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Database: UniProt
Entry: A0A2M9J714_9ACTN
LinkDB: A0A2M9J714_9ACTN
Original site: A0A2M9J714_9ACTN 
ID   A0A2M9J714_9ACTN        Unreviewed;       443 AA.
AC   A0A2M9J714;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=CG740_12645 {ECO:0000313|EMBL:PJN02648.1};
OS   Streptomyces sp. CB01201.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020324 {ECO:0000313|EMBL:PJN02648.1, ECO:0000313|Proteomes:UP000231916};
RN   [1] {ECO:0000313|Proteomes:UP000231916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01201 {ECO:0000313|Proteomes:UP000231916};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN02648.1}.
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DR   EMBL; NNBJ01000005; PJN02648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9J714; -.
DR   OrthoDB; 7055905at2; -.
DR   Proteomes; UP000231916; 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   CDD; cd05675; M20_yscS_like; 1.
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   PIRSF; PIRSF036696; ACY-1; 2.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          200..329
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   443 AA;  47182 MW;  7B5ACE4A4BDD064F CRC64;
     MAEVETADQV ALDEAVTFTS ELIRIDTSNR GGGDCRERPA AEYVAERLAA AGLEPRMLER
     TAGRTNVVAR IEGTDPSADA LLVHGHLDVV PAEAADWSVH PFSGEIADGV IWGRGAVDMK
     NMDAMVLAVV RAWARHGVRP RRDIVLAYTA DEEASAVDGS GFLADHHPEL FDGCTEGISE
     SGGVTFHAGR GLEVYPVGAG ERGTAWLRLT AHGRAGHGSK VNRANAVSRL AAAVARIGEH
     EWPVRLTPTV RASLVELAAL HGIDTDPDAP DFDADELLGK LGPAAALVEP VIRNSANPTM
     LDAGYKVNVI PGHATAHVDG RTVPGGEAEF RTTMDGLTGP DVDWDFDHGE VALQAPVDSP
     TYLKLKAAIE RFAPEGHVVP YCMSGGTDAK QFSRLGITGY GFAPLRMPPG LDYQALFHGV
     DERVPVDALH FGVRVLDHYL RSA
//
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