ID D4DIN8_TRIVH Unreviewed; 553 AA.
AC D4DIN8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=TRV_07048 {ECO:0000313|EMBL:EFE38271.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE38271.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE38271.1}.
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DR EMBL; ACYE01000408; EFE38271.1; -; Genomic_DNA.
DR RefSeq; XP_003018916.1; XM_003018870.1.
DR AlphaFoldDB; D4DIN8; -.
DR GeneID; 9582075; -.
DR KEGG; tve:TRV_07048; -.
DR HOGENOM; CLU_010246_4_0_1; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000008383; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 276..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 553 AA; 60481 MW; BF5FC1E4FA9E2B2F CRC64;
MSGASGGRSH RATSSTVDSD PSLHRRASSV SKPTDHGLDI ENIPPEPMKG SPTIAPMTQS
QRSRYLKTGG ILAFILFIIY VLAPSSRTPN LPPPGPDSAT KCTKPYDSSK PLIQYVLMID
AGSTGSRIHV YRFNNCGPTP ALENEEFKMT ETKEGGSGLS SYREDAEGAA KSLDPLMEVA
MKTVPEEYRS CSPIAVKATA GLRMLGKDMS DNILKAVRTR LETVYPFPVV SEAQGGVEIM
EGKDEGVYAW ITTNYLLGNI GSPEEIPTAA IFDLGGGSTQ IVFQPTYNGK GPDGLPEKMP
EGDHKYALKF GGREFILYQH SHLGYGLMAA RSAIHRYLIE TKHELSPNDK GWLKQKVVNP
CIVPGMSRNV SIDLGDNHAL GKEVEVLMVG PKESSAAQCR NLAEKILKKD ATCNLAPCSF
NGIHQPSLRK TFAKEDVFIF SYFYDRTSPL GMPDSFTLHD LHELTSIVCG GEDSWGVFQS
NSSAMKELSD RPEYCLDLNF MLALLHTGYE MPLQREVKTA KKIDGNELGW CLGASLPLLS
KNSGWECRIK QIS
//
