ID   C0CW18_9FIRM            Unreviewed;       401 AA.
AC   C0CW18;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EEG56710.1};
GN   ORFNames=CLOSTASPAR_01172 {ECO:0000313|EMBL:EEG56710.1};
OS   [Clostridium] asparagiforme DSM 15981.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Enterocloster.
OX   NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG56710.1, ECO:0000313|Proteomes:UP000004756};
RN   [1] {ECO:0000313|EMBL:EEG56710.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56710.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG56710.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56710.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:EEG56710.1}.
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DR   EMBL; ACCJ01000052; EEG56710.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0CW18; -.
DR   HOGENOM; CLU_023257_0_1_9; -.
DR   Proteomes; UP000004756; 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:EEG56710.1}.
FT   DOMAIN          191..284
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   401 AA;  43748 MW;  469EAAE14257884F CRC64;
     MGDNMTFQQF KDKYQDYLVT VRRRFHESPE LSMEEKETSR FIVAEVEACG LPYEMAGDYG
     VIAVVQGTKP GMGRNVLLRA DIDALPIQED ANNLAGPKNS CSKVPGVGHL CGHDAHTAMM
     LAVMKELTAI RDQFSGKFII CFEPAEENGK GCWLMLPYLE HYEIDRVYAC HVEEGLDTGT
     VSIVPGPRMA GVGAFEYTIY GEGTHGAAPH RGVDPILCTA EMITGLNQIL TRNIPPLSPM
     ALTIGHVESG TARNAIPSQA SFGGTMRFFD RGLGEFAYGR MKEIVNAIAA AHRCKVEQTF
     EYLSYPLVND PHLADLACQA VGEALGTKAV VETEPKTGSE GFTNYIRAYN GQGLHVLIGV
     RNREYGSGEA AHNPKFDVDE AALPYGAFTT LQIALKLNEC E
//