Detail Information for IndEnz0010000807
IED ID IndEnz0010000807
Enzyme Type ID esterase000807
Protein Name CRISPR-associated endonuclease Cas3-HD
EC 3.1.-.-
Gene Name cas3 cas3'' SSO2001
Organism Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Taxonomic Lineage cellular organisms Archaea TACK group Crenarchaeota Thermoprotei Sulfolobales Sulfolobaceae Saccharolobus Saccharolobus solfataricus (Sulfolobus solfataricus) Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Enzyme Sequence MIKPCAYEKQGLIDHAIGSYRVLDGKISESYYKIISRRLERYGIVLDLNGVKEMVKDVVVLHDMGKAGEYYQNQFDDNCNPLKSNFSFIYHELGSALFFYYDYEPIDVEKAEEVKSLLTLAVLNHLNAIRVISDYLVNKFPDNFDERMIKLNKYGSIMLQNLRGVISKSLKVRDYTFDDYHDMLYAFSKKSDKYLKLYNLFLAPIMLGDNLDSSLVRNNGSKTGFVRILEGELNGGSTL
Enzyme Length 239
Uniprot Accession Number Q97WW0
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.-.-
Enzyme Function FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Acts as a dsDNA and dsRNA endonuclease (in a fusion with Alicyclus caldarius esterase to increase solubility). {ECO:0000269|PubMed:19174159}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Expressed as a fusion protein to increase stability. {ECO:0000269|PubMed:19174159};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3 and 7-8. Expressed as a fusion protein to increase stability. {ECO:0000269|PubMed:19174159};
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Metal binding (2); Mutagenesis (3)
Keywords Antiviral defense;Endonuclease;Hydrolase;Magnesium;Metal-binding;Nuclease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 27,515
Kinetics
Metal Binding METAL 63; /note=Magnesium; /evidence=ECO:0000250; METAL 92; /note=Magnesium; /evidence=ECO:0000255
Rhea ID
Cross Reference Brenda 3.1.99.B5;