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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
 
 
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