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Database: UniProt
Entry: A0A062VF18_9MICO
LinkDB: A0A062VF18_9MICO
Original site: A0A062VF18_9MICO 
ID   A0A062VF18_9MICO        Unreviewed;       448 AA.
AC   A0A062VF18;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=DC31_02795 {ECO:0000313|EMBL:KDA04987.1};
OS   Microbacterium sp. CH12i.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA04987.1, ECO:0000313|Proteomes:UP000027096};
RN   [1] {ECO:0000313|EMBL:KDA04987.1, ECO:0000313|Proteomes:UP000027096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH12i {ECO:0000313|EMBL:KDA04987.1,
RC   ECO:0000313|Proteomes:UP000027096};
RA   Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT   "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT   shallow groundwater in Cape Hallet, Antarctica.";
RL   Submitted (MAR-2014) 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:KDA04987.1}.
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DR   EMBL; JHET01000010; KDA04987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A062VF18; -.
DR   STRING; 1479651.DC31_02795; -.
DR   Proteomes; UP000027096; 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   Reference proteome {ECO:0000313|Proteomes:UP000027096};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          196..342
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   448 AA;  48202 MW;  1F422392A2C14601 CRC64;
     MSTTTVRPGI AERLSRMIQL PTVSAELEER GTAPFEEFVA LIAELYPLTH QHLTLERHTE
     FGLLFHWKGA SDAGPLVLMA HYDVVPVDES DDWTHPPFAG VIADGWVYGR GTLDDKGPLI
     VVLEAVENLL ATDFTPARDV YLSFGGNEET FGAAAVEIAQ VLKDRGIMPW LVLDEGGAVV
     DAPLSFVKGR AAMIGVGEKG VLTLKLSARG QGGHASAPPT LTAVRRIARA VNRLAPGTFR
     PRTPKAISRM LSQFSAQSSG PSRLLLKVLS RVPFLTARVF AALGGEPAAM VRTTVAPTMQ
     SGGTAVNVIP SQASATVNLR IALGETVARA VARVRRRIHD PLVSIEVLEG SEPSPESPTD
     NAQFALLGRA LEEAFPGVPP VPYVMMAATD SRHFHRYSPA VYRFAPLEMS NAQRAAIHGV
     DESVEIATLE RGEVFHRALL ENLNGTDH
//
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