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Database: UniProt
Entry: A0A2J6Q3G5_9HELO
LinkDB: A0A2J6Q3G5_9HELO
Original site: A0A2J6Q3G5_9HELO 
ID   A0A2J6Q3G5_9HELO        Unreviewed;       563 AA.
AC   A0A2J6Q3G5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Amidase signature enzyme {ECO:0000313|EMBL:PMD20822.1};
GN   ORFNames=NA56DRAFT_573196 {ECO:0000313|EMBL:PMD20822.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD20822.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD20822.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD20822.1,
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.
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DR   EMBL; KZ613483; PMD20822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6Q3G5; -.
DR   STRING; 1745343.A0A2J6Q3G5; -.
DR   OrthoDB; 731186at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR46072:SF10; ACETAMIDASE; 1.
DR   PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   PIRSF; PIRSF001221; Amidase_fungi; 2.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT   DOMAIN          63..542
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   ACT_SITE        113
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT   ACT_SITE        188
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT   ACT_SITE        212
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT   BINDING         209..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ   SEQUENCE   563 AA;  62728 MW;  82E62D041D1D3D0B CRC64;
     MVYPLDYFQH RHDCKFKQTE RAQRIQDLTS YHGSFTSSER NVLSKPIEEL VQDVHKQVLQ
     PIDILRAYGK AALKAHTKAN CLTEIMISSA EKWTTDGSIN MKGPLAGIPI SLKDSIVVGG
     YDTSVGYSKN VGNKGEKDGA MVRILKDAGA VPYVKTNLPI TLLSFESTND LWGRCTNPHN
     NKYSPGGSTG GEAALLAAGG GRIGIGSDVA GSVRAPAHFS GIYSLRCSTG RWPKNGMVTS
     MPGQEGIPSV FSPMTRTLED LSYFTKSMIG MKPWKYDHSV HPIPWRDDVS KEFQEKKKFR
     IGVLRTDGVV DPSPACARAV DEVVAALRKE GHEIIDVNPP SPYEALVIAS QLLNADGCKT
     FKSFFRTGEW EDSGARQMSF LMGLPSPFKY VYYLWVKYVR RDDIWAGLIR NWSEKSAYEQ
     WKLVTKREAY KAKFHDWWEQ EAKIDFMITP PNATPAVPHD GMKEAVSSCG YTFLFNLLDY
     TCGILPITHV DKALDQLPSD FSIKKLNGVA QGAYKLYDAT AMHGLPVAVQ IVGQRLEEEK
     VLAVMQRVED ALGDEKYRLM DID
//
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