O54747

PR
Gene name
Pold1
Protein name
DNA polymerase delta catalytic subunit
Names
3'-5' exodeoxyribonuclease
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:59294
EC number
2.7.7.7: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-140 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O54747

Entry ID Method Resolution Chain Position Source
AF-O54747-F1 Predicted AlphaFoldDB

No variants for O54747

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O54747

No associated diseases with O54747

4 regional properties for O54747

Type Name Position InterPro Accession
domain DNA-directed DNA polymerase, family B, exonuclease domain 127 - 473 IPR006133
domain DNA-directed DNA polymerase, family B, multifunctional domain 538 - 969 IPR006134
conserved_site DNA-directed DNA polymerase, family B, conserved site 749 - 757 IPR017964
domain C4-type zinc-finger of DNA polymerase delta 1008 - 1078 IPR025687

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
Subcellular Localization
  • Nucleus
  • Colocalizes with PCNA and POLD3 at S phase replication sites
  • After UV irradiation, recruited to DNA damage sites within 2 hours, independently on the cell cycle phase, nor on PCNA ubiquitination
  • This recruitment requires POLD3, PCNA and RFC1-replication factor C complex
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
delta DNA polymerase complex A multimeric DNA polymerase enzyme complex which differs in composition amongst species; in humans it is a heterotetramer of four subunits of approximately 125, 50, 68 and 12kDa, while in S. cerevisiae, it has three different subunits which form a heterotrimer, and the active enzyme is a dimer of this heterotrimer. Functions in DNA replication, mismatch repair and excision repair.
nucleotide-excision repair complex Any complex formed of proteins that act in nucleotide-excision repair.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

10 GO annotations of molecular function

Name Definition
3'-5' exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
3'-5'-exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a DNA molecule.
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
damaged DNA binding Binding to damaged DNA.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
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.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
metal ion binding Binding to a metal ion.
nucleotide binding Binding to 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.

10 GO annotations of biological process

Name Definition
base-excision repair, gap-filling Repair of the damaged strand by the combined action of an apurinic endouclease that degrades a few bases on the damaged strand and a polymerase that synthesizes a 'patch' in the 5' to 3' direction, using the undamaged strand as a template.
cellular response to UV Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
DNA biosynthetic process The biosynthetic process resulting in the formation of DNA.
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.
DNA replication proofreading Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.
DNA synthesis involved in DNA repair Synthesis of DNA that proceeds from the broken 3' single-strand DNA end and uses the homologous intact duplex as the template.
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
error-free translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.
fatty acid homeostasis Any process involved in the maintenance of an internal steady state of fatty acid within an organism or cell.
nucleotide-excision repair, DNA gap filling Repair of the gap in the DNA helix by DNA polymerase and DNA ligase after the portion of the strand containing the lesion has been removed by pyrimidine-dimer repair enzymes.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P28339 POLD1 DNA polymerase delta catalytic subunit Bos taurus (Bovine) PR
P54358 PolD1 DNA polymerase delta catalytic subunit Drosophila melanogaster (Fruit fly) PR
P28340 POLD1 DNA polymerase delta catalytic subunit Homo sapiens (Human) PR
P52431 Pold1 DNA polymerase delta catalytic subunit Mus musculus (Mouse) PR
Q9LRE6 POLD1 DNA polymerase delta catalytic subunit Oryza sativa subsp japonica (Rice) PR
10 20 30 40 50 60
MDGKRRQAPS SGVPPKRACK GLWDEDEPSQ FEENLALLEE IEAENRLQEA EEELQLPPEG
70 80 90 100 110 120
IVGGQFSTAD IDPRWLRPTP LALDPSTEPL IFQQLEIDHY VGTSPPLPEG PPASRNSVPI
130 140 150 160 170 180
LRAFGVTDEG FSVCCHIHGF APYFYTPAPP GFGAEHLSEL QRELNAAISR DQRGGKELSG
190 200 210 220 230 240
PAVLAIELCS RESMFGYHGH GPSPFLRITL ALPRLMAPAR RLLEQGIRVP GLGTPSFAPY
250 260 270 280 290 300
EANVDFEIRF MVDADIVGCN WLELPAGKYV RRAEKKATLC QLEVDVLWSD VISHPPEGQW
310 320 330 340 350 360
QRIAPLRVLS FDIECAGRKG IFPEPERDPV IQICSLGLRW GEPEPFLRLA LTLRPCAPIL
370 380 390 400 410 420
GAKVQSYERE EDLLQAWATF ILAMDPDVIT GYNIQNFDLP YLISRAQTLK VDRFPFLGRV
430 440 450 460 470 480
TGLRSNIRDS SFQSRQVGRR DSKVVSMVGR VQMDMLQVLL REYKLRSYTL NAVSFHFLGE
490 500 510 520 530 540
QKEDVQHSII TDLQNGNEQT RRRLAVYCLK DAFLPLRLLE RLMVLVNNVE MARVTGVPLG
550 560 570 580 590 600
YLLSRGQQVK VVSQLLRQAM REGLLMPVVK TEGGEDYTGA TVIEPLKGYY DVPIATLDFS
610 620 630 640 650 660
SLYPSIMMAH NLCYTTLLRP GAAQKLGLKP DEFIKTPTGD EFVKASVRKG LLPQILENLL
670 680 690 700 710 720
SARKRAKAEL AQETDPLRRQ VLDGRQLALK VSPNSVYGFT GAQVGKLPCL EISQSVTGFG
730 740 750 760 770 780
RQMIEKTKQL VETKYTLENG YDANAKVVYG DTDSVMCRFG VSSVAEAMSL GREAANWVSS
790 800 810 820 830 840
HFPSPIRLEF EKVYFPYLLI SKKRYAGLLF SSRSDAHDRM DCKGLEAVRR DNCPLVANLV
850 860 870 880 890 900
TSSLRRILVD RDPDGAVAHA KDVISDLLCN RIDISQLVIT KELTRAAADY AGKQAHVELA
910 920 930 940 950 960
ERMRKRDPGS APNLGDRVPY VIIGAAKGVA AYMKSEDPLF VLEHSLPIDT QYYLEQQLAK
970 980 990 1000 1010 1020
PLLRIFEPIL GEGRAESVLL RGDHTRCKTV LTSKVGGLLA FTKRRNSCIG CRSVIDHQGA
1030 1040 1050 1060 1070 1080
VCKFCQPRES ELYQKEVSHL NALEERFSRL WTQCQRCQGS LHEDVICTSR DCPIFYMRKK
1090 1100
VRKDLEDQER LLQRFGPPGP EAW