ID A0A162X8F1_DIDRA Unreviewed; 721 AA.
AC A0A162X8F1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Apyrase {ECO:0000313|EMBL:UPX18752.1};
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:KZM19399.1};
GN ORFNames=EKO05_0009043 {ECO:0000313|EMBL:UPX18752.1}, EKO05_007685
GN {ECO:0000313|EMBL:KAF9705386.1}, ST47_g9450
GN {ECO:0000313|EMBL:KZM19399.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM19399.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM19399.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM19399.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9705386.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9705386.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9705386.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9705386.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9705386.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9705386.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX18752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX18752.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) 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; RYYQ01000015; KAF9705386.1; -; Genomic_DNA.
DR EMBL; JYNV01000292; KZM19399.1; -; Genomic_DNA.
DR EMBL; CP095303; UPX18752.1; -; Genomic_DNA.
DR STRING; 5454.A0A162X8F1; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 16.
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, ECO:0000313|EMBL:KZM19399.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 531..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 271..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 182..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 721 AA; 79724 MW; 567DDCF84C086881 CRC64;
MGKWRYGVVL DAGSSGTRVH VYRWLNSDAA RKGATDAQLH ALPVVETDRK WTKKIHPGIS
TFGTHPHDVG PNHLDKLLRH ALKHIPAADV PDTPLFLLAT AGMRILPPVQ RKEVLNEVCD
YARKHTALQL PDCALHVQVI PGETEGLYGW IAANYLLGGF DRPQSHDHGK GHSTYGFLDM
GGASAQMAFA PNATEADRHA NDLTLLRLRT LDGTPLEYKV FVTTWLGFGV NQARQRYVQA
LLDSTSSKEL PDPCLPAGLD VDVTKEGRFL EIDSGDDADD DDDSDDSDEP AAKLHGTGNF
QECLHQTFPL LEKEKECLDE PCLLNGQHVP AIDFDVNHFV GVSEYWHTTH DIFEDKHKDK
AYDFKTYQER VSDFCNQDWK HIQKGIDKGK WGKKVDEDKA REVCFKASWI INMLHDGIGV
PRVGIEPLPD SKNTTKAVLD EAKAKGFLDP FQAVNKINDV EVSWTLGKMV LYAASEVPPP
DSKALAVGFG SNEAGIPEDF QYPGGSYLPW NHDPLDDDNW HRLFVEYPSR IPALLVMIVI
VLLIFSIILG KEKRSVVRQY AASLFKKKPG KTHTPLKGKR RGFLPSKLFG LGGSGSGSHQ
TYERVDAGED GLSHNDFELE ETYLDSSDDD RHFSDDSEAS RVGRTSGWAT PQIQTSEPLT
AGYFGAAGQP DLVSAGQGLG LGPLNAIERG GLLARTDSRE RIRSRASSPK RGRSKMGNLD
E
//
