Q8IBK1 · Q8IBK1_PLAF7

Function

function

5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Function5'-3' DNA exonuclease activity
Molecular Function5'-3' exonuclease activity
Molecular Function5'-flap endonuclease activity
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Biological ProcessDNA recombination
Biological Processmismatch repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Exonuclease 1
  • EC number

Gene names

    • ORF names
      PF3D7_0725000

Organism names

  • Taxonomic identifier
  • Strain
    • Isolate 3D7
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)

Accessions

  • Primary accession
    Q8IBK1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)228PTMeXchangePhosphotyrosine
Modified residue (large scale data)230PTMeXchangePhosphothreonine
Modified residue (large scale data)308PTMeXchangePhosphoserine
Modified residue (large scale data)506PTMeXchangePhosphothreonine
Modified residue (large scale data)521PTMeXchangePhosphothreonine
Modified residue (large scale data)536PTMeXchangePhosphothreonine
Modified residue (large scale data)566PTMeXchangePhosphoserine
Modified residue (large scale data)568PTMeXchangePhosphoserine
Modified residue (large scale data)769PTMeXchangePhosphoserine
Modified residue (large scale data)789PTMeXchangePhosphoserine
Modified residue (large scale data)848PTMeXchangePhosphothreonine
Modified residue (large scale data)890PTMeXchangePhosphoserine
Modified residue (large scale data)922PTMeXchangePhosphoserine
Modified residue (large scale data)938PTMeXchangePhosphoserine
Modified residue (large scale data)998PTMeXchangePhosphoserine
Modified residue (large scale data)1041PTMeXchangePhosphoserine
Modified residue (large scale data)1049PTMeXchangePhosphothreonine
Modified residue (large scale data)1082PTMeXchangePhosphoserine
Modified residue (large scale data)1152PTMeXchangePhosphothreonine
Modified residue (large scale data)1165PTMeXchangePhosphoserine
Modified residue (large scale data)1168PTMeXchangePhosphoserine
Modified residue (large scale data)1182PTMeXchangePhosphoserine
Modified residue (large scale data)1202PTMeXchangePhosphoserine
Modified residue (large scale data)1266PTMeXchangePhosphoserine
Modified residue (large scale data)1285PTMeXchangePhosphoserine
Modified residue (large scale data)1293PTMeXchangePhosphoserine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-99XPG N-terminal
Domain142-210XPG-I
Region279-306Disordered
Compositional bias283-304Basic residues
Region477-534Disordered
Compositional bias483-534Basic and acidic residues
Region1030-1056Disordered
Compositional bias1036-1056Polar residues

Sequence similarities

Belongs to the XPG/RAD2 endonuclease family. EXO1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,347
  • Mass (Da)
    157,929
  • Last updated
    2003-03-01 v1
  • Checksum
    EA51A65CD219F778
MGISNLLQFLKPIIKNSHISKYKNEVVGVDIMCWIHRGLISCAYDIVTDQYNDSYLNFIEKMLVPIYNHNIKVVFVFDGEELPEKKKENMIRKNRREKAKMELQEIISKVKNPRTNEMVLKKCIQAISVSKEIIDSVKEFCRKKNIDYIISPYEADAQLSYLCRMGFISCAISEDSDLLVYGCPRVLYKLKNTGECNEISLMPINDLIDWNVINKIKNPLSNSYNEFYITPIKKLQNSDDYDSDISLDEETSVECINNDSYVQNNNEFINISKKTKSIVNSNNNNKKKKKKKNKNKKKTNKKKNMQKSKCDNIIKQYIQQFDWPEELFKLQYFNIDMFLTMCVLSGCDYSNDFHITGMGIKTAYNLIFQHKNIENIFHFLISNDRWRNKIPENLNTFDKLMNTFQKIKNAFLNHQVYDFILRKNIPINESFKSSFVNKNSHFIIQQITEASLLYDPLLKIDNCLNIYPQLNDIPLSSPQIQDDDYNKNDDTHNKGGDDNIKINHDTHNKGGDDNFKINHDTHNKGGDDNFKINHDTHNKGGDNFNINTVNCSFYNNHQIYTQSSKSPSFENIFKDFTSECFEYLEISPPAFIDPQNNNIQNNSKNEYFHNIITQEQVIQQADVCPPLIHKDTNISNEINDEYHHLISDITYNEYKNKTIENCNERINKRKTDDCISSFNLKKKVKTTSAHTSSSNSQDNLTIQHIEALDCNNQNVNDNEEKKNIYENSCNYDETFNSERVNILSMYDNNYQMWEKKDDLLKNNNNSFHSNNIMETYNDHYINKTYDEHSNNKVNINICDDITTTNNDHNEEMLDEKKEFAQIKSAKNIYENMKKNFFLFKTLNEDMNTPIKSLNVKGKMNMQDNCEQDDKVGNLKSDKMTEQNEKCDNISNEKCDNILNDKCDNILNDKCDNILNDKCDNISNEKCDNILNDKCDNISNEKCDNVPNDICDYVPNDICDYVPNNTPNLITNCIQNKMTTLLQITEENSLNSYNKNDTSFNKDFHINKTYLNKKDTEINFQINEKKKNDLLRNPLEESRKSSLTSYKNKTPSKNVNSKSQLRITSFFKRIDKKTNENHNMHNSTQKICNDHNNNPNDNIQNDKFYNNIYMNSPINYSVEYSEEDYINSFNDNYSDMKTFQKLKKKTKRNIKNTPQSYSIKDHFAVSLQSQDKNDKLSFTNYNSLEKDIFLNQGEKELQFNHNSINKEKNQNKHLQISSLTNHDNIIMNNHTSNLNTQQNEKQSSNHNTIIIHSNNHQPNFTNENVKSNNVSTEQDTYNKHITVLKSTEKLQNQSIEKNKETSQKINVEYILQNLNYNYQPKNQKINTFDYFKEKENVNHCNPYIDHNL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias283-304Basic residues
Compositional bias483-534Basic and acidic residues
Compositional bias1036-1056Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL844506
EMBL· GenBank· DDBJ
CAD50999.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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