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Database: UniProt
Entry: H1V7Z0_COLHI
LinkDB: H1V7Z0_COLHI
Original site: H1V7Z0_COLHI 
ID   H1V7Z0_COLHI            Unreviewed;       507 AA.
AC   H1V7Z0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE            EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN   ORFNames=CH063_01477 {ECO:0000313|EMBL:CCF36342.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF36342.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; CACQ02001935; CCF36342.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1V7Z0; -.
DR   STRING; 759273.H1V7Z0; -.
DR   EnsemblFungi; CCF36342; CCF36342; CH063_01477.
DR   VEuPathDB; FungiDB:CH63R_04368; -.
DR   eggNOG; KOG1385; Eukaryota.
DR   HOGENOM; CLU_010246_4_0_1; -.
DR   Proteomes; UP000007174; 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:0004382; F:GDP phosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0045134; F:UDP phosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0006486; P:protein glycosylation; IEA:EnsemblFungi.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         230..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   507 AA;  55458 MW;  28EA63CC37134922 CRC64;
     MSQAQKTRWM RTGAIAFFVV FLFWYLSPRG VNVYDGGVSR GGAGGQVPTD ASYGTEKCVQ
     SSSKSKPIVQ YVLMIDAGST GSRIHVYKFN NCGSTPELEH EEFKMTEKSV GGLSKYKDDP
     EAAAATLDVL MDVAMQNVPD KLKSCSPVAV KATAGLRMVG TENADKILAA VRNRLETKYP
     FPVVAKEQNG VAIMDGADEG VYAWITTNYL LGKIGGPDKS PTAAVFDLGG GSTQIVFEPT
     FKGAADGGMP EKLAEGDHKY DLAFGGQKFE LYQHSHLGYG LMSARKAVHK TLVQEIYESK
     KPDDSWVKQP IVHPCIAPGM VREVEVELDD NHPLGKTVTF NMTGPSQAAP AQCRNLAEKI
     LKKDEGCKLA PCSFNGIHQP SLAKTFSRED VYIFSYFYDR TKPLGMPDSF TLREMHDLAN
     SVCGGENSWD LFASIPGALK ELQGRPEHCL DLNFMMALLH TGYEMPIDRE VKIAKKIKGN
     ELGWCLGASL PLLSPNSGWK CRIDQVN
//
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