DPOE_DEBHA
ID DPOE_DEBHA Reviewed; 2226 AA.
AC Q6BNG2; B5RU53;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA polymerase epsilon catalytic subunit A;
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P15436};
DE AltName: Full=DNA polymerase II subunit A;
GN Name=POL2; OrderedLocusNames=DEHA2E22000g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC replication. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000250|UniProtKB:P15436};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P15436};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436};
CC -!- SUBUNIT: Heterotetramer. Consists of 4 subunits: POL2, DPB2, DPB3 and
CC DPB4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000250|UniProtKB:P15436}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250|UniProtKB:P15436}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382137; CAR65865.1; -; Genomic_DNA.
DR RefSeq; XP_002770523.1; XM_002770477.1.
DR AlphaFoldDB; Q6BNG2; -.
DR SMR; Q6BNG2; -.
DR STRING; 4959.XP_002770523.1; -.
DR PRIDE; Q6BNG2; -.
DR EnsemblFungi; CAR65865; CAR65865; DEHA2E22000g.
DR GeneID; 8998818; -.
DR KEGG; dha:DEHA2E22000g; -.
DR VEuPathDB; FungiDB:DEHA2E22000g; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q6BNG2; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 39650at2759; -.
DR Proteomes; UP000000599; Chromosome E.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670; PTHR10670; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08490; DUF1744; 1.
DR SMART; SM01159; DUF1744; 1.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2226
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046461"
FT ZN_FING 2112..2137
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 1240..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2168..2185
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2168
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2183
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2185
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2226 AA; 256529 MW; 6493E4DCFB1D1100 CRC64;
MPSKYGNGSG TGRFVKNSTI KSEFRNNGYN RAEVIDPSIA NNPMLNDSIQ KRELVNRIDQ
LDSIMGFDRI EHGEMDGAKP RRGWLVNMHA TTIPTDEYLA GYSGVDYYFL DEEGGSFKAT
IRYDPYFYLV VIPGHESEVE EMLRKVLEPC SLKGLLRVAK EDLSLPNHLV GLKKTLVKLS
FHNVVDLLSA RRLLNPIIKD NKMKRDTRDI YQVMNFNNVN NANGTEIQTN FNDKSTEQIA
DPATLIDDIR EYDVPYHVRV SIDEKIRVGK WYNVFVKHSE VRLEEDKEKI AFADPVILAF
DIETTKAPLK FPDAKTDQIM MISYMIDGEG FLITNREIIS EDIEDFEYTP KPEYPGLFTI
FNEPDEKMVL VRFFEHIRDS RPTVIATFNG DFFDWPFVEK RTTFHDMDMF EEIGFAKDNE
GEYKSKYCVH MDCYRWVKRD SYLPQGSQGL KAVTTAKLGY NPTELDPELM TPYAYEKPQL
LSEYSVSDAV ATYYLYYKYV HPFIFSLCTI IPLNPDEVLR KGTGTLCEML LMVQAYENGI
VLPNKHTEPI ERFYDGHLLE SETYVGGHVE SLEAGVFRSD LPNDFKVDPT AVDEILGDLH
NALKFCIEVE NNKKVEDVEN YDEVYNQIKD SLVNLRETPI RHENPLIFHV DVASMYPNIM
TSNRLQPDSM KSEEDCAACD FNRPGKNCDR RLPWSWRGEY YPAEMNEYGM IKRTLQNETF
PPAKPWLPAK TFDELSYSEQ ASLIKKRLSD YSRKVYHRIK QSKTVSREAI VCQRENPFYV
DTVRSFRDRR YEFKTLVKVW KGKTAKIDKH DTIAKDEAKK MVVLYDSLQL AHKVILNSFY
GYVMRKGSRW YSMEMAGITC LTGATIIQMA RSLVERLGRP LELDTDGIWC ILPKSFPENY
YFKCKDGKNI FLEYPCSMLN YLVHDKFTNH QYQDLVDPNT FKYKTRSENS IFFEVDGPYK
AMVLPTSKEE GKGLKKRYAV FNDDGSLAEL KGFELKRRGE LQLIKNFQSD IFKLFLDGDS
LENCYKSVAT VANNWLDVLD TKGGMLEDED LIELICENRS MSKSLAEYGN QKSTSITTAK
RLGEFLGEEM IKDAGLACKY IISSKPIGSP VTERAVPVSI FSSEKKEFFL KKWLKDPSLE
NFDPRSVIDW NYYYERLASV VQKIISIPAA LQDIKNPVPR VPHPEWLQKK INSKEDSKQQ
SSISSFFGQA TKKEVLQKSI KSIQDIEDFG ELDASIPKGR VSKVTSRKRR NGKANNVSDS
EEEERNNAIL NGECPSMTED YAGFLQYQKA KWKVQEKNRE RRKKLFGSNA ESSHRSSVGG
IIRRQAENIA GSDWEILEYK ADPSKPGDIK VYVSASNKVH SFTFHVPKKV YASFKTELSP
KKAIRNCEIE KSTAVLPNGH DGSNLYKLTM PEETYLEEST KVESLLQDSN ILGLYETQVG
AVERAIIDLG NNIRFDDTKV GALGKGLKNG FNVKDLMKVE RDSYLKRFGM DIIYFLHLVT
NSYEFFTIFK SWENTASIFV LKPSANAQEL PSNMDKIYRE IFEAKKDRLG KMYSIIEYPD
EMKFETTYFH DTAKIFKKMD NCISKIYESR SNRALLAVQS PYTTKVLNLL KSTSSFPTIK
MNVSELSLPA VGWQSLIIKR VVNHYFVLAS WIKKLISLAK YGNVPLCNLQ IENMGYLIDI
EYARRLSQSN IVLWLSSRPL PDHGGFEMDK AQDFENLEFP TINNPEIYET ACLEVEIGTL
TINTILTSAL INEAEGTDLA DDAVQFDNNN GASTIAEDSF STPALSILRG MVKDWWDDAL
KNNDNADSMM NNLVTWVQRS DSLLYDYSLH YHVHNLTTKA LLQLIGEFKR MNAQVIFANR
NKMLIQTTKV SIENSYAYGQ YILKAARSKP LFNFLDLRIV KYWDLLVWMD EYNFGGRCCT
EITNDEVQNL IPVNKWQITK FLPVIFQNEF EDWLIIFLDS LTKFKNDTLI PGTQTGTPRV
TQIAHILKGQ KKLDSNETEE ESISNGVMEL FRKPLQKRIE KLARRQNESI LNPELRQEYE
FPKLPGSYTS MKNPSLELVK FLCAVFGLSR KRNIEVRLLR RELLSIFDIK EFSDEAAFKN
PSSSLKIPHV ICDYCNYIRD IDFCRDEQKN IWNCSNCNKT YNRVAIEEEL VAQYNKLLTK
FYIQDLKCSK CHQIKSDNMS EYCKCSGKWT ETLKYTEVDK RLQIFSNVGG FFNLQLLKGI
IEELAL
