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.
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; 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
//