Reviewed, UniProtKB/Swiss-Prot O13830 (PTH2_SCHPO)

Names and origin

Protein names

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

Gene names

ORF Names:

SPAC19A8.14

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.
Sequence similarities	Belongs to the PTH2 family.

Ontologies

Keywords
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	aminoacyl-tRNA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 205	205	Probable peptidyl-tRNA hydrolase 2		PRO_0000120285
Amino acid modifications
	Modified residue	65	1	Phosphoserine Ref.2
	Modified residue	79	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O13830-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: AC260A8D4CF11EE7	FASTA	205	21,429
	10 20 30 40 50 60 MKVPFVNFMI SSFPAAVLVG AVVGFMIGRK YSVADASRGY SSKNANKASN PEKESPVSVS 70 80 90 100 110 120 NDEDSESETE LLDMLKGNSS LAALALAEGQ TKMVLVVRTD LGMTKGKIAA QCAHAALACY 130 140 150 160 170 180 KIASAVDPDL VRIWENAGQA KITLQAQTEE TLELLQAQAM SLGLCARVIH DAGRTQIASG 190 200 SATVLGIGPG PVSVINEVTG SLKLF

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-79, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB11650.1.
PIR	T37947.
RefSeq	NP_593778.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O13830.
Genome annotation databases
GeneID	2542124.
KEGG	spo:SPAC19A8.14.
NMPDR	fig|4896.1.peg.3748.
Organism-specific databases
GeneDB_Spombe	SPAC19A8.14.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001432-MON.
BRENDA	3.1.1.29. 653.
Gene expression databases
ArrayExpress	O13830.
Family and domain databases
InterPro	IPR002833. Pep_tRNA_hydro_PTH2. [Graphical view]
Pfam	PF01981. PTH2. 1 hit. [Graphical view]
ProDom	PD010667. UPF0099. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00283. Pep_tRNA_hydro_PTH2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PTH2_SCHPO

Accession

Primary (citable) accession number: O13830

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	September 1, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)