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Database: UniProt
Entry: A0A1X0UQ87_9NOCA
LinkDB: A0A1X0UQ87_9NOCA
Original site: A0A1X0UQ87_9NOCA 
ID   A0A1X0UQ87_9NOCA        Unreviewed;       531 AA.
AC   A0A1X0UQ87;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ORI22487.1};
GN   ORFNames=BJI47_17780 {ECO:0000313|EMBL:ORI22487.1};
OS   Rhodococcus sp. 1168.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=2018041 {ECO:0000313|EMBL:ORI22487.1, ECO:0000313|Proteomes:UP000192546};
RN   [1] {ECO:0000313|EMBL:ORI22487.1, ECO:0000313|Proteomes:UP000192546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1168 {ECO:0000313|EMBL:ORI22487.1,
RC   ECO:0000313|Proteomes:UP000192546};
RA   Nahar A.;
RT   "Metabolic and lipid synthesis pathways analysis of sub-Antarctic
RT   Rhodococcus luteus.";
RL   Submitted (OCT-2016) 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:ORI22487.1}.
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DR   EMBL; MKKY01000042; ORI22487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0UQ87; -.
DR   OrthoDB; 3238066at2; -.
DR   Proteomes; UP000192546; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
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   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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   Hydrolase {ECO:0000313|EMBL:ORI22487.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192546}.
FT   DOMAIN          46..528
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          496..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  55049 MW;  93F45D388717F933 CRC64;
     MSTQLLLGGR IYSPTAPDAS AIAITDGIVT WTGEDRTGRA LHPGAEEIDL AGSFVAPAFV
     DTHVHTTAYG LALGALDLSA CRSRGECVRE IRRYALKSSD PLIWGHGWDD TAWDEAGVLS
     TSDLDEAAPG RPIYLARVDS HSAASSTVLR AASSELNALA GFHPEHALTG DAHHAVRRAA
     LNLLTPAARA AARTSALDYA ASQGICAVHE CGGPDISGRD DFQELLAIDH GVEVRGYWGE
     SVSSADHART LAQETGAHAL GGDLFVDGSI GSRTAWLSAP YNDGPGTGLS FLDVDAIATH
     VAACTEAGIQ AGFHAIGDAA VSAVVQGFSR VAAAIGGPAL AALGHRVEHV EMVSGEQAAK
     LASWGVIASM QPMFDELWGG EEGMYARRLG VDRARTLNPL AQLASSGVSL AFSSDAPVTG
     LDPWRMLRAA VNHRTEGSAI SPRAAFSAAT RGAWRAGGVR DGLAGTLTPG APASYAIWDA
     TDLVVRAPKD SVARWSTDPR AGVPALPSLE PGSPSPTCLR TVHRGRTIHG A
//
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