ID A0A165KG96_9APHY Unreviewed; 357 AA.
AC A0A165KG96;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=DHH phosphoesterase {ECO:0000313|EMBL:KZT63094.1};
DE Flags: Fragment;
GN ORFNames=DAEQUDRAFT_734211 {ECO:0000313|EMBL:KZT63094.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT63094.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT63094.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT63094.1,
RC ECO:0000313|Proteomes:UP000076727};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV429267; KZT63094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165KG96; -.
DR STRING; 1314783.A0A165KG96; -.
DR OrthoDB; 1342473at2759; -.
DR Proteomes; UP000076727; 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 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:UP000076727}.
FT DOMAIN 46..205
FT /note="DDH"
FT /evidence="ECO:0000259|Pfam:PF01368"
FT DOMAIN 267..346
FT /note="DHHA2"
FT /evidence="ECO:0000259|Pfam:PF02833"
FT NON_TER 357
FT /evidence="ECO:0000313|EMBL:KZT63094.1"
SQ SEQUENCE 357 AA; 37811 MW; 2971E7789407ED5A CRC64;
MAPTMIPDLK SPQEVNPSDT LRAFLDRTKK GFIDAAHSGR GREWAVVMGN EAGDLDSLAC
AIAFAWYLSE IRQSLAVALV QTPRGDLDLR AENGYALQLA GVGPDEPLCI DDVLTSAAPS
SPFPSTAFAL VDHNRLGTPF SADNPDARVV AIIDHHADEG LYTNADPRVV TPGVGSCSSL
VATFLQEMCA DKVPPELAML LLSAIIIDTG GMHPGGKAID VDRRAAAFLA SRCTLAHGDV
SSSLASSSLD AIPPLHESPV IQQLNATLQT TKASVAHLGT RDLLRRDYKE YALTPAFAPG
RELLIGLASV PLALAAFVPR DTGEFVRDAT SWMDERGLSA LGVLTSFRDE KKAGKSG
//