ID A0A0L8HK24_OCTBM Unreviewed; 189 AA. AC A0A0L8HK24; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 20-JAN-2016, entry version 3. 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=3.6.1.19 {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}; GN ORFNames=OCBIM_22012863mg {ECO:0000313|EMBL:KOF89577.1}; OS Octopus bimaculoides (California two-spotted octopus). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Cephalopoda; Coleoidea; OC Neocoleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; OC Octopus. OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF89577.1}; RN [1] {ECO:0000313|EMBL:KOF89577.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF89577.1}; RC TISSUE=Gonad {ECO:0000313|EMBL:KOF89577.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. 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: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_03148, CC ECO:0000256|SAAS:SAAS00338620}. 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:SAAS00338610}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {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 --------------------------------------------------------------------------- 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; KQ417945; KOF89577.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. 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, KW ECO:0000256|SAAS:SAAS00003694}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00003705}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00003693}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_03148}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00003698}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00003692}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148, KW ECO:0000256|SAAS:SAAS00003702}. FT REGION 8 13 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT REGION 66 67 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT REGION 143 146 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT REGION 171 172 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03148}. FT METAL 38 38 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_03148}. FT METAL 66 66 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_03148}. FT BINDING 50 50 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03148}. FT BINDING 166 166 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03148}. SQ SEQUENCE 189 AA; 21073 MW; F2A738AA39269B1C CRC64; MTTITFVTGN ANKLKEFIQI LGKNFPYKLI NENIDIPEYQ GESDDISRAK CLEAAKIVKG PVVVEDTSLC FNALGGLPGP YIKWFLDKLK PEGLHHLLHG FEDKSAYALC TLAFSTGNLE TPVLLFKGQT DGKIVEPSGP NDFGWDPCFQ PDGFDQTYAE MPKELKNSLS HRGKAVMAFK EHFMNKTLK //