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Database: UniProt
Entry: A0A0L0JFX3_9ACTN
LinkDB: A0A0L0JFX3_9ACTN
Original site: A0A0L0JFX3_9ACTN 
ID   A0A0L0JFX3_9ACTN        Unreviewed;       434 AA.
AC   A0A0L0JFX3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=IQ63_42660 {ECO:0000313|EMBL:KND24379.1};
OS   Streptomyces acidiscabies.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=42234 {ECO:0000313|EMBL:KND24379.1, ECO:0000313|Proteomes:UP000037151};
RN   [1] {ECO:0000313|Proteomes:UP000037151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA   Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT   "Genome sequencing of plant-pathogenic Streptomyces species.";
RL   Submitted (JUL-2014) 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:KND24379.1}.
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DR   EMBL; JPPY01000244; KND24379.1; -; Genomic_DNA.
DR   RefSeq; WP_050375354.1; NZ_KQ257834.1.
DR   AlphaFoldDB; A0A0L0JFX3; -.
DR   PATRIC; fig|42234.21.peg.8761; -.
DR   OrthoDB; 7055905at2; -.
DR   Proteomes; UP000037151; 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.
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:UP000037151};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          195..318
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   434 AA;  46515 MW;  FAF13DA913F23318 CRC64;
     MADGQAYEEV VRFTSDLIRC DTTNRGGGDC RERPAAEYAA EQLAEIGLEP VLLERTPGRT
     NVVARIEGTD PSADALLVHG HLDVVPAEAA DWSVHPFSGE VRDGVVWGRG AVDMKNMDAM
     VLAVARSWAR EGVRPRRDVV IAFTADEEAS AEDGAGFLAD KHPGLFEGCT EGISESGAFT
     FHDGTGREIY PIAAGERGTA WLKLTARGRA GHGSKVNREN AVTRLAAAIT RIGAYEWPAR
     LTPTVSAALA ELAALYGIEA DLDDVDALLG KLGPAASLVE STVRNSANPT MLDAGYKVNV
     IPGEAVAYVD GRYLAGAEDE FRATLDKLTG PDVSWEFQHH SVALQAPLDT PTYAGLRAAV
     REFAPHGHTV PYCMSGGTDA KQFSRIGVVT YGFTPLRMPE GLDYQALFHG VDERVPVDAL
     HFGVDVLDRF LRTA
//
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