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Database: UniProt
Entry: F7VWV0_SORMK
LinkDB: F7VWV0_SORMK
Original site: F7VWV0_SORMK 
ID   F7VWV0_SORMK            Unreviewed;       554 AA.
AC   F7VWV0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE            EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN   ORFNames=SMAC_02571 {ECO:0000313|EMBL:CCC09991.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC09991.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC09991.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC09991.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC09991.1}.
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DR   EMBL; CABT02000011; CCC09991.1; -; Genomic_DNA.
DR   RefSeq; XP_003352136.1; XM_003352088.1.
DR   AlphaFoldDB; F7VWV0; -.
DR   STRING; 771870.F7VWV0; -.
DR   GeneID; 10809755; -.
DR   KEGG; smp:SMAC_02571; -.
DR   VEuPathDB; FungiDB:SMAC_02571; -.
DR   eggNOG; KOG1385; Eukaryota.
DR   HOGENOM; CLU_010246_4_0_1; -.
DR   InParanoid; F7VWV0; -.
DR   OMA; WTCRIKE; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000001881; 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:UP000001881};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        53..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        246
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         277..281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   554 AA;  60974 MW;  F341A3F0D7C28B58 CRC64;
     MRRTSVSLPT KHVAHDPHEK PDRYRRDQHN QEPASVFIRM QNAWMSQSQK ARYLKTGAIV
     FAVLFLFYLF SPSGVEIPGG APQNNNQGQV PSDSSYGTDR CTRSFSKEKP IVQYVSMIDA
     GSTGSRIHVY KFNNCGPAPE LEGEVLFKMT AKIEGQSSGL SAYKDDPLAA ATSLDPLMQA
     ALEVIPDKLK ACSPVAVKAT AGLRLIGPEK SQKILDAVRE HLENEYPFPV VSKEENGVAM
     MDGADEGVYA WITVNYLLGK IGGPDHSPTA AVFDLGGGST QIVFEPTFEG LSGGGMPQKL
     ADGDHKYELD FGGRKFDLYQ HSHLGYGLMS ARDAIFATLV NDLFELNKQD KSWMQKPVIN
     PCFSTGMTKA VKVPLGDNHP LGPKVELNMT GPSTPAPALC RSLAERILEK DAECKLAPCS
     FNGVHQPQIA KTFAREDIFL LSYFTDRTQP LGMPESFTLR EMHDLAAQVC GGEQSWDIFT
     SVPGALEEIS DRPEHCMDLN FMLALTHTGY EMPIDREVRI AKKIKDNELG WCLGASLPLL
     SQSSGWKCKI KEIH
//
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