ID A0A194UTZ3_9PEZI Unreviewed; 683 AA.
AC A0A194UTZ3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Golgi apyrase {ECO:0000313|EMBL:KUI55170.1};
GN ORFNames=VP1G_02548 {ECO:0000313|EMBL:KUI55170.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI55170.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; KN714678; KUI55170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UTZ3; -.
DR STRING; 694573.A0A194UTZ3; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000078576; 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:UP000078576};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 516..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 592..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 183..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 683 AA; 75569 MW; CA976D60CBC9EAF8 CRC64;
MGKKWRYGVV LDAGSSGTRL HIYKWKDPSR ARKHASKQEL SSLPKLHTEK KWTKKIKPGV
STFGENPTAV GPDHLKGLIH HALDVIPEDQ IEDTPIFLMA TAGMRLLPQA QQSALTSEIC
SYLQDTTDFS LPDCDLHIQV IPGETEGLYG WIATNYLLGG FDRPEDHDHG KGHKTYGFLD
MGGASAQIAF APNATEAAKH ANDLKLLRLR TLDGERSEYR VFTATWLGFG VNQAREAYVN
KLVEMYDPDV REIPDACLPK GLHITPAGEP VDAAPSTDLT LLGTGDFTSC LRHTYPLLGK
DAPCEDTPCL LNGQHVPAID FDVNHFVGVS EYWHTTHGVF DKGDQAYDLK TYQNKVEDFC
TQDWDTIVST KVDARKKNEN IKEAQEACFK ASWLINVLHD GIGVPRLGLD HTPDVNASQG
ALEEAKGKGF LDPFQPVDKI DGIEVSWTLG PMVLYAAGQT PPRNTDSLPV GFGSNVNGIP
ADFNYAGSSW KMDEDDDDDW DDTIEDLVDH AKPSKSSSFL LFILVLLLVG YVFRKRERRT
RFFNKFNGFT GRWRKFGSPK KSGRGFSGLT SKLFGRNTSH YERVIEEGEA NQFELGDVDS
DENEHSDSSD GSKLGKTSGL ATPKLNLERF DSGSVLDRGG LIVRTESRER LVPPNLSSVG
RSRSRAGSPT RLKSPLMTPL AED
//
