ID G0R9R9_HYPJQ Unreviewed; 201 AA.
AC G0R9R9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|RuleBase:RU366076};
GN ORFNames=TRIREDRAFT_2358 {ECO:0000313|EMBL:EGR52002.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR52002.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR52002.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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 EMBL; GL985057; EGR52002.1; -; Genomic_DNA.
DR RefSeq; XP_006961949.1; XM_006961887.1.
DR AlphaFoldDB; G0R9R9; -.
DR STRING; 431241.G0R9R9; -.
DR EnsemblFungi; EGR52002; EGR52002; TRIREDRAFT_2358.
DR GeneID; 18484292; -.
DR KEGG; tre:TRIREDRAFT_2358; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_2358; -.
DR eggNOG; KOG3379; Eukaryota.
DR HOGENOM; CLU_056776_7_0_1; -.
DR OrthoDB; 1365844at2759; -.
DR Proteomes; UP000008984; 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:UP000008984}.
FT DOMAIN 9..123
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT REGION 148..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..112
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT COMPBIAS 151..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
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 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 130
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 201 AA; 21982 MW; 47B1B454DD45715B CRC64;
MTSTNTEGMT IKFGPFEVTK QVFLTTPHSY GLVNLKPLLP GHILICPLKP HARLLDLSPA
ETADLFATVQ LAQKLLARLY FPDPSDPTSG SFTVALQDGA EAGQTIPHVH VHVIPRVKGD
MGEEPMDEIY VHLSSEKANV GGALWDREQA QRPRPGGKMP RIEDAERNAK TMEEMVEEAE
RYKAALGEMG VGNSARGGER L
//
