ID ITPA_DICDI Reviewed; 194 AA. AC Q54LQ6; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 28-JUN-2011, entry version 45. DE RecName: Full=Probable inosine triphosphate pyrophosphatase; DE Short=ITPase; DE Short=Inosine triphosphatase; DE EC=3.6.1.19; GN Name=itpa; ORFNames=DDB_G0286495; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Hydrolyzes ITP and dITP to their respective CC monophosphate derivatives (By similarity). CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. 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; AAFI02000086; EAL64198.1; -; Genomic_DNA. DR RefSeq; XP_637700.1; XM_632608.1. DR HSSP; Q9BY32; 2CAR. DR ProteinModelPortal; Q54LQ6; -. DR SMR; Q54LQ6; 3-185. DR STRING; Q54LQ6; -. DR EnsemblProtists; DDB0238062; DDB0238062; DDB_G0286495. DR GeneID; 8625642; -. DR GenomeReviews; CM000153_GR; itpa. DR KEGG; ddi:DDB_G0286495; -. DR dictyBase; DDB_G0286495; itpa. DR eggNOG; KOG3222; -. DR GeneTree; EPrGT00050000006107; -. DR HOGENOM; HBG697237; -. DR OMA; GPYAEYV; -. DR PhylomeDB; Q54LQ6; -. DR ProtClustDB; CLSZ2515582; -. DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase. DR GO; GO:0005634; C:nucleus; ISS:dictyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:dictyBase. DR GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; ISS:dictyBase. DR InterPro; IPR002637; Ham1p-like. DR PANTHER; PTHR11067; Ham1p_like; 1. DR Pfam; PF01725; Ham1p_like; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding. FT CHAIN 1 194 Probable inosine triphosphate FT pyrophosphatase. FT /FTId=PRO_0000328399. FT REGION 11 16 Substrate binding (By similarity). FT REGION 67 68 Substrate binding (By similarity). FT METAL 39 39 Magnesium (By similarity). FT METAL 67 67 Magnesium (By similarity). FT BINDING 146 146 Substrate (By similarity). FT BINDING 166 166 Substrate (By similarity). FT BINDING 172 172 Substrate (By similarity). SQ SEQUENCE 194 AA; 21730 MW; B8A4AB1217C26D0E CRC64; MSISKKIVFV TGNAKKLEEA LQILGTSFPI ESKKVDLPEL QGDPIDISIE KCKIAAREVG GPVLVEDTCL CFNALKGLPG PYVKWFLDKL EPEGLYKLLD AWEDKSAYAL CNFAFSEGPD SEPIVFAGKT DGIIVQPRGP RNFGWDPVFQ PDGYKETYAE MDKSIKNTIS HRTRSLQKVK EFLKSKGYEN CKFE //