NTPPA_SCHPO
ID NTPPA_SCHPO Reviewed; 241 AA.
AC O14141;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000250|UniProtKB:Q99210};
DE Short=dTTPase/UTPase {ECO:0000250|UniProtKB:Q99210};
DE EC=3.6.1.9 {ECO:0000250|UniProtKB:Q99210};
DE AltName: Full=Maf-like protein C3G6.03c;
DE AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000250|UniProtKB:Q99210};
DE AltName: Full=Nucleotide pyrophosphatase {ECO:0000250|UniProtKB:Q99210};
DE Short=Nucleotide PPase {ECO:0000250|UniProtKB:Q99210};
GN ORFNames=SPAC3G6.03c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP 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: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP
CC and UTP. May have a dual role in cell division arrest and in preventing
CC the incorporation of modified nucleotides into cellular nucleic acids.
CC {ECO:0000250|UniProtKB:Q99210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q99210};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q99210};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q99210};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB16279.2; -; Genomic_DNA.
DR PIR; T38722; T38722.
DR RefSeq; NP_594969.2; NM_001020400.2.
DR AlphaFoldDB; O14141; -.
DR SMR; O14141; -.
DR BioGRID; 279638; 6.
DR STRING; 4896.SPAC3G6.03c.1; -.
DR iPTMnet; O14141; -.
DR MaxQB; O14141; -.
DR PaxDb; O14141; -.
DR PRIDE; O14141; -.
DR EnsemblFungi; SPAC3G6.03c.1; SPAC3G6.03c.1:pep; SPAC3G6.03c.
DR GeneID; 2543209; -.
DR KEGG; spo:SPAC3G6.03c; -.
DR PomBase; SPAC3G6.03c; -.
DR VEuPathDB; FungiDB:SPAC3G6.03c; -.
DR eggNOG; KOG1509; Eukaryota.
DR HOGENOM; CLU_040416_0_2_1; -.
DR InParanoid; O14141; -.
DR OMA; RIDGDFY; -.
DR PRO; PR:O14141; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR GO; GO:1990748; P:cellular detoxification; ISM:PomBase.
DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; ISM:PomBase.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00555; Maf; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_00528; Maf; 1.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR003697; Maf-like.
DR PANTHER; PTHR43213; PTHR43213; 1.
DR Pfam; PF02545; Maf; 1.
DR PIRSF; PIRSF006305; Maf; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00172; maf; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleotide metabolism; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..241
FT /note="dTTP/UTP pyrophosphatase"
FT /id="PRO_0000123090"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99210"
FT SITE 40
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q99210"
FT SITE 106
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q99210"
FT SITE 199
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q99210"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 241 AA; 26895 MW; D12582F829B6D8C6 CRC64;
MSNEKMDTSP PSYDSHFTLE TSMHRQLKDK RIILASGSPR RKQLFEQMGF PNVETCVSGF
PEDLNKSMYI TPWEYAADTS VQKAIAVYEK LAAEEDSPDI VVSADTILIL DSEIMEKPND
PKHHLAMLKK LRNSKTPHKV FTAVSVIVPM EVPIHPGYVM KTHLEETQVK FDPSITDEFL
EAYVRCGEGS DKAGGYAIQG HGALLIESII GDFSNVVGLP IRATFKLMEE ALEQGDADNY
D
