ID   A0A1Y2UTJ0_9PEZI        Unreviewed;       538 AA.
AC   A0A1Y2UTJ0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN   ORFNames=M434DRAFT_399693 {ECO:0000313|EMBL:OTA86886.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA86886.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA86886.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA86886.1,
RC   ECO:0000313|Proteomes:UP000194361};
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; KZ112565; OTA86886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2UTJ0; -.
DR   STRING; 1001938.A0A1Y2UTJ0; -.
DR   Proteomes; UP000194361; Unassembled WGS sequence.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR018228; DNase_TatD-rel_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 2.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS01137; TATD_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194361}.
FT   DOMAIN          72..204
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          423..511
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   538 AA;  57773 MW;  47576DFE60F87E01 CRC64;
     MTITARPNAG PLTVLVTTRA VLTLPDDSLL LSPATISISP VTGKIVDIVP TVLPRSSFPP
     STTYINYGSK LLIPGLVDAH VHLNEPGRTE WEGFSTGTRA AASGGVTTVV DMPLNAIPPT
     TTLAGFKEKL AASEGQCWVD VGFYGGVIPG NADELLPLVE AGVRGFKGFL IESGVEEFPA
     ISSNDIALAM KMLKDAPTTL MFHAEMIPPI ADSVGDAVQA SDPPLAPHGD LQSYQTFLES
     RPPSFETYAI DQIVSLARLA PNLHLHIVHL SATQAIPILK AARKSGIDIT AETCFHYLGL
     AAEGVERGDC RYKCCPPIRE QLNQDGLWEE LTAPDSCIKT VVSDHSPCTP ELKLLPPRLQ
     TIEAPHMHHS DSGIDMTADL EREEEKQEVD TRAATKEVGD FFAAWGGISS VGLGLPILYT
     SAKNRAAAGS KSTPSIVDIV RLCCAATAKQ VGLSHRKGAL KVGMDADICV FDDTDEWVLH
     SNGMHWKNRC SPWEGHRFAG RVKETWLRGQ KVFEYGGING GFVSGKPLGE AIVEKRFA
//