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 |