ID   A0A0Q9C0Y7_9CELL        Unreviewed;       401 AA.
AC   A0A0Q9C0Y7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:KRD36959.1};
GN   ORFNames=ASE27_08920 {ECO:0000313|EMBL:KRD36959.1};
OS   Oerskovia sp. Root918.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Oerskovia.
OX   NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD36959.1, ECO:0000313|Proteomes:UP000051694};
RN   [1] {ECO:0000313|EMBL:KRD36959.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD36959.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD36959.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD36959.1,
RC   ECO:0000313|Proteomes:UP000051694};
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:KRD36959.1}.
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DR   EMBL; LMJG01000013; KRD36959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9C0Y7; -.
DR   Proteomes; UP000051694; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KRD36959.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051694}.
FT   DOMAIN          203..299
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   401 AA;  41672 MW;  7E999AFABDDDC0F3 CRC64;
     MPSGGGRTGA GDHVTAVAAS LADELVAIRR DIHAHPEVSR AETRTTALIA DRLRAAGLSP
     RLLQGTGLVC DIGGTEGPDG ETRGRVALRA DIDALPLQDR CELPWASTVP GVAHACGHDV
     HTTVVLGAGL VLAELARRGE LARPVRLIFQ PAEEVQPGGS LDVIAQGGLD GVDEIYAVHC
     DPKVDVGQIG TRIGPITSAS DEVSVTITSP GGHTSRPHLT GDVVYALGQV ITQVPAVLGR
     RLDPRSGVNL TWGAVHAGSA HNAIPSTGTV RGTLRCLDVR AWEFAGQVLH DAVEQVVAPY
     EVEVTVNHTR GVPPVENAED CTGALEAAAR DVLGPTSVLL TEQSLGGEDF AWYLTKVPGA
     MARLGTRTPG GRSYDIHQGD LQIDESAIGA GVRLLARVAL G
//