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Database: UniProt
Entry: I3J4V0_ORENI
LinkDB: I3J4V0_ORENI
Original site: I3J4V0_ORENI 
ID   I3J4V0_ORENI            Unreviewed;       149 AA.
AC   I3J4V0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   08-NOV-2023, entry version 51.
DE   RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE            EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN   Name=fhit {ECO:0000313|Ensembl:ENSONIP00000003890.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000003890.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000003890.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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};
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DR   RefSeq; XP_003446525.1; XM_003446477.3.
DR   RefSeq; XP_019214078.1; XM_019358533.1.
DR   AlphaFoldDB; I3J4V0; -.
DR   Ensembl; ENSONIT00000003891.2; ENSONIP00000003890.2; ENSONIG00000003104.2.
DR   GeneID; 100702722; -.
DR   KEGG; onl:100702722; -.
DR   CTD; 2272; -.
DR   GeneTree; ENSGT00510000047967; -.
DR   InParanoid; I3J4V0; -.
DR   OMA; HSYGFVN; -.
DR   OrthoDB; 1365844at2759; -.
DR   Proteomes; UP000005207; Linkage group LG5.
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; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   PANTHER; PTHR46981; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   PANTHER; PTHR46981:SF1; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR   Pfam; PF01230; HIT; 1.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS00892; HIT_1; 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:UP000005207}.
FT   DOMAIN          1..110
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   REGION          117..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           95..99
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        97
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         90..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            115
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   149 AA;  16928 MW;  E259B1B88A91321A CRC64;
     MATLRFGQHL IKLSAVFLQT ELSFALVNRK PVVPGHVLVC PLRPVERFRD LRPDELADLF
     STTQRVANLV EKHFSATSIT IAIQDGPEAG QTVKHVHVHV LPRKAGDFQH NDSIYDELQN
     HDQEDKDIPS KWRSEEEMAA EASDLRKQL
//
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