DPOE_KLULA
ID DPOE_KLULA Reviewed; 2185 AA.
AC Q6CUS7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=KLLA0C02585g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382123; CAH01163.1; -; Genomic_DNA.
DR RefSeq; XP_452312.1; XM_452312.1.
DR AlphaFoldDB; Q6CUS7; -.
DR SMR; Q6CUS7; -.
DR STRING; 28985.XP_452312.1; -.
DR PRIDE; Q6CUS7; -.
DR EnsemblFungi; CAH01163; CAH01163; KLLA0_C02585g.
DR GeneID; 2892428; -.
DR KEGG; kla:KLLA0_C02585g; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q6CUS7; -.
DR OMA; MLDQCRY; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:EnsemblFungi.
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..2185
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046463"
FT ZN_FING 2072..2097
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 2128..2145
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2072
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2075
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2094
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2097
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2185 AA; 252061 MW; A3ADD50528D033A8 CRC64;
MSAFKGSTTA KFVGRGNEYP TQANSFAQVA QQLLNSKKVD EIDEMMGFPR FIPSPALSDS
KVGWLSNMHP TIISQEMLEE EGNLHSATVS GISGVDFYFI DEEGGSFKTT VTYDPYFFVS
CTDETRIHDI EEYLKKTLEQ CIKKVELVLK DDLAMNNHLV GLKKHLIKLS FSNSNQLFEA
RRILRPILKI NEDENGKKDI YNTGSDYSTR DVKTLIEDIR EYDVPYHVRV SIDKNIRVGK
WYAVSAQGLV ELEEKVTFAD PVVLAFDIET TKAPLKFPDS AIDQIMMISY MIDGEGFLIT
NREIISEDIE DFEYTPKDEY KGQFAIFNEP DEMALLQRFF EHIRDVRPTV ISTFNGDFFD
WPFVENRAKF HGLNMFDEIG FAPDSEGEYK SSYCTHMDCF RWVKRDSYLP QGSQGLKAVT
QAKLGYNPLE LDPELMTPYA YEKPQILSEY SVSDAVATYY LYMKYVHPFI FSLCTIIPLN
PDEVLRKGTG TLCEMLLMVQ AYQNSVLLPN KHTDPIERFY DGHLLESETY VGGHVESLEA
GVFRSDLKND FKIDPTVIDI LLEDLPYALK FCIEVENNGN MEDVTNFEEI KQQITAQLTD
LKINNKRNEL PLIYHVDVAS MYPNIMTTNR LQPDSMKDEK DCASCDFNRP GKSCDRRLKW
AWRGEFFPAK MDEYGMVKRA LQNELFPNKN PKSKKQFLTF EELSYSDQVS HIKKRLTDYS
RKVYHRVKVT ETVEREAIVC QRENPFYVNT VRSFRDRRYE FKGLAKLWKG KLSKIKPDDV
HSKDEAKKMI VLYDSLQLAH KVILNSFYGY VMRKGSRWYS MEMAGITCLT GANIIQMARS
VVERIGRPLE LDTDGIWCIL PKSFPENFEI KLRNGKKLFL SYPCSMLNYK VHQKYTNHQY
QDLVDPMKFK YQTKSDNSIF FEVDGPYKAM ILPTSKEEGK GIKKRYAVFN EDGSLAELKG
FELKRRGELQ LIKNFQSDIF KLFLEGTTLE SCYAAVATVA NRWLDVLDSK GAMLETEDLI
ELICENKSMS KTLKEYQGQK STSITTARRL GEFLGEAMVK DAGLQCKFII SSKPHNAPVT
ERAIPVAIFS SDLHVKRTFL RRWLLDSSLN DFDPRAIIDW DYYRERLASV VQKIITIPAA
LQNIKNPVPR VEHPDWLRKK IAVSEDKFKQ TSLNRFFKST KAPPEVKDIE DSFDEHSANK
SRIAKVTYKR KSKRRNGDTA LEEESLLLPS EMPPMLDDYV GWLQYQKTKW KIQHIDRKKR
EKLFGKTSRA SDRSALGNLI RKHVESYADK SWEILQCKPS IDLGVVEIYA LIDRKIQLLK
VNIPKTVLMN FKTENFPSGG IENCIVEKSN AELPNVKGIN NESSSQLFKL TMSEDTYFNE
VNKASSVLNN ENVLGIYESS ISSNERVIMR LGTCIQFSSE KMGALGKGLQ NGFHMKNLHP
VEADRYLQRF DLDIAYLLHF VTDIGYEFYF LYKAWEDVVE IFVLKPSTHA QEVSNKAIES
LYNEIYEKKF EKLDKYYDLI KINKNVSFNV NDYTELKRLL KDLSKMLQNI KEEKGSHTMV
ILQSPYTHRV AKLLQPLNAF PVVEIATAET HLPALNWQGQ LMRKAVNHIL SLGSWISNLI
TLSKYSNIPI CNLKVDNLGY IIDLMYARQL KKNNIVLWWN DKSPLPDHGG VERDFDPRKA
ELMTDLVFPI MNNPDIYDDV IFEISVYNSV VNTVLSSTML NEAEGTDLAQ NSTSKEESFG
FVEDSFSSSA LSVLRALLKE LWDDALGDNI TADSLVHAFI GWVYNPDAKL FDYALRYHIH
TLTQKAVLQL INEFKLAGSS LIFADRNKLL IKTQKRSVEN SYAYGQYLMK AIRSKPMFAY
LDLKIDRYWD VLIWMDKYNY GGRACLQIED KEVQSFQAYS HWHIKDFLPA IYQQEFDDWL
VVILDSMVKT KEAYHERNAS TQRLTQLPKN TLADSDVDSQ TDSLGGFTHN FSKALIKRAE
KLYKNQQEYI LDPNFGKDYL SPTIPGSHLV VKNPLLELVK YLSHILSLSS NHLLEGRALR
KELLKTFEIR EFDRLAEFKD PSTSFVIPSF ICEHCSYISD IDICRESMER VFICQSCNRS
LNKNLIEEHV IERLQAQVAS FITQDVKCNK CHKIKEDAMS PYCPCSGKWE LAVSKESFMA
QLQIFKNLAE SFDFRTLKET LNDFL
