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Database: UniProt
Entry: A0A0G2FTQ0_9PEZI
LinkDB: A0A0G2FTQ0_9PEZI
Original site: A0A0G2FTQ0_9PEZI 
ID   A0A0G2FTQ0_9PEZI        Unreviewed;       249 AA.
AC   A0A0G2FTQ0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE            EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN   ORFNames=UCDDA912_g02431 {ECO:0000313|EMBL:KKY37542.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY37542.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY37542.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY37542.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY37542.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY37542.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-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:KKY37542.1}.
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DR   EMBL; LCUC01000082; KKY37542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FTQ0; -.
DR   STRING; 1214573.A0A0G2FTQ0; -.
DR   OrthoDB; 1365844at2759; -.
DR   Proteomes; UP000034680; 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; IPR019808; Histidine_triad_CS.
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; 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:UP000034680}.
FT   DOMAIN          26..157
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           142..146
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT   COMPBIAS        14..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        144
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         137..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            167
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   249 AA;  27627 MW;  9AB9F3533CDEF2F0 CRC64;
     MSSGPPAKKI SFGPFEVTSQ NRTEQNRTEP LLTQKPKVFL TTPHSFALVN LKPLLPGHVL
     VCPSRPHKRL TDLSLPEVTD LFATVQRVQR MLARHYFAHP GHHLHHHHHQ QQHQDPAPAP
     APGGSFNIAV QDGPEAGQTV AHVHVHVIPR VRGLSSKPED TAGDELYERM AREEGNVGGA
     LWDRRQQQQR QSGSARPVAG GAFDRIEDSQ REARSMEEMV AEADVFRRAF REMEEEEEEG
     AGPVGGEAS
//
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