DPOE2_DICDI
ID DPOE2_DICDI Reviewed; 676 AA.
AC Q54Y85;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA polymerase epsilon subunit 2;
DE AltName: Full=DNA polymerase II subunit 2;
DE AltName: Full=DNA polymerase epsilon subunit B;
GN Name=pole2; ORFNames=DDB_G0278367;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Accessory component of the DNA polymerase epsilon complex (By
CC similarity). Participates in DNA repair and in chromosomal DNA
CC replication (By similarity). {ECO:0000250|UniProtKB:P24482,
CC ECO:0000250|UniProtKB:P56282}.
CC -!- SUBUNIT: Consists of three subunits: pole, pole2 and pole3.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase epsilon subunit B family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68356.1; -; Genomic_DNA.
DR RefSeq; XP_642317.1; XM_637225.1.
DR AlphaFoldDB; Q54Y85; -.
DR SMR; Q54Y85; -.
DR STRING; 44689.DDB0216321; -.
DR PaxDb; Q54Y85; -.
DR EnsemblProtists; EAL68356; EAL68356; DDB_G0278367.
DR GeneID; 8621523; -.
DR KEGG; ddi:DDB_G0278367; -.
DR dictyBase; DDB_G0278367; -.
DR eggNOG; KOG3818; Eukaryota.
DR HOGENOM; CLU_010628_2_1_1; -.
DR InParanoid; Q54Y85; -.
DR OMA; EIVFFQQ; -.
DR PhylomeDB; Q54Y85; -.
DR Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DDI-68952; DNA replication initiation.
DR Reactome; R-DDI-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q54Y85; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 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 3: Inferred from homology;
KW DNA replication; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..676
FT /note="DNA polymerase epsilon subunit 2"
FT /id="PRO_0000328402"
FT REGION 513..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..670
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 78592 MW; 9F7C13DDCE38E0B3 CRC64;
MDIQWKKQIT KSFSLTGFSI KADAMKCIIN RIKNEGYDIT QLIDNLLKNL DKSQYLQTIE
GCFKLIDTIN SSDAIEKEAL KVIDAFNTPL FNFDSNSKQF IKSENFDRSL HGSSNSKSDL
YRKRYLKVLQ RTERNDYFST PVLASDKLKN EYQTITPLSS LLGNTGRKHV LGTISQIEED
QFYIEDLNTN VKIDISKAKF EFGIVTINSI IQASGEFIDG VFIADKIQLP PTEERCETLK
FLQNIDMFGE RPQKKTMEQL IKYEKEKEDN SILFLSDVWL DSERVMERLD YLFGGYKDCP
PFAMILMGNF TEHPLINGTQ YQLKKYFNQL AMVIQKYPNI HQFTQFIFVP GPTDPTGSLL
NILPKFPISN VFIKDFISLI PKSTFTTNPC RIRYCSQEII IFRDDLTNKM RRHCILEPSQ
SCDISQHLIE LICSNSHLCN LTLEDKPIYW NYDHAMSVYP LPDLLVIGDK SNQYEHSRAD
GTYSMNPSSF STDYSFAHYI PANKQFYYNK ADRPSDEIED DDDDEEVENQ NENENENENE
NENENENENN DNDKTQQKDT QGDGDDNDDD EIMIDENEKQ KSRKRNKKVV IITKEDELNK
LEDDEEILNS LDVQQQSENH ADNNNNNINN NNNDDDNEDD EDSNYNNIES EVQEVEKEEE
EDEEPIDNDK LDEFIE