ID   A0A395HTE3_ASPHC        Unreviewed;       453 AA.
AC   A0A395HTE3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Amidase {ECO:0000313|EMBL:RAL10683.1};
GN   ORFNames=BO97DRAFT_479050 {ECO:0000313|EMBL:RAL10683.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL10683.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL10683.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL10683.1,
RC   ECO:0000313|Proteomes:UP000248961};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ824293; RAL10683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HTE3; -.
DR   STRING; 1450537.A0A395HTE3; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_479050; -.
DR   OrthoDB; 5491171at2759; -.
DR   Proteomes; UP000248961; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   CDD; cd03884; M20_bAS; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01879; hydantase; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   PANTHER; PTHR32494:SF20; SYNTHASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248961}.
SQ   SEQUENCE   453 AA;  49363 MW;  F5BF96BFC72D87DD CRC64;
     MFKYSFSRGL AASSFRRHLS SLAGSGLKIN SDRLLETLHH TCQWGAAHRY GNGPTETGMN
     RLCLTDDDAR VRRWLLDEAE KLGCDVTIDQ MGNMFARQRG ALNSPAPMTA MGSHLDTQPR
     GGRYDGILGV IAALEVLRTM KDHGYQTQFD IGLVNWTNEE GARFPKSMCS SGVWAGEIPI
     ESAWKLADIF DPSVTLRSEL ERHGFMGDIP CSPKGYPLGA HFELHIEQGP ILEEANKKIG
     AVTGAQGYRW LTINVTGRDA HTGTTPLSAR RDPLLAASKM IAASNAVAKR HGALASTGVL
     KLPPTSSTNT VTSEVTFTLD IRHPRDSVVH TVQDECLGLF AEIAREDGKG VSFDWKVDTD
     SAAVEFDADC LSAVKEAAAQ LVGADGWLEI TSGAGHDSVY TNRHCPTAMI FVPCMEGVSH
     HPEEYCKPED CALGTQTLLE SVVNYDRMRS KLN
//