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Database: UniProt
Entry: A0A2H3D8E0_ARMGA
LinkDB: A0A2H3D8E0_ARMGA
Original site: A0A2H3D8E0_ARMGA 
ID   A0A2H3D8E0_ARMGA        Unreviewed;       239 AA.
AC   A0A2H3D8E0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Phosphatase phospho-type {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ARMGADRAFT_968170 {ECO:0000313|EMBL:PBK91489.1};
OS   Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK91489.1, ECO:0000313|Proteomes:UP000217790};
RN   [1] {ECO:0000313|Proteomes:UP000217790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR031051-3};
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DR   EMBL; KZ293661; PBK91489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3D8E0; -.
DR   STRING; 47427.A0A2H3D8E0; -.
DR   InParanoid; A0A2H3D8E0; -.
DR   OMA; HNLADCF; -.
DR   OrthoDB; 372892at2759; -.
DR   Proteomes; UP000217790; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR016965; Pase_PHOSPHO-typ.
DR   NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   PANTHER; PTHR20889:SF12; LP01149P; 1.
DR   PANTHER; PTHR20889; PHOSPHATASE, ORPHAN 1, 2; 1.
DR   Pfam; PF06888; Put_Phosphatase; 1.
DR   PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR031051-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR031051-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217790}.
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-1"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR031051-3"
SQ   SEQUENCE   239 AA;  27506 MW;  BE7F686A52DA242A CRC64;
     MRRLIVFDFD WSMADQDSDR WIFEVLAPDL RRKMKTLKDN IQWTDLVSQS LREAHARGIT
     REQIEDALRI MPFHPGMVRG IKRLKEEGNT TFLCLSNANN IFITTILETK GLLPAFEEIV
     TNRAEWESSG LLNLCRRIDP HGPQHDCTVG CSPNMCKGEE LDAFLARHAP AYDQIIYVGD
     GSNDFCPILR LRSQDMVLCR SFRGLQRRID KDGEKLGLKC QVKYWGGAWE VEEIFNALS
//
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