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UniProtKB - P42494 (DPOLX_ASFB7)

Entry version 105 (23 Feb 2022)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
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Protein

Repair DNA polymerase X

Gene

Ba71V-97

Organism
African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
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

Error-prone polymerase lacking a proofreading 3'-5' exonuclease which catalyzes the gap-filling reaction during the DNA repair process (PubMed:11685239, PubMed:28245220).

Specifically binds intermediates in the single-nucleotide base-excision repair process (PubMed:12595253).

Also catalyzes DNA polymerization with low nucleotide-insertion fidelity (PubMed:24617852).

Probably acts as a strategic DNA mutase, which gives rise to a rapid emergence of variants (PubMed:11685239).

Generates mismatched G-G pairs, in that case, the polymerase first binds the deoxynucleotide followed by mismatch formation (PubMed:24617852).

Together with the viral DNA ligase, fills the single nucleotide gaps generated by the AP endonuclease (Probable). Binds DNA with high affinity via the helix alphaE (PubMed:24617852).

Curated4 Publications

Miscellaneous

Consistent with its intracellular location, ASFV encodes its own replicative DNA polymerase and three base excision repair enzymes: a class II AP endonuclease, the repair polymerase Pol X, and an ATP-dependent DNA ligase.Curated

<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

Mg2+2 PublicationsNote: In the presence of magnesium, pol X shows a strong preference for the ssDNA gaps having one and two nucleotides.

<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>Kineticsi

  1. KM=0.26 µM for dGTP1 Publication
  2. KM=0.46 µM for dATP1 Publication
  3. KM=9.4 µM for dCTP1 Publication
  4. KM=8.6 µM for dTTP1 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 bindingi49Magnesium1 Publication1 Publication1
Metal bindingi51Magnesium1 Publication1 Publication1
Metal bindingi100Magnesium1 Publication1 Publication1
<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>Sitei115Stabilizes dGTP in a syn confromation to overcome the Watson-Crick base pairing constraint1 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair
LigandMagnesium, Metal-binding

<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:
Repair DNA polymerase X (EC:2.7.7.72 Publications)
Short name:
Pol X
Alternative name(s):
AsfvPolX
<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
Ordered Locus Names:Ba71V-97
ORF Names:O174L
<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>OrganismiAfrican swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
<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 identifieri10498 [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 lineageiViruses › Varidnaviria › Bamfordvirae › Nucleocytoviricota › Pokkesviricetes › Asfuvirales › Asfarviridae › Asfivirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 hostiOrnithodoros (relapsing fever ticks) [TaxID: 6937]
Sus scrofa (Pig) [TaxID: 9823]
<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
  • UP000000624 <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: Genome

<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

Virion

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi115H → A: Complete loss of MgdGTP binding and dG:dGTP ternary complex formation but not dG:dCTP ternary complex formation. 1 Publication1
Mutagenesisi115H → D: 18x decreased dG:dGTP misincorporation. 1 Publication1
Mutagenesisi115H → E: 36x decreased dG:dGTP misincorporation. 1 Publication1
Mutagenesisi115H → F: Slower dG:dGTP misincorporation. 1 Publication1
Mutagenesisi125R → A: Loss of DNA binding affinity. Decreased dG:dGTP misincorporation. 1 Publication1
Mutagenesisi127R → A: Slower dG:dGTP misincorporation. 1 Publication1
Mutagenesisi168R → A: Loss of DNA binding affinity. Decreased dGTP misincorporation. 1 Publication1

<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_00002187981 – 174Repair DNA polymerase XAdd BLAST174

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi81 ↔ 861 Publication

Keywords - PTMi

Disulfide bond

<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

1174
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P42494

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

More...SMRi		P42494

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P42494

<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>Regioni42 – 51Involved in ssDNA bindingBy similarity10

<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

Small DNA polymerase formed from only a palm and a C-terminal subdomain (PubMed:11685239). Unlike other polymerases, binds DNA via the helix alphaE (PubMed:24617852). The total DNA-binding site of pol X is composed of two DNA-binding subsites.2 Publications

<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-X family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.210.10, 1 hit
3.30.460.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR019843, DNA_pol-X_BS
IPR037160, DNA_Pol_thumb_sf
IPR022312, DNA_pol_X
IPR043519, NT_sf
IPR029398, PolB_thumb

The PANTHER Classification System

More...PANTHERi		PTHR11276, PTHR11276, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14791, DNA_pol_B_thumb, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF81301, SSF81301, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00522, DNA_POLYMERASE_X, 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.

P42494-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLTLIQGKKI VNHLRSRLAF EYNGQLIKIL SKNIVAVGSL RREEKMLNDV 
        60         70         80         90        100
DLLIIVPEKK LLKHVLPNIR IKGLSFSVKV CGERKCVLFI EWEKKTYQLD 
       110        120        130        140        150
LFTALAEEKP YAIFHFTGPV SYLIRIRAAL KKKNYKLNQY GLFKNQTLVP 
       160        170 
LKITTEKELI KELGFTYRIP KKRL
Length:174
Mass (Da):20,314
Last modified:November 1, 1995 - 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:i48E24A0ACDC0F9C7
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
U18466 Genomic DNA Translation: AAA65326.1

NCBI Reference Sequences

More...RefSeqi		NP_042790.1, NC_001659.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		22220326

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:22220326

<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
U18466 Genomic DNA Translation: AAA65326.1
RefSeqiNP_042790.1, NC_001659.2

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
1JAJNMR-A1-174[»]
1JQRNMR-A1-174[»]
2M2TNMR-A1-174[»]
2M2UNMR-A1-174[»]
2M2VNMR-A1-174[»]
2M2WNMR-A1-174[»]
5HR9X-ray2.20A/B1-174[»]
5HRBX-ray1.70A1-174[»]
5HRDX-ray1.80A/B/C/D1-174[»]
5HREX-ray1.75A1-174[»]
5HRFX-ray2.25A/B1-174[»]
5HRGX-ray2.00A/B1-174[»]
5HRHX-ray3.00A/B1-174[»]
5HRIX-ray2.20A/B1-174[»]
5HRKX-ray2.90A/B1-174[»]
5HRLX-ray2.40A/B1-174[»]
5XM8X-ray2.55A/B/C/D1-174[»]
5XM9X-ray3.05A/B/C/D1-174[»]
5XMAX-ray3.80A/B1-174[»]
BMRBiP42494
SMRiP42494
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

GeneIDi22220326
KEGGivg:22220326

Miscellaneous databases

EvolutionaryTraceiP42494

Family and domain databases

Gene3Di3.30.210.10, 1 hit
3.30.460.10, 1 hit
InterProiView protein in InterPro
IPR019843, DNA_pol-X_BS
IPR037160, DNA_Pol_thumb_sf
IPR022312, DNA_pol_X
IPR043519, NT_sf
IPR029398, PolB_thumb
PANTHERiPTHR11276, PTHR11276, 1 hit
PfamiView protein in Pfam
PF14791, DNA_pol_B_thumb, 1 hit
SUPFAMiSSF81301, SSF81301, 1 hit
PROSITEiView protein in PROSITE
PS00522, DNA_POLYMERASE_X, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...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 nameiDPOLX_ASFB7
<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: P42494
<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: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 23, 2022
This is version 105 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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