Q6C030

PR
Gene name
DPB2 (YALI0F28215g)
Protein name
DNA polymerase epsilon subunit B
Names
DNA polymerase II subunit 2
Species
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
KEGG Pathway
yli:YALI0F28215g
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

50-147 (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 Q6C030

Entry ID Method Resolution Chain Position Source
AF-Q6C030-F1 Predicted AlphaFoldDB

No variants for Q6C030

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6C030

No associated diseases with Q6C030

8 regional properties for Q6C030

Type Name Position InterPro Accession
domain SH3 domain 8 - 69 IPR001452
domain Dedicator of cytokinesis protein 2, DHR2 domain 1200 - 1620 IPR026799
domain C2 DOCK-type domain 419 - 615 IPR027007
domain DOCKER domain 1211 - 1622 IPR027357
domain Dedicator of cytokinesis, N-terminal domain 72 - 414 IPR032376
domain DOCKER, Lobe A 1205 - 1334 IPR046769
domain DOCKER, Lobe B 1395 - 1474 IPR046770
domain DOCKER, Lobe C 1516 - 1615 IPR046773

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
nuclear replication fork The Y-shaped region of a nuclear replicating DNA molecule, resulting from the separation of the DNA strands and in which the synthesis of new strands takes place. Also includes associated protein complexes.

4 GO annotations of molecular function

Name Definition
DNA polymerase processivity factor activity An enzyme regulator activity that increases the processivity of polymerization by DNA polymerase, by allowing the polymerase to move rapidly along DNA while remaining topologically bound to it.
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.
double-stranded DNA binding Binding to double-stranded DNA.
single-stranded DNA binding Binding to single-stranded DNA.

3 GO annotations of biological process

Name Definition
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.
DNA-templated DNA replication maintenance of fidelity A DNA metabolic process that prevents or corrects errors to ensure that DNA is replicated accurately. Errors can be corrected either by intrinsic DNA polymerase proofreading activity or via mismatch repair.
error-prone 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 and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPAVLPIKLN PSQMRPVAYR IFSKKHGLNL KSTGLETLTE IIGKNYGTEW RGAEAAKMME
70 80 90 100 110 120
EICRLWKEQE MGVFVEGKPL QELFDEITAS KKAKEKARVQ VVSKSVGLTG VEEIEDREGE
130 140 150 160 170 180
PQVNVIREAA PSVDVVWKEF FKVISAFDQP LFHYNARQQR FEKRKTKPTL FANAQSASNM
190 200 210 220 230 240
FLTRYHLVYN RLLRNDDTTD LKITSIRSLI GRQGEFSIFG MLSKNPEQKI CLQDDTGRIL
250 260 270 280 290 300
LILAAGCKPD PGVYYPEGSF VICNGRYMKS GDAEVFVVIT MGPPVAEKRQ ETITAYGNMD
310 320 330 340 350 360
YLGLHGNPHG SVVRRIERQV EASMLAEEKR LVDQKVIVFG GDMYLDNPLT LKALQKVFST
370 380 390 400 410 420
IELEFQDSGT KKPLAMVFSG DFTSQYQPPH LYKKGFDKLE ELFKEFSSII TGVKIIFVPG
430 440 450 460 470 480
QRDPWTNTFP TQNAVVPLQP LPTTMINRVA RLCGEDVSMS SNPCRMAYLT QDMVFYRDGL
490 500 510 520 530 540
SERLRKCNLQ LDSAKDDSDD SDDDIEIDND EVMINDVVVN EPESSFDFGE GLSNLTRPVD
550 560 570 580 590 600
ISTPMASQVG PTNTLSAKEV ESRKIVRTIC DQGHLSPFNR HDRPVAWDYD ETLWLSPLPT
610 620 630 640 650
ILFMVDTHAP KFSLRYEECM VVNPGPFLNR KIASWVEYDP SKKTVKERQL HI