Endonuclease/Exonuclease/phosphatase family
| Endonuclease/Exonuclease/phosphatase family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the multifunctional DNA-repair enzyme exonuclease III.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Exo_endo_phos | ||||||||
| Pfam | PF03372 | ||||||||
| InterPro | IPR005135 | ||||||||
| PROSITE | PDOC00598 | ||||||||
| SCOP2 | 1ako / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 139 | ||||||||
| OPM protein | 1zwx | ||||||||
| CDD | cd08372 | ||||||||
| |||||||||
Endonuclease/Exonuclease/phosphatase family is a structural domain found in the large family of proteins including magnesium dependent endonucleases and many phosphatases involved in intracellular signaling.[2]
Examples[edit]
- AP endonuclease proteins EC 4.2.99.18,
- DNase I proteins EC 3.1.21.1,
- Synaptojanin, an inositol-1,4,5-trisphosphate phosphatase EC 3.1.3.56
- Sphingomyelinase EC 3.1.4.12
- Nocturnin, an NADPH 2' phosphatase[3]
Subfamilies[edit]
Human proteins containing this domain[edit]
2'-PDE; 2-PDE; ANGEL1; ANGEL2; APEX1; APEX2; CCRN4L; CNOT6; CNOT6L; DNASE1; DNASE1L1; DNASE1L2; DNASE1L3; INPP5A; INPP5B; INPP5D; INPP5E; INPPL1; KIAA1706; OCRL; PIB5PA; SKIP; SMPD2; SMPD3; SYNJ1; SYNJ2; TTRAP; Nocturnin;
Notes[edit]
- ^ Mol CD, Kuo CF, Thayer MM, Cunningham RP, Tainer JA (March 1995). "Structure and function of the multifunctional DNA-repair enzyme exonuclease III". Nature. 374 (6520): 381–6. doi:10.1038/374381a0. PMID 7885481. S2CID 4335526.
- ^ Dlaki M (2000). "Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases". Trends Biochem. Sci. 25 (6): 272–273. doi:10.1016/S0968-0004(00)01582-6. PMID 10838565.
- ^ Estrella MA, Du J, Chen L, Rath S, Prangley E, Chitrakar A, Aoki T, Schedl P, Rabinowitz J, Korennykh A (May 2019). "The metabolites NADP+ and NADPH are the targets of the circadian protein Nocturnin (Curled)". Nature Communications. 10 (1): 2367. doi:10.1038/s41467-019-10125-z. PMC 6542800. PMID 31147539.
- "Circadian clock and fat metabolism linked through newly discovered mechanism". ScienceDaily (Press release). May 30, 2019.
References[edit]
- Dlakić M (June 2000). "Functionally unrelated signalling proteins contain a fold similar to Mg2+-dependent endonucleases". Trends Biochem. Sci. 25 (6): 272–3. doi:10.1016/S0968-0004(00)01582-6. PMID 10838565.
- Mol CD, Kuo CF, Thayer MM, Cunningham RP, Tainer JA (March 1995). "Structure and function of the multifunctional DNA-repair enzyme exonuclease III". Nature. 374 (6520): 381–6. doi:10.1038/374381a0. PMID 7885481. S2CID 4335526.
- Lahm A, Suck D (December 1991). "DNase I-induced DNA conformation. 2 A structure of a DNase I-octamer complex". J. Mol. Biol. 222 (3): 645–67. doi:10.1016/0022-2836(91)90502-W. PMID 1748997.
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