DPOE_YARLI
ID DPOE_YARLI Reviewed; 2183 AA.
AC Q6C4J0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=YALI0E26367g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382131; CAG80023.1; -; Genomic_DNA.
DR RefSeq; XP_504422.1; XM_504422.1.
DR AlphaFoldDB; Q6C4J0; -.
DR SMR; Q6C4J0; -.
DR STRING; 4952.CAG80023; -.
DR PRIDE; Q6C4J0; -.
DR EnsemblFungi; CAG80023; CAG80023; YALI0_E26367g.
DR GeneID; 2912373; -.
DR KEGG; yli:YALI0E26367g; -.
DR VEuPathDB; FungiDB:YALI0_E26367g; -.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; Q6C4J0; -.
DR OMA; MLDQCRY; -.
DR Proteomes; UP000001300; Chromosome E.
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..2183
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046466"
FT ZN_FING 2066..2093
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 2124..2141
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2066
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2069
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2090
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2093
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
SQ SEQUENCE 2183 AA; 250638 MW; 969273FC9800ED8A CRC64;
MGRPFNGNNT HVVKQRSDEF ERRRLERIEQ LGQKFAAVER RDAIDDRMGF TRFSGDEKRV
GWLVNMHETL LQSETAERGL AAVDYYFYDE EGGNFKSTVV FRPYFFVICK PHTEHAVKDL
MEKMFERVLA STEIVTKEDL NLTNHLTGKK RKAVKLEFHN SEDLSSTRFT LSKIVDRQTQ
QTEQHLNIYE LEGDVDTSTD VESSITGIKE FDVPFETRVA IDLDIRVGNW YEVTKENDTA
VLKHMVEREY RADPVVMAYD IETEKAPLRF PDSAVDRIMM ISYMIDGEGF LITNREMVSE
DIEDFEYTPK PEFPGNFTIF NEPNEKAVLE KWFEHIRDVC PTVMTSYNGD FFDFPFIDKR
TAFHGMNLYD EIGWKKVEEE RYECSYCVHM DCLNWVKRDS YLPQGSQGLK AVTKVKLSYD
PKELDPEKMT PYARDHPQIL AEYSVSDAVA TYYLYMKYVH PFIFSLCCII PLNPDAVLRK
GTGTLCEMLL MVKAYEGRII LPDKHKPALE RHYKGHLVDN ETYTGGHVES LAAGVFRSDI
MVDFDIDTNS IDELLVNLDE TLEFCVTVEA GKKSSDFENL DEVRDQIIEQ LQELKSNPKR
SDYPLIYHVD VASMYPNIMT TNRLQPDSMV DEKDCAVCDY NRPDKTCARE LEWARRVDYY
PVSKGDVNNL KQGLVEEYSG GRFGNGSSVE ISYDEGMTER EKFQKRKGWA GLSGQEQANK
LKERVAAFSL KTKARKTDSE TTVQKTIVCQ RENPFYVDVV QEFKQRRIDY KTKAKRWNKE
AASASDPASR EEAKKMAITN DSMQLAHKVI LNSFYGYVMR KGSRWYSMEM AGVTCYTGAK
IIKIARQTME GLGIPLELDT DGIWCMLPKT FPEKFKCKFK DGSSYELEYP CSIMNYLVHR
DFTNHQYQKL NPETGKYDTH SENSIFFELD GPYKCMMMPT STDKGKGLKK RYVVFDDRNK
IVELKGFEVK RRGELSLIKK FQSQLWDTFL EGSNLVECYA AQARVAEAWL AVIDSRGKNL
SDEELIDLVC ENKSMSKPVH EYGSQKSTAL TTARRLAEIM GDSILTGGKL STKYIIAVRT
KNSMPVPEAK KGSDEDSSTA DRAIPTLVFE TESLDEKLRF LKRWMGPRWE STDPRDVIDW
MYYRERLATT INKLVVIPAI LLGLKNPVRG CDPPEWASDI IKQRDNPIKQ STLSSYFVKG
KLPTPEPILS EEDEVMEIQV GDIESIGTTP SPSRPPGVPA RVVVSKRVRK TVEETDKSTP
SLPHKAPDPF ADYAAYIKYA KVKWKHQKAQ RDRRAHLFGE SDNGIASSWV SKNAHLAQDA
WHLVSIHAAE KPGQVEASVI IGDKMQRVQI NVPRKVYVGS REPLKWDKFT DVTNAMAVAE
EEQPKYLYRA VMSEDMYQTE MTNPESPLKD PHVTKIYEAD VSPDSRALIE LGSTFHLDAS
TPGILSKGFT HGFEAKWFKS GDSRSYLQNS GLSYAHIVHV VSSAVEIFVI TPTWDAPALV
FVHQSSSSEK LPDISKEYAR LRRGERYKQN MDDCTVFSFP DTMQYEVEYC SNHRRMLQKV
SKACDSLSGS RNGQLVFALH SPDRNVDEKV AALARIPCIR LRPVPPSTAA VGWQRDLVRR
LIASFLSHGA NISYLVEMAR YAKMPLCHVQ DTRDVIDVSY ARRLIQNSVV LWWSAALSTG
GALTDQAEVP VANNPGLYTN ICFEIKIEHL VLNALLQSAV IQDTEGDIHN ELLSNAFNPH
ALKTLKMVVK EWWEHGDKKR PPQDLLDNFT VWVYAPESRL FSPQLLYHTQ NLTKKTFLYL
AQECRKHQAQ LVYADQHKLV LQTEKTELQL VYSYSNYIVR QIRTHPILKY VSVDITRYWD
TFLWMDKWNY GGYSSDVIVD PSKQSESLLM HWHIANFLPE TLQQEFSKWV QEYIHLLRLR
KYPENRTTDV DDMPSDTPML TDGDKDDAAL LSDKFFGKGV VSYLHPKLVR RVKLLAQKLS
DVLSSGDSID AFKFPVLPGS MIQPETNPVV EFAKYVCHIY GINAKANFEV QILLRDLLNI
FDINEFSEEG TFRDPSMSLK LTNMMCFKCK NPCDLDLCKD SCCTKSGFRC PLCNSLYDMV
IVEQRLVGQL QRMILEYETQ DFRCDKCRRV KEYELTEFCP CSGSWVTIMS AEDVHKELSI
YDRCARWFEL KMLGSFLRQL GYV
