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Database: UniProt
Entry: DPB4_DEBHA
LinkDB: DPB4_DEBHA
Original site: DPB4_DEBHA 
ID   DPB4_DEBHA              Reviewed;         247 AA.
AC   Q6BIP4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   24-JAN-2024, entry version 100.
DE   RecName: Full=DNA polymerase epsilon subunit D;
DE   AltName: Full=DNA polymerase II subunit D;
GN   Name=DPB4; OrderedLocusNames=DEHA2G08756g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: As accessory component of the DNA polymerase epsilon (DNA
CC       polymerase II) participates in chromosomal DNA replication.
CC       {ECO:0000250|UniProtKB:Q04603}.
CC   -!- SUBUNIT: Heterotetramer. Consists of four subunits: POL2, DPB2, DPB3
CC       and DPB4 (By similarity). {ECO:0000250}.
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.
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DR   EMBL; CR382139; CAG90392.2; -; Genomic_DNA.
DR   RefSeq; XP_461927.2; XM_461927.1.
DR   AlphaFoldDB; Q6BIP4; -.
DR   SMR; Q6BIP4; -.
DR   STRING; 284592.Q6BIP4; -.
DR   GeneID; 2904813; -.
DR   KEGG; dha:DEHA2G08756g; -.
DR   VEuPathDB; FungiDB:DEHA2G08756g; -.
DR   eggNOG; KOG0870; Eukaryota.
DR   HOGENOM; CLU_087036_0_0_1; -.
DR   InParanoid; Q6BIP4; -.
DR   OMA; NTYRRKV; -.
DR   OrthoDB; 1384627at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   PANTHER; PTHR46172; DNA POLYMERASE EPSILON SUBUNIT 3; 1.
DR   PANTHER; PTHR46172:SF1; DNA POLYMERASE EPSILON SUBUNIT 3; 1.
DR   Pfam; PF00125; Histone; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   3: Inferred from homology;
KW   DNA replication; Nucleus; Reference proteome.
FT   CHAIN           1..247
FT                   /note="DNA polymerase epsilon subunit D"
FT                   /id="PRO_0000191750"
FT   REGION          128..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..213
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..247
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  27698 MW;  5E89FFD8EEEAA041 CRC64;
     MPPKGWRKNT EGQYPQPNKD QDLVSIDEIL FPRATVQKLA KNIMNASSDE GASNMILAKD
     SMIALQRSST VFVSHLMFQA RQISKDEGRK TINAQDILSA LEKAEFSGFI PEVKQKLSVF
     ESNIALRKKH KADKKVPKPE GVDASPSSKR LKDNDEQIIQ RDNSADMEDD PEAEADEDIT
     EELANDEDTN NKESKEEEEA DEELDDEKDG EEVEENPIAL LSREEDELRG EEAADEDEGQ
     NSSDDDS
//
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