Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-directed DNA polymerase

Gene

43

Organism
Enterobacteria phage RB69 (Bacteriophage RB69)
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

Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose.UniRule annotation4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Mg2+UniRule annotation13 Publications2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi114Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1
Metal bindingi116Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1
Metal bindingi222Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi327Magnesium 1; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi327Magnesium 2; catalytic; for 3'-5' exonuclease activityUniRule annotation1 Publication1
Metal bindingi411Magnesium 3; catalytic; for polymerase activityUniRule annotationCombined sources9 Publications5 Publications1
Metal bindingi411Magnesium 4; catalytic; for polymerase activityUniRule annotationCombined sources9 Publications5 Publications1
Metal bindingi412Magnesium 4; catalytic; via carbonyl oxygen; for polymerase activityUniRule annotationCombined sources3 Publications3 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei482SubstrateUniRule annotationCombined sources1
Binding sitei560SubstrateUniRule annotationCombined sources1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei621Optimization of metal coordination by the polymerase active siteUniRule annotation4 Publications1
Metal bindingi623Magnesium 3; catalytic; for polymerase activityUniRule annotationCombined sources8 Publications7 Publications1
Metal bindingi623Magnesium 4; catalytic; for polymerase activityUniRule annotationCombined sources8 Publications7 Publications1
Sitei706Optimization of metal coordination by the polymerase active siteUniRule annotation2 Publications1
Sitei714Essential for viral replicationUniRule annotation1 Publication1

<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, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA replication, Viral DNA replication
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q38087

<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_and_taxonomy_section">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-directed DNA polymeraseUniRule annotation (EC:2.7.7.7UniRule annotation5 Publications, EC:3.1.11.-UniRule annotation3 Publications)
Alternative name(s):
Gp43
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:43
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEnterobacteria phage RB69 (Bacteriophage RB69)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri12353 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeRb69virus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiEscherichia coli [TaxID: 562]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000876 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Genome

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi222D → A: Complete loss of 3'-5' exonuclease activity. 1 Publication1
Mutagenesisi327D → A: Complete loss of 3'-5' exonuclease activity. 1 Publication1
Mutagenesisi415L → A or G: Decreases base selectivity by several hundred fold. 1 Publication1
Mutagenesisi415L → G or F: Increased misinsertion, increased mismatch extension and inefficient proofreading. 1 Publication1
Mutagenesisi415L → M: No effect on base selectivity. 1 Publication1
Mutagenesisi561L → A: No effect on the ability to recognize damaged DNA. Increase in probability of nucleotide incorporation. 1 Publication1
Mutagenesisi565S → G: Increased incorporation efficiency of correct dNMPs; when associated with A-567. 1 Publication1
Mutagenesisi567Y → A: Inserts both dCMP and dAMP opposite 8-oxoG rapidly and with equal efficiency. 100-fold increase of dAMP and dGMP when situated opposite guanidinohydantoin. Increased incorporation efficiency of correct dNMPs; when associated with G-565. 3 Publications1
Mutagenesisi621D → A: Drastic decrease in the efficiency of incorporation of dGMP. 1 Publication1
Mutagenesisi706K → A: Almost complete loss of polymerase activity. 1 Publication1
Mutagenesisi714D → A: Complete loss of viral replication. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB08245 1-(2-DEOXY-5-O-PHOSPHONO-BETA-D-ERYTHRO-PENTOFURANOSYL)-5-NITRO-1H-INDOLE
DB02857 Guanosine
DB01972 Guanosine-5'-Monophosphate

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000465471 – 903DNA-directed DNA polymeraseAdd BLAST903

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of the replicase complex that includes the DNA polymerase, the polymerase clamp, the clamp loader complex, the single-stranded DNA binding protein, and the primase/helicase (By similarity). Interacts with the polymerase clamp; this interaction constitutes the polymerase holoenzyme (PubMed:10535734).UniRule annotation1 Publication

<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

Secondary structure

1903
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q38087

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

More...
SMRi
Q38087

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q38087

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni103 – 3403'-5'exonucleaseUniRule annotation1 PublicationAdd BLAST238
Regioni248 – 264Beta hairpinUniRule annotation1 PublicationAdd BLAST17
Regioni380 – 903PolymeraseUniRule annotation1 PublicationAdd BLAST524
Regioni414 – 416Substrate bindingUniRule annotationCombined sources3
Regioni705 – 708Binding of DNA in B-conformationUniRule annotation2 Publications4
Regioni897 – 903Interaction with the polymerase clampUniRule annotation7

<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 N-terminus contains the 3'-5' exonuclease activity (PubMed:9215631). The C-terminus contains the polymerase activity and is involved in binding to the polymerase clamp protein (PubMed:9215631). A beta hairpin structure is necessary for the proofreading function of the polymerase (By similarity).UniRule annotation1 Publication

<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

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K18942

Database of Orthologous Groups

More...
OrthoDBi
VOG0900001M

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.420.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_04100 DPOL_T4, 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
IPR034749 DPOL_T4
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf

Pfam protein domain database

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

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q38087-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKEFYLTVEQ IGDSIFERYI DSNGRERTRE VEYKPSLFAH CPESQATKYF
60 70 80 90 100
DIYGKPCTRK LFANMRDASQ WIKRMEDIGL EALGMDDFKL AYLSDTYNYE
110 120 130 140 150
IKYDHTKIRV ANFDIEVTSP DGFPEPSQAK HPIDAITHYD SIDDRFYVFD
160 170 180 190 200
LLNSPYGNVE EWSIEIAAKL QEQGGDEVPS EIIDKIIYMP FDNEKELLME
210 220 230 240 250
YLNFWQQKTP VILTGWNVES FDIPYVYNRI KNIFGESTAK RLSPHRKTRV
260 270 280 290 300
KVIENMYGSR EIITLFGISV LDYIDLYKKF SFTNQPSYSL DYISEFELNV
310 320 330 340 350
GKLKYDGPIS KLRESNHQRY ISYNIIDVYR VLQIDAKRQF INLSLDMGYY
360 370 380 390 400
AKIQIQSVFS PIKTWDAIIF NSLKEQNKVI PQGRSHPVQP YPGAFVKEPI
410 420 430 440 450
PNRYKYVMSF DLTSLYPSII RQVNISPETI AGTFKVAPLH DYINAVAERP
460 470 480 490 500
SDVYSCSPNG MMYYKDRDGV VPTEITKVFN QRKEHKGYML AAQRNGEIIK
510 520 530 540 550
EALHNPNLSV DEPLDVDYRF DFSDEIKEKI KKLSAKSLNE MLFRAQRTEV
560 570 580 590 600
AGMTAQINRK LLINSLYGAL GNVWFRYYDL RNATAITTFG QMALQWIERK
610 620 630 640 650
VNEYLNEVCG TEGEAFVLYG DTDSIYVSAD KIIDKVGESK FRDTNHWVDF
660 670 680 690 700
LDKFARERME PAIDRGFREM CEYMNNKQHL MFMDREAIAG PPLGSKGIGG
710 720 730 740 750
FWTGKKRYAL NVWDMEGTRY AEPKLKIMGL ETQKSSTPKA VQKALKECIR
760 770 780 790 800
RMLQEGEESL QEYFKEFEKE FRQLNYISIA SVSSANNIAK YDVGGFPGPK
810 820 830 840 850
CPFHIRGILT YNRAIKGNID APQVVEGEKV YVLPLREGNP FGDKCIAWPS
860 870 880 890 900
GTEITDLIKD DVLHWMDYTV LLEKTFIKPL EGFTSAAKLD YEKKASLFDM

FDF
Length:903
Mass (Da):104,613
Last modified:November 1, 1996 - 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:iA3983FC16D4C0509
GO

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
U34036 Genomic DNA Translation: AAA93077.1
AY303349 Genomic DNA Translation: AAP75958.1

NCBI Reference Sequences

More...
RefSeqi
NP_861746.1, NC_004928.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1494172

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:1494172

<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
U34036 Genomic DNA Translation: AAA93077.1
AY303349 Genomic DNA Translation: AAP75958.1
RefSeqiNP_861746.1, NC_004928.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B1Fmodel-R387-892[»]
1B8HX-ray3.00D893-903[»]
1CLQX-ray2.70A1-903[»]
1IG9X-ray2.60A1-903[»]
1IH7X-ray2.21A1-903[»]
1Q9XX-ray2.69A/B/C/D1-903[»]
1Q9YX-ray2.80A1-903[»]
1QE4model-F1-903[»]
1WAFX-ray3.20A/B1-903[»]
1WAGmodel-R1-903[»]
1WAHmodel-R1-903[»]
1WAImodel-R1-903[»]
1WAJX-ray2.80A1-903[»]
2ATQX-ray3.20A1-903[»]
2DTUX-ray2.37A/B/C/D1-902[»]
2DY4X-ray2.65A/B/C/D1-903[»]
2OYQX-ray2.86A/B/C/D1-903[»]
2OZMX-ray2.86A1-903[»]
2OZSX-ray2.75A1-903[»]
2P5GX-ray2.80A/B/C/D1-903[»]
2P5OX-ray2.80A/B/C/D1-903[»]
3CFOX-ray2.60A1-903[»]
3CFPX-ray2.50A1-903[»]
3CFRX-ray2.40A1-903[»]
3CQ8X-ray2.50A1-903[»]
3KD1X-ray2.66E1-903[»]
3KD5X-ray2.69E1-903[»]
3L8BX-ray2.15A/B1-903[»]
3LDSX-ray3.00A1-903[»]
3LZIX-ray2.30A1-903[»]
3LZJX-ray2.05A1-903[»]
3NAEX-ray2.00A1-903[»]
3NCIX-ray1.79A1-903[»]
3NDKX-ray2.00A1-903[»]
3NE6X-ray2.00A1-903[»]
3NGIX-ray1.89A1-903[»]
3NHGX-ray2.50A1-903[»]
3QEIX-ray2.18A1-903[»]
3QEPX-ray1.80A1-903[»]
3QERX-ray1.96A1-903[»]
3QESX-ray1.98A1-903[»]
3QETX-ray2.08A1-903[»]
3QEVX-ray1.77A1-903[»]
3QEWX-ray1.84A1-903[»]
3QEXX-ray1.73A1-903[»]
3QNNX-ray1.92A1-901[»]
3QNOX-ray1.88A1-901[»]
3RMAX-ray2.84A/B/C/D1-903[»]
3RMBX-ray2.65A/B/C/D1-903[»]
3RMCX-ray3.00A/B/C/D1-903[»]
3RMDX-ray2.98A/B/C/D1-903[»]
3RWUX-ray2.33A1-901[»]
3S9HX-ray1.95A1-903[»]
3SCXX-ray2.35A1-901[»]
3SI6X-ray1.85A1-901[»]
3SJJX-ray2.38A1-901[»]
3SNNX-ray2.00A1-901[»]
3SPYX-ray2.14A1-901[»]
3SPZX-ray2.43A1-903[»]
3SQ0X-ray2.00A1-903[»]
3SQ1X-ray1.82A1-901[»]
3SQ2X-ray2.10A1-902[»]
3SQ4X-ray2.23A1-902[»]
3SUNX-ray2.42A1-895[»]
3SUOX-ray2.23A1-900[»]
3SUPX-ray2.32A1-903[»]
3SUQX-ray3.15A1-897[»]
3TABX-ray2.80A/B/C/D1-903[»]
3TAEX-ray2.71A/B/C/D1-903[»]
3TAFX-ray3.00A/B/C/D1-903[»]
3TAGX-ray2.95A/B/C/D1-903[»]
3UIQX-ray1.88A1-903[»]
4DTJX-ray1.90A1-901[»]
4DTMX-ray1.95A1-901[»]
4DTNX-ray1.96A1-903[»]
4DTOX-ray2.05A1-903[»]
4DTPX-ray2.05A1-903[»]
4DTRX-ray2.04A1-903[»]
4DTSX-ray1.96A1-903[»]
4DTUX-ray1.86A1-903[»]
4DTXX-ray1.84A1-903[»]
4DU1X-ray2.15A1-903[»]
4DU3X-ray2.02A1-903[»]
4DU4X-ray2.28A1-903[»]
4E3SX-ray2.04A1-903[»]
4FJ5X-ray2.05A1-903[»]
4FJ7X-ray1.90A1-903[»]
4FJ8X-ray2.19A1-903[»]
4FJ9X-ray1.97A1-903[»]
4FJGX-ray2.02A1-903[»]
4FJHX-ray2.11A1-903[»]
4FJIX-ray2.20A1-903[»]
4FJJX-ray1.99A1-903[»]
4FJKX-ray2.00A1-903[»]
4FJLX-ray1.87A1-903[»]
4FJMX-ray2.02A1-903[»]
4FJNX-ray1.98A1-903[»]
4FJXX-ray2.11A1-903[»]
4FK0X-ray2.18A1-903[»]
4FK2X-ray1.98A1-903[»]
4FK4X-ray1.90A1-903[»]
4I9LX-ray2.60A1-903[»]
4I9QX-ray2.30A/B1-903[»]
4J2AX-ray1.80A1-901[»]
4J2BX-ray2.04A1-901[»]
4J2DX-ray1.76A1-901[»]
4J2EX-ray2.02A1-901[»]
4KHNX-ray2.55A/B1-903[»]
4KHQX-ray2.19A1-903[»]
4KHSX-ray2.12A1-903[»]
4KHUX-ray2.05A1-903[»]
4KHWX-ray2.37A1-903[»]
4KHYX-ray2.25A1-903[»]
4KI4X-ray2.45A1-903[»]
4KI6X-ray2.55A1-903[»]
4M3RX-ray2.07A1-903[»]
4M3TX-ray1.90A1-903[»]
4M3UX-ray2.07A1-903[»]
4M3WX-ray2.10A1-903[»]
4M3XX-ray2.20A1-903[»]
4M3YX-ray1.86A1-903[»]
4M3ZX-ray1.84A1-903[»]
4M41X-ray2.15A1-903[»]
4M42X-ray2.04A1-903[»]
4M45X-ray1.89A1-903[»]
5GNQX-ray2.10A/B1-903[»]
ProteinModelPortaliQ38087
SMRiQ38087
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB08245 1-(2-DEOXY-5-O-PHOSPHONO-BETA-D-ERYTHRO-PENTOFURANOSYL)-5-NITRO-1H-INDOLE
DB02857 Guanosine
DB01972 Guanosine-5'-Monophosphate

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1494172
KEGGivg:1494172

Phylogenomic databases

KOiK18942
OrthoDBiVOG0900001M

Enzyme and pathway databases

SABIO-RKiQ38087

Miscellaneous databases

EvolutionaryTraceiQ38087

Family and domain databases

Gene3Di3.30.420.10, 1 hit
HAMAPiMF_04100 DPOL_T4, 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
IPR034749 DPOL_T4
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PfamiView protein in Pfam
PF00136 DNA_pol_B, 1 hit
PF03104 DNA_pol_B_exo1, 1 hit
PRINTSiPR00106 DNAPOLB
SMARTiView protein in SMART
SM00486 POLBc, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS00116 DNA_POLYMERASE_B, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiDPOL_BPR69
<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: Q38087
Secondary accession number(s): Q76XX8
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 132 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 programViral 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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.

Do not show this banner again