ID A0A1V6TKT0_9EURO Unreviewed; 709 AA.
AC A0A1V6TKT0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Golgi apyrase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENFLA_c006G01121 {ECO:0000313|EMBL:OQE26881.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE26881.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE26881.1}.
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DR EMBL; MLQL01000006; OQE26881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TKT0; -.
DR STRING; 254877.A0A1V6TKT0; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000191342; 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:UP000191342};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 517..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 597..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..709
FT /note="Polar 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 709 AA; 78504 MW; 66687717D24BD87E CRC64;
MGKWRYGVVL DAGSSGTRVH VYRWLRNSAA RKHADVEELK SLPEIKTKEE WTKKIHPGVS
SFANRPELVG SDHLAQLLDH AKGIIPSEDA KDTPIFLLAT AGMRLLGNFE RQLLLDRICS
YARENSEFLL PDCGVHIQVI PGVTEGLYGW IATNYLMGSF DAPEKHDHGK GHNTYGFLDM
GGASAQIAFA PNVTETEKHA EDLKLLRLRN IDGSVQEHRV FVTSWLEFGV HEARRRYLEA
LHTAIGPGIK EMPDPCLPSG LRTTLDGKVA SSETETYLLG TGKFDECLRQ TFPLLDKDAP
CADEPCLLNG IHVPAIDFDV NHFIGISEYW HTTHEIFEMG YKDKAYDFNT YQERVQTFCS
QDWDSIEQGL GQHKWGKKVD RQKAYEVCFK ASWIINMLHD GIGVPRVGLE STTGSSHNGT
KEVLAHGKEK GYLDAFQAVN KIDSTEVSWT LGKIVLYASS QVPLEIEEGL PVGFGSNVPD
IPADFQYPSV QLLPDSDSFH SEHWHDALFD GDSPRRIPGF VLFMFIVAMV GFFLCGRSRR
SRIFNRVSNV LRRGGPSHPN HPKKRKGLKS MLPFISRSVP SYERVLEDGA QDYELGAIES
DESEDGGRLS EADSARLGPP KRASSWGSNS NTPSFKYALD NSSTGTIGLG ISGGSGIAMD
RAGLVVRTES RDHLAPIALG PTTNGRRSRA GSPTRSHQKS PSMTPLTDE
//
