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Database: UniProt
Entry: A0A0T1SRM4_9ACTN
LinkDB: A0A0T1SRM4_9ACTN
Original site: A0A0T1SRM4_9ACTN 
ID   A0A0T1SRM4_9ACTN        Unreviewed;       538 AA.
AC   A0A0T1SRM4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=N-acyl-D-amino acid deacylase {ECO:0000313|EMBL:KQX58905.1};
GN   ORFNames=ASD33_00915 {ECO:0000313|EMBL:KQX58905.1};
OS   Streptomyces sp. Root1304.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX58905.1, ECO:0000313|Proteomes:UP000051136};
RN   [1] {ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX58905.1, ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|EMBL:KQX58905.1,
RC   ECO:0000313|Proteomes:UP000051136};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQX58905.1}.
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DR   EMBL; LMEP01000001; KQX58905.1; -; Genomic_DNA.
DR   RefSeq; WP_056551687.1; NZ_LMEP01000001.1.
DR   AlphaFoldDB; A0A0T1SRM4; -.
DR   STRING; 1736450.ASD33_00915; -.
DR   Proteomes; UP000051136; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01297; D-aminoacylase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 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:UP000051136}.
FT   DOMAIN          49..512
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          518..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  58055 MW;  A280ACBEE9B44DED CRC64;
     MDLVFRDAEV VDGTGAPSYR ADVAVEGGRI ASIVQEGAAA GCLRPTARRI VDAEGLVLSP
     GFIDMHAHSD LALLRDPDHS AKAAQGVTLE VLGQDGLSYA PVDDRTLAEV RRAITGWNGY
     GDDIDFDWRT VGEYLDRLDR AHGGRGIAVN AAYLVPQGTV RMYAVGWDDR PATERELARM
     RRLVAEGLEQ GAFGMSSGLT YTPGMYAKDA ELTELCRVVA EYGGYYCPHH RSYGAGALEA
     YGEMVRLTRE AGCALHLAHA TMNFGVNEGR APELLALLDE ALDAGADISL DTYPYTPGCT
     TLVALLPGWA SEGGPEAVLA RLRDEATAER VRHHLEVLGS DGCHGVPVDW DTIEVSGVSA
     PGLAEYVGRR VDGWPTARRL LLEDGLGTTI LQHVGHEENV RAIMRHRVHT GGSDGILQGT
     KPHPRAYGTF PRYLGRYVRE LGVLSLEECV ARLTGRPAAR LRLPDRGRIR EGYVADLVLF
     DPETVAAGST YASPRTPPTG IPHVLVDGRF VIEDGRRTDA LPGKSLRSTR RGGARPQG
//
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