ID   HNT2_YEAS8              Reviewed;         206 AA.
AC   C8Z5L6;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Bis(5'-adenosyl)-triphosphatase;
DE            EC=3.6.1.29;
DE   AltName: Full=AP3A hydrolase;
DE            Short=AP3Aase;
DE   AltName: Full=Diadenosine 5',5'''-P1,P3-triphosphate hydrolase;
DE   AltName: Full=Dinucleosidetriphosphatase;
DE   AltName: Full=Hit family protein 2;
GN   Name=HNT2; Synonyms=APH1; ORFNames=EC1118_1D0_5886g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all
CC       dinucleoside polyphosphates, provided the phosphate chain contains at
CC       least 3 phosphates and that 1 of the 2 bases composing the nucleotide
CC       is a purine. Is most effective on dinucleoside triphosphates.
CC       Negatively regulates intracellular dinucleoside polyphosphate levels,
CC       which elevate following heat shock (By similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Mn(2+) is the preferred ion.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Mitochondrion {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAY78805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; FN393063; CAY78805.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C8Z5L6; -.
DR   SMR; C8Z5L6; -.
DR   EnsemblFungi; CAY78805; CAY78805; EC1118_1D0_5886g.
DR   HOGENOM; CLU_056776_7_2_1; -.
DR   Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D0.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
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; 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   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus.
FT   CHAIN           1..206
FT                   /note="Bis(5'-adenosyl)-triphosphatase"
FT                   /id="PRO_0000392107"
FT   DOMAIN          3..115
FT                   /note="HIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT   REGION          143..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           96..100
FT                   /note="Histidine triad motif"
FT   COMPBIAS        144..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        98
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  23542 MW;  4143F7371805B378 CRC64;
     MNKPIYFSKF LVTEQVFYKS KYTYALVNLK PIVPGHVLIV PLRTTVLNLS DLTMPESQDY
     FKTLQLIHRF IKWQYKADSI NVAIQDGPEA GQSVPHLHTH IIPRYKINNV GDLIYDKLDH
     WDGNGTLTDW QGRRDEYLGV GGRQARKNNS TSATVDGDEL SQGPNVLKPD SQRKVRALTE
     MKKEAEDLQA RLEEFVSSDP GLTQWL