ID   A0A3N4KMP6_9PEZI        Unreviewed;       263 AA.
AC   A0A3N4KMP6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   11-DEC-2019, entry version 7.
DE   RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            Short=ITPase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            Short=Inosine triphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE   AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE            Short=NTPase {ECO:0000256|HAMAP-Rule:MF_03148};
GN   ORFNames=P167DRAFT_536424 {ECO:0000313|EMBL:RPB11770.1};
OS   Morchella conica CCBAS932.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Morchellaceae; Morchella.
OX   NCBI_TaxID=1392247 {ECO:0000313|EMBL:RPB11770.1, ECO:0000313|Proteomes:UP000277580};
RN   [1] {ECO:0000313|EMBL:RPB11770.1, ECO:0000313|Proteomes:UP000277580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAS932 {ECO:0000313|EMBL:RPB11770.1,
RC   ECO:0000313|Proteomes:UP000277580};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
CC   -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC       nucleotides such as inosine triphosphate (ITP), deoxyinosine
CC       triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their
CC       respective monophosphate derivatives. The enzyme does not distinguish
CC       between the deoxy- and ribose forms. Probably excludes non-canonical
CC       purines from RNA and DNA precursor pools, thus preventing their
CC       incorporation into RNA and DNA and avoiding chromosomal lesions.
CC       {ECO:0000256|HAMAP-Rule:MF_03148}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC         deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC         Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03148,
CC         ECO:0000256|SAAS:SAAS01117280};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03148,
CC         ECO:0000256|SAAS:SAAS01117281};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC       Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC       or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_03148};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148,
CC       ECO:0000256|SAAS:SAAS00721538}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03148}.
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_03148, ECO:0000256|RuleBase:RU003781,
CC       ECO:0000256|SAAS:SAAS00721539}.
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; ML119133; RPB11770.1; -; Genomic_DNA.
DR   Proteomes; UP000277580; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00515; HAM1; 1.
DR   Gene3D; 3.90.950.10; -; 1.
DR   HAMAP; MF_03148; HAM1_NTPase; 1.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR027502; ITPase.
DR   InterPro; IPR029001; ITPase-like_fam.
DR   PANTHER; PTHR11067; PTHR11067; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   SUPFAM; SSF52972; SSF52972; 1.
DR   TIGRFAMs; TIGR00042; TIGR00042; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148, ECO:0000256|SAAS:SAAS00721512};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148, ECO:0000256|RuleBase:RU003781,
KW   ECO:0000256|SAAS:SAAS00721541};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03148, ECO:0000256|SAAS:SAAS00721547};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_03148};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721543};
KW   Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721522};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721527}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03148};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277580}.
FT   REGION          10..15
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT   REGION          67..68
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT   REGION          142..145
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT   REGION          168..169
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT   REGION          182..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           39
FT                   /note="Magnesium or manganese"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT   METAL           67
FT                   /note="Magnesium or manganese"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT   BINDING         51
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT   BINDING         163
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
SQ   SEQUENCE   263 AA;  28241 MW;  B21226B320C20897 CRC64;
     MSSRTLFFVT SNPGKLAEAK AILSASGVNL ESKNVEITEI QGTIEEITRD KAKRAAEQIG
     GPVIVEDTCL CFDALKGLPG PYVKHFLKEI GTRGLTNMLA AYDDKTAQAV CTFAYCEPGS
     EPILFEGRTK GKVVRARGEG SFGWDPIFEY EGSTYAEMDS YQKNKISHRF KALQKLTAWL
     EEKHGGGSGG SGGSAPPPAA PKPVDRRNMG GHDTSSDGGS FFDGFGEEVK SRAINIAGDG
     MGIRKAAGRE WQFDSPDGGR GKY
//