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Protein

DNA polymerase delta catalytic subunit

Gene

POL3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

DNA polymerase delta (DNA polymerase III) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. POL3 contains the polymerase active site and most likely the active site for the 3'-5' exonuclease activity.1 Publication

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_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

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

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 bindingi1009Zinc1
Metal bindingi1012Zinc1
Metal bindingi1024Zinc1
Metal bindingi1027Zinc1
Metal bindingi1056Iron-sulfur (4Fe-4S)1
Metal bindingi1059Iron-sulfur (4Fe-4S)1
Metal bindingi1069Iron-sulfur (4Fe-4S)1
Metal bindingi1074Iron-sulfur (4Fe-4S)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 fingeri1009 – 1027CysA-typeAdd BLAST19

<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

  • 3'-5'-exodeoxyribonuclease activity Source: SGD
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • DNA-directed DNA polymerase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • nucleotide binding Source: InterPro

GO - Biological processi

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

Molecular functionDNA-binding, DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA replication
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29505-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-2564818 Cytosolic iron-sulfur cluster assembly (yeast)
R-SCE-69166 Removal of the Flap Intermediate
R-SCE-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_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 polymerase delta catalytic subunit (EC:2.7.7.7)
Alternative name(s):
DNA polymerase III
<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:POL3
Synonyms:CDC2, TEX1
Ordered Locus Names:YDL102W
ORF Names:D2366
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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: Chromosome IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002260 POL3

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; 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

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>Mutagenesisi1009C → A: Impairs iron-sulfur-binding. 1 Publication1
Mutagenesisi1012C → A: Impairs iron-sulfur-binding. 1 Publication1
Mutagenesisi1024C → A: Impairs iron-sulfur-binding. 1 Publication1
Mutagenesisi1027C → A: Impairs iron-sulfur-binding. 1 Publication1
Mutagenesisi1056C → A: Abolishes iron-sulfur-binding. 1 Publication1
Mutagenesisi1059C → A: Abolishes iron-sulfur-binding. 1
Mutagenesisi1069C → A: Abolishes iron-sulfur-binding. 1 Publication1
Mutagenesisi1074C → A: Abolishes iron-sulfur-binding. 1 Publication1
Mutagenesisi1074C → S in pol3-13; synthetically lethal with mutations of NBP35, DRE2 and TAH18. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000464541 – 1097DNA polymerase delta catalytic subunitAdd BLAST1097

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 residuei30PhosphoserineCombined sources1
Modified residuei37PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P15436

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

More...
PaxDbi
P15436

PRoteomics IDEntifications database

More...
PRIDEi
P15436

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P15436

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P15436

<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

DNA polymerase delta is a heterotrimer of POL3, POL32 and HYS2. Interacts with PCNA.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
POL31P469575EBI-6134,EBI-6080

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31960, 669 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2101 DNA polymerase delta complex

Database of interacting proteins

More...
DIPi
DIP-2524N

Protein interaction database and analysis system

More...
IntActi
P15436, 5 interactors

Molecular INTeraction database

More...
MINTi
P15436

STRING: functional protein association networks

More...
STRINGi
4932.YDL102W

<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

11097
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
P15436

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

More...
SMRi
P15436

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Motifi1056 – 1074CysB motifAdd BLAST19

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1009 – 1027CysA-typeAdd BLAST19

Keywords - Domaini

Zinc-finger

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00560000077365

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000036616

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P15436

KEGG Orthology (KO)

More...
KOi
K02327

Identification of Orthologs from Complete Genome Data

More...
OMAi
CLVNYTE

Database of Orthologous Groups

More...
OrthoDBi
EOG092C0BQT

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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
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_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.

P15436-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEKRSLPMV DVKIDDEDTP QLEKKIKRQS IDHGVGSEPV STIEIIPSDS
60 70 80 90 100
FRKYNSQGFK AKDTDLMGTQ LESTFEQELS QMEHDMADQE EHDLSSFERK
110 120 130 140 150
KLPTDFDPSL YDISFQQIDA EQSVLNGIKD ENTSTVVRFF GVTSEGHSVL
160 170 180 190 200
CNVTGFKNYL YVPAPNSSDA NDQEQINKFV HYLNETFDHA IDSIEVVSKQ
210 220 230 240 250
SIWGYSGDTK LPFWKIYVTY PHMVNKLRTA FERGHLSFNS WFSNGTTTYD
260 270 280 290 300
NIAYTLRLMV DCGIVGMSWI TLPKGKYSMI EPNNRVSSCQ LEVSINYRNL
310 320 330 340 350
IAHPAEGDWS HTAPLRIMSF DIECAGRIGV FPEPEYDPVI QIANVVSIAG
360 370 380 390 400
AKKPFIRNVF TLNTCSPITG SMIFSHATEE EMLSNWRNFI IKVDPDVIIG
410 420 430 440 450
YNTTNFDIPY LLNRAKALKV NDFPYFGRLK TVKQEIKESV FSSKAYGTRE
460 470 480 490 500
TKNVNIDGRL QLDLLQFIQR EYKLRSYTLN AVSAHFLGEQ KEDVHYSIIS
510 520 530 540 550
DLQNGDSETR RRLAVYCLKD AYLPLRLMEK LMALVNYTEM ARVTGVPFSY
560 570 580 590 600
LLARGQQIKV VSQLFRKCLE IDTVIPNMQS QASDDQYEGA TVIEPIRGYY
610 620 630 640 650
DVPIATLDFN SLYPSIMMAH NLCYTTLCNK ATVERLNLKI DEDYVITPNG
660 670 680 690 700
DYFVTTKRRR GILPIILDEL ISARKRAKKD LRDEKDPFKR DVLNGRQLAL
710 720 730 740 750
KISANSVYGF TGATVGKLPC LAISSSVTAY GRTMILKTKT AVQEKYCIKN
760 770 780 790 800
GYKHDAVVVY GDTDSVMVKF GTTDLKEAMD LGTEAAKYVS TLFKHPINLE
810 820 830 840 850
FEKAYFPYLL INKKRYAGLF WTNPDKFDKL DQKGLASVRR DSCSLVSIVM
860 870 880 890 900
NKVLKKILIE RNVDGALAFV RETINDILHN RVDISKLIIS KTLAPNYTNP
910 920 930 940 950
QPHAVLAERM KRREGVGPNV GDRVDYVIIG GNDKLYNRAE DPLFVLENNI
960 970 980 990 1000
QVDSRYYLTN QLQNPIISIV APIIGDKQAN GMFVVKSIKI NTGSQKGGLM
1010 1020 1030 1040 1050
SFIKKVEACK SCKGPLRKGE GPLCSNCLAR SGELYIKALY DVRDLEEKYS
1060 1070 1080 1090
RLWTQCQRCA GNLHSEVLCS NKNCDIFYMR VKVKKELQEK VEQLSKW
Length:1,097
Mass (Da):124,619
Last modified:July 27, 2011 - v4
<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:i16E4245C5DCC66DB
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 conflicti78 – 79EL → DV in CAA33504 (PubMed:2670563).Curated2
Sequence conflicti78 – 79EL → DV in CAA64911 (PubMed:8896274).Curated2
Sequence conflicti78 – 79EL → DV in CAA98669 (PubMed:9169867).Curated2
Sequence conflicti189H → R in CAA33504 (PubMed:2670563).Curated1
Sequence conflicti204G → D in CAA33504 (PubMed:2670563).Curated1
Sequence conflicti347 – 363SIAGA…VFTLN → YLALRNHSFVMCYSD in CAA33504 (PubMed:2670563).CuratedAdd BLAST17
Sequence conflicti647 – 649TPN → HY in CAA33504 (PubMed:2670563).Curated3
Sequence conflicti870V → D in CAA33504 (PubMed:2670563).Curated1
Sequence conflicti974Missing in CAA33504 (PubMed:2670563).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
X15477 Genomic DNA Translation: CAA33504.1
X61920 Genomic DNA Translation: CAA43922.1
X95644 Genomic DNA Translation: CAA64911.1
Z74150 Genomic DNA Translation: CAA98669.1
BK006938 Genomic DNA Translation: DAA11758.2

Protein sequence database of the Protein Information Resource

More...
PIRi
S67644 RNBYL3

NCBI Reference Sequences

More...
RefSeqi
NP_010181.2, NM_001180161.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDL102W_mRNA; YDL102W_mRNA; YDL102W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851456

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDL102W

<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
X15477 Genomic DNA Translation: CAA33504.1
X61920 Genomic DNA Translation: CAA43922.1
X95644 Genomic DNA Translation: CAA64911.1
Z74150 Genomic DNA Translation: CAA98669.1
BK006938 Genomic DNA Translation: DAA11758.2
PIRiS67644 RNBYL3
RefSeqiNP_010181.2, NM_001180161.2

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
3IAYX-ray2.00A67-985[»]
ProteinModelPortaliP15436
SMRiP15436
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31960, 669 interactors
ComplexPortaliCPX-2101 DNA polymerase delta complex
DIPiDIP-2524N
IntActiP15436, 5 interactors
MINTiP15436
STRINGi4932.YDL102W

PTM databases

iPTMnetiP15436

Proteomic databases

MaxQBiP15436
PaxDbiP15436
PRIDEiP15436
TopDownProteomicsiP15436

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL102W_mRNA; YDL102W_mRNA; YDL102W
GeneIDi851456
KEGGisce:YDL102W

Organism-specific databases

SGDiS000002260 POL3

Phylogenomic databases

GeneTreeiENSGT00560000077365
HOGENOMiHOG000036616
InParanoidiP15436
KOiK02327
OMAiCLVNYTE
OrthoDBiEOG092C0BQT

Enzyme and pathway databases

BioCyciYEAST:G3O-29505-MONOMER
ReactomeiR-SCE-2564818 Cytosolic iron-sulfur cluster assembly (yeast)
R-SCE-69166 Removal of the Flap Intermediate
R-SCE-69183 Processive synthesis on the lagging strand

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P15436

Family and domain databases

Gene3Di3.30.420.10, 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
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

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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 nameiDPOD_YEAST
<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: P15436
Secondary accession number(s): D6VRP8
<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: April 1, 1990
Last sequence update: July 27, 2011
Last modified: December 5, 2018
This is version 192 of the entry and version 4 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 programFungal 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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