Protein : Qrob_P0678490.2 Q. robur
Protein Identifier  ? Qrob_P0678490.2 Organism . Name  Quercus robur
Score  95.0 Score Type  egn
Protein Description  (M=2) PTHR10670 - DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A Code Enzyme  EC:2.7.7.7
Gene Prediction Quality  validated Protein length 

Sequence

Length: 235  
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0 Synonyms

6 GO Terms

Identifier Name Description
GO:0003677 DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
GO:0006281 DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
GO:0000166 nucleotide binding Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0006260 DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
GO:0003887 DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.
GO:0008622 epsilon DNA polymerase complex A heterotetrameric DNA polymerase complex that catalyzes processive DNA synthesis in the absence of PCNA, but is further stimulated in the presence of PCNA. The complex contains a large catalytic subunit and three small subunits, and is best characterized in Saccharomyces, in which the subunits are named Pol2p, Dpb2p, Dpb3p, and Dpb4p. Some evidence suggests that DNA polymerase epsilon is the leading strand polymerase; it is also involved in nucleotide-excision repair and mismatch repair.

24 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|mdm:103448067 7 160 + 154 none 11.95 1289 92.21 5e-88 DNA polymerase epsilon catalytic subunit A-like
blastp_kegg lcl|pvu:PHAVU_011G091900g 7 160 + 154 none 6.93 2221 93.51 1e-87 hypothetical protein
blastp_kegg lcl|csv:101208568 7 160 + 154 none 6.98 2206 92.21 1e-87 DNA polymerase epsilon catalytic subunit A-like
blastp_kegg lcl|vvi:100241432 7 160 + 154 none 6.96 2214 92.21 2e-87 POLE polymerase (DNA directed) epsilon
blastp_kegg lcl|pxb:103954203 7 160 + 154 none 6.94 2220 92.86 2e-87 DNA polymerase epsilon catalytic subunit A-like
blastp_kegg lcl|pop:POPTR_0004s19660g 7 160 + 154 none 7.13 2160 91.56 3e-87 DNA-directed DNA polymerase epsilon catalytic subunit family protein
blastp_kegg lcl|pper:PRUPE_ppa000038mg 7 160 + 154 none 7.01 2197 92.21 3e-87 hypothetical protein
blastp_kegg lcl|pmum:103327021 7 160 + 154 none 6.94 2219 92.21 3e-87 DNA polymerase epsilon catalytic subunit A-like
blastp_kegg lcl|tcc:TCM_041469 7 160 + 154 none 6.96 2213 92.21 7e-87 DNA polymerase epsilon catalytic subunit isoform 1
blastp_kegg lcl|fve:101291492 7 160 + 154 none 6.95 2217 92.21 7e-87 DNA polymerase epsilon catalytic subunit A-like
blastp_uniprot_sprot sp|F4HW04|DPOE1_ARATH 7 160 + 154 none 7.13 2161 90.91 6e-86 DNA polymerase epsilon catalytic subunit A OS Arabidopsis thaliana GN POL2A PE 1 SV 1
blastp_uniprot_sprot sp|F4IFN6|DPOE2_ARATH 7 160 + 154 none 7.20 2138 88.31 9e-84 DNA polymerase epsilon catalytic subunit B OS Arabidopsis thaliana GN POL2B PE 2 SV 1
blastp_uniprot_sprot sp|Q4WXH8|DPOE_ASPFU 7 160 + 154 none 6.91 2230 62.99 3e-59 DNA polymerase epsilon catalytic subunit A OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) GN pol2 PE 3 SV 1
blastp_uniprot_sprot sp|P0CN26|DPOE_CRYNJ 7 159 + 153 none 6.80 2250 60.13 1e-58 DNA polymerase epsilon catalytic subunit A OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) GN POL2 PE 3 SV 1
blastp_uniprot_sprot sp|P0CN27|DPOE_CRYNB 7 159 + 153 none 6.80 2250 60.13 1e-58 DNA polymerase epsilon catalytic subunit A OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) GN POL2 PE 3 SV 1
blastp_uniprot_sprot sp|O93845|DPOE_EMENI 7 160 + 154 none 6.98 2207 61.69 2e-58 DNA polymerase epsilon catalytic subunit A OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) GN pol2 PE 3 SV 2
blastp_uniprot_sprot sp|Q6FNY7|DPOE_CANGA 7 159 + 153 none 6.90 2217 61.44 2e-57 DNA polymerase epsilon catalytic subunit A OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) GN POL2 PE 3 SV 1
blastp_uniprot_sprot sp|Q4PFV5|DPOE_USTMA 7 159 + 153 none 6.64 2305 60.78 3e-57 DNA polymerase epsilon catalytic subunit A OS Ustilago maydis (strain 521 / FGSC 9021) GN POL2 PE 3 SV 1
blastp_uniprot_sprot sp|P21951|DPOE_YEAST 7 159 + 153 none 6.89 2222 62.75 5e-57 DNA polymerase epsilon catalytic subunit A OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN POL2 PE 1 SV 1
blastp_uniprot_sprot sp|P87154|DPOE_SCHPO 7 160 + 154 none 7.00 2199 61.04 6e-57 DNA polymerase epsilon catalytic subunit A OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN pol2 PE 2 SV 1
rpsblast_cdd gnl|CDD|99918 14 160 + 147 none 23.67 621 68.71 2e-79 cd05535 POLBc_epsilon DNA polymerase type-B epsilon subfamily catalytic domain. Three DNA-dependent DNA polymerases type B (alpha delta and epsilon) have been identified as essential for nuclear DNA replication in eukaryotes. DNA polymerase (Pol) epsilon has been proposed to play a role in elongation of the leading strand during DNA replication. Pol epsilon might also have a role in DNA repair. The structure of pol epsilon is characteristic of this family with the exception that it contains a large c-terminal domain with an unclear function. Phylogenetic analyses indicate that Pol epsilon is the ortholog to the archaeal Pol B3 rather than to Pol alpha delta or zeta. This might be because pol epsilon is ancestral to both archaea and eukaryotes DNA polymerases type B..
rpsblast_cdd gnl|CDD|30766 27 156 + 130 Gaps:13 14.77 792 30.77 1e-15 COG0417 PolB DNA polymerase elongation subunit (family B) [DNA replication recombination and repair].
rpsblast_cdd gnl|CDD|99912 27 84 + 58 Gaps:5 19.50 323 28.57 4e-08 cd00145 POLBc DNA polymerase type-B family catalytic domain. DNA-directed DNA polymerases elongate DNA by adding nucleotide triphosphate (dNTP) residues to the 5'-end of the growing chain of DNA. DNA-directed DNA polymerases are multifunctional with both synthetic (polymerase) and degradative modes (exonucleases) and play roles in the processes of DNA replication repair and recombination. DNA-dependent DNA polymerases can be classified in six main groups based upon their phylogenetic relationships with E. coli polymerase I (class A) E. coli polymerase II (class B) E. coli polymerase III (class C) euryarchaeota polymerase II (class D) human polymerase beta (class x) E. coli UmuC/DinB and eukaryotic RAP 30/Xeroderma pigmentosum variant (class Y). Family B DNA polymerases include E. coli DNA polymerase II some eubacterial phage DNA polymerases nuclear replicative DNA polymerases (alpha delta epsilon and zeta) and eukaryotic viral and plasmid-borne enzymes. DNA polymerase is made up of distinct domains and sub-domains. The polymerase domain of DNA polymerase type B (Pol domain) is responsible for the template-directed polymerization of dNTPs onto the growing primer strand of duplex DNA that is usually magnesium dependent. In general the architecture of the Pol domain has been likened to a right hand with fingers thumb and palm sub-domains with a deep groove to accommodate the nucleic acid substrate. There are a few conserved motifs in the Pol domain of family B DNA polymerases. The conserved aspartic acid residues in the DTDS motifs of the palm sub-domain is crucial for binding to divalent metal ion and is suggested to be important for polymerase catalysis..
rpsblast_kog gnl|CDD|37009 7 160 + 154 none 7.09 2173 71.43 7e-78 KOG1798 KOG1798 KOG1798 DNA polymerase epsilon catalytic subunit A [Replication recombination and repair].

4 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 14 160 147 PTHR10670 none none none
PANTHER 14 160 147 PTHR10670:SF0 "KEGG:00230+2.7.7.7","KEGG:00240+2.7.7.7";signature_desc=DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A none IPR029703
Pfam 28 180 153 PF00136 "KEGG:00230+2.7.7.7","KEGG:00240+2.7.7.7" DNA polymerase family B IPR006134
SUPERFAMILY 14 158 145 SSF56672 none none none

0 Localization

9 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2004_QTL1_peak_Bud_burst_A4 Qrob_Chr01 1 s_1AMVCC_444 s_1BE1VC_321 4 0 31 lod 3,2 7,4
Bourran2_2003_QTL8_peak_Bud_burst_A4 Qrob_Chr01 1 s_1AH7I_610 s_1BE1VC_321 4,6 0 28 lod 3,5 7,4
Bourran2_2007_QTL6_peak_Bud_burst_3P Qrob_Chr01 1 s_1BE1VC_321 s_1A5JRZ_890 5 0 25 lod 2,4 6
Bourran2_2014_nEpiBC_3P Qrob_Chr01 1 v_1588_550 s_1AZJRA_1600 30,48 9,48 43,98 lod 2,3642 6,3
Bourran2_2014_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2014_nSeqBC*_A4 Qrob_Chr01 1 s_1CFE4C_2114 s_1BDNCB_819 15,25 2 28,5 lod 2,9903 8,3

0 Targeting