ID U4LVQ0_PYROM Unreviewed; 195 AA.
AC U4LVQ0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN ORFNames=PCON_13592 {ECO:0000313|EMBL:CCX32741.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX32741.1};
RN [1] {ECO:0000313|EMBL:CCX32741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX32741.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX32741.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00464}.
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DR EMBL; HF935907; CCX32741.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LVQ0; -.
DR STRING; 1076935.U4LVQ0; -.
DR eggNOG; KOG3379; Eukaryota.
DR OMA; RTIKFGP; -.
DR OrthoDB; 1365844at2759; -.
DR Proteomes; UP000018144; 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}.
FT DOMAIN 8..118
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT REGION 157..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 108
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 195 AA; 21819 MW; 576DCE771B6977B8 CRC64;
MPPTTPIKAL TFSIFPITNQ VFYCTALSFA IVNLKPLLPG HVLVCPQRVV PRIHDLRPDE
ISDLFLAVQK VSRVLEKVYS AEGLNIAIQD GAVAGQSHRA DLPEDEIYRL LESDDADICR
AYRQHEGIDT PSTGMLAKGL AQSKIGADAN LLREQLHKKN KFPVPSGERQ PRTQEEMQKE
AEWLAEKMEE FGDVE
//
