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Protein

Peptidyl-tRNA hydrolase 2

Gene

PTH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.By similarity2 Publications

Catalytic activityi

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.

GO - Molecular functioni

  • aminoacyl-tRNA hydrolase activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciYEAST:G3O-28955-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-tRNA hydrolase 2 (EC:3.1.1.29)
Short name:
PTH 2
Gene namesi
Name:PTH2
Ordered Locus Names:YBL057C
ORF Names:YBL0510, YBL0514
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL057C.
SGDiS000000153. PTH2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 208208Peptidyl-tRNA hydrolase 2PRO_0000120284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki152 – 152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP34222.
PeptideAtlasiP34222.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DSK2P4851011EBI-2345448,EBI-6174
RAD23P326285EBI-2345448,EBI-14668

Protein-protein interaction databases

BioGridi32642. 40 interactions.
IntActiP34222. 3 interactions.
MINTiMINT-2732035.

Structurei

3D structure databases

ProteinModelPortaliP34222.
SMRiP34222. Positions 86-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PTH2 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000015991.
HOGENOMiHOG000227349.
InParanoidiP34222.
KOiK04794.
OMAiLCARTIR.
OrthoDBiEOG7G7M1K.

Family and domain databases

Gene3Di3.40.1490.10. 1 hit.
InterProiIPR023476. Pep_tRNA_hydro_II_dom.
IPR002833. PTH2.
[Graphical view]
PfamiPF01981. PTH2. 1 hit.
[Graphical view]
SUPFAMiSSF102462. SSF102462. 1 hit.
TIGRFAMsiTIGR00283. arch_pth2. 1 hit.

Sequencei

Sequence statusi: Complete.

P34222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKMTVSSNY TIALWATFTA ISFAVGYQLG TSNASSTKKS SATLLRSKEM
60 70 80 90 100
KEGKLHNDTD EEESESEDES DEDEDIESTS LNDIPGEVRM ALVIRQDLGM
110 120 130 140 150
TKGKIAAQCC HAALSCFRHI ATNPARASYN PIMTQRWLNA GQAKITLKCP
160 170 180 190 200
DKFTMDELYA KAISLGVNAA VIHDAGRTQI AAGSATVLGL GPAPKAVLDQ

ITGDLKLY
Length:208
Mass (Da):22,435
Last modified:July 27, 2011 - v2
Checksum:iA77F3A5BAC578943
GO

Sequence cautioni

The sequence AAT92782.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA80790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA84877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23261 Genomic DNA. Translation: CAA80790.1. Different initiation.
Z35818 Genomic DNA. Translation: CAA84877.1. Different initiation.
AY692763 Genomic DNA. Translation: AAT92782.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07063.2.
PIRiS39831.
RefSeqiNP_009496.2. NM_001178297.2.

Genome annotation databases

EnsemblFungiiYBL057C; YBL057C; YBL057C.
GeneIDi852223.
KEGGisce:YBL057C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23261 Genomic DNA. Translation: CAA80790.1. Different initiation.
Z35818 Genomic DNA. Translation: CAA84877.1. Different initiation.
AY692763 Genomic DNA. Translation: AAT92782.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07063.2.
PIRiS39831.
RefSeqiNP_009496.2. NM_001178297.2.

3D structure databases

ProteinModelPortaliP34222.
SMRiP34222. Positions 86-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32642. 40 interactions.
IntActiP34222. 3 interactions.
MINTiMINT-2732035.

Proteomic databases

MaxQBiP34222.
PeptideAtlasiP34222.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL057C; YBL057C; YBL057C.
GeneIDi852223.
KEGGisce:YBL057C.

Organism-specific databases

EuPathDBiFungiDB:YBL057C.
SGDiS000000153. PTH2.

Phylogenomic databases

GeneTreeiENSGT00390000015991.
HOGENOMiHOG000227349.
InParanoidiP34222.
KOiK04794.
OMAiLCARTIR.
OrthoDBiEOG7G7M1K.

Enzyme and pathway databases

BioCyciYEAST:G3O-28955-MONOMER.

Miscellaneous databases

PROiP34222.

Family and domain databases

Gene3Di3.40.1490.10. 1 hit.
InterProiIPR023476. Pep_tRNA_hydro_II_dom.
IPR002833. PTH2.
[Graphical view]
PfamiPF01981. PTH2. 1 hit.
[Graphical view]
SUPFAMiSSF102462. SSF102462. 1 hit.
TIGRFAMsiTIGR00283. arch_pth2. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and functional analysis of a 32,560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes."
    Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.
    Yeast 9:1355-1371(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase are nonessential in yeast."
    Rosas-Sandoval G., Ambrogelly A., Rinehart J., Wei D., Cruz-Vera L.R., Graham D.E., Stetter K.O., Guarneros G., Soell D.
    Proc. Natl. Acad. Sci. U.S.A. 99:16707-16712(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: FUNCTION.
  8. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
    Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-152.
  9. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPTH2_YEAST
AccessioniPrimary (citable) accession number: P34222
Secondary accession number(s): D6VPU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2190 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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 one 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.