Detail Information for IndEnz0002012655
IED ID IndEnz0002012655
Enzyme Type ID protease012655
Protein Name DNA-dependent metalloprotease WSS1
EC 3.4.24.-
DNA damage response protein WSS1
SUMO-dependent isopeptidase WSS1
Weak suppressor of SMT3 protein 1
Gene Name WSS1 YHR134W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MKTEGIKSPSAKYHDMAGSQRIPHKNPHIQKVAVLQSKPNKEDALNLIKEIAHKVSYLMKENHFKVTNLVEFYPRDQRLLGMNVNHGSKIMLRLRCSTDEFQFLPMECIMGTMLHELTHNLFGPHDKKFYNKLDELIGRQWVIEQRGLYDTFLGNGQRLGGRANLRSNRYPMTGISTNTGIVRKRGKGVKLGSLHPEGISSIDRGNSPRELAAFAAERRYRDDRWCGETKNNKDQIISDNISSSLEVVILDDDDEVLPGDTLIEVIDLT
Enzyme Length 269
Uniprot Accession Number P38838
Absorption
Active Site ACT_SITE 116; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation ACTIVITY REGULATION: Inactivated by EDTA. {ECO:0000269|PubMed:24998930}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Metalloendopeptidase that acts selectively on DNA-binding proteins. DNA is needed to bring the protease and substrates together to enable proteolysis. Involved in the repair of toxic DNA-protein cross-links (DPCs) such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesions or DPCs induced by reactive compounds such as formaldehyde. Involved in DNA damage response and processing of stalled or collapsed replication forks by removing the covalently trapped TOP1 from chromatin. DPC proteolysis enables the repair of the lesions via downstream DNA repair pathways. May be recruited to DPCs via the SUMOylation of substrate proteins at damaged DNA sites. {ECO:0000269|PubMed:11606525, ECO:0000269|PubMed:11606770, ECO:0000269|PubMed:15598824, ECO:0000269|PubMed:18085829, ECO:0000269|PubMed:20516210, ECO:0000269|PubMed:24998930}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Domain (1); Metal binding (3); Motif (4); Mutagenesis (3); Region (2)
Keywords DNA damage;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18336552}. Note=Present in a single sharp spot near the nuclear membrane, distinct from the spindle pole bodies and nucleolus. In dividing cells, the spot is exclusively present in the mother cell.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10688190; 12402242; 15590687; 17323081; 17360454; 17696614; 17923678; 18562670; 18719252; 19536198; 20429770; 23357952; 25496645; 26130008; 26349035; 27852435; 31276951;
Motif MOTIF 152..160; /note=SHP box; MOTIF 209..219; /note=VCP-interaction motif (VIM); /evidence=ECO:0000269|PubMed:24998930; MOTIF 247..254; /note=SUMO interaction motif 1 (SIM); /evidence=ECO:0000269|PubMed:24998930; MOTIF 266..269; /note=SUMO interaction motif 2 (SIM); /evidence=ECO:0000269|PubMed:24998930
Gene Encoded By
Mass 30,627
Kinetics
Metal Binding METAL 115; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 119; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 125; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Rhea ID
Cross Reference Brenda