ID A0A3B3Q5V9_9TELE Unreviewed; 497 AA.
AC A0A3B3Q5V9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 8 {ECO:0000256|ARBA:ARBA00039598};
DE EC=3.6.1.5 {ECO:0000256|ARBA:ARBA00012148};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000001543.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000001543.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000211};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR AlphaFoldDB; A0A3B3Q5V9; -.
DR STRING; 1676925.ENSPKIP00000001543; -.
DR Ensembl; ENSPKIT00000025464.1; ENSPKIP00000001543.1; ENSPKIG00000019801.1.
DR GeneTree; ENSGT01100000263542; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF31; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 8; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 209..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 497 AA; 54671 MW; 3D31047091C3DB17 CRC64;
MGKLPARHAV LGILMSMVLG ATIIALILMV VQNQTVDRPL GPKYGIVIDA GSTHTALFLY
RWPAGKENNT AIVSQVGLCD VDGPGISSYG LDPPRAGQSL VKCLRDLKQA IPAGQWGATP
VYLGATAGMR LLKLQNATQA DEVMKEVSKA IQRYPFDFRG ARILSGVAEG AYGWITINYL
LEGFVKFSFQ GKWLHPVGNN ILGALDMGGA STQITFVPAG PVQDPQTAAD FRLYGFNYRV
YTHSYLCYGK EQAMKQLQVQ LHTVNFSQNI SHPCYHTGFR LNLTLGDLYN SPCVKKPTSF
DPAANVTFYG SSDPEKCSQL VQRLFNFSGC TFSPSCSFNG IYQPPVNGNF FAFSAYFYTF
NFLGLVPQAS LSRVNSTIDS FCRRNWTSVK TAYPSEKDKY LQDYCGSAVY MKALLLDGFN
FTQNWNSISF QKKAGDADIG WTLGYMLNLT NLIPSEPLAP VTGVEHGQWA AGIFFIVFVM
ILSILVLFIL SVRNTAN
//
