| IED ID | IndEnz0002003631 |
| Enzyme Type ID | protease003631 |
| Protein Name |
Abasic site processing protein HMCES Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein ES cell-specific 5hmC-binding protein Peptidase HMCES EC 3.4.-.- SRAP domain-containing protein 1 |
| Gene Name | hmces srapd1 TGas027m07.1 |
| Organism | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Silurana Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Enzyme Sequence | MCGRTACTLAPDDVRKACTYRDKQGGRKWPNWRDGDSDKYQPSYNKSPQSNSPVLLSLKHFQKDADSSERVLAAMRWGLIPSWFNEPDPSKMQYKTNNCRSDTMTEKALYKASLFKGKRCVVLADGFYEWQRQNSEKQPYYIYFPQIKAEKSPAEQDITDWNGQRLLTMAGLFDCWEPPNGGETLYSYTVITVDSSKTMNWIHDRMPAILDGDEAVRKWLDFGEVPTKDALKLIHPIENITYHPVSTVVNNSRNNTPECMAAIILTQKKGPALSASSKKMLDWLQNKSPKKEESHSIQSPKLSQFGAPPKKTSAGLMQQWLKKEDGEPSPKRAKK |
| Enzyme Length | 335 |
| Uniprot Accession Number | Q6P7N4 |
| Absorption | |
| Active Site | ACT_SITE 2; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q96FZ2 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Acts as an enzyme that recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue. The HMCES DNA-protein cross-link is then degraded by the proteasome. Promotes error-free repair of abasic sites by acting as a 'suicide' enzyme that is degraded, thereby protecting abasic sites from translesion synthesis (TLS) polymerases and endonucleases that are error-prone and would generate mutations and double-strand breaks. Has preference for ssDNA, but can also accommodate double-stranded DNA with 3' or 5' overhang (dsDNA), and dsDNA-ssDNA 3' junction (By similarity). Acts as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). {ECO:0000250|UniProtKB:Q8R1M0, ECO:0000250|UniProtKB:Q96FZ2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Initiator methionine (1); Modified residue (1); Region (2); Site (2) |
| Keywords | Autocatalytic cleavage;Chromosome;Covalent protein-DNA linkage;DNA damage;DNA-binding;Hydrolase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q96FZ2}. Note=Recruited to chromatin following DNA damage. Localizes to replication forks. {ECO:0000250|UniProtKB:Q96FZ2}. |
| Modified Residue | MOD_RES 2; /note=Thiazolidine linkage to a ring-opened DNA abasic site; /evidence=ECO:0000250|UniProtKB:Q96FZ2 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 38,164 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |