ID   DPB2_SCHPO              Reviewed;         594 AA.
AC   O94263;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=DNA polymerase epsilon subunit B;
DE   AltName: Full=DNA polymerase II subunit 2;
GN   Name=dpb2; ORFNames=SPBP8B7.14c;
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   INTERACTION WITH DPB3.
RX   PubMed=15388803; DOI=10.1093/nar/gkh811;
RA   Spiga M.-G., D'Urso G.;
RT   "Identification and cloning of two putative subunits of DNA polymerase
RT   epsilon in fission yeast.";
RL   Nucleic Acids Res. 32:4945-4953(2004).
CC   -!- FUNCTION: As accessory component of the DNA polymerase epsilon (DNA
CC       polymerase II) participates in chromosomal DNA replication.
CC       {ECO:0000250|UniProtKB:P24482}.
CC   -!- SUBUNIT: Heterotetramer. Consists of four subunits: pol2, dpb2, dpb3
CC       and dpb4 (By similarity). Interacts with dpb3. {ECO:0000250,
CC       ECO:0000269|PubMed:15388803}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC       beta, gamma, delta, and epsilon which are responsible for different
CC       reactions of DNA synthesis.
CC   -!- SIMILARITY: Belongs to the DNA polymerase epsilon subunit B family.
CC       {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; CAA21799.1; -; Genomic_DNA.
DR   PIR; T40808; T40808.
DR   RefSeq; NP_596521.1; NM_001022442.2.
DR   AlphaFoldDB; O94263; -.
DR   SMR; O94263; -.
DR   BioGRID; 277858; 15.
DR   ComplexPortal; CPX-2111; DNA polymerase epsilon complex.
DR   IntAct; O94263; 2.
DR   MINT; O94263; -.
DR   STRING; 4896.SPBP8B7.14c.1; -.
DR   MaxQB; O94263; -.
DR   PaxDb; O94263; -.
DR   EnsemblFungi; SPBP8B7.14c.1; SPBP8B7.14c.1:pep; SPBP8B7.14c.
DR   GeneID; 2541347; -.
DR   KEGG; spo:SPBP8B7.14c; -.
DR   PomBase; SPBP8B7.14c; dpb2.
DR   VEuPathDB; FungiDB:SPBP8B7.14c; -.
DR   eggNOG; KOG3818; Eukaryota.
DR   HOGENOM; CLU_010628_1_0_1; -.
DR   InParanoid; O94263; -.
DR   OMA; GWVDFLG; -.
DR   PhylomeDB; O94263; -.
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:O94263; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; IC:PomBase.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0043596; C:nuclear replication fork; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0140529; P:CMG complex assembly; IMP:PomBase.
DR   GO; GO:1902983; P:DNA strand elongation involved in mitotic DNA replication; IC:PomBase.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   GO; GO:1902975; P:mitotic DNA replication initiation; IMP:PomBase.
DR   InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR   InterPro; IPR016266; POLE2.
DR   PANTHER; PTHR12708; PTHR12708; 1.
DR   Pfam; PF04042; DNA_pol_E_B; 1.
PE   1: Evidence at protein level;
KW   DNA replication; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..594
FT                   /note="DNA polymerase epsilon subunit B"
FT                   /id="PRO_0000071571"
SQ   SEQUENCE   594 AA;  67224 MW;  272CC46AA42ED74A CRC64;
     MNNSITDSVE KKPEQVSFEV QPNALRPVAF HVFTRKYDLN INRDSLQELA SFVSKKCGSQ
     WRSQCEPLLD EIAKTWKRVH ETQPIVTRPL LIPVLANLNV PHEVRVSSLA RVQTLETTGS
     FLNSSNSEIR ETIKNEKYFR VLDAFKMPKF KYDSSRKVFV LSKQSPTLMA SASACTDMLN
     RRFNVVYSRI LRNESFQTPS FSGSFSQTGT YQLTPIRNLL GRAGNTFLLF GLLTIAPDGT
     LWLEDLDSQV QLDVSQAEQG FGLFCPGCLV LVNGQFLSSG LFLVFELGHP PIERRDASLK
     ALNNLDILGL NMDAKQLALL RHAEQAYQSQ AFVCISEVHL DNHQTFYALE KIFQKYESSE
     AVPFCIILCG SFMSSAFHNS GSSIQYKEGF NKLAASLEKF PKICEKTKFI FVPGPNDPWT
     TNGISLMPKH SIPLHFVNRI QRVCKHTIFA SNPCRIIFFS QEVLIYRDDI SGRFQRNSLK
     FGKTPQGTSN INSIPLAEQQ VHQQRKLVKT VLDQSHLSPF PSRTRPILWD FDYALSVFPL
     PSCMGLIDSE SSAFDVHYGG CPTFNPGALL LGVHYNWQEV FPVKKEIITH KERI