PTH2_SCHPO
ID PTH2_SCHPO Reviewed; 205 AA.
AC O13830;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable peptidyl-tRNA hydrolase 2;
DE Short=PTH 2;
DE EC=3.1.1.29;
GN ORFNames=SPAC19A8.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC EC=3.1.1.29;
CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11650.1; -; Genomic_DNA.
DR PIR; T37947; T37947.
DR RefSeq; NP_593778.1; NM_001019207.2.
DR AlphaFoldDB; O13830; -.
DR SMR; O13830; -.
DR BioGRID; 278600; 4.
DR IntAct; O13830; 1.
DR STRING; 4896.SPAC19A8.14.1; -.
DR iPTMnet; O13830; -.
DR MaxQB; O13830; -.
DR PaxDb; O13830; -.
DR PRIDE; O13830; -.
DR EnsemblFungi; SPAC19A8.14.1; SPAC19A8.14.1:pep; SPAC19A8.14.
DR GeneID; 2542124; -.
DR KEGG; spo:SPAC19A8.14; -.
DR PomBase; SPAC19A8.14; -.
DR VEuPathDB; FungiDB:SPAC19A8.14; -.
DR eggNOG; KOG3282; Eukaryota.
DR HOGENOM; CLU_073661_0_0_1; -.
DR InParanoid; O13830; -.
DR OMA; PNSYDVK; -.
DR PhylomeDB; O13830; -.
DR PRO; PR:O13830; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; ISS:PomBase.
DR GO; GO:0032543; P:mitochondrial translation; ISO:PomBase.
DR CDD; cd02430; PTH2; 1.
DR Gene3D; 3.40.1490.10; -; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR002833; PTH2.
DR PANTHER; PTHR12649; PTHR12649; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; SSF102462; 1.
DR TIGRFAMs; TIGR00283; arch_pth2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..205
FT /note="Probable peptidyl-tRNA hydrolase 2"
FT /id="PRO_0000120285"
FT REGION 40..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 205 AA; 21429 MW; AC260A8D4CF11EE7 CRC64;
MKVPFVNFMI SSFPAAVLVG AVVGFMIGRK YSVADASRGY SSKNANKASN PEKESPVSVS
NDEDSESETE LLDMLKGNSS LAALALAEGQ TKMVLVVRTD LGMTKGKIAA QCAHAALACY
KIASAVDPDL VRIWENAGQA KITLQAQTEE TLELLQAQAM SLGLCARVIH DAGRTQIASG
SATVLGIGPG PVSVINEVTG SLKLF
