Reviewed, UniProtKB/Swiss-Prot P34222 (PTH2_YEAST)

Names and origin

Protein names

Recommended name:
    Peptidyl-tRNA hydrolase 2
      Short name=PTH 2
    EC=3.1.1.29

Gene names

Name:	PTH2
Ordered Locus Names:	YBL057C
ORF Names:	YBL0510, YBL0514

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	214 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis By similarity. Ref.4 Ref.6
Catalytic activity	N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 2190 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the PTH2 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: SGD translation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial outer membrane Inferred from direct assay. Source: SGD
Molecular function	aminoacyl-tRNA hydrolase activity Ref.4 Ref.6 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 214	214	Peptidyl-tRNA hydrolase 2		PRO_0000120284
Amino acid modifications
	Cross-link	158		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P34222-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: C8F4F099E7497436	FASTA	214	23,128
	10 20 30 40 50 60 MITSFLMEKM TVSSNYTIAL WATFTAISFA VGYQLGTSNA SSTKKSSATL LRSKEMKEGK 70 80 90 100 110 120 LHNDTDEEES ESEDESDEDE DIESTSLNDI PGEVRMALVI RQDLGMTKGK IAAQCCHAAL 130 140 150 160 170 180 SCFRHIATNP ARASYNPIMT QRWLNAGQAK ITLKCPDKFT MDELYAKAIS LGVNAAVIHD 190 200 210 AGRTQIAAGS ATVLGLGPAP KAVLDQITGD LKLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8154187] [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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 12475929] [Abstract] Cited for: FUNCTION.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Peptidyl-tRNA hydrolase from Sulfolobus solfataricus." Fromant M., Ferri-Fioni M.-L., Plateau P., Blanquet S. Nucleic Acids Res. 31:3227-3235(2003) [PubMed: 12799450] [Abstract] Cited for: FUNCTION.
[7]	"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: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-158, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z23261 Genomic DNA. Translation: CAA80790.1. Z35818 Genomic DNA. Translation: CAA84877.1. AY692763 Genomic DNA. Translation: AAT92782.1.
PIR	S39831.
RefSeq	NP_009496.1.
3D structure databases
SMR	P34222. Positions 92-214.
ModBase	Search...
Protein-protein interaction databases
IntAct	P34222. 1 interaction.
STRING	P34222.
Proteomic databases
PeptideAtlas	P34222.
Genome annotation databases
Ensembl	YBL057C; YBL057C; YBL057C; Saccharomyces cerevisiae. [Genome view]
GeneID	852223.
KEGG	sce:YBL057C.
NMPDR	fig|4932.3.peg.186.
Organism-specific databases
CYGD	YBL057c.
SGD	S000000153. PTH2.
Phylogenomic databases
eggNOG	fuNOG09818.
HOGENOM	HBG526257.
OMA	RMALVIR.
OrthoDB	EOG980KD5.
PhylomeDB	P34222.
Enzyme and pathway databases
BRENDA	3.1.1.29. 250.
Gene expression databases
ArrayExpress	P34222.
Genevestigator	P34222.
GermOnline	YBL057C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002833. Pep_tRNA_hydro_PTH2. [Graphical view]
Pfam	PF01981. PTH2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00283. Pep_tRNA_hydro_PTH2. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	970745.

Entry information

Entry name

PTH2_YEAST

Accession

Primary (citable) accession number: P34222

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	February 9, 2010
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)