P87154 · DPOE_SCHPO

Function

function

DNA polymerase II participates in chromosomal DNA replication.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.

Features

Showing features for binding site.

121992004006008001,0001,2001,4001,6001,8002,000
TypeIDPosition(s)Description
Binding site2069Zn2+ (UniProtKB | ChEBI)
Binding site2072Zn2+ (UniProtKB | ChEBI)
Binding site2104Zn2+ (UniProtKB | ChEBI)
Binding site2107Zn2+ (UniProtKB | ChEBI)
Binding site2138[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site2141[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site2153[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site2155[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromosome, telomeric repeat region
Cellular Componentepsilon DNA polymerase complex
Cellular Componentnuclear replication fork
Molecular Function4 iron, 4 sulfur cluster binding
Molecular FunctionDNA binding
Molecular FunctionDNA-directed DNA polymerase activity
Molecular Functionnucleotide binding
Molecular Functionsingle-stranded DNA 3'-5' DNA exonuclease activity
Molecular Functionzinc ion binding
Biological Processbase-excision repair, gap-filling
Biological ProcessCENP-A containing chromatin assembly
Biological Processchromatin organization
Biological ProcessCMG complex assembly
Biological ProcessDNA replication proofreading
Biological ProcessDNA strand elongation involved in mitotic DNA replication
Biological ProcessDNA-templated DNA replication
Biological Processleading strand elongation
Biological Processmitotic cell cycle
Biological Processmitotic DNA replication initiation
Biological Processmitotic DNA replication leading strand elongation
Biological Processnucleotide-excision repair, DNA gap filling
Biological Processpremeiotic DNA replication
Biological Processregulatory ncRNA-mediated heterochromatin formation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA polymerase epsilon catalytic subunit A
  • EC number
  • Alternative names
    • DNA polymerase II subunit A

Gene names

    • Name
      pol2
    • Synonyms
      cdc20
    • ORF names
      SPBC25H2.13c

Organism names

Accessions

  • Primary accession
    P87154
  • Secondary accessions
    • P78873

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000464641-2199DNA polymerase epsilon catalytic subunit A

Proteomic databases

PTM databases

Interaction

Subunit

Heterotetramer. Consists of 4 subunits: pol2, dpb2, dpb3 and dpb4 (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P87154raf2 O745602EBI-876811, EBI-904886

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for zinc finger, motif.

TypeIDPosition(s)Description
Zinc finger2069-2107CysA-type
Motif2138-2155CysB motif

Domain

The CysA-type zinc finger is required for PCNA-binding.
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.

Sequence similarities

Belongs to the DNA polymerase type-B family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,199
  • Mass (Da)
    252,887
  • Last updated
    1997-07-01 v1
  • Checksum
    A80A5D0865EEBC3E
MPLKTARGASKYQFRKFNGNYNGKSKSNGRTFAKSTEEVGFNDPMKIVYKKNEIDRMMGFDSYEGGQPREAWLLNVHPTVIESTKGNSTLSAVDFYFIQDDGDTFRCTIPYSPYFYIAAREGKEALVDDYLKKKFVGLIKSTTRIFKEDLQLKNHIVGYQKLYIKLVFDNLNDLQAVRKSLMSAVKANSSQQDAVDAYTNLSSENLNGIIENAFEDPLNHVLDIREYDVPYHSRTLIDLNIRVGQWYTVSYHEGHVQISLLASRIERAEPTIMAFDIETTKLPLKFPDSSFDKIMMISYMIDGQGFLITNREIISQNIEDFHYTPREEFEGPFIIFNEPDEVGLLHRFFKHIRSAKPSVIVTYNGDFFDWPFVDARAAFHGLNLTEETGFFRDAEDEYKSSYCSHMDAFRWVKRDSYLPQGSQGLKAVTVSKLGYNPIELDPELMTPYASEKPQVLAQYSVSDAVATYFLYMKYVHPFIFSLCNIIPLNPDEVLRKGTGTLCETLLTVEACTKNIILPNKHVDASQKFFDGHLLASETYVGGHVESLESGVFRSDLPTNFNMDPKVYEELILQLDKALDFSLTVENNVNVDEIENYEEVRDSILKKLSDLRDRPKRSEKPRIYHLDVASMYPNIMITNRLQPDSVKDESFCATCDLNVPNKTCDRRMVWAWRGEYYPAKKGEYHMIYSALQSERFPGPTPFSPFRSFQELSPSEQAAMVQKRIADYSRKVYHRLYDNTVIERETIICQKENSFYIDTVKSFRDRRYDFKGLQKKWVKQLAAIKEKGGLAEIEEAKKMVVLYDSLQLAHKVILNSFYGYVMRKGSRWYSIEMAGITCLTGATIIQMARQIVERAGRPLELDTDGIWCILPESFPENFEFKKKSGGKVFISYPCVMLNHLVHEKFTNHQYSALKDPEKLVYETTSENSIFFEVDGPYRAMILPASTEEGKNLKKRYAVFNFDGSLAELKGFEVKRRGELKLIKDFQSQIFKVFLKGDSLEECYQEVAYVADTWLEILFTKGSNLTDDELIELISENRSMSKALSEYGSQKSTSITTARRLADFLGDQMTKDKGLACRFIISASPKGRPVAERAVPVAIFFAEESVKRHFLRLWLKDNGLYDVDIRDIIDWDYYLKRLGSVVQKLISIPAALQRISNPVTRFPLPDWLQKRVAVLNSKYQQKKIDSIFSLAPTNPSTINNTKVTDIEDLGSVTHKDKRIVARVTKRKLLQQSGNSEAPVSFEVKPVSFMDGYSNWLKYAKKKWKYQKQVKLRRRHLIGFQSRQFTNVLQSSAEVMFENLWHILQIRETDVPGILHAWVIIRNRLTSIRFIVNRKFFVCFKDETLPNVEIEGCLIEKSNAILPHGSTSDKLFLLEIPEKSYLTEKVSISMIFAHPSVSGIYETRIEPIERLILEMGSRKRFNNSVPGALGKGFEFGFESKMFTDPSDNDVSYLDGVEMNYLYAFHFSISNRFVFSLFMPHLKKVEAIIYDKLPGSDMSFPSISKIYEELRSKFDNLIKESSIEYPDTLSCNVIFSGNERKAYKLIDEKLLQYFSTKTKNSLLIIESSLPHILKANVKQIEELPYIMIPRLESNIQSLSWKQHIATKMIQHFLAIGSWLFHRIQLSRFSDIPLCNFESDDIQYSIDVVYSRKLKEHNIILWWNKGPTPDLGGIEKDSILQIASPKDPLEVNNPGAYSNACVDISLSNLALCSILNSALINDIEGIGDMAALNDNYMTAINDDLEEKLGIHDNIGLTHSLPVLKALVKTWWNEAASGNNLADLIIQHLARWISSSKSYLYSPLLSSHVEVIMRKTFLQLLSEIKRLGAHIIHASANKILIKTSKLIVQNAVTYSNYLLKSIKTLPLFHFLDLNVTEYWDYLLWMDSVNYGGKMVAANFSATNEEPQTVVSWHIKSHLPPIIQPEFQSWIVEFIEEVYKQKLEKSNTKVGFVRVKNNNADEDSEIVGSGILKSKLIHPLKRKVAQVRRCFQELQLDENTREDLKFPKLPGSFLNYTDGALELVKSICAVFELSHDLNLEVRFLKKSLLSLLQIQEFSTQAVFRYPSRRLSLDQIPCKQCGVHQDFDLCLHEHLWPTRDDMGTLVFSDGWSCSSCNLVYDRWVFEETLVDNLYHQLTLYQLQDLICSKCKTVKQWSLKERCSCSGEWVLQLSPTKFREMLNVYQSVADFYEFSILQNSVQSILSVLN

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict2116-2126in Ref. 2; BAA13884
Sequence conflict2182in Ref. 2; BAA13884
Sequence conflict2196-2199in Ref. 2; BAA13884

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329671
EMBL· GenBank· DDBJ
CAB08772.1
EMBL· GenBank· DDBJ
Genomic DNA
D89223
EMBL· GenBank· DDBJ
BAA13884.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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