ID F0XFD7_GROCL Unreviewed; 921 AA.
AC F0XFD7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Nucleoside diphosphatase {ECO:0000313|EMBL:EFX04595.1};
GN ORFNames=CMQ_1523 {ECO:0000313|EMBL:EFX04595.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX04595.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; GL629765; EFX04595.1; -; Genomic_DNA.
DR RefSeq; XP_014174077.1; XM_014318602.1.
DR AlphaFoldDB; F0XFD7; -.
DR STRING; 655863.F0XFD7; -.
DR GeneID; 25974411; -.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_3_0_1; -.
DR InParanoid; F0XFD7; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000007796; 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:UP000007796};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 756..774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..843
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 429..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 921 AA; 100856 MW; 61BCEBFC30FD3C26 CRC64;
MEAKRINATD AGRPVSSEHS LGQGEYRLTP SSSTSFVANH VDFRCPDADV RRKTEGTRRV
QWIVDIQRKA HEVYMQAAHS HTQLAKSRTR RLPIDGDEDE LGDEATNVGD LLDQLAACMV
SDRGQGQGMD WRQPGQLEAF LGKCLESWQA HGAILEIHAQ LQEHLQDSLR AIGCLKRHLK
QTEEDNELLR WYAVQLRDGA GTSGLTTPVS LASSSTTANI LQEAREAAAR AAAIQAADVA
ETAQVLFLMG KKWRYGVIID AGSSGSRVHV YRWIDHLRAT KDATTDELHS LPKIKTKWTK
KIRPGISTFG DKASTVGADH LKGLIDYALD VVPAEMVADT PIFLMATAGM RFLPQQQQNA
VLRESCAYLR QNTQFSLPDC TQNIQVISGE TEGLFGWIAA NYLLGGFDHP EQHAHGQDHH
TYGFLDMGGA SAQIAFAPNS TEAAQHADDL KLVRLRTLDG RLAEHRVFTA TWLGFGVNKA
RESYVAELVR QSSSAEGDIS DPCMPKGLQT TLEGPTLVGA GDFAGCLTAT KPLLAQDKTC
GDGSHPCLIH DSVPSIDFNV NHFIGVSEYY HSTHGFFGEK GDQAYDFSTY QHNVLEFCDQ
DWSQIQTDIE EKQKQKQSDT TRTLQDAQQA CFKASWVINV LHEGIGIPRV GLEKLPGINV
SHEALEGAKE QGFATPFRPV DKIDSVEVSW TLGRMLLYAA GQVQPYKGDG KEDLAVGFGS
NVQDDSTPAD FSYAGSTWER PQAGGSLADT TQKRSVSPGL VVFVLVVAVV VSLLRKKEKR
TRLSSWFGSW TRRPRGPGGR LLSSLAGKLF GQRQSRDYER VLEEGGMEQL ELGELEADES
EISDGSDGSG PGSGRSQLAR TSGLATPRIG VDGFEDVRMF SGLDRSGLVV RTESRERLVP
KSRAGSPTRL KSPMMAALHE D
//
