DPOE_ASHGO
ID DPOE_ASHGO Reviewed; 2180 AA.
AC Q752B8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=AFR657C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 223; 226; 244 AND 272-273.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS54029.2; -; Genomic_DNA.
DR RefSeq; NP_986205.2; NM_212341.2.
DR AlphaFoldDB; Q752B8; -.
DR SMR; Q752B8; -.
DR STRING; 33169.AAS54029; -.
DR PRIDE; Q752B8; -.
DR EnsemblFungi; AAS54029; AAS54029; AGOS_AFR657C.
DR GeneID; 4622494; -.
DR KEGG; ago:AGOS_AFR657C; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q752B8; -.
DR OMA; MLDQCRY; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IBA:GO_Central.
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:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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; IBA:GO_Central.
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..2180
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046457"
FT ZN_FING 2067..2092
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 2123..2140
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2067
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2089
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2180 AA; 250381 MW; 6534A7A5B8DB7FE1 CRC64;
MSNRFKGSST GHYVRAGAGG QPNTYGLTAH QLLQSKKVDD IDAMMGFERH ISPQDGAGAG
NSERIGWLCN MHPTVVADEL NAGASGVGVA GVDFYFLDEE GGSFKSTILY DPYFLLSCQD
SNRVHDVEEF LKKYLEGCLK TVEVVQKDDL AMDNHLVGLK RTLLKLNFVN TNNLFEARKL
LRPILKDNEE NQQQRDIYSL NDTTNRRDAK MLIDDIREYD VPYHVRVCID KEIRVGKWYR
VTSGGLVEYT DKVAFADPVV LAFDIETTKA PLKFPDSAID QIMMISYMID GEGYLITNRE
IISEDIEDFE YTPKPEYQGL FTVFNEEDER SLLERFFEHI RDVRPTVIST FNGDFFDWPF
VEARSKIRGL SMFDEIGFAP DSEGEYKSSY CAHMDCYRWV KRDSYLPQGS QGLKAVTQVK
LGYNPIELDP ELMTPYAYEK PQHLSEYSVS DAVATYYLYM KYVHPFIFSL CTVLPLNPDE
VLRKGTGTLC EMLLMVQAYD HGILLPNKHT EPIERFYDGH LLESETYVGG HVESLEAGVF
RSDIDCDFTI DSTAIDELLQ DLPHALKFCI EVENKTKVED VLDFEDILNT ITEQLQELKM
NNKRKELPLI YHVDVASMYP NIMTTNRLQP DSMKTERDCA SCDFNRPGKK CDRRLKWTWR
GEFLPAKMDE YAMVKRALMN EVFPNKYKNT TKKLLTFDEL SYSEQVSHIK KRLSEYSRKV
YHRVKVTESV VRESIVCQRE NPFYVNTVRS FRDRRYEFKG HAKTWKKKLS QIDPEDKVAR
DEARKMIVLY DSLQLAHKVI LNSFYGYAMR KGSRWYSIEM AGITCSTGAT IIQMARALVE
RIGRPLELDT DGIWCIIPRS FPENFEFTLK NGKKLYLSYP CSMLNYKVHQ SFTNHQYQEL
VNDAKHKYKI SSDNSIFFEV DGPYKAMILP TSKEEGKGIK KRYAVFNEDG SLAELKGFEL
KRRGELQLIK NFQQDIFKVF LEGRTLEECY GAVAKVANRW LDILDSKGSM LETEDLIDLI
CENKSMSKKL KEYDGQKSTS ITTARRLGEF LGQEMVKDAG LQCKFIISSK PANAPVTERA
IPVAIFSADH NIKKLFLRKW LLDSSLDNFD LRAILDWNYY RERLASVIQK IITIPAALQN
VNNPVPRVDH PEWLRKKIAT SESKFKQTSI GRFFKKSNGM PEIADIEDNA FSTESSSGAK
VARVVTKKKR KRENETKDNQ PVLPSVMPAI DEDYVGWLNY QKIKWQLQAE ERHRRKQLFG
SSSTLNDRSA LGNIIKKHAE SYANSDWEIL QYKNSSEPGV VEVHALISGK VQSLKFHIHK
TVFLKFKTDT LPPGGIPNCV IEKSNAILPN TKEDSYNTSS SLFRVTCPET VFLDEQNKVS
SVFNSGNILG IYESTIPASE RAIMELGNAV KFKSNVMGAL SKGLQHGFQA KNLLSVTSER
YLQRFDLEVI YLLNLTTNLG YEFFVLFNGW GDQAKVFVLK PSIAAQELSR HALEAAYEQQ
YLKKVKNFEK FRHYFMPAES AKFELHHFTD KSVLLRSLSK VVSSWSELKG SQLLLLLQSP
TPSRLLKSIR ILNQLPVVQL STCELAFPTL NWQDQLIKKT VSHILQLGSW LSNLTILSNY
TRIPICNLNL TNLGYVIDIM YARRLKLENI VLWWNQKQPL PDRGGIQNEY NPHTLSLATD
LTSPVINNPE FYDSAVLEIE VNNLLVNTIL TSTLINEAEG GDVAGPESGG REGGGFVEDA
FSTASVNILR SLLKDLWDDA LQNNSTADSL VHSFIGWVQS VDSKLFDYTL RYYVNMLTKK
ALFQLINEFR FMGSQVVFLD RNKILLKTSK NTIDNSYAYG QYLIKAIRTR PLFSYLDLKI
VRYWDILLWM DQYNHGGCAC LKIEEKERQD IQAYSSWHIK NFLAPIYQQE FDDWLVIILD
SMIKCKQQFY ELSGTQRLTQ LPNRSQAADE DDENSVFAGF TKRFYQPFIN RISKLYKTQQ
EYILDPNFRA DYIIPDLPGR NPKMKAGNPL LELVKSLCHV LLLCKERTLE VRALRKEALE
VFEIREFDSS ASFENPASSL IINNFMCENC AYFSDLDICM SDLRSMFKCS KCYRTLRKPF
IEENLIQKLQ IQTIAYISQD LRCAKCRKIK SDTMSAYCTC SGKWVQTISK DTYLKNVQLF
YHVAEYFGFS LLLSAIKGGI
