DPOE_CANGA
ID DPOE_CANGA Reviewed; 2217 AA.
AC Q6FNY7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=CAGL0J08030g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
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DR EMBL; CR380956; CAG61008.1; -; Genomic_DNA.
DR RefSeq; XP_448057.1; XM_448057.1.
DR AlphaFoldDB; Q6FNY7; -.
DR SMR; Q6FNY7; -.
DR STRING; 5478.XP_448057.1; -.
DR PRIDE; Q6FNY7; -.
DR EnsemblFungi; CAG61008; CAG61008; CAGL0J08030g.
DR GeneID; 2889864; -.
DR KEGG; cgr:CAGL0J08030g; -.
DR CGD; CAL0133406; CAGL0J08030g.
DR VEuPathDB; FungiDB:CAGL0J08030g; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q6FNY7; -.
DR OMA; MLDQCRY; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:EnsemblFungi.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0032183; F:SUMO binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:EnsemblFungi.
DR GO; GO:0045004; P:DNA replication proofreading; IEA:EnsemblFungi.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0035822; P:gene conversion; IEA:EnsemblFungi.
DR GO; GO:0006272; P:leading strand elongation; IEA:EnsemblFungi.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:EnsemblFungi.
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..2217
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046459"
FT ZN_FING 2104..2129
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 2160..2177
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2163
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2217 AA; 256211 MW; 86979C27DB4A4268 CRC64;
MSTARFKRGN GQAGSLSNGY AVTAQQLLQA AKVDDIDAMM GFERYVPPQY NGRVDPDRLD
QVPGRTGWLV NMHPTLISEE IASGGGSDYN PSAAGIAGVD FYFLDEEGGS FKSSITYDPY
FFVTVTDDAR LNDVEEFLKK YLETCLKDIS TLKKEDLKLD NHLLGLQKSL IKLSFVNSNQ
LFEARKLLRP ILAENESNKQ QRNVFKHSNI SNGNGMLSSN VNRFASSSVQ DKKDAKQYIE
DIREYDVPYH VRVSIDKDIR VGKWYKVTHE GFFVWPDKVA FADPVVLAFD IETTKAPLKF
PEASVDQVMM ISYMIDGDGF LITNREIISE DIEDFEYTPK PELQGHVTIF NEVDELAVLQ
RFFEHIRDVR PTVISTFNGD FFDWPFIEKR ASVRGLDMFE EIGFAPDSEG EYKSSYCVHM
DCFRWVKRDS YLPQGSQGLK AVTQAKLGYN PIELDPELMT PYAYERPQQL SEYSVSDAVA
TYYLYMKYVH PFIFSLCTII PLNPDEVLRK GTGTLCEMLL MVQAYQGNIL LPNKHTDPLE
RFYDGHLLES ETYVGGHVES LEAGVFRSDL ATEFKIDTSA IDELIEDLPH ALKFAVEVEN
KAKMEDVTNF EEIKEQIKEQ LLELKENNKR HEKPLIYHVD VASMYPNIMT TNRLQPDSIK
TEKDCASCDF NRPGKSCARR LKWAWRGEFY PAKSDEYNMI KRALQNETFP NKNKFSKKPY
LTFDELSYSE QVAHIKKRLT EYSKKVYHRI KVSEIVEREA IVCQRENPFY VNTVKSFRDR
RYEFKGLAKK WKGKMSSIDR NDKHGKDEAN KMVVLYDSLQ LAHKVILNSF YGYVMRKGSR
WYSMEMAGIT CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPEN FFLKLENGKK
LFVSYPCSML NYRVHQKFTN HQYQELVDPV KHKYETHSEN TIFFEVDGPY KAMILPTSKE
EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS DIFKVFLDGK TLEECYASVA
AVSNRWLDIL DNKGSMLEDE DLVSLICENR SMSKSLKEYE GQKSTSITTA KRLGEFLGED
MVKDKGLQCK YIISSKPHGA PVTERAIPVA IFSSDINVKR SFLRRWTMDH SLDNFDIRTI
LDWGYYRERL ASVIQKIITI PAALQNVPNP VPRVEHPDWL KRRIAVKEDK FKQSKLERFL
SKSSQEPQNR RIKDIEELFH EDDDIKRIKL AKVTSRNKNK RNRDVQKNDE ESLVLPATMP
SMEEDYVSWL SYQKIKWKIQ RRDRIRRTQL FGKSGETNSR SVLGSMIRKQ AEMFANGSWE
VLQYRDNYEA GAVDAYVIIN GKVQVLKIYV PRTLYINFKT DSVPLKKIKN CEVERSNAIL
PNDARINNDS ASPLFKLTLS EQVYLDELED SGSVLNDESV LGIYESHISP AQKALMDLGT
TISFKSKKVG SLGKSLQDGF HLKDLTSVGN DRYLSHFDLN VCYLLHIDTN IDYEFFVIFR
SWENKLSIFV KKPSNNAQEL LESTIIGIFK EQYHKRKDRI TKFNKYINLS DNVDMNSNHY
TDKKKLFKAI NQEFAMIKEQ KGQQVLLLMQ SPFPSLIKKN IRYSTQIPII ELSMNILALP
QLNWQNVMIN KLCSYIISTS YWVSHLVSLS QHSNVPICNI NLEKMDFVID VIYARRLKLD
NIILWWNEQS PLPDHGGMEN DFDQNTSWIM NDLDFPNINV PDVYDNVVLE VSIENLVVNT
ILCSTLINEA EGSDLVDMNT VDVSDKPVGN NQGIVQDSFS HDALAVLKSL LKEWWDRALE
KNITADLLVN SLVSWVYSTD SKLFDGSLRY HIHNLTKKSL FQLMNEFNEL GSFIVSADRN
RLLIKTNKIS PETCYAYSHY MIKSIRSNPM FTYLDLNIER YWDLLIWMDK YNFSGLSCSQ
IEEREKQDYT AYSNWQIKYY LPRIYQSEFE DWAMIILDSM VKTKRAFLES SYGTQRATQI
VTGLTPQSDT EDISPLSSFS KEIGKPLLQR VNKLFRNQRE FILDPGFSED YAFPILPGSH
IKMDDPLLEF IKSLFQILLL SKSTTLEVRQ LRKEVLKFLE IREFAKEAEF QNPSDSLVIN
GILCEYCSYV SDLDLCRDGL DGKFQCPRCD KSINDSLLQE HMIQNLAIEY QTYITQDLRC
EKCHTVKRDL MSTNCNCSGN WVCTTKPEKL SNIVKIYKQV AEFYNYSLVK NALESLY
