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Database: UniProt
Entry: A0A229WYI9_9EURO
LinkDB: A0A229WYI9_9EURO
Original site: A0A229WYI9_9EURO 
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
//
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