ID   A0A1Y2USE9_9PEZI        Unreviewed;       597 AA.
AC   A0A1Y2USE9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Amidase domain-containing protein {ECO:0000259|Pfam:PF01425};
GN   ORFNames=M434DRAFT_156155 {ECO:0000313|EMBL:OTA86301.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA86301.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA86301.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA86301.1,
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   -!- SIMILARITY: Belongs to the amidase family.
CC       {ECO:0000256|ARBA:ARBA00009199}.
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DR   EMBL; KZ112574; OTA86301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2USE9; -.
DR   STRING; 1001938.A0A1Y2USE9; -.
DR   Proteomes; UP000194361; 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:UP000194361}.
FT   DOMAIN          151..562
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  64219 MW;  2A33AB4B7D974177 CRC64;
     MASTQRFSGY PLPKEGPKTP YTPTVDKNPV LRGWSLVIGA KLVNYSSAIA HATWTNAKFG
     CVRDIPELHE YDWRLQPIVT PLVPDGVVQS KAEITPELCE RQPDDLAGRF HSAADYHELF
     KSGKLTPLQV VKALLPIISR GQKPPAKYES AFAVTREDLV LAAAKKSTER YATGQPLGVL
     DGVPIGVKDD MDVEGYTSHM GQPLDPTNPF FEPATKTIWP IAQLEAAGAI VVGKLVMHEL
     GSDVSGCNPH WGTPINWNNP AYYPGGSSSG GGSALSAGLV PIAIGTDAGG SIRIPASFCG
     AYGLKPTLHR AHTMKSSICV IGPMAATASD LAISYRIMTA PNPEDPVQGA FALSIPPSPA
     TKKTIGIYRD WFDKSSPDVL EVTRKAISYF TDKLGYEVVD ITIPYLVEGQ YSHSAWALTE
     GVDHQRSHVP DPAKALSNLN HCNQLLLAVG ACMSGVDMIK GGQLRGLLME HLAFLFKKHP
     NLLIVTPTVP EAGWKIHPGD QAYGFSDGNA TIRNMMYIWL ANATGCPAVS APVGYVDAEV
     GEGKLPVGLM AMGEWGAEEQ LLAWAKDAET YLNTVQEGGR FRPKDWADVV EIAKSAK
//