ID A0A0F8V7Z0_9EURO Unreviewed; 171 AA.
AC A0A0F8V7Z0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN ORFNames=ARAM_006628 {ECO:0000313|EMBL:KKK19101.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK19101.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK19101.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK19101.1};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-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|RuleBase:RU366076};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={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:KKK19101.1}.
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DR EMBL; JZBS01002342; KKK19101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8V7Z0; -.
DR STRING; 308745.A0A0F8V7Z0; -.
DR OrthoDB; 1365844at2759; -.
DR Proteomes; UP000034291; 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 Hydrolase {ECO:0000256|RuleBase:RU366076};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366076};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT DOMAIN 8..116
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT MOTIF 101..105
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 103
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 96..99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 121
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 171 AA; 18923 MW; 40E7D9814C85A9E0 CRC64;
MALPLKGSPI HFGPFLVTSQ VVFHLTPLSF ALVNLKPILP GHVLVSPRRI VARLADLTPS
ETADLFLTVR RVGRMIERVY GATSLNVAVQ DGVDAGQSVP HVHAHIIPRR RADLPRTDAV
YDALDGREGD VMRNFRGALR VDELGRKARE MREMEEEACR LAGEMEGEPL D
//
