ID U1GPS4_ENDPU Unreviewed; 581 AA.
AC U1GPS4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=EPUS_02010 {ECO:0000313|EMBL:ERF74323.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF74323.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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; KE720882; ERF74323.1; -; Genomic_DNA.
DR RefSeq; XP_007800033.1; XM_007801842.1.
DR AlphaFoldDB; U1GPS4; -.
DR GeneID; 19237064; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_4_0_1; -.
DR OMA; WTCRIKE; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000019373; 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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373}.
FT REGION 40..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 299..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 581 AA; 63898 MW; 298652446514177A CRC64;
MSTSIDPGRR TGIWSYIPFG SSSPRRRSVS LPYRANGDLS DPFDPFEKPN RHTPTSSGRH
SASPTLIENL QNAWMTQSQR SRYFKTGGVL VFILFVLSYV SKSWSGIPDV GSNIYNISNS
PTSKCTKPHD GSKPLVQYAL MIDAGSTGSR IHVYRFNNCG PTPELEDEVF KMTEKRQGGS
GLSSYAADAE GAARSLDPLM DTAMQSVPDE YKSCSPVAVK ATAGLRLLGE EMSTKILEAV
RQRLETKFPF PVVSREKDGV VIMKGEDEGV YAWITTNYLL GKIGGPDKTP TAAVFDLGGG
STQVVFQPTF KDAASGGMPE HLADGDHKYE LKFGGRDFTL YQHSHLGYGL MSARNAVHKR
VIDNMHESNK NSRGWLSSPI PNPCIAPGMS KTVNVTLSPD HDLGGWVQVT MEGPRDSIPA
QCRALAEGIL YKDAACNLAP CSFNGVHQPS LEKTFAREDV YIFSYFYDRT HPLGMPESFT
LRELHDLTAK VCGGEESWDA FAGLQGEDAP TVLEDLRGRP EWCLDLSFMG ALLHTGYEMP
IDREVKIAKK IKGNELGWCL GASLPLLEKQ SGWQCKIREV E
//
