ID   A0A1Q3WLE1_9BACT        Unreviewed;       382 AA.
AC   A0A1Q3WLE1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OJW76093.1};
GN   ORFNames=BGO59_02900 {ECO:0000313|EMBL:OJW76093.1};
OS   Spirosoma sp. 48-14.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW76093.1, ECO:0000313|Proteomes:UP000186057};
RN   [1] {ECO:0000313|EMBL:OJW76093.1, ECO:0000313|Proteomes:UP000186057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=48-14 {ECO:0000313|EMBL:OJW76093.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJW76093.1}.
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DR   EMBL; MKUD01000027; OJW76093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3WLE1; -.
DR   STRING; 1895854.BGO59_02900; -.
DR   Proteomes; UP000186057; 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:SF170; CLAN MH, FAMILY M20, PEPTIDASE T-LIKE METALLOPEPTIDASE; 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:OJW76093.1}.
FT   DOMAIN          179..272
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   382 AA;  42189 MW;  96DB336DEC267E9C CRC64;
     MSTPNTDRFT QFRRELHQFP EVSGQEVQTQ QRIKTFVSQF HPDALHDIGG TGLLLQYGTA
     KTGAVTLIRA DTDALPIQEV NRFAHRSQIA GVSHKCGHDG HTAILARVAA LLDEKPVTSG
     AVYLLFQPAE ETGQGAQAVI NDPLFATIQP DQVFALHNLP GYEQGVIVCK SGPFTASVLS
     MIVAFTGKVS HSAEPEKGIN PAYVMAEFML KARTLQNPDP ASDEFTLITP VHTTMGEKSY
     GISAGYGEVH LTLRTRTALK MEWLTNQLES VLLALTAGSG IDTQTTYTEA FFANENDPKT
     FEQIKQSAHR LGYPFLEKQE PFKWGEDFGL FTQRYKGAMF GIGAGVNSPA LHNDDYDFND
     ELIEPAAQLF FNLIERIHRN QE
//