ID A0A0W0C789_CANGB Unreviewed; 190 AA. AC A0A0W0C789; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 12-AUG-2020, entry version 18. DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076}; DE EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076}; GN ORFNames=AO440_001656 {ECO:0000313|EMBL:KTB07688.1}; OS Candida glabrata (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces; OC Nakaseomyces/Candida clade. OX NCBI_TaxID=5478 {ECO:0000313|EMBL:KTB07688.1, ECO:0000313|Proteomes:UP000054886}; RN [1] {ECO:0000313|EMBL:KTB07688.1, ECO:0000313|Proteomes:UP000054886} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=910700640 {ECO:0000313|EMBL:KTB07688.1}; RA Haavelsrud O.E., Gaustad P.; RT "Draft genomes sequences of Candida glabrata isolates 1A, 1B, 2A, 2B, 3A RT and 3B."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2 CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; CC EC=3.6.1.29; Evidence={ECO:0000256|ARBA:ARBA00001475, CC ECO:0000256|RuleBase:RU366076}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936, CC ECO:0000256|RuleBase:RU366076}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KTB07688.1}. 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; LLZZ01000107; KTB07688.1; -; Genomic_DNA. DR EnsemblFungi; KTA95434; KTA95434; AO439_001735. DR EnsemblFungi; KTB07309; KTB07309; AO441_001552. DR EnsemblFungi; KTB07688; KTB07688; AO440_001656. DR EnsemblFungi; KTB21311; KTB21311; AO438_001740. DR Proteomes; UP000054886; Unassembled WGS sequence. DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR CDD; cd01275; FHIT; 1. DR Gene3D; 3.30.428.10; -; 1. DR InterPro; IPR039383; FHIT. DR InterPro; IPR019808; Histidine_triad_CS. DR InterPro; IPR001310; Histidine_triad_HIT. DR InterPro; IPR011146; HIT-like. DR InterPro; IPR036265; HIT-like_sf. DR Pfam; PF01230; HIT; 1. DR SUPFAM; SSF54197; SSF54197; 1. DR PROSITE; PS00892; HIT_1; 1. DR PROSITE; PS51084; HIT_2; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|RuleBase:RU366076}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU366076}. FT DOMAIN 5..117 FT /note="HIT" FT /evidence="ECO:0000259|PROSITE:PS51084" FT COILED 156..176 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 98..102 FT /note="Histidine triad motif" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464" SQ SEQUENCE 190 AA; 22284 MW; 6123A27F85AD2162 CRC64; MSGSTPIYFS KFLVTEQVFF RTRFSYALVN LKPITKGHVL VVPLRSQVVQ LSQLTPQENA DYFNTVQLIH QFMKWVYKAQ AVNIAIQDGP EAGQSVPHLH THIIPRYKEN NIGDKVYEHL DEWDLRRDEY MKARDMNEEG TNLRPDQDDV RIARSMEEMK KEVDFLKAQL EEFLSNHCDV KKWLATDARQ //