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Database: UniProt
Entry: R6SHE3_9FIRM
LinkDB: R6SHE3_9FIRM
Original site: R6SHE3_9FIRM 
ID   R6SHE3_9FIRM            Unreviewed;       383 AA.
AC   R6SHE3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:CDC46017.1};
GN   ORFNames=BN652_01271 {ECO:0000313|EMBL:CDC46017.1};
OS   Firmicutes bacterium CAG:424.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263022 {ECO:0000313|EMBL:CDC46017.1, ECO:0000313|Proteomes:UP000018167};
RN   [1] {ECO:0000313|EMBL:CDC46017.1, ECO:0000313|Proteomes:UP000018167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:424 {ECO:0000313|Proteomes:UP000018167};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDC46017.1}.
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DR   EMBL; CBFI010000065; CDC46017.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6SHE3; -.
DR   Proteomes; UP000018167; 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:CDC46017.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018167}.
FT   DOMAIN          180..275
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   383 AA;  42498 MW;  C8F0C7C00D3EFA5C CRC64;
     MSVCKAYEKE LLRLRHWLHQ HPELSMEEGL TTQFIYDYLN ALEIPCYKTG DTGVIATLML
     NPAYKTIAIR SEIDGLPIQE ATGLPFSSLY PGKMHACGHD AITAVTLCLA KVLAEHKEVL
     ACNVRFLFEP GEETGQGAKH LIAHGALENP KVDAILVFHF GNQETRHMEI QKSITTAAVG
     GITLHVTGKS SHWFQPQDGI DALYAASRLA VEIHRLNDTL KTQHPFVLGF GTMEAGTAGN
     IVADTAQLYG SLRAFTMEDF HYVWNQLEQV MRQVEQETGA SICLEPGRMI PPMINDASLV
     KQGSRIGKEL MQDHFSLGEE PFLVGDNAAF YLEHVPGMRT VFLGGKKQGS NEPVHNPAFN
     LDEQILLDAL EFFYQMVTDK SLC
//
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