ID A0A3N4KMP6_9PEZI Unreviewed; 263 AA. AC A0A3N4KMP6; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 03-JUL-2019, entry version 5. 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}. 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 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000277580}. 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 //