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Database: UniProt
Entry: A0A0S8B803_9PROT
LinkDB: A0A0S8B803_9PROT
Original site: A0A0S8B803_9PROT 
ID   A0A0S8B803_9PROT        Unreviewed;       402 AA.
AC   A0A0S8B803;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=DM13 domain-containing protein {ECO:0000259|PROSITE:PS51549};
GN   ORFNames=AMJ64_05765 {ECO:0000313|EMBL:KPK07743.1};
OS   Betaproteobacteria bacterium SG8_39.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK07743.1, ECO:0000313|Proteomes:UP000051483};
RN   [1] {ECO:0000313|EMBL:KPK07743.1, ECO:0000313|Proteomes:UP000051483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_39 {ECO:0000313|EMBL:KPK07743.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK07743.1}.
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DR   EMBL; LJTQ01000039; KPK07743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8B803; -.
DR   STRING; 1703390.AMJ64_05765; -.
DR   PATRIC; fig|1703390.3.peg.1894; -.
DR   Proteomes; UP000051483; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd05666; M20_Acy1-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; IPR019545; DM13_domain.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51549; DM13; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          318..402
FT                   /note="DM13"
FT                   /evidence="ECO:0000259|PROSITE:PS51549"
SQ   SEQUENCE   402 AA;  43261 MW;  4E054B31558985BD CRC64;
     MNRPVENAVT SPVEQVRKYH GELRAIRHDI HAHPELGFHE KRTSDIVAEK LAAWGIEAHR
     GLAKTGVVGV IEGRRRTSGR AVGLRADMDC LPMHELGNVP YRSTHEGRMH ACGHDGHTTM
     LLGCGRYLAE TRNFNGTVYL IFQPAEEGGG GGQVMVKEGL FERFPANEVY ALHNWPGLAP
     GQIAVRPGPM MAATDEIQIT VRGRGGHGAM PHLAADPVVA TAHIISALQT IASRNTNPVD
     AVVVSVCSMQ TSQLGAFNVI PEFVKLVGTV RSFRPETREL AERRVREIVA GVAASLGASA
     EIEYRHGYPP TVNTEKEAEF AARVGERVFG AANVLRDADP TMGGEDFSYM LQARPGAYVW
     LGQGGGPLGC SLHNANYDFN DEVIPLGAGY LAALAEAALP LD
//
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