P12000 · DNLI1_SCHPO
- ProteinDNA ligase 1
- Genecdc17
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids768 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic activity
Cofactor
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 165 | Interaction with target DNA | ||||
Sequence: R | ||||||
Binding site | 414 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 416 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 421 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 437 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 438 | Interaction with target DNA | ||||
Sequence: N | ||||||
Binding site | 469 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 568 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 573 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 587 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 593 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 619 | Interaction with target DNA | ||||
Sequence: K | ||||||
Site | 644 | Interaction with target DNA | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nuclear replication fork | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA ligase (ATP) activity | |
Molecular Function | DNA ligase activity | |
Molecular Function | metal ion binding | |
Biological Process | base-excision repair | |
Biological Process | cell division | |
Biological Process | DNA biosynthetic process | |
Biological Process | DNA ligation | |
Biological Process | DNA recombination | |
Biological Process | DNA repair | |
Biological Process | lagging strand elongation | |
Biological Process | mitochondrial DNA metabolic process | |
Biological Process | nucleotide-excision repair | |
Biological Process | Okazaki fragment processing involved in mitotic DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA ligase 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionP12000
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059585 | 1-768 | DNA ligase 1 | |||
Sequence: MRTVFSQIPRFKQVNQYIRMSTRQSDISNFFISSASHKSEHVEVSQSSSDSKNVDGRSTSEKRKVESVKLVDESKHNNHDDTGTQNVERENNIVSEAKKQKTLGSSSSSSDAVSSNNDSGASTPIPLPIKEPPLESNARNDKLKGHATFAEMVKAFTKIENTSKRLEIIDIMGTYFFGILRDHPSDLLACVYLSINKLGPDYSGLELGIGESIIMKAIGESTGQTLQQIKLSFHKVGDLGLVAQTSRQNQPTMFKPAALTIPFLFDSLKKIAQMSGNQSQNRKIGVIKRLLSSCEGAEPKYLIRALEGKLRLQLAEKTILVALANATAQYHADKNGEKLSQQDRIEGEQILRDVYCQLPSYDLIVPHLIEHGLGTLRETCKLTPGIPTKPMLAKPTKQISEVLNTFDQAAFTCEYKYDGERAQVHFTEDGKFYVFSRNSENMSVRYPDISVSVSKWKKPDARSFILDCEAVGWDRDENKILPFQKLATRKRKDVKIGDIKVRACLFAFDILYLNGQPLLETPLNERRKLLYSMFQPSTGDFTFAKHSDQKSIESIEEFLEESVKDSCEGLMVKMLEGPDSHYEPSKRSRHWLKVKKDYLSGVGDSLDLIVIGAYYGKGKRTSVYGAFLLGCYDPDTETVQSICKLGTGFSEEHLETFYNQLKDIVISKKKDFYAHSDVPAHQPDVWFEPKYLWEVLAADLSLSPVYKAAIGYVQEDKGISLRFPRFIRIREDKSWEDATTSEQVSEFYRSQVAYSQKEKEGSPAAEDY |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 42-139 | Disordered | ||||
Sequence: VEVSQSSSDSKNVDGRSTSEKRKVESVKLVDESKHNNHDDTGTQNVERENNIVSEAKKQKTLGSSSSSSDAVSSNNDSGASTPIPLPIKEPPLESNAR | ||||||
Compositional bias | 55-96 | Basic and acidic residues | ||||
Sequence: DGRSTSEKRKVESVKLVDESKHNNHDDTGTQNVERENNIVSE | ||||||
Compositional bias | 97-123 | Polar residues | ||||
Sequence: AKKQKTLGSSSSSSDAVSSNNDSGAST | ||||||
Region | 309-318 | Interaction with target DNA | ||||
Sequence: KLRLQLAEKT | ||||||
Region | 490-492 | Interaction with target DNA | ||||
Sequence: KRK |
Sequence similarities
Belongs to the ATP-dependent DNA ligase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length768
- Mass (Da)86,581
- Last updated1989-10-01 v1
- Checksum6783FF3DDC675F31
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 55-96 | Basic and acidic residues | ||||
Sequence: DGRSTSEKRKVESVKLVDESKHNNHDDTGTQNVERENNIVSE | ||||||
Compositional bias | 97-123 | Polar residues | ||||
Sequence: AKKQKTLGSSSSSSDAVSSNNDSGAST |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X05107 EMBL· GenBank· DDBJ | CAA28754.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CU329670 EMBL· GenBank· DDBJ | CAB08176.2 EMBL· GenBank· DDBJ | Genomic DNA |