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UniProtKB - P54358 (DPOD1_DROME)

Entry version 174 (17 Jun 2020)
Sequence version 2 (21 Feb 2001)
Previous versions | rss
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Protein

DNA polymerase delta catalytic subunit

Gene

DNApol-delta

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

As the catalytic component of the DNA polymerase delta complex, plays a crucial role in high fidelity genome replication, including lagging strand synthesis, DNA recombination and repair (By similarity). Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities (PubMed:7907087, PubMed:8415662, PubMed:1360647). Required at the nucleus of rapidly dividing embryonic cells to activate genome replication during the earliest cell cycles (PubMed:31100062). Likely to require the presence of accessory proteins Pol31 and Pol32 for full activity (PubMed:31100062).By similarity4 Publications

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

Protein has several cofactor binding sites:

<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 KCL (PubMed:7907087, PubMed:1360647). Also inhibited by carbonyldiphosphonate, aphidicolin and N-ethylmaleimide (NEM) (PubMed:7907087, PubMed:8415662, PubMed:1360647).3 Publications

<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 7.2.1 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 bindingi997ZincBy similarity1
Metal bindingi1000ZincBy similarity1
Metal bindingi1014ZincBy similarity1
Metal bindingi1017ZincBy similarity1
Metal bindingi1046Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1049Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1059Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1064Iron-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 fingeri997 – 1017CysA-typeBy similarityAdd BLAST21

<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, Exonuclease, Hydrolase, Nuclease, 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-174437 Removal of the Flap Intermediate from the C-strand
R-DME-69166 Removal of the Flap Intermediate
R-DME-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:2.7.7.73 Publications)
Alternative name(s):
3'-5' exodeoxyribonucleaseCurated (EC:3.1.11.-3 Publications)
<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-deltaImported
Synonyms:DNApolD1Curated, PolD1 Publication
ORF Names:CG5949Imported
<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)
<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 lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<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 3L

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0263600 DNApol-delta

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3124738

<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_00000464471 – 1092DNA polymerase delta catalytic subunitAdd BLAST1092

Proteomic databases

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

More...PaxDbi		P54358

PRoteomics IDEntifications database

More...PRIDEi		P54358

<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 ovaries (at the protein level) (PubMed:31100062). Expressed in embryos (at the protein level) (PubMed:31100062, PubMed:7907087, PubMed:8415662, PubMed:1360647).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0263600 Expressed in secondary oocyte and 48 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P54358 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

Catalytic component of the DNA polymerase delta complex consisting of three subunits: the catalytic subunit POLD1/DNApol-delta and two accessory subunits POLD2/Pol31 and POLD3/Pol32 (PubMed:31100062). Within the delta complex, interacts with both Pol31 and Pol32, and is able to interact with Pol31 in the absence of Pol32 (PubMed:31100062).

Interacts with PCNA AND PCNA2 (PubMed:17087725).

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		65057, 13 interactors

Database of interacting proteins

More...DIPi		DIP-22360N

Protein interaction database and analysis system

More...IntActi		P54358, 8 interactors

STRING: functional protein association networks

More...STRINGi		7227.FBpp0075277

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P54358

<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		P54358

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 – 19Nuclear localization signalSequence analysisAdd BLAST16
Motifi1046 – 1064CysB motifBy similarityAdd 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 fingeri997 – 1017CysA-typeBy similarityAdd BLAST21

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0968 Eukaryota
COG0417 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00560000077365

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000203_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P54358

KEGG Orthology (KO)

More...KOi		K02327

Identification of Orthologs from Complete Genome Data

More...OMAi		GQQVKFI

Database of Orthologous Groups

More...OrthoDBi		20210at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P54358

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
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

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>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.

P54358-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDGKRKFNGT SNGHAKKPRN PDDDEEMGFE AELAAFENSE DMDQTLLMGD 
        60         70         80         90        100
GPENQTTSER WSRPPPPELD PSKHNLEFQQ LDVENYLGQP LPGMPGAQIG 
       110        120        130        140        150
PVPVVRMFGV TMEGNSVCCH VHGFCPYFYI EAPSQFEEHH CEKLQKALDQ 
       160        170        180        190        200
KVIADIRNNK DNVQEAVLMV ELVEKLNIHG YNGDKKQRYI KISVTLPRFV 
       210        220        230        240        250
AAASRLLKKE VIMSEIDFQD CRAFENNIDF DIRFMVDTDV VGCNWIELPM 
       260        270        280        290        300
GHWRIRNSHS KPLPESRCQI EVDVAFDRFI SHEPEGEWSK VAPFRILSFD 
       310        320        330        340        350
IECAGRKGIF PEAKIDPVIQ IANMVIRQGE REPFIRNVFT LNECAPIIGS 
       360        370        380        390        400
QVLCHDKETQ MLDKWSAFVR EVDPDILTGY NINNFDFPYL LNRAAHLKVR 
       410        420        430        440        450
NFEYLGRIKN IRSVIKEQML QSKQMGRREN QYVNFEGRVP FDLLFVLLRD 
       460        470        480        490        500
YKLRSYTLNA VSYHFLQEQK EDVHHSIITD LQNGDEQTRR RLAMYCLKDA 
       510        520        530        540        550
YLPLRLLEKL MAIVNYMEMA RVTGVPLESL LTRGQQIKVL SQLLRKAKTK 
       560        570        580        590        600
GFIMPSYTSQ GSDEQYEGAT VIEPKRGYYA DPISTLDFAS LYPSIMMAHN 
       610        620        630        640        650
LCYTTLVLGG TREKLRQQEN LQDDQVERTP ANNYFVKSEV RRGLLPEILE 
       660        670        680        690        700
SLLAARKRAK NDLKVETDPF KRKVLDGRQL ALKISANSVY GFTGAQVGKL 
       710        720        730        740        750
PCLEISGSVT AYGRTMIEMT KNEVESHYTQ ANGYENNAVV IYGDTDSVMV 
       760        770        780        790        800
NFGVKTLERS MELGREAAEL VSSKFVHPIK LEFEKVYYPY LLINKKRYAG 
       810        820        830        840        850
LYFTRPDTYD KMDCKGIETV RRDNSPLVAN LMNSCLQKLL IERDPDGAVA 
       860        870        880        890        900
YVKQVIADLL CNRIDISHLV ITKELAKTDY AAKQAHVELA AKMKKRDPGT 
       910        920        930        940        950
APKLGDRVPY VICAAAKNTP AYQKAEDPLY VLENSVPIDA TYYLEQQLSK 
       960        970        980        990       1000
PLLRIFEPIL GDNAESILLK GEHTRTRTVV TSKVGGLAGF MTKKTSCLGC 
      1010       1020       1030       1040       1050
KSLMPKGYEQ ACLCPHCEPR MSELYQKEVG AKRELEETFS RLWTECQRCQ 
      1060       1070       1080       1090 
ESLHEEVICS NRDCPIFYMR QKVRMDLDNQ EKRVLRFGLA EW
Length:1,092
Mass (Da):124,905
Last modified:February 21, 2001 - v2
<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:i2FA380420298EA5C
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 conflicti492L → S in CAA61369 (PubMed:8543168).Curated1

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
X88928 mRNA Translation: CAA61369.1
AE014296 Genomic DNA Translation: AAF49555.1
AY113526 mRNA Translation: AAM29531.1

NCBI Reference Sequences

More...RefSeqi		NP_524099.2, NM_079375.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0075522; FBpp0075277; FBgn0263600

Database of genes from NCBI RefSeq genomes

More...GeneIDi		39746

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG5949

<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
X88928 mRNA Translation: CAA61369.1
AE014296 Genomic DNA Translation: AAF49555.1
AY113526 mRNA Translation: AAM29531.1
RefSeqiNP_524099.2, NM_079375.3

3D structure databases

SMRiP54358
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi65057, 13 interactors
DIPiDIP-22360N
IntActiP54358, 8 interactors
STRINGi7227.FBpp0075277

Chemistry databases

BindingDBiP54358
ChEMBLiCHEMBL3124738

Proteomic databases

PaxDbiP54358
PRIDEiP54358

Genome annotation databases

EnsemblMetazoaiFBtr0075522; FBpp0075277; FBgn0263600
GeneIDi39746
KEGGidme:Dmel_CG5949

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		39746
FlyBaseiFBgn0263600 DNApol-delta

Phylogenomic databases

eggNOGiKOG0968 Eukaryota
COG0417 LUCA
GeneTreeiENSGT00560000077365
HOGENOMiCLU_000203_2_0_1
InParanoidiP54358
KOiK02327
OMAiGQQVKFI
OrthoDBi20210at2759
PhylomeDBiP54358

Enzyme and pathway databases

ReactomeiR-DME-174437 Removal of the Flap Intermediate from the C-strand
R-DME-69166 Removal of the Flap Intermediate
R-DME-69183 Processive synthesis on the lagging strand

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		39746 0 hits in 1 CRISPR screen

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

More...GenomeRNAii		39746

Protein Ontology

More...PROi		PR:P54358

Gene expression databases

BgeeiFBgn0263600 Expressed in secondary oocyte and 48 other tissues
GenevisibleiP54358 DM

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
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
PROSITEiView protein in PROSITE
PS00116 DNA_POLYMERASE_B, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiDPOD1_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: P54358
Secondary accession number(s): Q9VUW8
<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 1, 1996
Last sequence update: February 21, 2001
Last modified: June 17, 2020
This is version 174 of the entry and version 2 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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