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Q5SM01 (Q5SM01_THET8) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesSubmitted name:
Peptide chain release factor 2 EMBL BAD69965.1
Gene names
Ordered Locus Names:TTHA0142 EMBL BAD69965.1
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP] EMBL BAD69965.1
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA By similarity.

Subcellular location

Cytoplasm By similarity SAAS SAAS004374.

Sequences

Sequence LengthMass (Da)Tools
Q5SM01 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 55B4AC9C891AEEB7

FASTA37842,734
        10         20         30         40         50         60 
MRLASQSAIL VKVWTWNASR NAWKASGGIF DIPQKETRLK ELERRLEDPS LWNDPEAARK 

        70         80         90        100        110        120 
VSQEAARLRR TVDTFRSLES DLQGLLELME ELPAEEREAL KPELEEAAKK LDELYHQTLL 

       130        140        150        160        170        180 
NFPHAEKNAI LTIQPGAGGT EACDWAEMLL RMYTRFAERQ GFQVEVVDLT PGPEAGIDYA 

       190        200        210        220        230        240 
QILVKGENAY GLLSPEAGVH RLVRPSPFDA SGRRHTSFAG VEVIPEVDEE VEVVLKPEEL 

       250        260        270        280        290        300 
RIDVMRASGP GGQGVNTTDS AVRVVHLPTG ITVTCQTTRS QIKNKELALK ILKARLYELE 

       310        320        330        340        350        360 
RKKREEELKA LRGEVRPIEW GSQIRSYVLD KNYVKDHRTG LMRHDPENVL DGDLMDLIWA 

       370 
GLEWKAGRRQ GTEEVEAE

« 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]"Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon."
Petry S., Brodersen D.E., Murphy F.V., Dunham C.M., Selmer M., Tarry M.J., Kelley A.C., Ramakrishnan V.
Cell 123:1255-1266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (6.76 ANGSTROMS) OF 31-378.
[3]"Release factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies."
Zoldak G., Redecke L., Svergun D.I., Konarev P.V., Voertler C.S., Dobbek H., Sedlak E., Sprinzl M.
Nucleic Acids Res. 35:1343-1353(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 27-378.
[4]"Insights into translational termination from the structure of RF2 bound to the ribosome."
Weixlbaumer A., Jin H., Neubauer C., Voorhees R.M., Petry S., Kelley A.C., Ramakrishnan V.
Science 322:953-956(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 31-369.
[5]"Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release."
Jin H., Kelley A.C., Loakes D., Ramakrishnan V.
Proc. Natl. Acad. Sci. U.S.A. 107:8593-8598(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 31-369.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008226 Genomic DNA. Translation: BAD69965.1.
RefSeqYP_143408.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B9MX-ray6.76Y31-378[»]
2IHRX-ray2.50127-378[»]
2WH1X-ray3.45Y31-369[»]
2WH3X-ray3.45Y31-369[»]
2X9RX-ray3.10Y31-369[»]
2X9TX-ray3.10Y31-369[»]
ProteinModelPortalQ5SM01.
SMRQ5SM01. Positions 27-369.
ModBaseSearch...

Protein-protein interaction databases

STRING300852.TTHA0142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD69965; BAD69965; BAD69965.
GeneID3168831.
KEGGttj:TTHA0142.
PATRIC23955223. VBITheThe93045_0140.

Phylogenomic databases

eggNOGCOG1186.
HOGENOMHOG000074814.
KOK02836.
OMAITGRYAY.
ProtClustDBCLSK445704.

Family and domain databases

Gene3D3.30.160.20. 1 hit.
InterProIPR014720. dsRNA-bd-like_dom.
IPR005139. PCRF.
IPR000352. Pep_chain_release_fac_I_II.
IPR004374. PrfB.
[Graphical view]
PANTHERPTHR11075:SF6. PTHR11075:SF6. 1 hit.
PfamPF03462. PCRF. 1 hit.
PF00472. RF-1. 1 hit.
[Graphical view]
SMARTSM00937. PCRF. 1 hit.
[Graphical view]
TIGRFAMsTIGR00020. prfB. 1 hit.
PROSITEPS00745. RF_PROK_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5SM01.

Entry information

Entry nameQ5SM01_THET8
AccessionPrimary (citable) accession number: Q5SM01
Entry history
Integrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info