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Database: UniProt
Entry: S5VZD7_STRC3
LinkDB: S5VZD7_STRC3
Original site: S5VZD7_STRC3 
ID   S5VZD7_STRC3            Unreviewed;       166 AA.
AC   S5VZD7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN   ORFNames=B446_32780 {ECO:0000313|EMBL:AGS73360.1};
OS   Streptomyces collinus (strain DSM 40733 / Tue 365).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS73360.1, ECO:0000313|Proteomes:UP000015423};
RN   [1] {ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA   Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA   Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT   "The complete genome sequence of Streptomyces collinus Tu 365.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGS73360.1, ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX   PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA   Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT   "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT   Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL   J. Biotechnol. 168:739-740(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}.
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DR   EMBL; CP006259; AGS73360.1; -; Genomic_DNA.
DR   RefSeq; WP_020943769.1; NC_021985.1.
DR   AlphaFoldDB; S5VZD7; -.
DR   STRING; 1214242.B446_32780; -.
DR   KEGG; sci:B446_32780; -.
DR   PATRIC; fig|1214242.5.peg.6719; -.
DR   eggNOG; COG0622; Bacteria.
DR   HOGENOM; CLU_063749_3_2_11; -.
DR   OMA; ADTHVPK; -.
DR   Proteomes; UP000015423; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
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:UP000015423}.
FT   DOMAIN          1..152
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   166 AA;  18457 MW;  1005A50423305B27 CRC64;
     MRLLLMSDTH LPKRAKRLPD PLLAELPHAD VVFHAGDWVD TATLDLLESR SRRLVGVYGN
     NDGPELRARL PEVAYAELDG LRFGVVHETG PAKGREARCA ARFPDLDVLV FGHSHIPWDS
     TAPGGPRLLN PGSPTDRRRQ PYRTYLTATL ADGTLTDVTL HRLPER
//
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