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P60492 (RL21_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L21
Gene names
Name:rplU
Ordered Locus Names:TTHA1783
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds to 23S rRNA in the presence of protein L20 By similarity. Found on the solvent side of the large subunit. HAMAP-Rule MF_01363

Subunit structure

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

Sequence similarities

Belongs to the ribosomal protein L21P family.

Mass spectrometry

Molecular mass is 11048 Da from positions 1 - 101. Determined by MALDI. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10110150S ribosomal protein L21 HAMAP-Rule MF_01363
PRO_0000181018

Secondary structure

1 ....................... 101
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60492 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 3117549029950A0C

FASTA10111,047
        10         20         30         40         50         60 
MFAIVKTGGK QYRVEPGLKL RVEKLDAEPG ATVELPVLLL GGEKTVVGTP VVEGASVVAE 

        70         80         90        100 
VLGHGRGKKI LVSKFKAKVQ YRRKKGHRQP YTELLIKEIR G

« Hide

References

« Hide 'large scale' references
[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]"Crystal structure of the ribosome at 5.5 A resolution."
Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F.
Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract]
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]"Structure of the 70S ribosome complexed with mRNA and tRNA."
Selmer M., Dunham C.M., Murphy F.V. IV, Weixlbaumer A., Petry S., Kelley A.C., Weir J.R., Ramakrishnan V.
Science 313:1935-1942(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-101 OF THE RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008226 Genomic DNA. Translation: BAD71606.1.
RefSeqYP_145049.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YL3X-ray5.5021-89[»]
2HGJX-ray5.00U1-101[»]
2HGQX-ray5.50U1-101[»]
2HGUX-ray4.51U1-101[»]
2J01X-ray2.80V1-101[»]
2J03X-ray2.80V1-101[»]
2V47X-ray3.80V1-101[»]
2V49X-ray3.80V1-101[»]
2WDIX-ray3.30V1-101[»]
2WDJX-ray3.30V1-101[»]
2WDLX-ray3.50V1-101[»]
2WDNX-ray3.50V1-101[»]
2WH2X-ray3.45V1-101[»]
2WH4X-ray3.45V1-101[»]
2WRJX-ray3.60V1-101[»]
2WRLX-ray3.60V1-101[»]
2WROX-ray3.60V1-101[»]
2WRRX-ray3.60V1-101[»]
2X9SX-ray3.10V1-101[»]
2X9UX-ray3.10V1-101[»]
2XG0X-ray3.20V1-101[»]
2XG2X-ray3.20V1-101[»]
2XQEX-ray3.10V1-101[»]
2XTGelectron microscopy7.80V1-101[»]
2XUXelectron microscopy7.60V1-101[»]
2Y0VX-ray3.10V1-101[»]
2Y0XX-ray3.10V1-101[»]
2Y0ZX-ray3.10V1-101[»]
2Y11X-ray3.10V1-101[»]
2Y13X-ray3.10V1-101[»]
2Y15X-ray3.10V1-101[»]
2Y17X-ray3.10V1-101[»]
2Y19X-ray3.10V1-101[»]
3FINelectron microscopy6.40V1-101[»]
3HUXX-ray3.10V1-101[»]
3HUZX-ray3.10V1-101[»]
3I8FX-ray3.1021-101[»]
3I8IX-ray3.1021-101[»]
3I9CX-ray3.5021-101[»]
3I9EX-ray3.5021-101[»]
3KIRX-ray3.30V1-101[»]
3KITX-ray3.30V1-101[»]
3KIWX-ray3.60V1-101[»]
3KIYX-ray3.60V1-101[»]
3KNIX-ray3.00V1-101[»]
3KNKX-ray3.00V1-101[»]
3KNMX-ray3.45V1-101[»]
3KNOX-ray3.45V1-101[»]
3TVEX-ray3.1021-101[»]
3TVHX-ray3.1021-101[»]
3UXQX-ray3.20V1-101[»]
3UXRX-ray3.20V1-101[»]
3UYEX-ray3.0021-101[»]
3UYGX-ray3.0021-101[»]
3UZ1X-ray3.3021-101[»]
3UZ2X-ray3.3021-101[»]
3UZ8X-ray3.0021-101[»]
3UZ9X-ray3.0021-101[»]
3UZFX-ray3.3021-101[»]
3UZHX-ray3.3021-101[»]
3UZKX-ray3.3021-101[»]
3UZNX-ray3.3021-101[»]
3V23X-ray3.00V1-101[»]
3V25X-ray3.00V1-101[»]
3V27X-ray3.10V1-101[»]
3V29X-ray3.10V1-101[»]
3V2DX-ray2.70V1-101[»]
3V2FX-ray2.70V1-101[»]
3ZVPX-ray3.80V1-101[»]
4ABSX-ray3.10V1-101[»]
4DHAX-ray3.20V1-101[»]
4DHCX-ray3.20V1-101[»]
4G5LX-ray3.3021-101[»]
4G5NX-ray3.3021-101[»]
4G5UX-ray3.1021-101[»]
4G5WX-ray3.1021-101[»]
ProteinModelPortalP60492.
SMRP60492. Positions 1-101.
ModBaseSearch...

Protein-protein interaction databases

STRING300852.TTHA1783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71606; BAD71606; BAD71606.
GeneID3169471.
KEGGttj:TTHA1783.
PATRIC23958527. VBITheThe93045_1753.

Phylogenomic databases

eggNOGCOG0261.
HOGENOMHOG000036265.
KOK02888.
OMAKVTIIKF.
ProtClustDBPRK05573.

Family and domain databases

HAMAPMF_01363. Ribosomal_L21.
InterProIPR001787. Ribosomal_L21.
[Graphical view]
PANTHERPTHR21349. PTHR21349. 1 hit.
PfamPF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
TIGRFAMsTIGR00061. L21. 1 hit.
PROSITEPS01169. RIBOSOMAL_L21. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60492.

Entry information

Entry nameRL21_THET8
AccessionPrimary (citable) accession number: P60492
Secondary accession number(s): Q5SHE7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 29, 2005
Last modified: May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents