BV1-101[»]
4V8BX-ray3.00B2/D21-101[»]
4V8CX-ray3.30A2/B21-101[»]
4V8DX-ray3.00B2/D21-101[»]
4V8EX-ray3.30A2/C21-101[»]
4V8FX-ray3.30A2/D21-101[»]
4V8GX-ray3.00BV/DV1-101[»]
4V8HX-ray3.10BV/DV1-101[»]
4V8IX-ray2.70BV/DV1-101[»]
4V8JX-ray3.90BV/DV1-101[»]
4V8NX-ray3.10BV/DV1-101[»]
4V8OX-ray3.80BV1-101[»]
4V8QX-ray3.10AV1-101[»]
4V8UX-ray3.70BV/DV1-101[»]
4V8XX-ray3.35BV/DV1-101[»]
4V90X-ray2.95BV1-101[»]
4V95X-ray3.20BV/DV1-101[»]
4V97X-ray3.52BV/DV1-101[»]
4V9AX-ray3.30B2/D21-101[»]
4V9BX-ray3.10B2/D21-101[»]
4V9HX-ray2.86BV1-101[»]
4V9IX-ray3.30BV/DV1-101[»]
4V9RX-ray3.00BV/DV1-101[»]
4V9SX-ray3.10BV/DV1-101[»]
4W2EX-ray2.90V1-101[»]
4W2FX-ray2.40BV/DV1-101[»]
4W2GX-ray2.55BV/DV1-101[»]
4W2HX-ray2.70BV/DV1-101[»]
4W2IX-ray2.70BV/DV1-101[»]
4WPOX-ray2.80AV/CV1-101[»]
4WQFX-ray2.80AV/CV1-101[»]
4WQUX-ray2.80AV/CV1-101[»]
4WQYX-ray2.80AV/CV1-101[»]
4WWEX-ray3.40U1-101[»]
4WWTX-ray3.40U1-101[»]
4Y4OX-ray2.301V/2V1-101[»]
4Y4PX-ray2.501V/2V1-101[»]
4Z3QX-ray2.601V/2V1-101[»]
4Z3RX-ray3.101V/2V1-101[»]
4Z3SX-ray2.651V/2V1-101[»]
4Z8CX-ray2.901V/2V1-101[»]
4ZERX-ray3.101V/2V1-101[»]
ProteinModelPortaliP60492.
SMRiP60492. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60492.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L21P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0261.
HOGENOMiHOG000036265.
KOiK02888.
OMAiQGHRQPF.
OrthoDBiEOG6TJ84X.
PhylomeDBiP60492.

Family and domain databases

HAMAPiMF_01363. Ribosomal_L21.
InterProiIPR028909. L21p-like.
IPR001787. Ribosomal_L21.
[Graphical view]
PfamiPF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
SUPFAMiSSF141091. SSF141091. 1 hit.
TIGRFAMsiTIGR00061. L21. 1 hit.

Sequencei

Sequence statusi: Complete.

P60492-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAIVKTGGK QYRVEPGLKL RVEKLDAEPG ATVELPVLLL GGEKTVVGTP
60 70 80 90 100
VVEGASVVAE VLGHGRGKKI LVSKFKAKVQ YRRKKGHRQP YTELLIKEIR

G
Length:101
Mass (Da):11,047
Last modified:March 29, 2005 - v2
Checksum:i3117549029950A0C
GO

Mass spectrometryi

Molecular mass is 11048 Da from positions 1 - 101. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71606.1.
RefSeqiWP_008633581.1. NC_006461.1.
YP_145049.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71606; BAD71606; BAD71606.
GeneIDi3169471.
KEGGittj:TTHA1783.
PATRICi23958527. VBITheThe93045_1753.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71606.1.
RefSeqiWP_008633581.1. NC_006461.1.
YP_145049.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RV/YV1-101[»]
1VY4X-ray2.60BV/DV1-101[»]
1VY5X-ray2.55BV/DV1-101[»]
1VY6X-ray2.90BV/DV1-101[»]
1VY7X-ray2.80BV/DV1-101[»]
4L47X-ray3.22RV/YV1-101[»]
4L71X-ray3.90RV/YV1-101[»]
4LELX-ray3.90RV/YV1-101[»]
4LFZX-ray3.92RV/YV1-101[»]
4LNTX-ray2.94RV/YV1-101[»]
4LSKX-ray3.48RV/YV1-101[»]
4LT8X-ray3.14RV/YV1-101[»]
4P6FX-ray3.60RV/YV1-101[»]
4P70X-ray3.68RV/YV1-101[»]
4TUAX-ray3.60RV/YV1-101[»]
4TUBX-ray3.60RV/YV1-101[»]
4TUCX-ray3.60RV/YV1-101[»]
4TUDX-ray3.60RV/YV1-101[»]
4TUEX-ray3.50RV/YV1-101[»]
4V4PX-ray5.5021-101[»]
4V4XX-ray5.00BU1-101[»]
4V4YX-ray5.50BU1-101[»]
4V4ZX-ray4.51BU1-101[»]
4V51X-ray2.80BV/DV1-101[»]
4V5AX-ray3.50BV/DV1-101[»]
4V5CX-ray3.30BV/DV1-101[»]
4V5DX-ray3.50BV/DV1-101[»]
4V5EX-ray3.45BV/DV1-101[»]
4V5FX-ray3.60BV/DV1-101[»]
4V5GX-ray3.60BV/DV1-101[»]
4V5JX-ray3.10BV/DV1-101[»]
4V5KX-ray3.20BV/DV1-101[»]
4V5LX-ray3.10BV1-101[»]
4V5Melectron microscopy7.80BV1-101[»]
4V5Nelectron microscopy7.60BV1-101[»]
4V5PX-ray3.10BV/DV1-101[»]
4V5QX-ray3.10BV/DV1-101[»]
4V5RX-ray3.10BV/DV1-101[»]
4V5SX-ray3.10BV/DV1-101[»]
4V68electron microscopy6.40BV1-101[»]
4V6AX-ray3.10BV/DV1-101[»]
4V6FX-ray3.10A2/D21-101[»]
4V6GX-ray3.50B2/D21-101[»]
4V7JX-ray3.30AV/BV1-101[»]
4V7KX-ray3.60AV/BV1-101[»]
4V7LX-ray3.00BV/DV1-101[»]
4V7MX-ray3.45BV/DV1-101[»]
4V7WX-ray3.00BV/DV1-101[»]
4V7XX-ray3.00BV/DV1-101[»]
4V7YX-ray3.00BV/DV1-101[»]
4V7ZX-ray3.10BV/DV1-101[»]
4V87X-ray3.10A2/D21-101[»]
4V8AX-ray3.20AV/BV1-101[»]
4V8BX-ray3.00B2/D21-101[»]
4V8CX-ray3.30A2/B21-101[»]
4V8DX-ray3.00B2/D21-101[»]
4V8EX-ray3.30A2/C21-101[»]
4V8FX-ray3.30A2/D21-101[»]
4V8GX-ray3.00BV/DV1-101[»]
4V8HX-ray3.10BV/DV1-101[»]
4V8IX-ray2.70BV/DV1-101[»]
4V8JX-ray3.90BV/DV1-101[»]
4V8NX-ray3.10BV/DV1-101[»]
4V8OX-ray3.80BV1-101[»]
4V8QX-ray3.10AV1-101[»]
4V8UX-ray3.70BV/DV1-101[»]
4V8XX-ray3.35BV/DV1-101[»]
4V90X-ray2.95BV1-101[»]
4V95X-ray3.20BV/DV1-101[»]
4V97X-ray3.52BV/DV1-101[»]
4V9AX-ray3.30B2/D21-101[»]
4V9BX-ray3.10B2/D21-101[»]
4V9HX-ray2.86BV1-101[»]
4V9IX-ray3.30BV/DV1-101[»]
4V9RX-ray3.00BV/DV1-101[»]
4V9SX-ray3.10BV/DV1-101[»]
4W2EX-ray2.90V1-101[»]
4W2FX-ray2.40BV/DV1-101[»]
4W2GX-ray2.55BV/DV1-101[»]
4W2HX-ray2.70BV/DV1-101[»]
4W2IX-ray2.70BV/DV1-101[»]
4WPOX-ray2.80AV/CV1-101[»]
4WQFX-ray2.80AV/CV1-101[»]
4WQUX-ray2.80AV/CV1-101[»]
4WQYX-ray2.80AV/CV1-101[»]
4WWEX-ray3.40U1-101[»]
4WWTX-ray3.40U1-101[»]
4Y4OX-ray2.301V/2V1-101[»]
4Y4PX-ray2.501V/2V1-101[»]
4Z3QX-ray2.601V/2V1-101[»]
4Z3RX-ray3.101V/2V1-101[»]
4Z3SX-ray2.651V/2V1-101[»]
4Z8CX-ray2.901V/2V1-101[»]
4ZERX-ray3.101V/2V1-101[»]
ProteinModelPortaliP60492.
SMRiP60492. Positions 1-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71606; BAD71606; BAD71606.
GeneIDi3169471.
KEGGittj:TTHA1783.
PATRICi23958527. VBITheThe93045_1753.

Phylogenomic databases

eggNOGiCOG0261.
HOGENOMiHOG000036265.
KOiK02888.
OMAiQGHRQPF.
OrthoDBiEOG6TJ84X.
PhylomeDBiP60492.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1825-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60492.

Family and domain databases

HAMAPiMF_01363. Ribosomal_L21.
InterProiIPR028909. L21p-like.
IPR001787. Ribosomal_L21.
[Graphical view]
PfamiPF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
SUPFAMiSSF141091. SSF141091. 1 hit.
TIGRFAMsiTIGR00061. L21. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "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 1-18.
  3. "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.
  4. Cited for: STRUCTURE OF THE RIBOSOME.
  5. "Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding."
    Jenner L., Romby P., Rees B., Schulze-Briese C., Springer M., Ehresmann C., Ehresmann B., Moras D., Yusupova G., Yusupov M.
    Science 308:120-123(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-101 OF THE RIBOSOME.

Entry informationi

Entry nameiRL21_THET8
AccessioniPrimary (citable) accession number: P60492
Secondary accession number(s): Q5SHE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 29, 2005
Last modified: July 22, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.