ID   A0A2G4SGS2_RHIZD        Unreviewed;       798 AA.
AC   A0A2G4SGS2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Nucleoside phosphatase GDA1/CD39 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RHIMIDRAFT_270785 {ECO:0000313|EMBL:PHZ07967.1};
OS   Rhizopus microsporus ATCC 52813.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ07967.1, ECO:0000313|Proteomes:UP000242254};
RN   [1] {ECO:0000313|EMBL:PHZ07967.1, ECO:0000313|Proteomes:UP000242254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ07967.1,
RC   ECO:0000313|Proteomes:UP000242254};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ303869; PHZ07967.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4SGS2; -.
DR   STRING; 1340429.A0A2G4SGS2; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000242254; 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: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:UP000242254};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        538..561
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          700..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..798
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         206..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   798 AA;  89852 MW;  D2EA0747F6C6BFD1 CRC64;
     MSLDVKRPLV EDWKKNRKYG VIIDAGSSGS RVYIYSWKDH EHAKSAFTID ELKGKIPVVE
     RADYNGLKWT SREEPGISTY GSKPSEVGEH LDMLLNFAKE VVPEENQSST PIFLMATAGM
     RLLPQDQQEA LLKSTCDYIH TNSHFFMSNC EAHVRIISGE LEGVYGWVAV NYLMGGFDTS
     IKAYIDQQPK KPEEQHHTFG FLDMGGASAQ IAFEPEHHQK EEHRDDLTQV TLRTLDGRTV
     EYDVFVTTFL GYGSNEARRR YLEKRVEEVF AEVNGKEQQK HLLDEHHLLH LQDPCLPLNL
     NLTDSHSTSI PLYLHGTGDF NECIKYTEPL LNKDAACPTQ PCLFNGVHTP HIDWSVNKFV
     GISEYWYSTH DILGLGGVYD FTEYEEKATQ YCSKDWNAVI EEHKDVSQME LNRYQMQCFK
     SAWIVNVLHE GIQIPRINNP SGHLNLTEDE QLLEQVKQSV ESKNWHPLFQ SIDTINDIQV
     SWTLGAMLLH VANQIPLEDH HDGFLGHNTD DEDVHEIADG VGVTDGHRVE SVPEREKISA
     AVLGVIFFII LIAILFMFFV CKKMRKRRSF NLGASGGLLG SNNDLSTQKR FLSALTKSIS
     RATIMIRQWI NHHGQYTSVN TTDVSLDSLD EPSNTSEMVT ISIPATLGPS TKTPSVISKQ
     YWSKKRYSGD SHSTLFPHEH SIVEGGILPF RTTSALGLAN RNGSSSNLTA RTGSAPNLSG
     LMDRSPSPAD IQRSRSRLGF VIHEQSDEEE YVIHDGPVES GTAATLWLQQ QTGSRRGSPR
     GSPRGSLDER RKKKEDVS
//