ID   HNT2_YEAS1              Reviewed;         206 AA.
AC   B3LFZ1;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 60.
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=SCRG_00225;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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=EDV08020.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH408043; EDV08020.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B3LFZ1; -.
DR   SMR; B3LFZ1; -.
DR   PRIDE; B3LFZ1; -.
DR   EnsemblFungi; EDV08020; EDV08020; SCRG_00225.
DR   HOGENOM; CLU_056776_7_2_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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_0000392103"
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