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Database: UniProt
Entry: R7GMX8_9FIRM
LinkDB: R7GMX8_9FIRM
Original site: R7GMX8_9FIRM 
ID   R7GMX8_9FIRM            Unreviewed;       267 AA.
AC   R7GMX8;
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=Cof-like hydrolase {ECO:0000313|EMBL:CDE27302.1};
GN   ORFNames=BN591_01584 {ECO:0000313|EMBL:CDE27302.1};
OS   Catenibacterium sp. CAG:290.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Catenibacterium; environmental samples.
OX   NCBI_TaxID=1262767 {ECO:0000313|EMBL:CDE27302.1, ECO:0000313|Proteomes:UP000018308};
RN   [1] {ECO:0000313|EMBL:CDE27302.1, ECO:0000313|Proteomes:UP000018308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:290 {ECO:0000313|Proteomes:UP000018308};
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:CDE27302.1}.
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DR   EMBL; CBIQ010000023; CDE27302.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7GMX8; -.
DR   STRING; 1262767.BN591_01584; -.
DR   Proteomes; UP000018308; Unassembled WGS sequence.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   Gene3D; 3.30.1240.10; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR000150; Cof.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR00099; Cof-subfamily; 1.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10000:SF25; PHOSPHATASE YKRA-RELATED; 1.
DR   PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CDE27302.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018308}.
SQ   SEQUENCE   267 AA;  30448 MW;  941E66F9748DDE62 CRC64;
     MKEKVLFFDI DGTLVDNTYG VHEVPAGVKR ELKRIQNDGH KLFICSGRPK AMINQQFLDL
     GFDGYVLYNG GYIEIAGESI FEERMDTELA TQTVDMLEEL NCDYMIETAH HIYIDKRYKE
     LYTFFKNLGM EEMFSMDFDR DDVLKRAIKI EANVTNKDKQ KVSDYLDGKF GTTISFDQHG
     SDNSFEFFSP TMSKAIGIKK VLEYYGLDIK DTYAFGDGLN DIEMIQLCQI GVAMGNAVDE
     LKAQADIICK SIDKNGLEDI LKALFPQ
//
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