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Database: UniProt
Entry: R7GKQ7_9FIRM
LinkDB: R7GKQ7_9FIRM
Original site: R7GKQ7_9FIRM 
ID   R7GKQ7_9FIRM            Unreviewed;       180 AA.
AC   R7GKQ7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN   ORFNames=BN591_01917 {ECO:0000313|EMBL:CDE27670.1};
OS   Catenibacterium sp. CAG:290.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Catenibacterium; environmental samples.
OX   NCBI_TaxID=1262767 {ECO:0000313|EMBL:CDE27670.1, ECO:0000313|Proteomes:UP000018308};
RN   [1] {ECO:0000313|EMBL:CDE27670.1, 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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|RuleBase:RU362039};
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. YfcE
CC       family. {ECO:0000256|ARBA:ARBA00008950, ECO:0000256|RuleBase:RU362039}.
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:CDE27670.1}.
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DR   EMBL; CBIQ010000056; CDE27670.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7GKQ7; -.
DR   STRING; 1262767.BN591_01917; -.
DR   Proteomes; UP000018308; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00841; MPP_YfcE; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041802; MPP_YfcE.
DR   InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR   NCBIfam; TIGR00040; yfcE; 1.
DR   PANTHER; PTHR11124:SF26; PHOSPHODIESTERASE YFCE; 1.
DR   PANTHER; PTHR11124; VACUOLAR SORTING PROTEIN VPS29; 1.
DR   Pfam; PF12850; Metallophos_2; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU362039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018308}.
FT   DOMAIN          1..159
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   180 AA;  21015 MW;  52FCF59E8C2B4CB5 CRC64;
     MKLMIISDIH GSYNDLEKVM HYFDEEQPDR LIILGDILYH GPRNDLPEGY APKKCIPLLN
     KYKDKILAVR GNCDAEVDQM VLDFPMRSDS ALLNVDGHDF YITHGHLYNK DNMPYLKKGD
     VFLYGHYHVP VFEDHGFYTV NPNSISLPKQ GVKSFLVYEN ETFTLYNLEH KEIWCKKITK
//
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