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DNA polymerase epsilon catalytic subunit A (EC 2.7.7.7) (DNA polymerase II subunit A)

 DPOE_KLULA              Reviewed;        2185 AA.
Q6CUS7;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
23-MAY-2018, entry version 96.
RecName: Full=DNA polymerase epsilon catalytic subunit A;
EC=2.7.7.7;
AltName: Full=DNA polymerase II subunit A;
Name=POL2; OrderedLocusNames=KLLA0C02585g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: DNA polymerase II participates in chromosomal DNA
replication. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
-!- SUBUNIT: Heterotetramer. Consists of 4 subunits: POL2, DPB2, DPB3
and DPB4 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- DOMAIN: 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. {ECO:0000250}.
-!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for
the formation of polymerase complexes. {ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
{ECO:0000305}.
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EMBL; CR382123; CAH01163.1; -; Genomic_DNA.
RefSeq; XP_452312.1; XM_452312.1.
ProteinModelPortal; Q6CUS7; -.
SMR; Q6CUS7; -.
STRING; 284590.XP_452312.1; -.
PRIDE; Q6CUS7; -.
EnsemblFungi; CAH01163; CAH01163; KLLA0_C02585g.
GeneID; 2892428; -.
KEGG; kla:KLLA0C02585g; -.
eggNOG; KOG1798; Eukaryota.
eggNOG; COG0417; LUCA.
HOGENOM; HOG000196287; -.
InParanoid; Q6CUS7; -.
KO; K02324; -.
OMA; IHSKEIF; -.
OrthoDB; EOG092C00WD; -.
Proteomes; UP000000598; Chromosome C.
GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:EnsemblFungi.
GO; GO:0005657; C:replication fork; IEA:EnsemblFungi.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IEA:EnsemblFungi.
GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006284; P:base-excision repair; IEA:EnsemblFungi.
GO; GO:0045004; P:DNA replication proofreading; IEA:EnsemblFungi.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
GO; GO:0035822; P:gene conversion; IEA:EnsemblFungi.
GO; GO:0070868; P:heterochromatin organization involved in chromatin silencing; IEA:EnsemblFungi.
GO; GO:0031573; P:intra-S DNA damage checkpoint; IEA:EnsemblFungi.
GO; GO:0006272; P:leading strand elongation; IEA:EnsemblFungi.
GO; GO:0033314; P:mitotic DNA replication checkpoint; IEA:EnsemblFungi.
GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:EnsemblFungi.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR006172; DNA-dir_DNA_pol_B.
InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
InterPro; IPR013697; DNA_pol_e_suA_C.
InterPro; IPR029703; POL2.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
PANTHER; PTHR10670; PTHR10670; 1.
Pfam; PF00136; DNA_pol_B; 1.
Pfam; PF03104; DNA_pol_B_exo1; 1.
Pfam; PF08490; DUF1744; 1.
SMART; SM01159; DUF1744; 1.
SMART; SM00486; POLBc; 1.
SUPFAM; SSF53098; SSF53098; 3.
3: Inferred from homology;
4Fe-4S; Complete proteome; DNA replication; DNA-binding;
DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
Nucleotidyltransferase; Nucleus; Reference proteome; Transferase;
Zinc; Zinc-finger.
CHAIN 1 2185 DNA polymerase epsilon catalytic subunit
A.
/FTId=PRO_0000046463.
ZN_FING 2072 2097 CysA-type.
MOTIF 2128 2145 CysB motif.
METAL 2072 2072 Zinc. {ECO:0000250}.
METAL 2075 2075 Zinc. {ECO:0000250}.
METAL 2094 2094 Zinc. {ECO:0000250}.
METAL 2097 2097 Zinc. {ECO:0000250}.
METAL 2128 2128 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 2131 2131 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 2143 2143 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 2145 2145 Iron-sulfur (4Fe-4S). {ECO:0000250}.
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


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