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Protein

DNA polymerase epsilon catalytic subunit A

Gene

POL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA polymerase epsilon (DNA polymerase II) 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.1 Publication

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi2108ZincBy similarity1
Metal bindingi2111ZincBy similarity1
Metal bindingi2130ZincBy similarity1
Metal bindingi2133ZincBy similarity1
Metal bindingi2164Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2167Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2179Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi2181Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2108 – 2133CysA-typeAdd BLAST26

GO - Molecular functioni

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

GO - Biological processi

  • base-excision repair Source: SGD
  • DNA-dependent DNA replication Source: SGD
  • DNA replication proofreading Source: SGD
  • double-strand break repair Source: SGD
  • double-strand break repair via nonhomologous end joining Source: SGD
  • error-prone translesion synthesis Source: SGD
  • gene conversion Source: SGD
  • heterochromatin organization involved in chromatin silencing Source: SGD
  • intra-S DNA damage checkpoint Source: SGD
  • leading strand elongation Source: SGD
  • mitotic DNA replication checkpoint Source: SGD
  • mitotic sister chromatid cohesion Source: SGD
  • nucleotide-excision repair, DNA gap filling Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33258-MONOMER.
ReactomeiR-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase epsilon catalytic subunit A (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit A
Gene namesi
Name:POL2
Synonyms:DUN2
Ordered Locus Names:YNL262W
ORF Names:N0825
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL262W.
SGDiS000005206. POL2.

Subcellular locationi

GO - Cellular componenti

  • epsilon DNA polymerase complex Source: SGD
  • replication fork Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi644M → I in POL2-9; temperature-sensitive mutant. 1 Publication1
Mutagenesisi710P → S in POL2-18; temperature-sensitive mutant. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000464671 – 2222DNA polymerase epsilon catalytic subunit AAdd BLAST2222

Proteomic databases

MaxQBiP21951.
PRIDEiP21951.

PTM databases

iPTMnetiP21951.

Interactioni

Subunit structurei

DNA polymerase epsilon is a heterotetramer consisting of POL2, DPB2, DPB3 and DPB4.1 Publication

Protein-protein interaction databases

BioGridi35577. 351 interactors.
DIPiDIP-2532N.
IntActiP21951. 18 interactors.
MINTiMINT-670401.

Structurei

Secondary structure

12222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 49Combined sources17
Turni67 – 71Combined sources5
Beta strandi72 – 87Combined sources16
Beta strandi114 – 123Combined sources10
Beta strandi128 – 134Combined sources7
Beta strandi138 – 144Combined sources7
Helixi146 – 148Combined sources3
Helixi149 – 159Combined sources11
Turni160 – 163Combined sources4
Beta strandi166 – 173Combined sources8
Helixi180 – 182Combined sources3
Beta strandi186 – 192Combined sources7
Helixi196 – 215Combined sources20
Turni222 – 224Combined sources3
Helixi235 – 238Combined sources4
Beta strandi239 – 244Combined sources6
Helixi249 – 257Combined sources9
Beta strandi263 – 268Combined sources6
Beta strandi271 – 274Combined sources4
Beta strandi286 – 293Combined sources8
Turni303 – 305Combined sources3
Beta strandi308 – 315Combined sources8
Beta strandi318 – 324Combined sources7
Turni325 – 327Combined sources3
Beta strandi328 – 330Combined sources3
Beta strandi346 – 354Combined sources9
Helixi355 – 369Combined sources15
Beta strandi372 – 378Combined sources7
Turni379 – 382Combined sources4
Helixi383 – 393Combined sources11
Helixi398 – 402Combined sources5
Beta strandi415 – 421Combined sources7
Helixi422 – 429Combined sources8
Helixi434 – 436Combined sources3
Helixi439 – 447Combined sources9
Helixi456 – 458Combined sources3
Helixi459 – 465Combined sources7
Helixi467 – 487Combined sources21
Helixi489 – 497Combined sources9
Beta strandi500 – 502Combined sources3
Helixi504 – 509Combined sources6
Helixi512 – 526Combined sources15
Beta strandi546 – 553Combined sources8
Beta strandi558 – 560Combined sources3
Beta strandi564 – 567Combined sources4
Beta strandi572 – 575Combined sources4
Helixi578 – 597Combined sources20
Helixi604 – 606Combined sources3
Beta strandi607 – 609Combined sources3
Helixi610 – 626Combined sources17
Beta strandi629 – 632Combined sources4
Beta strandi634 – 641Combined sources8
Helixi644 – 652Combined sources9
Helixi656 – 658Combined sources3
Beta strandi659 – 662Combined sources4
Beta strandi664 – 666Combined sources3
Beta strandi678 – 689Combined sources12
Helixi694 – 705Combined sources12
Beta strandi708 – 710Combined sources3
Beta strandi720 – 722Combined sources3
Helixi723 – 725Combined sources3
Helixi728 – 747Combined sources20
Beta strandi752 – 766Combined sources15
Helixi769 – 797Combined sources29
Turni798 – 800Combined sources3
Beta strandi801 – 803Combined sources3
Helixi808 – 832Combined sources25
Helixi833 – 835Combined sources3
Helixi844 – 868Combined sources25
Beta strandi869 – 875Combined sources7
Beta strandi878 – 884Combined sources7
Beta strandi890 – 895Combined sources6
Beta strandi900 – 904Combined sources5
Helixi905 – 918Combined sources14
Beta strandi920 – 928Combined sources9
Turni929 – 932Combined sources4
Beta strandi933 – 939Combined sources7
Beta strandi944 – 955Combined sources12
Beta strandi969 – 972Combined sources4
Beta strandi978 – 984Combined sources7
Turni985 – 987Combined sources3
Beta strandi988 – 992Combined sources5
Helixi993 – 1002Combined sources10
Helixi1003 – 1007Combined sources5
Beta strandi1009 – 1011Combined sources3
Helixi1012 – 1031Combined sources20
Turni1032 – 1036Combined sources5
Helixi1039 – 1046Combined sources8
Beta strandi1048 – 1051Combined sources4
Helixi1056 – 1059Combined sources4
Helixi1065 – 1077Combined sources13
Helixi1079 – 1082Combined sources4
Beta strandi1083 – 1086Combined sources4
Beta strandi1088 – 1095Combined sources8
Beta strandi1097 – 1099Combined sources3
Helixi1102 – 1104Combined sources3
Beta strandi1106 – 1108Combined sources3
Helixi1109 – 1113Combined sources5
Helixi1116 – 1127Combined sources12
Helixi1137 – 1140Combined sources4
Helixi1143 – 1157Combined sources15
Helixi1159 – 1164Combined sources6
Helixi1178 – 1183Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M8OX-ray2.20A1-1228[»]
4PTFX-ray2.81A1-1187[»]
ProteinModelPortaliP21951.
SMRiP21951.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2164 – 2181CysB motifAdd BLAST18

Domaini

The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C.
The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated
Contains 1 CysA-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2108 – 2133CysA-typeAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000010194.
HOGENOMiHOG000196287.
InParanoidiP21951.
KOiK02324.
OMAiCENKSMS.
OrthoDBiEOG092C00WD.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR013697. DNA_pol_e_suA_C.
IPR029703. POL2.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10670. PTHR10670. 2 hits.
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08490. DUF1744. 1 hit.
[Graphical view]
SMARTiSM01159. DUF1744. 1 hit.
SM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.

Sequencei

Sequence statusi: Complete.

P21951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM
60 70 80 90 100
GFERYVPPQY NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG
110 120 130 140 150
NSNDGERVTT NQGISGVDFY FLDEEGGSFK STVVYDPYFF IACNDESRVN
160 170 180 190 200
DVEELVKKYL ESCLKSLQII RKEDLTMDNH LLGLQKTLIK LSFVNSNQLF
210 220 230 240 250
EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE DIREYDVPYH
260 270 280 290 300
VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF
310 320 330 340 350
PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF
360 370 380 390 400
NENDEVALLQ RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD
410 420 430 440 450
EIGFAPDAEG EYKSSYCSHM DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN
460 470 480 490 500
PIELDPELMT PYAFEKPQHL SEYSVSDAVA TYYLYMKYVH PFIFSLCTII
510 520 530 540 550
PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE RFYDGHLLES
560 570 580 590 600
ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN
610 620 630 640 650
KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT
660 670 680 690 700
TNRLQPDSIK AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI
710 720 730 740 750
KRALQNETFP NKNKFSKKKV LTFDELSYAD QVIHIKKRLT EYSRKVYHRV
760 770 780 790 800
KVSEIVEREA IVCQRENPFY VDTVKSFRDR RYEFKGLAKT WKGNLSKIDP
810 820 830 840 850
SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR WYSMEMAGIT
860 870 880 890 900
CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK
910 920 930 940 950
LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY
960 970 980 990 1000
KAMILPSSKE EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS
1010 1020 1030 1040 1050
DIFKVFLEGD TLEGCYSAVA SVCNRWLDVL DSHGLMLEDE DLVSLICENR
1060 1070 1080 1090 1100
SMSKTLKEYE GQKSTSITTA RRLGDFLGED MVKDKGLQCK YIISSKPFNA
1110 1120 1130 1140 1150
PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI IDWGYYRERL
1160 1170 1180 1190 1200
GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF
1210 1220 1230 1240 1250
SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT
1260 1270 1280 1290 1300
NEEDPLVLPS EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS
1310 1320 1330 1340 1350
RERSALGSMI RKQAESYANS TWEVLQYKDS GEPGVLEVFV TINGKVQNIT
1360 1370 1380 1390 1400
FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS ASLPNNPKTS NPAGGQLFKI
1410 1420 1430 1440 1450
TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD LGASVTFRSK
1460 1470 1480 1490 1500
AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS
1510 1520 1530 1540 1550
LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV
1560 1570 1580 1590 1600
DIKEDINFEF VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL
1610 1620 1630 1640 1650
LGTIRLLNQM PIVKLSLNEV LLPQLNWQPT LLKKLVNHVL SSGSWISHLI
1660 1670 1680 1690 1700
KLSQYSNIPI CNLRLDSMDY IIDVLYARKL KKENIVLWWN EKAPLPDHGG
1710 1720 1730 1740 1750
IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT VNTILTSALI
1760 1770 1780 1790 1800
NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD
1810 1820 1830 1840 1850
EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE
1860 1870 1880 1890 1900
FSALGSTIVY ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL
1910 1920 1930 1940 1950
NIKRYWDLLI WMDKFNFSGL ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ
1960 1970 1980 1990 2000
PEFEDWMMII LDSMLKTKQS YLKLNSGTQR PTQIVNVKKQ DKEDSVENSL
2010 2020 2030 2040 2050
NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL PGSHLNVKNP
2060 2070 2080 2090 2100
LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS
2110 2120 2130 2140 2150
LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL
2160 2170 2180 2190 2200
RSDIESYLIQ DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV
2210 2220
FKQVAKYYGF DILLSCIADL TI
Length:2,222
Mass (Da):255,671
Last modified:August 1, 1991 - v1
Checksum:iCBCDDE2AB147D65B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60416 Genomic DNA. Translation: AAA88711.1.
X92494 Genomic DNA. Translation: CAA63235.1.
Z71538 Genomic DNA. Translation: CAA96169.1.
BK006947 Genomic DNA. Translation: DAA10297.1.
PIRiA36028.
RefSeqiNP_014137.1. NM_001183100.1.

Genome annotation databases

EnsemblFungiiYNL262W; YNL262W; YNL262W.
GeneIDi855459.
KEGGisce:YNL262W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60416 Genomic DNA. Translation: AAA88711.1.
X92494 Genomic DNA. Translation: CAA63235.1.
Z71538 Genomic DNA. Translation: CAA96169.1.
BK006947 Genomic DNA. Translation: DAA10297.1.
PIRiA36028.
RefSeqiNP_014137.1. NM_001183100.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M8OX-ray2.20A1-1228[»]
4PTFX-ray2.81A1-1187[»]
ProteinModelPortaliP21951.
SMRiP21951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35577. 351 interactors.
DIPiDIP-2532N.
IntActiP21951. 18 interactors.
MINTiMINT-670401.

PTM databases

iPTMnetiP21951.

Proteomic databases

MaxQBiP21951.
PRIDEiP21951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL262W; YNL262W; YNL262W.
GeneIDi855459.
KEGGisce:YNL262W.

Organism-specific databases

EuPathDBiFungiDB:YNL262W.
SGDiS000005206. POL2.

Phylogenomic databases

GeneTreeiENSGT00390000010194.
HOGENOMiHOG000196287.
InParanoidiP21951.
KOiK02324.
OMAiCENKSMS.
OrthoDBiEOG092C00WD.

Enzyme and pathway databases

BioCyciYEAST:G3O-33258-MONOMER.
ReactomeiR-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.

Miscellaneous databases

PROiP21951.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR013697. DNA_pol_e_suA_C.
IPR029703. POL2.
IPR012337. RNaseH-like_dom.
[Graphical view]
PANTHERiPTHR10670. PTHR10670. 2 hits.
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08490. DUF1744. 1 hit.
[Graphical view]
SMARTiSM01159. DUF1744. 1 hit.
SM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDPOE_YEAST
AccessioniPrimary (citable) accession number: P21951
Secondary accession number(s): D6W0T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 2, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Present with 1970 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.