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Entry version 198 (02 Jun 2021)
Sequence version 2 (15 Mar 2004)
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Protein

DNA polymerase alpha catalytic subunit

Gene

PolA1

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

Annotation score:5 out of 5

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

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

Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis (PubMed:9858578, PubMed:6773966, PubMed:6806812, PubMed:6403945, PubMed:6409898).

During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit PolA1, an accessory subunit PolA2 and two primase subunits, the catalytic subunit Prim1 and the regulatory subunit Prim2) is recruited to DNA at the replicative forks (PubMed:9858578, PubMed:6773966, PubMed:6806812, PubMed:6409898).

The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity).

These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity).

In addition to polymerase activity, exhibits 3' to 5' exonuclease activity (PubMed:3112771, PubMed:3129427).

By similarity7 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

[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

Inhibited by N2-(p-n-butylphenyl) deoxyguanosine 5'-triphosphate and N2-(p-n-butylphenyl) deoxyadenosine 5'-triphosphate (PubMed:3129427). DNA synthesis is not inhibited by fungal toxin alpha-amaitin (PubMed:6806812). The 3'-5' exonuclease activity is inhibited by 10mM dGMP (PubMed:3129427).2 Publications

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 bindingi1296ZincBy similarity1
Metal bindingi1299ZincBy similarity1
Metal bindingi1324ZincBy similarity1
Metal bindingi1329ZincBy similarity1
Metal bindingi1362Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1367Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1385Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1388Iron-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 fingeri1296 – 1327CysA-typeBy similarityAdd BLAST32

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

GO - Biological processi

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

Molecular functionDNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA damage, 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-DME-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-DME-68952, DNA replication initiation
R-DME-68962, Activation of the pre-replicative complex
R-DME-69091, Polymerase switching
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 alpha catalytic subunit (EC:2.7.7.74 Publications)
Alternative name(s):
3'-5' exodeoxyribonucleaseCurated (EC:3.1.11.-2 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:PolA1Imported
Synonyms:DNApol-alphaImported, DNApol-alpha180Imported, POLAImported
ORF Names:CG6349Imported
<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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3R

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0259113, PolA1

<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 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
CHEMBL6039

<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_00000464321 – 1488DNA polymerase alpha catalytic subunitAdd BLAST1488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei239Phosphoserine1 Publication1
Modified residuei262Phosphoserine1 Publication1
Modified residuei269Phosphoserine1 Publication1
Modified residuei314Phosphothreonine1 Publication1
Modified residuei317Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

In embryos, a cleaved form of 130 kDa is produced up to cycle 14 and then disappears.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P26019

PRoteomics IDEntifications database

More...
PRIDEi
P26019

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P26019

<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 embryos (at protein level).4 Publications

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

Expressed both maternally and zygotically. Highest level of zygotic expression seen in second-instar larva, level is reduced at other stages of development.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0259113, Expressed in embryo and 28 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P26019, DM

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

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

Component of the alpha DNA polymerase complex (also known as the alpha DNA polymerase-primase complex) consisting of four subunits: the catalytic subunit PolA1, the regulatory subunit PolA2, and the primase complex subunits Prim1 and Prim2 respectively (PubMed:6773966, PubMed:6403945, PubMed:6409898, PubMed:7592543). PolA1 associates with the DNA primase complex before association with PolA2 (PubMed:6409898).

Interacts with Dpit47; the interaction inhibits the activity of the DNA polymerase and occurs only in proliferating cells but not in quiescent cells (PubMed:11493638).

5 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
67519, 15 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2090, DNA polymerase alpha:primase complex

Database of interacting proteins

More...
DIPi
DIP-23937N

Protein interaction database and analysis system

More...
IntActi
P26019, 6 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0083514

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P26019

<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
P26019

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

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>Regioni1 – 22DisorderedSequence analysisAdd BLAST22
Regioni79 – 124DisorderedSequence analysisAdd BLAST46
Regioni236 – 325DisorderedSequence analysisAdd BLAST90
Regioni638 – 758Contains conserved residues essential for 3' -> 5' exonuclease activities1 PublicationAdd BLAST121
Regioni675 – 734DNA-bindingSequence analysisAdd BLAST60
Regioni1255 – 1380DNA-bindingSequence analysisAdd BLAST126

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>Motifi96 – 103Nuclear localization signalSequence analysis8
Motifi1362 – 1388CysB motifBy similarityAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi247 – 262Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi283 – 303Polar residuesSequence analysisAdd BLAST21
Compositional biasi304 – 325Basic and acidic residuesSequence analysisAdd BLAST22

<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 CysA-type zinc finger is required for PCNA-binding.By similarity
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

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

Belongs to the DNA polymerase type-B family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1296 – 1327CysA-typeBy similarityAdd BLAST32

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0970, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074891

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001718_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P26019

Identification of Orthologs from Complete Genome Data

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OMAi
NIMPLAL

Database of Orthologous Groups

More...
OrthoDBi
293315at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P26019

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.132.60, 1 hit
1.10.3200.20, 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
IPR024647, DNA_pol_a_cat_su_N
IPR042087, DNA_pol_B_C
IPR023211, DNA_pol_palm_dom_sf
IPR038256, Pol_alpha_znc_sf
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR015088, Znf_DNA-dir_DNA_pol_B_alpha

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12254, DNA_pol_alpha_N, 1 hit
PF00136, DNA_pol_B, 1 hit
PF03104, DNA_pol_B_exo1, 1 hit
PF08996, zf-DNA_Pol, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00106, DNAPOLB

Simple Modular Architecture Research Tool; a protein domain database

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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

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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.

P26019-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSESPSEPRA KRQRVDKNGR FAAMERLRQL KGTKNKCKVE DQVDDVYDVV
60 70 80 90 100
DEREYAKRAQ EKYGDDWIEE DGTGYAEDLR DFFEDEDEYS DGEEDRKDSK
110 120 130 140 150
KKKGVAPNSK KRPRENEKPV TGKASIKNLF SNAVPKKMDV KTSVKDDDIL
160 170 180 190 200
ADILGEIKEE PAATSEKAEK VIAPAKISVT SRKFDAAAAK EYMNSFLNNI
210 220 230 240 250
KVQEQERKKA EASSDNEMLE RILKPKAAVP NTKVAFFSSP TIKKEPMPEK
260 270 280 290 300
TPAKKATEDP FSDNEMDFSC LDDDENQFDV EKTQQTEKVS QTKTAAEKTS
310 320 330 340 350
QSKVAEKSAP KKETTGSPKE SESEDISRLL NNWESICQMD DDFEKSVLTT
360 370 380 390 400
EQDSTISSDQ QLRFWYWEAY EDPVKMPGEV FLFGRTADGK SVCLRVQNIN
410 420 430 440 450
RVLYLLPRQF LLDPISKEPT KQKVTVADIY KEFDSEVANQ LKLEFFRSRK
460 470 480 490 500
VTKSFAHHAI GIEVPQSCDY LEVHYDGKKP LPNLSADKKY NSIAHIFGAT
510 520 530 540 550
TNALERFLLD RKIKGPCWLQ VTGFKVSPTP MSWCNTEVTL TEPKNVELVQ
560 570 580 590 600
DKGKPAPPPP LTLLSLNVRT SMNPKTSRNE ICMISMLTHN RFHIDRPAPQ
610 620 630 640 650
PAFNRHMCAL TRPAVVSWPL DLNFEMAKYK STTVHKHDSE RALLSWFLAQ
660 670 680 690 700
YQKIDADLIV TFDSMDCQLN VITDQIVALK IPQWSRMGRL RLSQSFGKRL
710 720 730 740 750
LEHFVGRMVC DVKRSAEECI RARSYDLQTL CKQVLKLKES ERMEVNADDL
760 770 780 790 800
LEMYEKGESI TKLISLTMQD NSYLLRLMCE LNIMPLALQI TNICGNTMTR
810 820 830 840 850
TLQGGRSERN EFLLLHAFHE KNYIVPDKKP VSKRSGAGDT DATLSGADAT
860 870 880 890 900
MQTKKKAAYA GGLVLEPMRG LYEKYVLLMD FNSLYPSIIQ EYNICFTTVQ
910 920 930 940 950
QPVDADELPT LPDSKTEPGI LPLQLKRLVE SRKEVKKLMA APDLSPELQM
960 970 980 990 1000
QYHIRQMALK LTANSMYGCL GFAHSRFFAQ HLAALVTHKG REILTNTQQL
1010 1020 1030 1040 1050
VQKMNYDVVY GDTDSLMINT NITDYDQVYK IGHNIKQSVN KLYKQLELDI
1060 1070 1080 1090 1100
DGVFGCLLLL KKKKYAAIKL SKDSKGNLRR EQEHKGLDIV RRDWSQLAVM
1110 1120 1130 1140 1150
VGKAVLDEVL SEKPLEEKLD AVHAQLEKIK TQIAEGVVPL PLFVITKQLT
1160 1170 1180 1190 1200
RTPQEYANSA SLPHVQVALR MNRERNRRYK KGDMVDYVIC LDGTTNAAMQ
1210 1220 1230 1240 1250
RAYHLDELKT SEDKKLQLDT NYYLGHQIHP VVTRMVEVLE GTDASRIAEC
1260 1270 1280 1290 1300
LGMDPTKFRQ NAQRTQRENT EQSEGESLLK TTLQLYRLCE PFRFQCVTCK
1310 1320 1330 1340 1350
TEQLMASAYR PGPSNSHIAV LQQCAKSECQ TAPIQYLASV RNQLQLSMRQ
1360 1370 1380 1390 1400
YVQRFYKNWL VCDHPDCNFN TRTHSLRKKS HRPLCQKCRS GSLLRQYTER
1410 1420 1430 1440 1450
DLYNQLCYLR FMFDLGKQTL QQKPTLTPEL EQAYQLLYET VDQQLQSSSY
1460 1470 1480
VIISLSKLFA RSLAQMSLQP SVAQPQIEAI PSALADVV
Length:1,488
Mass (Da):169,903
Last modified:March 15, 2004 - 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:i76C65EE2E2D5B065
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAL48000 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA14340 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAA32745 differs from that shown. Reason: Erroneous gene model prediction.Curated

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 conflicti99S → L in S48157 (PubMed:1429896).Curated1
Sequence conflicti117E → A in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti117E → A in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti137K → KK in S48157 (PubMed:1429896).Curated1
Sequence conflicti148D → DD in S48157 (PubMed:1429896).Curated1
Sequence conflicti200I → M in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti200I → M in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti210 – 227AEASS…LKPKA → RRPVAITRCWSAFSPRQ in S48157 (PubMed:1429896).CuratedAdd BLAST18
Sequence conflicti364F → L in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti364F → L in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti376M → I in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti376M → I in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti379E → Q in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti379E → Q in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti478K → N in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti478K → N in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti739E → G in S48157 (PubMed:1429896).Curated1
Sequence conflicti818 – 819FH → ST in BAA14340 (PubMed:1923767).Curated2
Sequence conflicti818 – 819FH → ST in BAA32745 (PubMed:9858578).Curated2
Sequence conflicti819H → Y in AAL48000 (PubMed:12537569).Curated1
Sequence conflicti842A → R in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti842A → R in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti881F → L in BAA14340 (PubMed:1923767).Curated1
Sequence conflicti881F → L in BAA32745 (PubMed:9858578).Curated1
Sequence conflicti897 – 898TT → NP in BAA14340 (PubMed:1923767).Curated2
Sequence conflicti897 – 898TT → NP in BAA32745 (PubMed:9858578).Curated2
Sequence conflicti992 – 993EI → D in BAA14340 (PubMed:1923767).Curated2
Sequence conflicti992 – 993EI → D in BAA32745 (PubMed:9858578).Curated2
Sequence conflicti1155 – 1157EYA → DYR in BAA14340 (PubMed:1923767).Curated3
Sequence conflicti1155 – 1157EYA → DYR in BAA32745 (PubMed:9858578).Curated3
Sequence conflicti1178R → L in S48157 (PubMed:1429896).Curated1
Sequence conflicti1187 – 1189YVI → LCD in BAA14340 (PubMed:1923767).Curated3
Sequence conflicti1187 – 1189YVI → LCD in BAA32745 (PubMed:9858578).Curated3
Sequence conflicti1197 – 1205AAMQRAYHL → WPCSEHTIS in S48157 (PubMed:1429896).Curated9
Sequence conflicti1222 – 1223YY → LL in S48157 (PubMed:1429896).Curated2
Sequence conflicti1292 – 1310FRFQC…ASAYR → SASSALPVRRSSWRLRTD in S48157 (PubMed:1429896).CuratedAdd BLAST19
Sequence conflicti1325 – 1351AKSEC…SMRQY → VSPSAKRHRFSTWQACAILQ LSM in BAA14340 (PubMed:1923767).CuratedAdd BLAST27
Sequence conflicti1392S → T in S48157 (PubMed:1429896).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D90310 Genomic DNA Translation: BAA14340.1 Sequence problems.
S48157 mRNA No translation available.
AB011813 Genomic DNA Translation: BAA32745.1 Sequence problems.
AE014297 Genomic DNA Translation: AAF55908.2
AY070529 mRNA Translation: AAL48000.1 Different initiation.

Protein sequence database of the Protein Information Resource

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PIRi
S28079

NCBI Reference Sequences

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RefSeqi
NP_536736.2, NM_080488.3

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
FBtr0084115; FBpp0083514; FBgn0259113

Database of genes from NCBI RefSeq genomes

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GeneIDi
42553

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG6349

<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
D90310 Genomic DNA Translation: BAA14340.1 Sequence problems.
S48157 mRNA No translation available.
AB011813 Genomic DNA Translation: BAA32745.1 Sequence problems.
AE014297 Genomic DNA Translation: AAF55908.2
AY070529 mRNA Translation: AAL48000.1 Different initiation.
PIRiS28079
RefSeqiNP_536736.2, NM_080488.3

3D structure databases

SMRiP26019
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi67519, 15 interactors
ComplexPortaliCPX-2090, DNA polymerase alpha:primase complex
DIPiDIP-23937N
IntActiP26019, 6 interactors
STRINGi7227.FBpp0083514

Chemistry databases

BindingDBiP26019
ChEMBLiCHEMBL6039

PTM databases

iPTMnetiP26019

Proteomic databases

PaxDbiP26019
PRIDEiP26019

Genome annotation databases

EnsemblMetazoaiFBtr0084115; FBpp0083514; FBgn0259113
GeneIDi42553
KEGGidme:Dmel_CG6349

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
42553
FlyBaseiFBgn0259113, PolA1

Phylogenomic databases

eggNOGiKOG0970, Eukaryota
GeneTreeiENSGT00550000074891
HOGENOMiCLU_001718_0_0_1
InParanoidiP26019
OMAiNIMPLAL
OrthoDBi293315at2759
PhylomeDBiP26019

Enzyme and pathway databases

ReactomeiR-DME-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-DME-68952, DNA replication initiation
R-DME-68962, Activation of the pre-replicative complex
R-DME-69091, Polymerase switching
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

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BioGRID-ORCSi
42553, 0 hits in 3 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
DNApol-alpha50, fly

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

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GenomeRNAii
42553

Protein Ontology

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PROi
PR:P26019

Gene expression databases

BgeeiFBgn0259113, Expressed in embryo and 28 other tissues
GenevisibleiP26019, DM

Family and domain databases

Gene3Di1.10.132.60, 1 hit
1.10.3200.20, 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
IPR024647, DNA_pol_a_cat_su_N
IPR042087, DNA_pol_B_C
IPR023211, DNA_pol_palm_dom_sf
IPR038256, Pol_alpha_znc_sf
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
IPR015088, Znf_DNA-dir_DNA_pol_B_alpha
PfamiView protein in Pfam
PF12254, DNA_pol_alpha_N, 1 hit
PF00136, DNA_pol_B, 1 hit
PF03104, DNA_pol_B_exo1, 1 hit
PF08996, zf-DNA_Pol, 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

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 nameiDPOLA_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: P26019
Secondary accession number(s): O77034, Q8T992, Q9VD90
<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: May 1, 1992
Last sequence update: March 15, 2004
Last modified: June 2, 2021
This is version 198 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

Direct protein sequencing, Reference proteome

Documents

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