ID A0A0D2DDX8_9EURO Unreviewed; 594 AA.
AC A0A0D2DDX8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Amidase domain-containing protein {ECO:0000259|Pfam:PF01425};
GN ORFNames=PV06_07824 {ECO:0000313|EMBL:KIW40645.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW40645.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW40645.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW40645.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847338; KIW40645.1; -; Genomic_DNA.
DR RefSeq; XP_016260861.1; XM_016409107.1.
DR AlphaFoldDB; A0A0D2DDX8; -.
DR STRING; 215243.A0A0D2DDX8; -.
DR GeneID; 27359898; -.
DR VEuPathDB; FungiDB:PV06_07824; -.
DR HOGENOM; CLU_009600_9_3_1; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000053342; 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:UP000053342}.
FT DOMAIN 64..548
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 114
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 213
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT BINDING 210..213
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ SEQUENCE 594 AA; 65905 MW; 2BE819D65B44B6E3 CRC64;
MYPPFDYFEH RRACVIKQRQ RDARFESLPD VYKGPLTSHQ RSILNAPIAT LVQDVHSGTL
SPVDILRTYG KTAAIAQERT NCVTELLLPE AEAWSRSSDV NLQGPLAGIP VSLKDSIAVA
GFDVSVGYSR HVFKPCAEDG VMVQLLKRAG AIPHVKTALP ITLLSFESTN DLWGVARNPH
NDRYSPGGST GGEGALLALN GSRIGIGSDV AGSVRTPAAW AGINSLRCST GRWPKVGMNT
SMPGQEGIPS VFSPMARTLD DLTYFTKAFI EMKPWEVDYT VHPIPWRQEL YDEARSAEKL
RIGLISTDGV VRPSPAIARG LKLTADALRK AGHQVVEIPL ESFPQKATPA QGLQIASVLL
CADGGKTFGS FFRTGEHNDP GAAQIKFYMS LPRPVKYLWY LWTRYVKCDP LWASILQYFH
PLSAAEQWQW VAKREAFRAT WYEWWNRPEQ AFDLILCPAN ATPALPHGAM KDAVASCGYT
FLWNLLDYSA GIVPVAKVDK ELDALEAGWK PNNSIERGTY KYYDASKMEG LPIAVQVVGR
RLTEEKTLGY MGVVEYCLRE AGIVYEHLDV DNLPELKDIE RQKSNVSVHP GRIW
//
