GenomeNet

Database: UniProt
Entry: D8Q936_SCHCM
LinkDB: D8Q936_SCHCM
Original site: D8Q936_SCHCM 
ID   D8Q936_SCHCM            Unreviewed;       546 AA.
AC   D8Q936;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE            EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN   ORFNames=SCHCODRAFT_57532 {ECO:0000313|EMBL:EFI95582.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFI95582.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL377308; EFI95582.1; -; Genomic_DNA.
DR   RefSeq; XP_003030485.1; XM_003030439.1.
DR   AlphaFoldDB; D8Q936; -.
DR   STRING; 578458.D8Q936; -.
DR   GeneID; 9588051; -.
DR   KEGG; scm:SCHCO_02632240; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02632240; -.
DR   eggNOG; KOG1385; Eukaryota.
DR   HOGENOM; CLU_010246_4_2_1; -.
DR   InParanoid; D8Q936; -.
DR   OMA; WTCRIKE; -.
DR   OrthoDB; 180318at2759; -.
DR   Proteomes; UP000007431; 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:UP000007431};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          57..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        244
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   546 AA;  60195 MW;  1D9DEEEEBF7BBF7D CRC64;
     MGPSRGARRG GAAWKKYAIG AAAVIGLIVL FGPRPSPRYL YSDDTDVDTV TDDPLFTDPA
     EPIVHNPVIE EEETTRPTRP SDEKPTLKPG EHPTSFETDP DPLHTTYCTT TTADRIVQYA
     LMIDAGSTGS RIHVYKFNNC NPNSGPSFEY EVFKMTQPGL SSFAGRPEEA AKSLDVLMDE
     AMRVVPESLR KCTPVAVKAT AGLRLLPGSQ SADILDAVRQ RLETAYPFPI HGEDGIVIMD
     GKDEGVYAWI TANYLLNTIR PDTPKDTPTF AVLDLGGAST QIVFEPKFPN GAEMADGDHK
     YELKFGGKDH VLYQHSYLGY GLMRARRHVH QLIEFMDSLR GKNGGGTFIE KDRRVSNPCL
     AQGTQRSVEV EDERNGVTRS VIMDGEGIGS FESCSRTMQL VMAKDAICEL KPCSFDGVYQ
     PSLLDAFSDG KVLLLSYFYD RIHPLIPEDK SKVTVSSIKD LASTVCMGRS AWLDRWGAQP
     DVMKELEDRP EWCLDLTFMH SLLTLGYEFT EERDVQLGKQ IEGTELGWCL GAALGVVSGA
     ELKCKA
//
DBGET integrated database retrieval system