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Entry version 138 (02 Dec 2020)
Sequence version 1 (01 Jun 1998)
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Protein

DNA polymerase delta catalytic subunit

Gene

Pold1

Organism
Rattus norvegicus (Rat)
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 transcript 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

As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, in the presence of POLD3 and POLD4, may catalyze the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine, 8oxoG or abasic sites.By similarity

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

<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 similarityNote: 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

Regulated by alteration of quaternary structure. Exhibits burst rates of DNA synthesis are about 5 times faster in the presence of POLD4 (Pol-delta4 complex) than in its absence (Pol-delta3 complex), while the affinity of the enzyme for its DNA and dNTP substrates appears unchanged. The Pol-delta3 complex is more likely to proofread DNA synthesis because it cleaves single-stranded DNA twice as fast and transfers mismatched DNA from the polymerase to the exonuclease sites 9 times faster compared to the Pol-delta3 complex. Pol-delta3 also extends mismatched primers 3 times more slowly in the absence of POLD4. The conversion of Pol-delta4 into Pol-delta3 is induced by genotoxic stress or by replication stress leading POLD4 degradation. Stimulated in the presence of PCNA (By similarity). This stimulation is further increased in the presence of KCTD13/PDIP1, most probably via direct interaction between KCTD13 and POLD2 (By similarity).By similarity

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 bindingi1008ZincBy similarity1
Metal bindingi1011ZincBy similarity1
Metal bindingi1022ZincBy similarity1
Metal bindingi1025ZincBy similarity1
Metal bindingi1054Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1057Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1067Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1072Iron-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 fingeri1008 – 1025CysA-typeAdd BLAST18

<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, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA excision, DNA repair, DNA replication
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-110314, Recognition of DNA damage by PCNA-containing replication complex
R-RNO-174411, Polymerase switching on the C-strand of the telomere
R-RNO-174414, Processive synthesis on the C-strand of the telomere
R-RNO-174417, Telomere C-strand (Lagging Strand) Synthesis
R-RNO-174437, Removal of the Flap Intermediate from the C-strand
R-RNO-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-RNO-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-RNO-5651801, PCNA-Dependent Long Patch Base Excision Repair
R-RNO-5656169, Termination of translesion DNA synthesis
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-RNO-5696400, Dual Incision in GG-NER
R-RNO-6782135, Dual incision in TC-NER
R-RNO-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-RNO-69091, Polymerase switching
R-RNO-69166, Removal of the Flap Intermediate
R-RNO-69183, Processive synthesis on the lagging strand

<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 delta catalytic subunitCurated (EC:2.7.7.7By similarity)
Alternative name(s):
3'-5' exodeoxyribonucleaseCurated (EC:3.1.11.-By similarity)
<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:Pold1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
621839, Pold1

<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

Keywords - Cellular componenti

Nucleus

<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_00000464451 – 1103DNA polymerase delta catalytic subunitAdd BLAST1103

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki570Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O54747

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

More...
PaxDbi
O54747

PRoteomics IDEntifications database

More...
PRIDEi
O54747

<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 tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing both DNA polymerase and 3' to 5' proofreading exonuclease activities. Within Pol-delta4, directly interacts with POLD2 and POLD4. Following genotoxic stress by DNA-damaging agents, such as ultraviolet light and methyl methanesulfonate, or by replication stress induced by treatment with hydroxyurea or aphidicolin, Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3) by POLD4 degradation. Pol-delta3 is the major form at S phase replication sites and DNA damage sites. POLD1 displays different catalytic properties depending upon the complex it is found in. It exhibits higher proofreading activity and fidelity than Pol-delta4, making it particularly well suited to respond to DNA damage. Directly interacts with PCNA, as do POLD3 and POLD4; this interaction stimulates Pol-delta4 polymerase activity. As POLD2 and POLD4, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA. This stimulation may be due predominantly to an increase of initiation frequency and also to increased processivity. Also observed as a dimeric complex with POLD2 (Pol-delta2). Pol-delta2 is relatively insensitive to the PCNA stimulation (2-5-fold) compared to Pol-delta4 that is stimulated by over 50-fold. The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2.

Interacts with CIAO1.

Interacts with POLDIP2 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2099, DNA polymerase delta heterotetramer

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000026797

<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
O54747

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>Motifi4 – 17Nuclear localization signalSequence analysisAdd BLAST14
Motifi1054 – 1072CysB motifAdd BLAST19

<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 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.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1008 – 1025CysA-typeAdd BLAST18

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0969, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O54747

Database of Orthologous Groups

More...
OrthoDBi
20210at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O54747

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
3.90.1600.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006172, DNA-dir_DNA_pol_B
IPR017964, DNA-dir_DNA_pol_B_CS
IPR006133, DNA-dir_DNA_pol_B_exonuc
IPR006134, DNA-dir_DNA_pol_B_multi_dom
IPR043502, DNA/RNA_pol_sf
IPR042087, DNA_pol_B_C
IPR023211, DNA_pol_palm_dom_sf
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR025687, Znf-C4pol

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00136, DNA_pol_B, 1 hit
PF03104, DNA_pol_B_exo1, 1 hit
PF14260, zf-C4pol, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00106, DNAPOLB

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53098, SSF53098, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00116, DNA_POLYMERASE_B, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O54747-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDGKRRQAPS SGVPPKRACK GLWDEDEPSQ FEENLALLEE IEAENRLQEA
60 70 80 90 100
EEELQLPPEG IVGGQFSTAD IDPRWLRPTP LALDPSTEPL IFQQLEIDHY
110 120 130 140 150
VGTSPPLPEG PPASRNSVPI LRAFGVTDEG FSVCCHIHGF APYFYTPAPP
160 170 180 190 200
GFGAEHLSEL QRELNAAISR DQRGGKELSG PAVLAIELCS RESMFGYHGH
210 220 230 240 250
GPSPFLRITL ALPRLMAPAR RLLEQGIRVP GLGTPSFAPY EANVDFEIRF
260 270 280 290 300
MVDADIVGCN WLELPAGKYV RRAEKKATLC QLEVDVLWSD VISHPPEGQW
310 320 330 340 350
QRIAPLRVLS FDIECAGRKG IFPEPERDPV IQICSLGLRW GEPEPFLRLA
360 370 380 390 400
LTLRPCAPIL GAKVQSYERE EDLLQAWATF ILAMDPDVIT GYNIQNFDLP
410 420 430 440 450
YLISRAQTLK VDRFPFLGRV TGLRSNIRDS SFQSRQVGRR DSKVVSMVGR
460 470 480 490 500
VQMDMLQVLL REYKLRSYTL NAVSFHFLGE QKEDVQHSII TDLQNGNEQT
510 520 530 540 550
RRRLAVYCLK DAFLPLRLLE RLMVLVNNVE MARVTGVPLG YLLSRGQQVK
560 570 580 590 600
VVSQLLRQAM REGLLMPVVK TEGGEDYTGA TVIEPLKGYY DVPIATLDFS
610 620 630 640 650
SLYPSIMMAH NLCYTTLLRP GAAQKLGLKP DEFIKTPTGD EFVKASVRKG
660 670 680 690 700
LLPQILENLL SARKRAKAEL AQETDPLRRQ VLDGRQLALK VSPNSVYGFT
710 720 730 740 750
GAQVGKLPCL EISQSVTGFG RQMIEKTKQL VETKYTLENG YDANAKVVYG
760 770 780 790 800
DTDSVMCRFG VSSVAEAMSL GREAANWVSS HFPSPIRLEF EKVYFPYLLI
810 820 830 840 850
SKKRYAGLLF SSRSDAHDRM DCKGLEAVRR DNCPLVANLV TSSLRRILVD
860 870 880 890 900
RDPDGAVAHA KDVISDLLCN RIDISQLVIT KELTRAAADY AGKQAHVELA
910 920 930 940 950
ERMRKRDPGS APNLGDRVPY VIIGAAKGVA AYMKSEDPLF VLEHSLPIDT
960 970 980 990 1000
QYYLEQQLAK PLLRIFEPIL GEGRAESVLL RGDHTRCKTV LTSKVGGLLA
1010 1020 1030 1040 1050
FTKRRNSCIG CRSVIDHQGA VCKFCQPRES ELYQKEVSHL NALEERFSRL
1060 1070 1080 1090 1100
WTQCQRCQGS LHEDVICTSR DCPIFYMRKK VRKDLEDQER LLQRFGPPGP

EAW
Length:1,103
Mass (Da):123,601
Last modified:June 1, 1998 - v1
<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:i361086DDC1B50639
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V8M1G3V8M1_RAT
DNA polymerase
Pold1 rCG_54119
1,103Annotation score:

Annotation score:3 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ222691 mRNA Translation: CAA10946.1

NCBI Reference Sequences

More...
RefSeqi
NP_067694.1, NM_021662.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
59294

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:59294

UCSC genome browser

More...
UCSCi
RGD:621839, rat

<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
AJ222691 mRNA Translation: CAA10946.1
RefSeqiNP_067694.1, NM_021662.2

3D structure databases

SMRiO54747
ModBaseiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-2099, DNA polymerase delta heterotetramer
STRINGi10116.ENSRNOP00000026797

Proteomic databases

jPOSTiO54747
PaxDbiO54747
PRIDEiO54747

Genome annotation databases

GeneIDi59294
KEGGirno:59294
UCSCiRGD:621839, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5424
RGDi621839, Pold1

Phylogenomic databases

eggNOGiKOG0969, Eukaryota
InParanoidiO54747
OrthoDBi20210at2759
PhylomeDBiO54747

Enzyme and pathway databases

ReactomeiR-RNO-110314, Recognition of DNA damage by PCNA-containing replication complex
R-RNO-174411, Polymerase switching on the C-strand of the telomere
R-RNO-174414, Processive synthesis on the C-strand of the telomere
R-RNO-174417, Telomere C-strand (Lagging Strand) Synthesis
R-RNO-174437, Removal of the Flap Intermediate from the C-strand
R-RNO-5358565, Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-RNO-5358606, Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-RNO-5651801, PCNA-Dependent Long Patch Base Excision Repair
R-RNO-5656169, Termination of translesion DNA synthesis
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-RNO-5696400, Dual Incision in GG-NER
R-RNO-6782135, Dual incision in TC-NER
R-RNO-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-RNO-69091, Polymerase switching
R-RNO-69166, Removal of the Flap Intermediate
R-RNO-69183, Processive synthesis on the lagging strand

Miscellaneous databases

Protein Ontology

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PROi
PR:O54747

Family and domain databases

Gene3Di1.10.132.60, 1 hit
3.30.420.10, 1 hit
3.90.1600.10, 1 hit
InterProiView protein in InterPro
IPR006172, DNA-dir_DNA_pol_B
IPR017964, DNA-dir_DNA_pol_B_CS
IPR006133, DNA-dir_DNA_pol_B_exonuc
IPR006134, DNA-dir_DNA_pol_B_multi_dom
IPR043502, DNA/RNA_pol_sf
IPR042087, DNA_pol_B_C
IPR023211, DNA_pol_palm_dom_sf
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR025687, Znf-C4pol
PfamiView protein in Pfam
PF00136, DNA_pol_B, 1 hit
PF03104, DNA_pol_B_exo1, 1 hit
PF14260, zf-C4pol, 1 hit
PRINTSiPR00106, DNAPOLB
SMARTiView protein in SMART
SM00486, POLBc, 1 hit
SUPFAMiSSF53098, SSF53098, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS00116, DNA_POLYMERASE_B, 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
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<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 nameiDPOD1_RAT
<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: O54747
<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: December 15, 1998
Last sequence update: June 1, 1998
Last modified: December 2, 2020
This is version 138 of the entry and version 1 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 programChordata Protein Annotation Program

<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
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