ID   A6WE80_KINRD            Unreviewed;       420 AA.
AC   A6WE80;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   04-NOV-2026, entry version 80.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ABS05119.1};
GN   OrderedLocusNames=Krad_3656 {ECO:0000313|EMBL:ABS05119.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kineosporiales;
OC   Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS05119.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
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DR   EMBL; CP000750; ABS05119.1; -; Genomic_DNA.
DR   RefSeq; WP_012086617.1; NC_009664.2.
DR   AlphaFoldDB; A6WE80; -.
DR   STRING; 266940.Krad_3656; -.
DR   KEGG; kra:Krad_3656; -.
DR   eggNOG; COG1228; Bacteria.
DR   HOGENOM; CLU_046987_0_0_11; -.
DR   OMA; AACIHIE; -.
DR   Proteomes; UP000001116; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01309; Met_dep_hydrolase_C; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR051781; Metallo-dep_Hydrolase.
DR   PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 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:UP000001116}.
FT   DOMAIN          288..384
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   REGION          167..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   420 AA;  44011 MW;  D4564DDF8F3A1085 CRC64;
     MSPYDPARPA GPARDVAVVG GTLVELTPDW RGQRRPGTVL VRDGRIAAVG PGVPVPAGVP
     VLDATGRLVL PGFVDAHTHL GVHAEGEGWH GADVNEKGEP RGARLRSWDG VDPADRGFLD
     ALSAGVTTVA VLPGSANVVG GQTAALRTWG TTVEQMLLRA PIGVKSALGE NPRKNGQSSG
     GPTTRMGIAA SLRDSFAAAQ RFTARRERAR AGGEPLDPPT DRERDAEVLA RVLAGEIVWQ
     QHAHRADDIA TAVRLADEFG YRLVLNHVTE GHRVLDLLVE RGLPAVVGPL LTSRSKPELR
     HRSMAVPGLL AAAGLRVALT TDHPVVPIQL LPVSAALAVK EGLDPDEALR ALTLNPAVIL
     GIDDRVGSLA PGLDGDVVVW SGDPLEVASR ALHVVSGGRA VYRWDGAGEV LAPDGTWRAL
//