ID   A0A166TMF3_9AGAM        Unreviewed;       425 AA.
AC   A0A166TMF3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   SubName: Full=DHH phosphoesterase {ECO:0000313|EMBL:KZP30777.1};
GN   ORFNames=FIBSPDRAFT_850217 {ECO:0000313|EMBL:KZP30777.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP30777.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP30777.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP30777.1,
RC   ECO:0000313|Proteomes:UP000076532};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; KV417492; KZP30777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166TMF3; -.
DR   STRING; 436010.A0A166TMF3; -.
DR   OrthoDB; 1342473at2759; -.
DR   Proteomes; UP000076532; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   PANTHER; PTHR12112:SF39; EG:152A3.5 PROTEIN (FBGN0003116_PN PROTEIN); 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076532}.
FT   DOMAIN          247..422
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
SQ   SEQUENCE   425 AA;  45879 MW;  CCBA71B6615A7F08 CRC64;
     MTTTSLSQFL SSSKAGYLKD VDSGKGDAWT VIMGNEAGDL DSIASSIAYA WIRSQTMNVN
     VVPLIQTKRE DMRLREENMH ALSLAGLQSG CPEVLCVDEV PHPGSGTFPS HSFALVDHNR
     LLPKYTSADA KVVAVIDHHA DEGFHTGSDT SPRIVGPSGS CASHVALLCP ADAEIPAGLA
     TLLLSAILVD TGGLKVKAGG KTLPVDLQAA ALLLPRSTIY TSFNIAGASP ITPADDFANM
     DSIANLTADL SEKKNDVSRL DSRDLLRRDY KQYRLDLSWA GPGAFTNAGL STVPVGFKTW
     VPKDSAAFWT ATREWMQERD LGVLGVLTSF RGEKKHKHKR EQLWLIRDTA GAQVDAGRIA
     EKLWTGLEAS KELRLETKDF ASFGTSEEEA HTENSKVRVK VYNQGNVDAT RKATAPLMMG
     VLESP
//