P34222 (PTH2_YEAST) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	208 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.5 Ref.7
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.6
Sequence similarities	Belongs to the PTH2 family.
Sequence caution	The sequence AAT92782.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA80790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA84877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: SGD
Cellular component	mitochondrial outer membrane Inferred from direct assay. Source: SGD
Molecular function	aminoacyl-tRNA hydrolase activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 208	208	Peptidyl-tRNA hydrolase 2		PRO_0000120284
Amino acid modifications
	Cross-link	152		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P34222 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: A77F3A5BAC578943	FASTA	208	22,435
	10 20 30 40 50 60 MEKMTVSSNY TIALWATFTA ISFAVGYQLG TSNASSTKKS SATLLRSKEM KEGKLHNDTD 70 80 90 100 110 120 EEESESEDES DEDEDIESTS LNDIPGEVRM ALVIRQDLGM TKGKIAAQCC HAALSCFRHI 130 140 150 160 170 180 ATNPARASYN PIMTQRWLNA GQAKITLKCP DKFTMDELYA KAISLGVNAA VIHDAGRTQI 190 200 AAGSATVLGL GPAPKAVLDQ ITGDLKLY

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]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[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: 12475929] [Abstract] Cited for: FUNCTION.
[6]	"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].
[7]	"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.
[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: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-152, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S39831.
RefSeq	NP_009496.2. NM_001178297.2.
3D structure databases
ProteinModelPortal	P34222.
SMR	P34222. Positions 86-208.
ModBase	Search...
Protein-protein interaction databases
IntAct	P34222. 1 interaction.
MINT	MINT-2732035.
STRING	P34222.
Proteomic databases
PeptideAtlas	P34222.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	852223.
KEGG	sce:YBL057C.
NMPDR	fig|4932.3.peg.186.
Organism-specific databases
CYGD	YBL057c.
SGD	S000000153. PTH2.
Phylogenomic databases
eggNOG	fuNOG09818.
GeneTree	EFGT00050000005903.
HOGENOM	HBG526257.
OMA	CARVIQD.
OrthoDB	EOG49GPRW.
Gene expression databases
ArrayExpress	P34222.
Genevestigator	P34222.
GermOnline	YBL057C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR023476. Pep_tRNA_hydro_II_dom. IPR002833. Pep_tRNA_hydro_PTH2. [Graphical view]
Gene3D	G3DSA:3.40.1490.10. G3DSA:3.40.1490.10. 1 hit.
KO	K04794.
Pfam	PF01981. PTH2. 1 hit. [Graphical view]
SUPFAM	SSF102462. SSF102462. 1 hit.
TIGRFAMs	TIGR00283. Arch_pth2. 1 hit.
ProtoNet	Search...
Other
NextBio	970745.

Entry information

Entry name

PTH2_YEAST

Accession

Primary (citable) accession number: P34222
Secondary accession number(s): D6VPU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program