ID   A0A3N4KMP6_9PEZI        Unreviewed;       263 AA.
AC   A0A3N4KMP6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   05-JUN-2019, entry version 4.
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.,
RA   Dockter R.B., Fauchery L., Guy J., Iotti M., Le Tacon F.,
RA   Lindquist E.A., Lipzen A., Malagnac F., Mello A., Molinier V.,
RA   Miyauchi S., Poulain J., Riccioni C., Rubini A., Sitrit Y.,
RA   Splivallo R., Traeger S., Wang M., Zifcakova L., Wipf D.,
RA   Zambonelli A., Paolocci F., Nowrousian M., Ottonello S., Baldrian P.,
RA   Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M., Wincker P.,
RA   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
CC       distinguish between the deoxy- and ribose forms. Probably excludes
CC       non-canonical purines from RNA and DNA precursor pools, thus
CC       preventing their incorporation into RNA and DNA and avoiding
CC       chromosomal lesions. {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;
CC         EC=3.6.1.9; Evidence={ECO:0000256|HAMAP-Rule:MF_03148,
CC         ECO:0000256|SAAS:SAAS01117280};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03148};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03148};
CC       Note=Binds 1 divalent metal cation per subunit; can use either
CC       Mg(2+) 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}.
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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   Complete proteome {ECO:0000313|Proteomes:UP000277580};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|SAAS:SAAS00721512};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148,
KW   ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00721541};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03148,
KW   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};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03148}.
FT   REGION       10     15       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   REGION       67     68       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   REGION      142    145       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   REGION      168    169       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03148}.
FT   REGION      182    224       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A3N4KMP6}.
FT   METAL        39     39       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_03148}.
FT   METAL        67     67       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_03148}.
FT   BINDING      51     51       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03148}.
FT   BINDING     163    163       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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
//