ID A0A364N0M5_9PLEO Unreviewed; 770 AA.
AC A0A364N0M5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=DDE83_005873 {ECO:0000313|EMBL:RAR08669.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR08669.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: After transfer of sugars to endogenous macromolecular
CC acceptors, the enzyme converts nucleoside diphosphates to nucleoside
CC monophosphates which in turn exit the Golgi lumen in a coupled
CC antiporter reaction, allowing entry of additional nucleotide sugar from
CC the cytosol. {ECO:0000256|ARBA:ARBA00037742}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}.
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:RAR08669.1}.
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DR EMBL; QGDH01000084; RAR08669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364N0M5; -.
DR STRING; 183478.A0A364N0M5; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF83; NTPASE, ISOFORM F; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR SUPFAM; SSF47473; EF-hand; 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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 493..497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 770 AA; 84409 MW; 2026C6396A80BE57 CRC64;
MAVHASPPKR RGPPARAPVK RPSKLAKENG LTAEQEAEIR EAFGLFAVPH PDHEDSKEGV
LKKADVRRCL ISLNLTPEKS EMSSILSTID PLNTGFVEFV PFISYAAIAI HSKDHGSDDD
DDEDEYREES NAEEVSAAYQ LFTHGAAGPI TLAHLRRVAK ELREDVPDDV LKDMILEANG
GVKGQGRDVG GVSLEDFESV MKRAGLSFGF SGPRRRVSVS LPRNFDPNRA AADDDDPHQK
AARHTRHRSS YSDAFMNESK GGAVMNQGQR LRYLKTGGVI AFILLVLYFV APRDSIPRPG
AVSHPSGGNT AAGDAKAECT KSYSKDKPLI QYALMIDAGS TGSRIHVYKF NNCGPSPELE
NEDFEMTPKR EGGSGLSAYG DDPEAAARSL DVLLDVALKN VPKEYQSCTP IAVKATAGLR
KLGEQKSNDI LAAVRRHLEN DYPFPLVSEE KKGVEVMPGE MEGVYAWITV NYLLGKIGGP
DKNPTAAVLD LGGGSTQIIF EPTFPDTPRG GLPTKLAEGD HKYMLNFGNR DFDLYQHSYL
GYGLMEARNN LHSTILAGLH ETNKDNREYL KKPIVNPCIA PGMSREVEVQ MPKGHELGES
VTVNMTGPST ASPTQCRGLA EKTLHKDDEC AIAPCAFKGV HQPPFAQTFA TEDVYLLSYF
YDRTQDLGMP ESFTLRELQD LANKVCTGEK GWDSFSAVPN ALDELKGRPE WCLDLNFQFE
LLRSGYGMPI DREVKIAKKI KGNELGWCLG ASLPLLEANS GWQCKIKQVQ
//
