ID   DCTP1_HUMAN             Reviewed;         170 AA.
AC   Q9H773;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=dCTP pyrophosphatase 1 {ECO:0000305};
DE            EC=3.6.1.12 {ECO:0000269|PubMed:24467396};
DE   AltName: Full=Deoxycytidine-triphosphatase 1;
DE            Short=dCTPase 1;
DE   AltName: Full=RS21C6 {ECO:0000312|EMBL:AAK48422.1};
DE   AltName: Full=XTP3-transactivated gene A protein {ECO:0000312|EMBL:AAR26724.1};
GN   Name=DCTPP1 {ECO:0000312|HGNC:HGNC:28777};
GN   Synonyms=XTP3TPA {ECO:0000312|EMBL:AAR26724.1};
GN   ORFNames=CDA03 {ECO:0000312|EMBL:AAK14927.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang C., Cheng J., Lang Z., Wu Y., Yang Y., Zhang L., Ji D.;
RT   "Screening and cloning of the target genes transactivated by XTP3 using a
RT   suppression subtractive hybridization technique.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pheochromocytoma;
RA   Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT   "A novel gene expressed in human pheochromocytoma.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Zhang J., Chen W.F., Wang H.;
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-12 AND SER-85, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-85, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, MUTAGENESIS OF GLU-63, INDUCTION BY DCTP, SUBCELLULAR LOCATION,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=24467396; DOI=10.1042/bj20130894;
RA   Requena C.E., Perez-Moreno G., Ruiz-Perez L.M., Vidal A.E.,
RA   Gonzalez-Pacanowska D.;
RT   "The NTP pyrophosphatase DCTPP1 contributes to the homoeostasis and
RT   cleansing of the dNTP pool in human cells.";
RL   Biochem. J. 459:171-180(2014).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the
CC       corresponding nucleoside monophosphates. Has a strong preference for
CC       dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which
CC       it may even have a higher efficiency. May protect DNA or RNA against
CC       the incorporation of these genotoxic nucleotide analogs through their
CC       catabolism. {ECO:0000269|PubMed:24467396}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.12;
CC         Evidence={ECO:0000269|PubMed:24467396};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9QY93};
CC       Note=Probably binds two or three Mg(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:Q9QY93};
CC   -!- ACTIVITY REGULATION: Inhibited by the reaction end product PPi.
CC       Inhibited by dCDP. Inhibited by triptolide.
CC       {ECO:0000269|PubMed:24467396}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=47.6 uM for dCTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=65 uM for dTTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=79.3 uM for dATP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=75.9 uM for dUTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=16.8 uM for 5I-dCTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=36.5 uM for 5Br-dCTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=33.3 uM for 5me-dCTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=62.9 uM for 5hme-dCTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=9.2 uM for 5fo-dCTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC         KM=142.9 uM for CTP (at pH 8.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:24467396};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9QY93}.
CC   -!- INTERACTION:
CC       Q9H773; Q9H773: DCTPP1; NbExp=6; IntAct=EBI-723569, EBI-723569;
CC       Q9H773; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-723569, EBI-742054;
CC       Q9H773; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-723569, EBI-739832;
CC       Q9H773; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-723569, EBI-741158;
CC       Q9H773; P25786: PSMA1; NbExp=3; IntAct=EBI-723569, EBI-359352;
CC       Q9H773; O00560: SDCBP; NbExp=3; IntAct=EBI-723569, EBI-727004;
CC       Q9H773; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-723569, EBI-742688;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24467396}.
CC       Nucleus {ECO:0000269|PubMed:24467396}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:24467396}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases during mitosis (at protein
CC       level). {ECO:0000269|PubMed:24467396}.
CC   -!- INDUCTION: Up-regulated by an increase in cellular dCTP pool.
CC       {ECO:0000269|PubMed:24467396}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY453409; AAR26724.1; -; mRNA.
DR   EMBL; AF212242; AAK14927.1; -; mRNA.
DR   EMBL; AF210430; AAK48422.1; -; mRNA.
DR   EMBL; CR457335; CAG33616.1; -; mRNA.
DR   EMBL; AK024843; BAB15025.1; -; mRNA.
DR   EMBL; BC001344; AAH01344.1; -; mRNA.
DR   CCDS; CCDS10680.1; -.
DR   RefSeq; NP_077001.1; NM_024096.1.
DR   PDB; 7MU5; X-ray; 2.20 A; A/B/C/D/E/F/G/H=21-130.
DR   PDBsum; 7MU5; -.
DR   AlphaFoldDB; Q9H773; -.
DR   SMR; Q9H773; -.
DR   BioGRID; 122527; 66.
DR   IntAct; Q9H773; 27.
DR   MINT; Q9H773; -.
DR   STRING; 9606.ENSP00000322524; -.
DR   BindingDB; Q9H773; -.
DR   ChEMBL; CHEMBL3769292; -.
DR   GlyGen; Q9H773; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9H773; -.
DR   PhosphoSitePlus; Q9H773; -.
DR   SwissPalm; Q9H773; -.
DR   BioMuta; DCTPP1; -.
DR   DMDM; 74733624; -.
DR   EPD; Q9H773; -.
DR   jPOST; Q9H773; -.
DR   MassIVE; Q9H773; -.
DR   MaxQB; Q9H773; -.
DR   PaxDb; 9606-ENSP00000322524; -.
DR   PeptideAtlas; Q9H773; -.
DR   ProteomicsDB; 81085; -.
DR   Pumba; Q9H773; -.
DR   TopDownProteomics; Q9H773; -.
DR   Antibodypedia; 1233; 146 antibodies from 24 providers.
DR   DNASU; 79077; -.
DR   Ensembl; ENST00000319285.5; ENSP00000322524.4; ENSG00000179958.10.
DR   GeneID; 79077; -.
DR   KEGG; hsa:79077; -.
DR   MANE-Select; ENST00000319285.5; ENSP00000322524.4; NM_024096.2; NP_077001.1.
DR   UCSC; uc002dyf.4; human.
DR   AGR; HGNC:28777; -.
DR   CTD; 79077; -.
DR   DisGeNET; 79077; -.
DR   GeneCards; DCTPP1; -.
DR   HGNC; HGNC:28777; DCTPP1.
DR   HPA; ENSG00000179958; Low tissue specificity.
DR   MIM; 615840; gene.
DR   neXtProt; NX_Q9H773; -.
DR   OpenTargets; ENSG00000179958; -.
DR   PharmGKB; PA164718733; -.
DR   VEuPathDB; HostDB:ENSG00000179958; -.
DR   eggNOG; ENOG502S210; Eukaryota.
DR   GeneTree; ENSGT00390000017709; -.
DR   HOGENOM; CLU_110454_0_1_1; -.
DR   InParanoid; Q9H773; -.
DR   OMA; HFQWLTE; -.
DR   OrthoDB; 5485883at2759; -.
DR   PhylomeDB; Q9H773; -.
DR   TreeFam; TF300237; -.
DR   BRENDA; 3.6.1.12; 2681.
DR   PathwayCommons; Q9H773; -.
DR   Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR   SignaLink; Q9H773; -.
DR   SIGNOR; Q9H773; -.
DR   BioGRID-ORCS; 79077; 8 hits in 1162 CRISPR screens.
DR   ChiTaRS; DCTPP1; human.
DR   GeneWiki; XTP3-transactivated_gene_A_protein; -.
DR   GenomeRNAi; 79077; -.
DR   Pharos; Q9H773; Tchem.
DR   PRO; PR:Q9H773; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q9H773; Protein.
DR   Bgee; ENSG00000179958; Expressed in mucosa of transverse colon and 198 other cell types or tissues.
DR   ExpressionAtlas; Q9H773; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0047840; F:dCTP diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0032556; F:pyrimidine deoxyribonucleotide binding; IEA:Ensembl.
DR   GO; GO:0006253; P:dCTP catabolic process; IMP:UniProtKB.
DR   GO; GO:0042262; P:DNA protection; IMP:UniProtKB.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; IDA:UniProtKB.
DR   CDD; cd11537; NTP-PPase_RS21-C6_like; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   InterPro; IPR025984; DCTPP.
DR   PANTHER; PTHR46523; DCTP PYROPHOSPHATASE 1; 1.
DR   PANTHER; PTHR46523:SF1; DCTP PYROPHOSPHATASE 1; 1.
DR   Pfam; PF12643; MazG-like; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR   Genevisible; Q9H773; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..170
FT                   /note="dCTP pyrophosphatase 1"
FT                   /id="PRO_0000291769"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         47..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         63
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18691976"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163"
FT   MUTAGEN         63
FT                   /note="E->Q: Loss of dCTP diphosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:24467396"
FT   HELIX           31..45
FT                   /evidence="ECO:0007829|PDB:7MU5"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:7MU5"
FT   HELIX           53..71
FT                   /evidence="ECO:0007829|PDB:7MU5"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:7MU5"
FT   HELIX           86..109
FT                   /evidence="ECO:0007829|PDB:7MU5"
FT   HELIX           114..128
FT                   /evidence="ECO:0007829|PDB:7MU5"
SQ   SEQUENCE   170 AA;  18681 MW;  23BC932D5461320B CRC64;
     MSVAGGEIRG DTGGEDTAAP GRFSFSPEPT LEDIRRLHAE FAAERDWEQF HQPRNLLLAL
     VGEVGELAEL FQWKTDGEPG PQGWSPRERA ALQEELSDVL IYLVALAARC RVDLPLAVLS
     KMDINRRRYP AHLARSSSRK YTELPHGAIS EDQAVGPADI PCDSTGQTST
//