ID A0A1I7XR52_HETBA Unreviewed; 477 AA.
AC A0A1I7XR52;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000313|WBParaSite:Hba_20280};
OS Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC Heterorhabditis.
OX NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_20280};
RN [1] {ECO:0000313|WBParaSite:Hba_20280}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR AlphaFoldDB; A0A1I7XR52; -.
DR WBParaSite; Hba_20280; Hba_20280; Hba_20280.
DR Proteomes; UP000095283; Unplaced.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd01275; FHIT; 1.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR PANTHER; PTHR23088:SF27; DEAMINATED GLUTATHIONE AMIDASE; 1.
DR PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR Pfam; PF00795; CN_hydrolase; 2.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 20..296
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT DOMAIN 329..437
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT MOTIF 422..426
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 424
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 417..420
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 426
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 443
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 477 AA; 54283 MW; F71B797C603BAFB9 CRC64;
MLSSIGVALR KAMSSSAYKR SLIAVCQLTS DNDIKGNFET CKEMIERASE RKCKMVFFPE
CFDFIGRDKD EQITLAMDEN GDYIERYRAL ARQHGLWLSL GGMHHKDMTD PLKPWNTHLI
IDCEGNTRAE YKKLHLFDLE IPGKVRLLES EFSKAGTKMV HPVDTPIGRL GLSICYDLRF
AELSLWNRNK GAQVLSFPSA FTLNTGLAHW EYYIVVTIHL EYSHTLNIIV SLFISTFKKV
FFLTLLRTRA IETQSQTGKH NEKRISYGHA MVVDPWGAVI AQCSERIGMC FAEIDLQYVD
ELRAMQPVFS HRRHDLYTLH VNECDLDDSV LMFSEFPIAS ECIFYRSALS FAFVNLKPVL
NGHVLISPKR PALRLTDLTD AETADLFIVA KKVQKMLEKV HGATSSTICV QDGPAAGQTV
KHVHIHILVR RSGDFGPTPD NLYSDLAAHD RNPEICPRTH EEMSTEAYIY REAIRNM
//
