ID C1ATH1_RHOOB Unreviewed; 421 AA.
AC C1ATH1;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN OrderedLocusNames=ROP_49880 {ECO:0000313|EMBL:BAH53235.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH53235.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH53235.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH53235.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|PIRNR:PIRNR037226}.
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DR EMBL; AP011115; BAH53235.1; -; Genomic_DNA.
DR AlphaFoldDB; C1ATH1; -.
DR STRING; 632772.ROP_49880; -.
DR KEGG; rop:ROP_49880; -.
DR PATRIC; fig|632772.20.peg.5213; -.
DR HOGENOM; CLU_031812_1_0_11; -.
DR OrthoDB; 9781032at2; -.
DR Proteomes; UP000002212; Chromosome.
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:BAH53235.1}.
FT DOMAIN 190..280
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 43205 MW; 0D17AFBB52AB86A8 CRC64;
MTDNAIAANI DTPAGPHGTA EKLKRRVEDT VLEWRDRLVA ASHDLHAHPE LAFEEHRSAA
LVADLLRDAG FAVEVGVWGQ ATALEAVYGS GELTVVVCAE YDALPGIGHA CGHNIIATAG
AGAAIALSRV ADELGIRVKL LGTPAEEKGA GKAHMLEAGA WEDATVSLMV HPGPGVVVPT
AGSTSQSRDR FRVEFTGRAS HAAAAPTVGI NAGDAATVMQ VSVGLLRQHL PDTVRVSAVT
LSGGDVSNII PASAVVEAEV RSFDLAETAD LKKKVLACVD GAATATGCTY AVTPVDPIYE
PLVQHPFLAD RFDAALEHRG RVMPPREGSA LGGGSTDMGN VSQAVPSIHP LIGVMGSTAA
PHTAAFAADA VTPGADDAVV DGAYALAAAI VDLATDSEAR AAVLEQQHNR APGATRRPAY
V
//
