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Database: UniProt
Entry: A0A0B2JYZ7_9FIRM
LinkDB: A0A0B2JYZ7_9FIRM
Original site: A0A0B2JYZ7_9FIRM 
ID   A0A0B2JYZ7_9FIRM        Unreviewed;       158 AA.
AC   A0A0B2JYZ7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN   ORFNames=NZ47_08300 {ECO:0000313|EMBL:KHM51821.1};
OS   Anaerovibrio lipolyticus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Anaerovibrio.
OX   NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM51821.1, ECO:0000313|Proteomes:UP000030993};
RN   [1] {ECO:0000313|EMBL:KHM51821.1, ECO:0000313|Proteomes:UP000030993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5S {ECO:0000313|EMBL:KHM51821.1,
RC   ECO:0000313|Proteomes:UP000030993};
RX   PubMed=23950883;
RA   Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA   Scollan N.D., Huws S.A., Newbold C.J.;
RT   "Identification and characterization of three novel lipases belonging to
RT   families II and V from Anaerovibrio lipolyticus 5ST.";
RL   PLoS ONE 8:E69076-E69076(2013).
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:KHM51821.1}.
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DR   EMBL; JSCE01000171; KHM51821.1; -; Genomic_DNA.
DR   RefSeq; WP_039209105.1; NZ_SVBT01000024.1.
DR   AlphaFoldDB; A0A0B2JYZ7; -.
DR   STRING; 82374.NZ47_08300; -.
DR   eggNOG; COG0622; Bacteria.
DR   Proteomes; UP000030993; 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:SF12; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 29; 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:UP000030993}.
FT   DOMAIN          1..148
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   158 AA;  17157 MW;  400AA7ABEF71A58E CRC64;
     MRVGVMSDSH GNTMAVDRAI ELAGEVDCWL HAGDLIEDAE YLAMVTDKKV INVAGNCDWP
     SSGTDDEILV EIGSHKIFLT HGHIYGVKRD ISLLRQAAVS KGADIAVYGH THVAVIDDGE
     DCLVINPGSV SHPRDGKAQS FMVLNIEGDR VKVEHFHL
//
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