ID A0A0Q4HES0_9MICO Unreviewed; 461 AA.
AC A0A0Q4HES0;
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=ASE68_06365 {ECO:0000313|EMBL:KQM82922.1};
OS Agromyces sp. Leaf222.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM82922.1, ECO:0000313|Proteomes:UP000050813};
RN [1] {ECO:0000313|EMBL:KQM82922.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM82922.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM82922.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM82922.1,
RC ECO:0000313|Proteomes:UP000050813};
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 -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:KQM82922.1}.
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DR EMBL; LMKQ01000001; KQM82922.1; -; Genomic_DNA.
DR RefSeq; WP_055856384.1; NZ_LMKQ01000001.1.
DR AlphaFoldDB; A0A0Q4HES0; -.
DR STRING; 1735688.ASE68_06365; -.
DR OrthoDB; 3665926at2; -.
DR Proteomes; UP000050813; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 212..358
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 49107 MW; B8D810F6AA27883C CRC64;
MPDSPTVPAA PAVSPASPAP TVRPGAPERL SRMIALPTVS AELEQRGMAD FDAFRDLLAG
LYPLTHERLA FEQPHPLGLL FHWRGRSDAD PVVLMAHYDV VPAVEADGWT FPPFEGRIHD
GSVWGRGTLD DKGPMLVLLE AVENLLADGF TPARDVYLAF GGNEEDHGSA GKAIADLFQA
RGITPWLVLD EGGAVIDAPF PFVSLPSAMV GVGEKGIVSL RLAAESKGGH ASAPPTHTPT
DRIARAVHRL HPNPFPKRVP ASARAMLRSF TPHTKGAPRL LLQALTALPW VTARVFAKLG
GEPAAIVHTT VAATMLEGGT AHNVLPSQAA AVLNLRIAPG ETIAGTAERV RRVIRDRHVS
VTVLDGSEPS PESATDSPAF HAIEAAVAAS YPEAVTAPYL VMAATDSRWF HRFAPAVFRF
APLAMTAAQR AAIHGVDESV TFDSLERGER FHRTLIASLD S
//
