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Database: UniProt
Entry: L8DK98_9NOCA
LinkDB: L8DK98_9NOCA
Original site: L8DK98_9NOCA 
ID   L8DK98_9NOCA            Unreviewed;       387 AA.
AC   L8DK98;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=RHODMAR_3789 {ECO:0000313|EMBL:CCQ17174.1};
OS   Rhodococcus sp. AW25M09.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ17174.1, ECO:0000313|Proteomes:UP000011207};
RN   [1] {ECO:0000313|EMBL:CCQ17174.1, ECO:0000313|Proteomes:UP000011207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ17174.1,
RC   ECO:0000313|Proteomes:UP000011207};
RA   Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA   Smalaas A.O., Altermark B.;
RT   "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT   from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL   Submitted (DEC-2012) 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:CCQ17174.1}.
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DR   EMBL; CAPS01000104; CCQ17174.1; -; Genomic_DNA.
DR   RefSeq; WP_008717984.1; NZ_CAPS01000104.1.
DR   AlphaFoldDB; L8DK98; -.
DR   STRING; 1268303.RHODMAR_3789; -.
DR   eggNOG; COG1473; Bacteria.
DR   OrthoDB; 9781032at2; -.
DR   Proteomes; UP000011207; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   CDD; cd05672; M20_ACY1L2-like; 1.
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;
FT   DOMAIN          160..252
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   387 AA;  39657 MW;  0F857D0B8DD74548 CRC64;
     MDRALAAVTD EVVALSHSIH AEPEVAFEEH RSVAKILDTL RAHHFEVETS VAGMDTAFTA
     SFGSGDLVVG ICAEYDALPE IGHACGHNII AASAVAAALS LAPVADALGI TVRVLGTPAE
     ETGGGKVLML ERGVFDGIGA ALMVHPGPFD IVGATSLALA DVAVKFTGRA AHASAAPEWG
     INAGDAVTVS QVALGLLRQH LSPGQQFHGI VSDGGVAPNI VPGHAELLYY LRANTTESLE
     TLTAKAFACF EAGAVATGCT HEIRTVSPTY AALTPDAWLV AAFRQEIEAL GRSPLAPDLE
     GFRPLGSTDM GNVTNVLPGI HPVVGLDAGG AVTHQPEFAA ACVTESADRA LRDGALGLAR
     TAARAAADPD TRARLLDAVI ARSAAQQ
//
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