ID A0A367YEM5_9ASCO Unreviewed; 186 AA.
AC A0A367YEM5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|ARBA:ARBA00014605, ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|ARBA:ARBA00012377, ECO:0000256|RuleBase:RU366076};
GN Name=HNT2_1 {ECO:0000313|EMBL:RCK64315.1};
GN ORFNames=Cantr_00325 {ECO:0000313|EMBL:RCK64315.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK64315.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK64315.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK64315.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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. {ECO:0000256|ARBA:ARBA00025241}.
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:RCK64315.1}.
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DR EMBL; QLNQ01000022; RCK64315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YEM5; -.
DR STRING; 5486.A0A367YEM5; -.
DR Proteomes; UP000253472; 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; HIT-like; 1.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR46243; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR46243:SF1; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF54197; HIT-like; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472}.
FT DOMAIN 4..116
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT COILED 121..148
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 97..101
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 99
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 116
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 186 AA; 21561 MW; E45F8666BFA2B261 CRC64;
MATTDIFFYK FLVTKQVFFR SRHTYALVNL KPLVPGHVLV VPLRTSILRF ADLTPEESID
YMNTLQLVHR FIKHIYHADA LNIAIQDGPE LGQSVPHLHT HIIPRCKTDG YGDSIYTKLE
VEDLESQYEE FFARKKAYQE KYEDLVDKEL AKSDSDRVPR NEETMEKEAN WLAQELEKFR
AAGGGL
//
