ID A0A0Q5L9W6_9MICO Unreviewed; 445 AA.
AC A0A0Q5L9W6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=ASF82_06580 {ECO:0000313|EMBL:KQR47373.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR47373.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR47373.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47373.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR47373.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47373.1,
RC ECO:0000313|Proteomes:UP000051005};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KQR47373.1}.
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DR EMBL; LMOX01000001; KQR47373.1; -; Genomic_DNA.
DR RefSeq; WP_056055929.1; NZ_LMOX01000001.1.
DR AlphaFoldDB; A0A0Q5L9W6; -.
DR STRING; 1736282.ASF82_06580; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000051005; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF32; CONSERVED PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051005};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 205..342
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 445 AA; 47572 MW; 573A2FE9DD1705EE CRC64;
MTTTPESEPA TTDREVELDE TATIARDLIR FDTSNYGGGR SNGEADAAEY VADALRALDL
EPLVFESEPG RVSVLARVEG ADRSKPGLVV HGHLDVVPAD PANWSVDPFA GVVRDGMLWG
RGAVDMKNMD AMMLSSLGDI IRAGERPARD LVVGFLADEE AGGVLGSHFL VTEHPEVFEG
ATEAISEVGG YSTFIDGRRS YLLQTGEKAL IWIKLRTRGT AGHGSQMIVA NAVTRLAEAV
AVLGRQQWPI ALTDTTTALL SEVARILDVD LEQTSPDELV LHTGTAAGFI RGSLRTTTNP
TMLTAGYKHN VVPDTAEALV DIRCMPGQEE AVLAEVRALI GDDVEIETMH TDIGLETPFS
GPLVEAITGT LERHDPGAPV LPYLLSGGTD NKALSLLGIA GYGFAPLRLD EGMDFPAMFH
GVDERVPLDA LSFGSRVLRD LLATY
//
