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Database: UniProt
Entry: A0A239KMN6_9ACTN
LinkDB: A0A239KMN6_9ACTN
Original site: A0A239KMN6_9ACTN 
ID   A0A239KMN6_9ACTN        Unreviewed;       421 AA.
AC   A0A239KMN6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:SNT18839.1};
GN   ORFNames=SAMN05421812_103618 {ECO:0000313|EMBL:SNT18839.1};
OS   Asanoa hainanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Asanoa.
OX   NCBI_TaxID=560556 {ECO:0000313|EMBL:SNT18839.1, ECO:0000313|Proteomes:UP000198362};
RN   [1] {ECO:0000313|EMBL:SNT18839.1, ECO:0000313|Proteomes:UP000198362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNT18839.1,
RC   ECO:0000313|Proteomes:UP000198362};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZPH01000003; SNT18839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239KMN6; -.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000198362; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:SNT18839.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198362}.
FT   DOMAIN          215..306
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  44150 MW;  45DC39C4B778AA94 CRC64;
     MTSALTLPSN SSPMASSWPE TPPGADPLPG QLDRWLAARG AELVAVRRHI HAHPELSHQE
     FETASLVARE LAVAGLTPRL LPKGNGVICD VGEGDRVIAL RADLDALPLP DGKDVPYRST
     VDGVAHACGH DVHTTILLGT GLALAQLAER DELPGRVRLL FQPGEECIPS GAPEVISAGG
     LKDVAAIYAL HCAPQLPVGL VGVRSGPFTA AADTIEVNLR GRGGHTARPH LTTDLVHAMG
     RVIVDVPSLL DRRVDARAGV SMVWGRAHAG EAYNAIPAVA NLKGTVRILN REAWREAPEL
     ITKLIHDVVA ATGAEVEVTY TRGVPPVIND RMATAVVAGA AGAALGPDRV VEAEISMGGE
     DFAFYLEQVP GAMIRLGTTP QGAEVKPDIH QSTFDVDEKA IGYGVRVMVH TALAALAAGT
     F
//
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