ID   A0A1Y2WUI2_9PEZI        Unreviewed;       672 AA.
AC   A0A1Y2WUI2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Adenosine deaminase domain-containing protein {ECO:0000259|Pfam:PF00962};
GN   ORFNames=K445DRAFT_320163 {ECO:0000313|EMBL:OTB13314.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB13314.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB13314.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB13314.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; KZ112949; OTB13314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2WUI2; -.
DR   STRING; 1001832.A0A1Y2WUI2; -.
DR   OrthoDB; 4403at2759; -.
DR   Proteomes; UP000243732; Unassembled WGS sequence.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11409:SF37; A_DEAMINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732}.
FT   DOMAIN          419..628
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   672 AA;  78399 MW;  1AEE55FDF3F90AB5 CRC64;
     MAGSFLHSRS GPSKVQPNHH GGAQAGLHFQ DAMRKRASRE EEDANEALLK TRDADEKRYG
     ENGFPGDHFS RNVHIIDDTQ LLKAAHSLPK GAHLHLHFNS TLLPGFLLGI AKEMPNMYIS
     SPTHKLRSKS DFDNCEIVFT LQNTKAILDD PNVDSTSQEA ELSSKDLGGP NLFHDDYEPR
     QLMRYRYFRS VWNEERKARK VAALQNEEKA TLAQPNLWEM DMECDDWLVS KLVFHKEQID
     EIFSSEDRSS ESTRKSKTKE EEQERQKQIE DERWPENIEL NFQTSPYKST RERAARAWEK
     FNGRTRMMKG LFNYEKAFRA YTRKCLEEFV NENVQYAEIR PNFMKSNQVL RDDGSEGFNN
     FGLMKIIIEE YENFMKDIGD MDEDGKIKEN RKLDSKGNPV YLDGTDIPQG NGHIPSFGGM
     KVIYCTPRSF PKPMVKEALD ECIRMKKKWP QYIAGFDLVG EEAYDKKYPL RYFTEEFKQF
     QEDCKEEGLD IPFLFHCGET PDDIEGNLEC ALDLNARRIG HGYALPQKPA IMEQMKTNQV
     CVEACPISNM ILGLVEHMHE HRIYKLLEHE VHCSLNSDNG TLFRSTLSHD FYETMIGNRD
     IDLFGWRQLA RWSIDHACMD QVERERVLVE WERRWKEEFI PEIRGKESTN RLTRLDRLSQ
     IDEGRKRREA NL
//