A0A7I8KLV8 · A0A7I8KLV8_SPIIN

Function

Catalytic activity

  • ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
    EC:6.5.1.1 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentDNA ligase IV complex
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA ligase (ATP) activity
Biological ProcessDNA biosynthetic process
Biological ProcessDNA ligation involved in DNA repair
Biological ProcessDNA recombination
Biological Processdouble-strand break repair via nonhomologous end joining
Biological Processnucleotide-excision repair, DNA gap filling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA ligase
  • EC number

Gene names

    • ORF names
      SI8410_06009418

Organism names

Accessions

  • Primary accession
    A0A7I8KLV8

Proteomes

Subcellular Location

Keywords

  • Cellular component

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain331-480ATP-dependent DNA ligase family profile
Region604-630Disordered
Domain650-738BRCT
Domain837-909BRCT
Region953-977Disordered
Compositional bias954-972Basic and acidic residues
Region1000-1047Disordered

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,047
  • Mass (Da)
    118,344
  • Last updated
    2021-04-07 v1
  • Checksum
    53E1B41A89B9E5AD
MSDETVRFSVVCAMFQAMLRDRSSAKKRKHLRTFLDRVFTARDRYFAALRLILPGLDRERGTYGVKEHALAACLVDALGISKDSEDAARLVNWRKGGPRSGANAGNFSLIATEVLQRRQGLASGGLTIKELNEALDQLASRESRGEKASVLSDLIKKTNSTEMKWILIIILKDLKLGISEKSIFHEFHPDAEDLFNVTCDLKLVCEKLKDRTQRHKRQDIEVGKAVRPQLALRVSDAATAWKKLHGKQVVVECKFDGDRIQIHKNGSDIRFFSRNFLDHSEYAPGMSSIVQHNILIDRCILDGEMLVWDTSTNRFAEFGSNQEIAKVAREGLETDRQLCYVAFDVLYAGDTSVIHQSLAERHALLQKVLRPVRGRLEILVPDGGLNNSRPLGEPCWSVVANTLDDVERFYKETIENRDEGIILKDLGSKWEPSDRSGKWLKLKPDYIHAGADLDVLIIGGYFGSGRRGGQVAQFLMGLSDSSTPDTHPRRFISFCRVGSGLSDEELDSLVNKLKPYFRKNEYPKKAPRFYEVTYNSKERPDVWVDSPDKSVILSITSDIRTIKSEVFAAPYSLRFPRIDRVRYDKPWHECLDVQSFVDLVHSSHGTTQSAQDRGTLQEHSKHEKVSKKGKNKIHVVPPHLTKTDISGIKEETLIFTDMMLYFVNIPSSSSIDYFHKLVAENGGTFSMNLNDSVTHCIAADKKGIKYRAAMRHGDIFHYSWVLDCCAQKRLLHLQPKYFLFVSESSKKKFQEEIDSYSDYYYWDIDLSDIKQIFANMAGSGGSSDLSRHQNKYCPSKRWRLLQDCRIFFHEASPDMDADHRAILQLALRRMKLEVNWHGGQVSGDLSGATHLVAYSAPPSSERLFGTIYDSCSPGERRLLHSRRLHVVDHSWLEESLVNEERLPEDHFSLRPDTFEGFEKTRYYLGTIGGKFGNFSSSFFVLCSALVWGPPPVEGAEEPRKRGGGDARPAARRTRRRMVTSAAKVHSGEWEGDDILHVAEEKRDSVDDPLPAMLQLPSLQGNRSPSPAGGAKRKVSYKEAAAQLLGDP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias954-972Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR746269
EMBL· GenBank· DDBJ
CAA7398753.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp