ID A0A093JGC4_STRCA Unreviewed; 484 AA.
AC A0A093JGC4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 8 {ECO:0000313|EMBL:KFV77849.1};
DE Flags: Fragment;
GN ORFNames=N308_04810 {ECO:0000313|EMBL:KFV77849.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV77849.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV77849.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV77849.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; KL205999; KFV77849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093JGC4; -.
DR STRING; 441894.ENSSCUP00000001368; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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:SF117; 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 Hydrolase {ECO:0000256|RuleBase:RU003833, ECO:0000313|EMBL:KFV77849.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..484
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001885123"
FT TRANSMEM 460..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 198..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV77849.1"
FT NON_TER 484
FT /evidence="ECO:0000313|EMBL:KFV77849.1"
SQ SEQUENCE 484 AA; 53599 MW; E6EFAFC85C94EA38 CRC64;
AVLGALAMLS IIALVLSLVK IKDVTLPPMV KYGMVFDAGS SHTSLFIYEW DSDKENNTGV
VSQTLSCDVQ GQGISSYASD PPKAGESLRE CLDKALKVIP PMKQREVSTY LGATAGMRLL
REQNSSAADQ VLAEIAKTMQ EYPVDFHGAR IITGEEEGAY GWITINYLLD SFTKYSPKEH
LWVRPEAANI LGALDLGGAS TQISFIPKGS VIKWNETSKF TLYGYNYNIY THSYLCYGQN
EVLKRLAKEL IVVRGKLGVE HPCYPKNYNE IISLSSFGTS PCTSQNDLHL TLADRNVTLE
GSGNASRCLA AIKKLFNFSA CGQSQDCTFN GVYQPPVSGQ FFAFSAFYYN FRFLNLTNGQ
PLATVRETIQ NFCTRSWEDL SSSYPKDKPE RLRSYCANAN YILTLLLDAY KFNETSWNSI
IFQMKAGSTD IGWTLGYMLN LTNMIPAEAP EHVKGHDPSL WAAAIAFIVL TLALGLVALL
MCLW
//
