ID   A0A1G4MIA2_LACFM        Unreviewed;       656 AA.
AC   A0A1G4MIA2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=LAFE_0G11276g1_1 {ECO:0000313|EMBL:SCW03475.1};
GN   ORFNames=LAFE_0G11276G {ECO:0000313|EMBL:SCW03475.1};
OS   Lachancea fermentati (Zygosaccharomyces fermentati).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW03475.1, ECO:0000313|Proteomes:UP000190831};
RN   [1] {ECO:0000313|EMBL:SCW03475.1, ECO:0000313|Proteomes:UP000190831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6772 {ECO:0000313|EMBL:SCW03475.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
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DR   EMBL; LT598486; SCW03475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4MIA2; -.
DR   STRING; 4955.A0A1G4MIA2; -.
DR   OMA; WHDALFD; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000190831; Chromosome g.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        513..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          599..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         188..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   656 AA;  74564 MW;  F2E4EB45C3957F07 CRC64;
     MHIEDIEDKK SDQYGVIIDA GSSGSRVYVY RWQDPSFTLK EGSDKELKSV PQIYLNKDWT
     TKTSPGLSSF EKQPEKAFKK HVKPLLEYAE KLIPKEKVRE TPVFIQATAG MRLLPKKRRE
     KILKNVCADM QHSTNFLIKD CELQVQIIDG ETEGLYGWTG LNYLLGNFNE YDVSQDFHPS
     YGFMDMGGAS AQIAFVPSNI DEIKTHDDDI STITLKSING DTQNWRVFVS TWLGFGANQA
     RMRYLAQLIN ALPENTNEYD DDDFSTLELT DPCMLRGSRN TFKFKDKEFQ VSGSGNYEHC
     LKSIYPLLLK DLPCMEEPCL FNGVHAPQID FNKDKFVGTS EFWYTANDVF KIGGEYNFNE
     FSQKVKEFCE AEWDVVKDRN EKGMYNNIPT QILLESCFKA NWVLNVLHEG FDMPRVGIEL
     PAEEHNDDAD EYIPVAAAFQ SADSINGQEL SWTLGRIVLY SSSLIESDDK DHKVGILPSD
     NEINSFEKSF IPGSIGTIDE LSTSIGSVKS SPAHSLLIVG VLIFLWILVI KLRCGKRSLP
     LSVGVLFTHA KSKFSKFKYS RAPRDTLADL EEGFSRRGTY ESDDREGFQF RSRSMMNLND
     SKSSHEEEYP LDERSKSATS SPSINQSAKL RTAFSLADFS KFTNPRDKER KNKPFI
//