DPOE_SCHPO
ID DPOE_SCHPO Reviewed; 2199 AA.
AC P87154; P78873;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
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; Synonyms=cdc20; ORFNames=SPBC25H2.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1891-2199.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
CC -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC replication. {ECO:0000250|UniProtKB:P15436}.
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 -!- INTERACTION:
CC P87154; O74560: raf2; NbExp=2; IntAct=EBI-876811, EBI-904886;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB08772.1; -; Genomic_DNA.
DR EMBL; D89223; BAA13884.1; -; mRNA.
DR PIR; T40008; T40008.
DR PIR; T43044; T43044.
DR RefSeq; NP_596354.1; NM_001022274.2.
DR AlphaFoldDB; P87154; -.
DR SMR; P87154; -.
DR BioGRID; 277153; 44.
DR ComplexPortal; CPX-2111; DNA polymerase epsilon complex.
DR DIP; DIP-36490N; -.
DR IntAct; P87154; 3.
DR MINT; P87154; -.
DR STRING; 4896.SPBC25H2.13c.1; -.
DR iPTMnet; P87154; -.
DR MaxQB; P87154; -.
DR PaxDb; P87154; -.
DR PRIDE; P87154; -.
DR EnsemblFungi; SPBC25H2.13c.1; SPBC25H2.13c.1:pep; SPBC25H2.13c.
DR GeneID; 2540627; -.
DR KEGG; spo:SPBC25H2.13c; -.
DR PomBase; SPBC25H2.13c; -.
DR VEuPathDB; FungiDB:SPBC25H2.13c; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; P87154; -.
DR OMA; MLDQCRY; -.
DR PhylomeDB; P87154; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-68952; DNA replication initiation.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR PRO; PR:P87154; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
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; IDA:PomBase.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0140529; P:CMG complex assembly; IMP:PomBase.
DR GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR GO; GO:1902983; P:DNA strand elongation involved in mitotic DNA replication; IMP:PomBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IC:ComplexPortal.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
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:1902975; P:mitotic DNA replication initiation; IMP:PomBase.
DR GO; GO:1903460; P:mitotic DNA replication leading strand elongation; IMP:PomBase.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR GO; GO:0006279; P:premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0061806; P:regulation of DNA recombination at centromere; IMP:PomBase.
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 1: Evidence at protein level;
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..2199
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046464"
FT ZN_FING 2069..2107
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 2138..2155
FT /note="CysB motif"
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 2072
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 2138
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"
FT BINDING 2153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT CONFLICT 2116..2126
FT /note="FEETLVDNLYH -> LRKLWWITYN (in Ref. 2; BAA13884)"
FT /evidence="ECO:0000305"
FT CONFLICT 2182
FT /note="Y -> N (in Ref. 2; BAA13884)"
FT /evidence="ECO:0000305"
FT CONFLICT 2196..2199
FT /note="SVLN -> FCAELTFLD (in Ref. 2; BAA13884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2199 AA; 252887 MW; A80A5D0865EEBC3E CRC64;
MPLKTARGAS KYQFRKFNGN YNGKSKSNGR TFAKSTEEVG FNDPMKIVYK KNEIDRMMGF
DSYEGGQPRE AWLLNVHPTV IESTKGNSTL SAVDFYFIQD DGDTFRCTIP YSPYFYIAAR
EGKEALVDDY LKKKFVGLIK STTRIFKEDL QLKNHIVGYQ KLYIKLVFDN LNDLQAVRKS
LMSAVKANSS QQDAVDAYTN LSSENLNGII ENAFEDPLNH VLDIREYDVP YHSRTLIDLN
IRVGQWYTVS YHEGHVQISL LASRIERAEP TIMAFDIETT KLPLKFPDSS FDKIMMISYM
IDGQGFLITN REIISQNIED FHYTPREEFE GPFIIFNEPD EVGLLHRFFK HIRSAKPSVI
VTYNGDFFDW PFVDARAAFH GLNLTEETGF FRDAEDEYKS SYCSHMDAFR WVKRDSYLPQ
GSQGLKAVTV SKLGYNPIEL DPELMTPYAS EKPQVLAQYS VSDAVATYFL YMKYVHPFIF
SLCNIIPLNP DEVLRKGTGT LCETLLTVEA CTKNIILPNK HVDASQKFFD GHLLASETYV
GGHVESLESG VFRSDLPTNF NMDPKVYEEL ILQLDKALDF SLTVENNVNV DEIENYEEVR
DSILKKLSDL RDRPKRSEKP RIYHLDVASM YPNIMITNRL QPDSVKDESF CATCDLNVPN
KTCDRRMVWA WRGEYYPAKK GEYHMIYSAL QSERFPGPTP FSPFRSFQEL SPSEQAAMVQ
KRIADYSRKV YHRLYDNTVI ERETIICQKE NSFYIDTVKS FRDRRYDFKG LQKKWVKQLA
AIKEKGGLAE IEEAKKMVVL YDSLQLAHKV ILNSFYGYVM RKGSRWYSIE MAGITCLTGA
TIIQMARQIV ERAGRPLELD TDGIWCILPE SFPENFEFKK KSGGKVFISY PCVMLNHLVH
EKFTNHQYSA LKDPEKLVYE TTSENSIFFE VDGPYRAMIL PASTEEGKNL KKRYAVFNFD
GSLAELKGFE VKRRGELKLI KDFQSQIFKV FLKGDSLEEC YQEVAYVADT WLEILFTKGS
NLTDDELIEL ISENRSMSKA LSEYGSQKST SITTARRLAD FLGDQMTKDK GLACRFIISA
SPKGRPVAER AVPVAIFFAE ESVKRHFLRL WLKDNGLYDV DIRDIIDWDY YLKRLGSVVQ
KLISIPAALQ RISNPVTRFP LPDWLQKRVA VLNSKYQQKK IDSIFSLAPT NPSTINNTKV
TDIEDLGSVT HKDKRIVARV TKRKLLQQSG NSEAPVSFEV KPVSFMDGYS NWLKYAKKKW
KYQKQVKLRR RHLIGFQSRQ FTNVLQSSAE VMFENLWHIL QIRETDVPGI LHAWVIIRNR
LTSIRFIVNR KFFVCFKDET LPNVEIEGCL IEKSNAILPH GSTSDKLFLL EIPEKSYLTE
KVSISMIFAH PSVSGIYETR IEPIERLILE MGSRKRFNNS VPGALGKGFE FGFESKMFTD
PSDNDVSYLD GVEMNYLYAF HFSISNRFVF SLFMPHLKKV EAIIYDKLPG SDMSFPSISK
IYEELRSKFD NLIKESSIEY PDTLSCNVIF SGNERKAYKL IDEKLLQYFS TKTKNSLLII
ESSLPHILKA NVKQIEELPY IMIPRLESNI QSLSWKQHIA TKMIQHFLAI GSWLFHRIQL
SRFSDIPLCN FESDDIQYSI DVVYSRKLKE HNIILWWNKG PTPDLGGIEK DSILQIASPK
DPLEVNNPGA YSNACVDISL SNLALCSILN SALINDIEGI GDMAALNDNY MTAINDDLEE
KLGIHDNIGL THSLPVLKAL VKTWWNEAAS GNNLADLIIQ HLARWISSSK SYLYSPLLSS
HVEVIMRKTF LQLLSEIKRL GAHIIHASAN KILIKTSKLI VQNAVTYSNY LLKSIKTLPL
FHFLDLNVTE YWDYLLWMDS VNYGGKMVAA NFSATNEEPQ TVVSWHIKSH LPPIIQPEFQ
SWIVEFIEEV YKQKLEKSNT KVGFVRVKNN NADEDSEIVG SGILKSKLIH PLKRKVAQVR
RCFQELQLDE NTREDLKFPK LPGSFLNYTD GALELVKSIC AVFELSHDLN LEVRFLKKSL
LSLLQIQEFS TQAVFRYPSR RLSLDQIPCK QCGVHQDFDL CLHEHLWPTR DDMGTLVFSD
GWSCSSCNLV YDRWVFEETL VDNLYHQLTL YQLQDLICSK CKTVKQWSLK ERCSCSGEWV
LQLSPTKFRE MLNVYQSVAD FYEFSILQNS VQSILSVLN
