ID A0A177C657_9PLEO Unreviewed; 575 AA.
AC A0A177C657;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=CC84DRAFT_1097332 {ECO:0000313|EMBL:OAG03113.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03113.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG03113.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03113.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441555; OAG03113.1; -; Genomic_DNA.
DR RefSeq; XP_018033478.1; XM_018174708.1.
DR AlphaFoldDB; A0A177C657; -.
DR STRING; 1460663.A0A177C657; -.
DR GeneID; 28758194; -.
DR InParanoid; A0A177C657; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000077069; 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; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
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 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:UP000077069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 28..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 296..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 575 AA; 63147 MW; 0E4BAECBD5B8A9B7 CRC64;
MSSGVDVRRS RPGIWSYFPF SGPRRRISVS LPRSEPPSTA RDDPYEKPDR HARHRSTSMN
DFKTAATMNG GQRARYLKTG GFIAFVLLVL YFIAPSDGLA RAESFSKGQG QTAAPGSAAV
ACTKSYSKDK PLIQYALMID AGSTGSRIHA YKFNNCGPTP ELEQEFFKMT EKKEGGSGLS
SYDADAEGAA ASLDVLMDYA LESVPESYRA CSPIAVKATA GLRKLGEEKS NNTLKAVRKR
LETKYPFPVV SEAKGGVEVM PGEQEGVYAW ITTNYLLGKI GGPDKTPTAA VLDLGGGSTQ
IVFEPTFPKE PRGGLPNKLA DGDHKYELSF GGREFTLYQH SYLGYGLMEA RNNLHSAIVD
SIYQETKESG DREWLKKPII NPCIAPGMSR KVDVALPKDH ALGATVSVNM TGPATGAPAQ
CRGFAEKTLE KDAECKVAPC AFRGVHQPSI EKTFAREDVF LFSYFYDRTK PLGMPDSFSL
SELKDLTHRV CHGEQTWDAF QSVEGATKEL RGRPEWCLDL NFQLALLHTG YEMPIDREVK
IAKKIKGNEL GWCLGASLPL LEKESGWQCK IKQIQ
//
