ID   A0A2J6QBB3_9HELO        Unreviewed;       612 AA.
AC   A0A2J6QBB3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Amidase {ECO:0000313|EMBL:PMD23549.1};
GN   ORFNames=NA56DRAFT_595920 {ECO:0000313|EMBL:PMD23549.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD23549.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD23549.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD23549.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the amidase family.
CC       {ECO:0000256|ARBA:ARBA00009199}.
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DR   EMBL; KZ613474; PMD23549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6QBB3; -.
DR   STRING; 1745343.A0A2J6QBB3; -.
DR   OrthoDB; 5902at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895:SF67; AMIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT   DOMAIN          163..577
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  66227 MW;  ED143089A145AC33 CRC64;
     MATTPGTGKR WLQGPEPIQG PETPYDDIRK SNPPVRGWFN LTTSVLLLEW FGFIRTIIWQ
     NTGFANLRKL QVHIENTPPR FDPTVIPFPE PSGTEKKDLA NGSNGHVAAK NLSRKYYTVA
     DYHRMYVSGE LTPTAVAKAI LPLIRKDISP PGEHSISFFD SKVELVLAAA EASTLRYKEK
     RSLGPLDGVP TAVKDEYDID GYTTCLGSKN DYTGKPKDGA SITSWCVKKL EEAGAVVVGK
     LHMHEFGLDT SGNNPFKGTP PNPYNPQYYT GGSSSGCAYT VSTGLVPIAL GSDGGGSIRI
     PASFCSVYGL KPTHGRLSFK PALNHSITCA VNGPLASDIV SLSAMYTVLG APDDESLFAP
     PSPTVLTPSP TRKKVLGICE AWFSRATPAI QTLCRNMLDR LVSEYGYTLV SIKIPFLPEG
     QTAHAMTVLT DAATLLPVTK GLTPANRIML ALGNVTPSTD FLLAQKLRHV LMQHLAWLWT
     QHPGMIIVTP TTACAGWKVG KPVDLKYGIS DGDQTLKTME YVWMGNFCGL PSISVPAGFV
     VPHGAKGAGE VAEEKTEGKV PVGFMGMGEW ATEEELLWFG ADCEEIGQEG SSRPPIWVDV
     VELAKEEMRR TG
//