O16810 · ORC1_DROME

Function

function

Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.

Features

Showing features for binding site.

1924100200300400500600700800900
TypeIDPosition(s)Description
Binding site564ATP (UniProtKB | ChEBI)
Binding site598-606ATP (UniProtKB | ChEBI)
Binding site684Mg2+ (UniProtKB | ChEBI)
Binding site685ATP (UniProtKB | ChEBI)
Binding site685Mg2+ (UniProtKB | ChEBI)
Binding site718ATP (UniProtKB | ChEBI)
Binding site784ATP (UniProtKB | ChEBI)

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 Componentnuclear origin of replication recognition complex
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionchromatin binding
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Biological ProcessDNA amplification
Biological ProcessDNA replication initiation
Biological Processmitotic DNA replication checkpoint signaling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Origin recognition complex subunit 1
  • Short names
    DmORC1

Gene names

    • Name
      Orc1
    • ORF names
      CG10667

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    O16810
  • Secondary accessions
    • Q9V4N1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00001270691-924Origin recognition complex subunit 1
Modified residue293Phosphoserine
Modified residue368Phosphoserine
Modified residue419Phosphothreonine
Modified residue426Phosphoserine
Modified residue430Phosphoserine
Modified residue533Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

ORC is composed of six subunits.

Complex viewer

View interactors in UniProtKB
View CPX-2369 in Complex Portal

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

Type
IDPosition(s)Description
Domain45-187BAH
Compositional bias196-237Basic and acidic residues
Region196-239Disordered
Region377-440Disordered
Compositional bias412-437Polar residues
Compositional bias460-485Basic and acidic residues
Region460-523Disordered
Compositional bias491-521Polar residues

Sequence similarities

Belongs to the ORC1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    924
  • Mass (Da)
    103,281
  • Last updated
    2001-02-21 v2
  • Checksum
    AACD002DEB10A136
MVNKENARSVGQQVKWIGSQDELPPVKNLEHKNVYFYQKCIYGPLTLSVGDFILVSNADAAEPDTVSGCDVARILHMYELRELTDREPCRAIVQWYSWPKAIPHNKYDDDEVAIDFSLEVIEEHRPYDNDVALGAIYRKCIVLEGTSKTSAEEILKRHANKLKSTACPMFVSRYRFVKVKRSYRLIPLEIHLEQPEDNARPTRSSRKSLTAHRESKRSISARHDDTAGNKGSSVEKRRRASMAASSSVEFIDVNSFICENKVSPIKIVGGRSVVRLSEKKNAPEINANYLPASPLTEKNAKVETPKSRASAARRNLNLSLDRGADTTADSDCLNYSIVQQTPDPKTPSNDMKIKLRLSERRRSVRLASMDVDPLSLEEAVQEPNAQGRKRLGVANGDIYHTPTKKSKEPLESAAATEQTPSTRRKSILKSATSRLAEGTPRRSIHLSNIVEQRVFEDDEIISTPKRGRSKKTVQDNDEDYSPKKSVQKTPTRTRRSSTTTKTATTPSKGITTATATPMTPSQKMKKIRAGELSPSMQQRTDLPAKDSSKSELQLAREQLHVSVVPKSLPCREREFENIYAFLEGKIQDQCGGCMYVSGVPGTGKTATVTGVIRTLQRMAKQNELPAFEYLEINGMRLTEPRQAYVQIYKQLTGKTVSWEQAHALLEKRFTTPAPRRVTTVLLVDELDILCNRRQDVVYNLLDWPTKSAAKLVVVTIANTMDLPERLLMGKVTSRLGLTRLTFQPYSHKQLQEIVTARLGGSETFKGEAVQLVARKVAAVSGDARRALDICRRATEIADTAAVKCVTMLHVQQALAEMIASAKVQAIRNCSRMEQIFLQAIAAEVTRTGVEETTFMGVYQQVETIAAFMGVTFPPPGRALRLCSKLGAERLIISEHSRNDLFQKILLNVSADDIHYALRVEEMVN

Features

Showing features for sequence conflict, compositional bias.

Type
IDPosition(s)Description
Sequence conflict159in Ref. 1; AAC47802
Compositional bias196-237Basic and acidic residues
Compositional bias412-437Polar residues
Compositional bias460-485Basic and acidic residues
Compositional bias491-521Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF017647
EMBL· GenBank· DDBJ
AAC47802.1
EMBL· GenBank· DDBJ
mRNA
AE013599
EMBL· GenBank· DDBJ
AAF59236.1
EMBL· GenBank· DDBJ
Genomic DNA
AY094780
EMBL· GenBank· DDBJ
AAM11133.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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