A0A7S0ZBA2 · A0A7S0ZBA2_9RHOD

Function

function

Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.

Catalytic activity

  • Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
    EC:3.1.4.1 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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 Componentnucleus
Molecular Function5'-3' exonuclease activity
Molecular Function5'-flap endonuclease activity
Molecular Functionflap-structured DNA binding
Molecular Functionmetal ion binding
Biological Processinterstrand cross-link repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fanconi-associated nuclease
  • EC number

Gene names

    • ORF names
      TOLI1172_LOCUS895

Organism names

  • Taxonomic identifier
  • Strain
    • CCMP3278
  • Taxonomic lineage
    Eukaryota > Rhodophyta > Bangiophyceae > Porphyridiales > Porphyridiaceae > Timspurckia

Accessions

  • Primary accession
    A0A7S0ZBA2

Subcellular Location

Keywords

  • Cellular component

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain684-803VRR-NUC

Sequence similarities

Belongs to the FAN1 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    814
  • Mass (Da)
    92,076
  • Last updated
    2021-06-02 v1
  • Checksum
    A77AA60F89B95B7C
EWRGSMGGLNGRGILHQLKNASNTKNVDSERMKRCNGASKSKVQCPLCGLGNISSLLINQHVDDCLRRSEVSQSTRKQSLSQPLPVYSSILDDPFNICKTHSVSINPEQESIELLEYCALDESLDELNRLCIENSAYYMRSFLKVLAFCRKNEHLFGQEQSGMISVFLALSESAKRLFVRLFRRKEGAWFRIDNLVLKYPEIESMNDAVNELCQDFNNSTSFLQTANNFVQKTLLQSALDLTQQDRVQINPPVDNIDQFLHSILLVLSESELHELAKVALLSNNVERKKSKSVSMLRSRLIQKVRSESKQKTCQGSPVLSVILRQLYKQSVCGALVRVNPQIAHVFREMHALYHPVGGADSTQLILAECGKLKYHAVRCSRSPLFPNRAQFLEYLNARECSQRIDTLVLTRGPESEILRLADTAESLLLAQLESGEQNAQQHQTKMCADRYRASYHYANALWHSVKVLEKLGHYDRAIERLRILLRTKVLPLKRGKFFDRLSIDLHQHKNLLNESLEVCLEGISLEERVHTRRGDLLALARRAVRLWKKIHRDMDIPDVIGRVVFCDTAAWAIIPTRKIVGRPLDCRKETGKSSGFLGLNEQVVGVEELCLQSYGQQGWIGVHCEGTMVTSLFGLLMWDIIFCDSVDIVFQTSVQDAPLDLGDPQFYKRREASIDAQLNRLALLTVAEIALCTKQSLEDHEQVQCRGVSWSLIESVDVCYIAGCIGGRSLAHMFRLLCLDYDYWSGGFPDLTMWKPASDSSASNLAMFVEVKGPRDQLSDRQRAWMHELLAVGCSAEVCRVVEPSSRVVLADES

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HBFP01001238
EMBL· GenBank· DDBJ
CAD8816507.1
EMBL· GenBank· DDBJ
Transcribed RNA

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