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Database: UniProt
Entry: D9XDB2_STRVT
LinkDB: D9XDB2_STRVT
Original site: D9XDB2_STRVT 
ID   D9XDB2_STRVT            Unreviewed;       164 AA.
AC   D9XDB2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN   ORFNames=SSQG_07277 {ECO:0000313|EMBL:EFL36759.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL36759.1, ECO:0000313|Proteomes:UP000004184};
RN   [1] {ECO:0000313|Proteomes:UP000004184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC   {ECO:0000313|Proteomes:UP000004184};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) 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}.
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DR   EMBL; GG657757; EFL36759.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9XDB2; -.
DR   STRING; 591159.SSQG_07277; -.
DR   eggNOG; COG0622; Bacteria.
DR   HOGENOM; CLU_063749_3_2_11; -.
DR   Proteomes; UP000004184; 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   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:UP000004184}.
FT   DOMAIN          1..147
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF12850"
SQ   SEQUENCE   164 AA;  18232 MW;  267D3926E59282E4 CRC64;
     MSDTHLPKRA RELPARLLAE LPRADVVFHA GDWVDTATLD LLEDRCRRLV AVYGNNDGPD
     LRARLPEVAH AELGGLRFGV IHETGPAQGR EKRCAARFPD LDVLVFGHSH IPWDTTAPTG
     LRLLNPGSPT DRRRQPHCTY MTATVADGLL TDVELHRLPA RTPR
//
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