ID R4X812_TAPDE Unreviewed; 625 AA.
AC R4X812;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Putative Nucleoside diphosphatase {ECO:0000313|EMBL:CCG81584.1};
GN ORFNames=TAPDE_001230 {ECO:0000313|EMBL:CCG81584.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG81584.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG81584.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCG81584.1}.
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DR EMBL; CAHR02000046; CCG81584.1; -; Genomic_DNA.
DR AlphaFoldDB; R4X812; -.
DR STRING; 1097556.R4X812; -.
DR VEuPathDB; FungiDB:TAPDE_001230; -.
DR eggNOG; KOG1386; Eukaryota.
DR Proteomes; UP000013776; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
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:SF121; NUCLEOSIDE-DIPHOSPHATASE MIG-23; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000013776};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 515..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 599..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 195..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 625 AA; 69027 MW; 0E0267EC29870099 CRC64;
MTSFASRAPI NEWSTNRKYA VIIDAGSSGS RIQVYSWRDH SLAASFANQT ELSSLPRIEK
GVESGEDWMM KVHPGVSSFA DDPSEIGEKH LKELYAYALK IVPADQVKET PVYLLATAGM
RLLTEDQQED ILEEACEYTQ DHTDFLLPEC ESHFQVITGE TEGLYGWIAI NYLLGGFDAK
TDGNHHTYGF LDMGGASAQI AFVPNKTEAA AHKEDLTLLR LRTLEGETKE WQVFVSTWLG
FGANEARRRY LESLAKGKVD QISGHFLDPC KPKGLVETVA STKDKKVISA EGSGNLNECL
TRLEPLLSKN APCPDPPCLF AGVHVPSIDF DINHFIGISE YYYSTQDVFG LGGAYDYHTL
SNAVENYCSR EWVDILQDLA DGQYPSGVEQ KKLEEVCFKA SWMMNVLHDG IGIPRVTKEF
STDSSSHNGT EELREGARIK GFDGAFNSAE SLAGTEVSWT LGKMVLYSSS SVESSNAEPV
GFGPNSVDHT MFQIAGELES NYQRPGLAHR VHQNGASALV LCLCIIALLL YIIKGPRKAS
LMAGMSYFWH KNQRKIIGAR GDQSYERVME EGDAEEERQF QMGQLGRSSL TRSAVFSNGL
ARSSSQLRLS RSSKDGSDDE GVKRS
//
