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Database: UniProt
Entry: I9LCC7_9FIRM
LinkDB: I9LCC7_9FIRM
Original site: I9LCC7_9FIRM 
ID   I9LCC7_9FIRM            Unreviewed;       184 AA.
AC   I9LCC7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN   ORFNames=FB4_3558 {ECO:0000313|EMBL:EIW18084.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW18084.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW18084.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW18084.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
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:EIW18084.1}.
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DR   EMBL; AKVJ01000028; EIW18084.1; -; Genomic_DNA.
DR   RefSeq; WP_007934636.1; NZ_AKVJ01000028.1.
DR   AlphaFoldDB; I9LCC7; -.
DR   PATRIC; fig|1149862.3.peg.2518; -.
DR   OrthoDB; 9800565at2; -.
DR   Proteomes; UP000004324; 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; PTHR43165; METALLOPHOSPHOESTERASE; 1.
DR   PANTHER; PTHR43165:SF1; PHOSPHODIESTERASE MJ0936; 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}.
FT   DOMAIN          1..164
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   184 AA;  20146 MW;  7D2A7F7ABAFD9B67 CRC64;
     MNIGIISDTH GCAKTWETIY EKYFTQCDFI IHAGDILYHG PRNDIPAEYN PKQLANVLNN
     CPIPIIAACG NCDAEVDSMV LTMPIQSPYA YMVVDGLHII ATHGHNLTED AKKEMAIKFK
     ANLFITGHTH VAVLEKNNNI VYLNPGSPAM SKRADGLGTF ARLTGDTIEV LDAASGQVLM
     SERL
//
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