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Database: UniProt
Entry: C0W504_9ACTO
LinkDB: C0W504_9ACTO
Original site: C0W504_9ACTO 
ID   C0W504_9ACTO            Unreviewed;       453 AA.
AC   C0W504;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=HMPREF0058_0948 {ECO:0000313|EMBL:EEH66211.1};
OS   Actinomyces urogenitalis DSM 15434.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=525246 {ECO:0000313|EMBL:EEH66211.1, ECO:0000313|Proteomes:UP000004778};
RN   [1] {ECO:0000313|EMBL:EEH66211.1, ECO:0000313|Proteomes:UP000004778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15434 {ECO:0000313|EMBL:EEH66211.1,
RC   ECO:0000313|Proteomes:UP000004778};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|PIRNR:PIRNR037226}.
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:EEH66211.1}.
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DR   EMBL; ACFH01000060; EEH66211.1; -; Genomic_DNA.
DR   RefSeq; WP_006547915.1; NZ_DS999574.1.
DR   AlphaFoldDB; C0W504; -.
DR   STRING; 103621.GCA_001067145_02018; -.
DR   GeneID; 81708615; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_031812_1_2_11; -.
DR   OrthoDB; 9781032at2; -.
DR   Proteomes; UP000004778; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EEH66211.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004778}.
FT   DOMAIN          219..309
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          24..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  47924 MW;  1F81C099F2FEC67D CRC64;
     MSELRDLSRP TTPSTAVQDL MARETAARQA SVPPAQELAE QAGADAAARQ HLAEVITELS
     PQIVALSRDI HAHPEVGYTE HHAVAAVAGV LRQHGIEPDE AVFGMDTALR AQVGPQEGVG
     TIAILAEFDA LPGIGHGCGH NVMCANSVGA FLALAELERR QPGTLPGRVI LQTTPAEESD
     TAKERLAVAG MLDGVDAAIQ THSYAHDVVD QPWLGVRRIR AVFTGVPAHA ASQPFMGRNA
     LDAATLALTG IGLLRQQITP WDRLHAVMVD GGQVANIIPE RTELSMFVRS KYAATLKDLV
     GRVEDVLRGA ALMTGTGVEI ITADYSNEMP VRANGPLLES WTRSQRARGR DPLAADVLPE
     QVAAGTDFGN VSQRVPGIHP LIKVTQDGDV ALHTREMTTA AGSPTGDAAA VDGAYGLAAV
     ALDWLSDADL REAVRANFEA SGGVVDVEHF WDE
//
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