ID A0A229WYI9_9EURO Unreviewed; 552 AA.
AC A0A229WYI9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=CDV55_100894 {ECO:0000313|EMBL:RHZ68408.1}, CFD26_103424
GN {ECO:0000313|EMBL:RLL95207.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL95207.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL95207.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ68408.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLL95207.1}.
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DR EMBL; NKHV02000045; RHZ68408.1; -; Genomic_DNA.
DR EMBL; NIDN02000163; RLL95207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229WYI9; -.
DR STRING; 1245748.A0A229WYI9; -.
DR OrthoDB; 147994at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.10.310.70; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000215289}.
FT DOMAIN 56..546
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 552 AA; 59637 MW; 27507180DF70E59C CRC64;
MATFKDAVTY YNGKVHTLND SSQVVEAFIV SPEGDFLAVG TTEEILTKAR ANQNVTYNLN
GRFVMPGIHD AHVHLLSAGI SYLSAVSLPE DTTVDNIGQR MQEGLCTCAY QHAFQDWVVG
HTFAIPEYDR ASLDRDFPDT PLVIHGGAGH SAFLNTAGLL KAGYDVDNEP DVKGAIFGRR
ADGSLTGELA ELAMSKAMIS KGNPNLAHAK RAIKAAIHRL HQAGVTSCQE AATNTVILDV
IRELDNDNSL KMDIAAHSAY APEFLGSERQ SSLKALIERA PGLATKHVHT NFVKILLDGV
PLPPMFSSAG LDGKGNVERQ KILVDDVVDA VKRFDERGLT VKIHATGQGS TRLALNAINE
ARKHNGSNTK HEIAHCNGIH PDDFEYFAKQ NVTAELSPAT FFDHPLTQAS NGAMNWDFVK
LLEAHAYPIT IGSDWGSRGD PCLLPKIHHV ARRVGDWAIK SNVKTGGAVR GTQSNPVSLG
ARLVLELLTK QGAAAVGLSA VSGSIEVGKR ANFIMLDKDV VGDSEEKVAD FENVKVLKTW
FEGELVWDAE AE
//