ID A0A371DUX9_9APHY Unreviewed; 762 AA.
AC A0A371DUX9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Nucleoside phosphatase GDA1/CD39 {ECO:0008006|Google:ProtNLM};
GN ORFNames=OH76DRAFT_1460067 {ECO:0000313|EMBL:RDX56346.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX56346.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX56346.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX56346.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; KZ857380; RDX56346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DUX9; -.
DR STRING; 139420.A0A371DUX9; -.
DR Proteomes; UP000256964; 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 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:UP000256964};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 562..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 645..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 196..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 762 AA; 83707 MW; 21B73653EF43680A CRC64;
MPPPTVVDPW FASRRFGVVI DAGSSGSRLQ IYSWKDARTV RLEQGADALR SLPQVGKGTE
NGEEWSVKVE PGLSTFGDDP DGIGPYLVPL LEHARTHIPP SLQPDTPLFL LATAGMRLLA
PEKQAEVLQT TCHFLKFHSN FKIDEPSAAG PCGSSVRIIT GEEEGLYGWV AVNYLMDGFK
GSDDTPLTYG FLDMGGASTQ IAFEPSREEQ ERAQNLIDVR LRRLDGHDIN HKVFVTTWLG
YGTNQARERY VGQLINEYEA NRTLSTGTEE QIDDPCLPKD LMLTNTPVQP DAASPHAKTP
HKFVGTGSWE QCLERTLPLL NKDTPCPDSH CLFNGVYVPP IDFNASHFIG VSEYWYSSEQ
SFGLGGPYDF VEYERAAAEF CAKDWTDILK GHEETRQKGH LGGDGEVEEG GVVVDTGKWG
LDVEIRRLQM QCFKAAWIVN VLHEGIGMPR IVDPEGNSTT SGEKVAAQAQ TKGLGRPSFQ
SMDSVGDIAI SWTLGKMVLE ASREVPAATA QARPIVDPLD DIPDISTSPV QPIRPPFIDF
DAFEDKISHH LPHSLTRHSL GFSPIAFAFY LLICAFCAAT LYRMRHRIRG TVRRFVNKRD
RSYLSEGFMM EEGLSLTGGA PASSPSRLSK FISPLTRLSS SLGLRASRPS PISVSREPSL
RSGQYSPARV SPLRSFSFPP QPKGQNGLTV QDEPNGTATS YVPSSPRLPD GSFMSNGSVS
SLQSRSRNSS HINLSSLAPR QTVSRTLTGM YHGQSASYRD EE
//