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Entry version 153 (17 Jun 2020)
Sequence version 3 (01 Oct 2002)
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Protein

DNA polymerase epsilon catalytic subunit 1

Gene

DNApol-epsilon255

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalytic component of the DNA polymerase epsilon complex (PubMed:15135399). Participates in chromosomal DNA replication (PubMed:15135399). Required during synthesis of the leading DNA strands at the replication fork, binds at/or near replication origins and moves along DNA with the replication fork (By similarity). Has 3'-5' proofreading exonuclease activity that corrects errors arising during DNA replication (PubMed:15135399). Has a role in the G1-S transition and/or S-phase progression of the mitotic cycle and endocycle progression (PubMed:11054539, PubMed:15135399, PubMed:21898761). Involved in DNA synthesis during DNA repair (By similarity). Plays roles in larval tissue development (PubMed:22245183, PubMed:21898761).By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] clusterBy similarity, Mg2+1 Publication, Mn2+1 PublicationNote: Binds 1 [4Fe-4S] cluster.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by the small molecule aphidicolin (PubMed:15135399). Activity is markedly inhibited by manganese ions (PubMed:15135399).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 7.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi2113ZincBy similarity1
Metal bindingi2116ZincBy similarity1
Metal bindingi2141ZincBy similarity1
Metal bindingi2144ZincBy similarity1
Metal bindingi2175Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2178Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2190Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2192Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri2113 – 2144CysA-typeBy similarityAdd BLAST32

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Hydrolase, Nucleotidyltransferase, Transferase
Biological processDNA replication
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-110314 Recognition of DNA damage by PCNA-containing replication complex
R-DME-174430 Telomere C-strand synthesis initiation
R-DME-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-DME-5656169 Termination of translesion DNA synthesis
R-DME-5696400 Dual Incision in GG-NER
R-DME-6782135 Dual incision in TC-NER
R-DME-68952 DNA replication initiation
R-DME-68962 Activation of the pre-replicative complex

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA polymerase epsilon catalytic subunit 1Curated (EC:2.7.7.71 Publication)
Alternative name(s):
3'-5' exodeoxyribonucleaseCurated (EC:3.1.11.-1 Publication)
DNA polymerase epsilon 255kD subunitImported
DNA polymerase epsilon catalytic subunitUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DNApol-epsilon255Imported
Synonyms:DNApol-epsilonImported, DNApolE1Curated, l(3)pl101 PublicationImported, l(3)pl10RImported, PolepsilonImported
ORF Names:CG6768Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3R

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0264326 DNApol-epsilon255

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown in the eye disks induces a small eye phenotype and inhibits DNA synthesis (PubMed:22245183). RNAi-mediated knockdown in the salivary glands results in a reduction of salivary glands size together with decreased number and size of nuclei in the tissue (PubMed:22245183). Also causes endoreplication defects (PubMed:22245183).1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004482581 – 2236DNA polymerase epsilon catalytic subunit 1Add BLAST2236

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9VCN1

PRoteomics IDEntifications database

More...
PRIDEi
Q9VCN1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in salivary glands (at protein level).1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in embryos (at protein level) (PubMed:11054539). Expressed at various developmental stages (PubMed:11054539).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0264326 Expressed in embryo and 19 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9VCN1 differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9VCN1 DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the DNA polymerase epsilon complex consisting of four subunits: the catalytic subunit DNApol-epsilon255/DNApolE1 and the accessory subunits DNApol-epsilon58/DNApolE2, Chrac-14/DNApolE3 and Mes4/DNApolE4.

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q9VCN1, 7 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0083800

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9VCN1

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi2175 – 2192CysB motifBy similarityAdd BLAST18

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for maintenance of the complex.By similarity
The C-terminal domain (1001-2236 aa) is required for mitotic DNA replication in the eye but not for DNA endoreplication in salivary glands.1 Publication
The CysA-type zinc finger is required for PCNA-binding.By similarity
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DNA polymerase type-B family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2113 – 2144CysA-typeBy similarityAdd BLAST32

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1798 Eukaryota
COG0417 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000010194

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000556_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9VCN1

KEGG Orthology (KO)

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KOi
K02324

Identification of Orthologs from Complete Genome Data

More...
OMAi
VYDLDMK

Database of Orthologous Groups

More...
OrthoDBi
39650at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9VCN1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.132.60, 1 hit
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR042087 DNA_pol_B_C
IPR013697 DNA_pol_e_suA_C
IPR029703 POL2
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10670 PTHR10670, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08490 DUF1744, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01159 DUF1744, 1 hit
SM00486 POLBc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53098 SSF53098, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9VCN1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDSSKGKVL QNTGKFVSEN RTEGDDFFNE AGYRQSREND KIDSKYGFDR
60 70 80 90 100
VKDSQERTGY LINMHSNEVL DEDRRLIAAL DLFFIQMDGS RFKCTVAYQP
110 120 130 140 150
YLLIRPEDNM HLEVARFLGR KYSGQISGLE HITKEDLDLP NHLSGLQQQY
160 170 180 190 200
IKLSFLNQTA MTKVRRELMS AVKRNQERQK SNTYYMQMLA TSLAQSSAGS
210 220 230 240 250
EDATLGKRQQ DYMDCIVDIR EHDVPYHVRV SIDLRIFCGQ WYNIRCRSGV
260 270 280 290 300
ELPTITCRPD ILDRPEPVVL AFDIETTKLP LKFPDAQTDQ VMMISYMIDG
310 320 330 340 350
QGYLITNREI ISSNVDDFEY TPKPEFEGNF IVFNEENEMQ LLQRFFDHIM
360 370 380 390 400
EVRPHIIVTY NGDFFDWPFV ETRAAVYDLD MKQEIGFSKL RDGNYLSRPA
410 420 430 440 450
IHMDCLCWVK RDSYLPVGSQ GLKAVAKAKL RYDPVELDPE DMCRMAVEQP
460 470 480 490 500
QVLANYSVSD AVATYYLYMK YVHPFIFALN TIIPMEPDEI LRKGSGTLCE
510 520 530 540 550
TLLMVEAYHA QIVYPNKHQS ELNKLSNEGH VLDSETYVGG HVEALESGVF
560 570 580 590 600
RADIPCRFRL DPAMVKQLQE QVDAVLRHAI EVEEGIPLEK VLNLDEVRQE
610 620 630 640 650
IVQGLQGLHD IPNRLEQPVI YHLDVGAMYP NIILTNRLQP SAMVSDLDCA
660 670 680 690 700
ACDFNKPGVR CKRSMDWLWR GEMLPASRNE FQRIQQQLET EKFPPLFPGG
710 720 730 740 750
PQRAFHELSK EDQAAYEKKR LTDYCRKAYK KTKLTKLETR TSTICQKENS
760 770 780 790 800
FYVDTVRAFR DRRYEYKGLT KVAKASVNAA VASGDAAEIK AAKGREVLYD
810 820 830 840 850
SLQLAHKCIL NSFYGYVMRR GARWHSMPMA GIVCLTGSNI ITKAREIIER
860 870 880 890 900
VGRPLELDTD GIWCILPGSF PQEFTIHTSH EKKKKINISY PNAVLNTMVK
910 920 930 940 950
DHFTNDQYHE LRKDKENNLP KYDIRDENSI FFEVDGPYLA MVLPAAKEEG
960 970 980 990 1000
KKLKKRYAVF NFDGTLAELK GFEVKRRGEL QLIKNFQSSV FEAFLAGSTL
1010 1020 1030 1040 1050
EECYASVAKV ADYWLDVLYS RGSNLPDSEL FELISENKSM SKKLEEYGAQ
1060 1070 1080 1090 1100
KSTSISTAKR LAEFLGEQMV KDAGLACKYI ISKKPEGAPV TERAIPLAIF
1110 1120 1130 1140 1150
QSEPSVRRHH LRRWLKDNTM GDADIRDVLD WNYYIERLGG TIQKIITIPA
1160 1170 1180 1190 1200
ALQGLANPVP RVQHPDWLHK KMLEKNDVLK QRRINEMFTS RPKPKPLATE
1210 1220 1230 1240 1250
EDKLADMEDL AGKDGGEGAA GCPIVTKRKR IQLEEHDDEE AQPQATTWRQ
1260 1270 1280 1290 1300
ALGAPPPIGE TRKTIVEWVR FQKKKWKWQQ DQRQRNRQAS KRTRGEDPPV
1310 1320 1330 1340 1350
VRATGSTATL GGFLRRAQRT LLDQPWQIVQ LVPVDDLGHF TVWALIGEEL
1360 1370 1380 1390 1400
HKIKLTVPRI FYVNQRSAAP PEEGQLWRKV NRVLPRSRPV FNLYRYSVPE
1410 1420 1430 1440 1450
QLFRDNSLGM LADLATPDIE GIYETQMTLE FRALMDMGCI CGVQREEARR
1460 1470 1480 1490 1500
LAQLATKDLE TFSIEQLEQR PQTQVKYLAS ANNRLRKIYL YQHNTPTAKK
1510 1520 1530 1540 1550
EIWSLILMPS KKAFVFALDT VRANQMPNMR QLYTAERLAL LKNLTAEEQD
1560 1570 1580 1590 1600
KIPVEDYTFE VLIEVDVKQI YRHIQRALTT YKQEHQGPTI LCLQTALSAR
1610 1620 1630 1640 1650
KLSLAMPILL EFPQAEIHIS DDASLLSGLD WQRQGSRAVI RHFLNLNNVL
1660 1670 1680 1690 1700
DLMLDQCRYF HVPIGNMPPD TVLFGADLFF ARLLQRHNFV LWWSASTRPD
1710 1720 1730 1740 1750
LGGREADDSR LLAEFEESIS VVQNKAGFYP DVCVELALDS LAVSALLQST
1760 1770 1780 1790 1800
RIQEMEGASS AITFDVMPQV SLEEMIGTVP AATLPSYDET ALCSAAFRVM
1810 1820 1830 1840 1850
RSMVNGWLRE VSINRNIFSD FQIVHFYRWV RSSNALLYDP ALRRSLNNLM
1860 1870 1880 1890 1900
RKMFLRIIAE FKRLGATIIY ADFNRIILSS GKKTVSDALG YVDYIVQSLR
1910 1920 1930 1940 1950
NKEMFHSIQL SFEQCWNFML WMDQANFSGI RGKLPKGIDE TVSSIVSTTM
1960 1970 1980 1990 2000
IRDSERNQDD DEDEEEDSEN RDPVESNEAE QDQEDELSLE LNWTIGEHLP
2010 2020 2030 2040 2050
DENECREKFE SLLTLFMQSL AEKKTTEQAI KDISHCAFDF ILKLHKNYGK
2060 2070 2080 2090 2100
GKPSPGLELI RTLIKALSVD KTLAEQINEL RRNMLRLVGI GEFSDLAEWE
2110 2120 2130 2140 2150
DPCDSHIINE VICKACNHCR DLDLCKDKHR AMKDGVPVWL CAQCYVAYDN
2160 2170 2180 2190 2200
EEIEMRMLDA LQRKMMSYVL QDLRCSRCSE IKRENLAEFC TCAGNFVPLI
2210 2220 2230
SGKDIQTLLG TFNKVAANHK MQLLQQTVHQ ALTTPR
Length:2,236
Mass (Da):256,702
Last modified:October 1, 2002 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD21E00C08EF8A6DD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1616E → Q in AAL29168 (PubMed:12537569).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AE014297 Genomic DNA Translation: AAF56126.3
AY061620 mRNA Translation: AAL29168.1

NCBI Reference Sequences

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RefSeqi
NP_524462.2, NM_079738.3

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
FBtr0084408; FBpp0083800; FBgn0264326

Database of genes from NCBI RefSeq genomes

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GeneIDi
42758

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG6768

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA Translation: AAF56126.3
AY061620 mRNA Translation: AAL29168.1
RefSeqiNP_524462.2, NM_079738.3

3D structure databases

SMRiQ9VCN1
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ9VCN1, 7 interactors
STRINGi7227.FBpp0083800

Proteomic databases

PaxDbiQ9VCN1
PRIDEiQ9VCN1

Genome annotation databases

EnsemblMetazoaiFBtr0084408; FBpp0083800; FBgn0264326
GeneIDi42758
KEGGidme:Dmel_CG6768

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
42758
FlyBaseiFBgn0264326 DNApol-epsilon255

Phylogenomic databases

eggNOGiKOG1798 Eukaryota
COG0417 LUCA
GeneTreeiENSGT00390000010194
HOGENOMiCLU_000556_0_0_1
InParanoidiQ9VCN1
KOiK02324
OMAiVYDLDMK
OrthoDBi39650at2759
PhylomeDBiQ9VCN1

Enzyme and pathway databases

ReactomeiR-DME-110314 Recognition of DNA damage by PCNA-containing replication complex
R-DME-174430 Telomere C-strand synthesis initiation
R-DME-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-DME-5656169 Termination of translesion DNA synthesis
R-DME-5696400 Dual Incision in GG-NER
R-DME-6782135 Dual incision in TC-NER
R-DME-68952 DNA replication initiation
R-DME-68962 Activation of the pre-replicative complex

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
42758 0 hits in 5 CRISPR screens

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
42758

Gene expression databases

BgeeiFBgn0264326 Expressed in embryo and 19 other tissues
ExpressionAtlasiQ9VCN1 differential
GenevisibleiQ9VCN1 DM

Family and domain databases

Gene3Di1.10.132.60, 1 hit
3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR006172 DNA-dir_DNA_pol_B
IPR006133 DNA-dir_DNA_pol_B_exonuc
IPR006134 DNA-dir_DNA_pol_B_multi_dom
IPR042087 DNA_pol_B_C
IPR013697 DNA_pol_e_suA_C
IPR029703 POL2
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PANTHERiPTHR10670 PTHR10670, 1 hit
PfamiView protein in Pfam
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PF08490 DUF1744, 1 hit
SMARTiView protein in SMART
SM01159 DUF1744, 1 hit
SM00486 POLBc, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDPOE1_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9VCN1
Secondary accession number(s): Q95R46
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 16, 2019
Last sequence update: October 1, 2002
Last modified: June 17, 2020
This is version 153 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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