Q6FXD0

PR
Gene name
DPB4 (CAGL0B01903g)
Protein name
DNA polymerase epsilon subunit D
Names
DNA polymerase II subunit D
Species
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
KEGG Pathway
cgr:CAGL0B01903g
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-191 (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 Q6FXD0

Entry ID Method Resolution Chain Position Source
AF-Q6FXD0-F1 Predicted AlphaFoldDB

No variants for Q6FXD0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FXD0

No associated diseases with Q6FXD0

No regional properties for Q6FXD0

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q6FXD0

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
CHRAC An ISWI complex that contains an ATPase subunit of the ISWI family (SNF2H in mammals, Isw2 in S. cerevisiae), an ACF1 homolog, and additional small histone fold subunits (generally two of these, but Xenopus has only one and some additional non-conserved subunits). CHRAC plays roles in the regulation of RNA polymerase II transcription and in DNA replication and repair.
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.

6 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.
double-stranded DNA binding Binding to double-stranded DNA.
nucleosomal DNA binding Binding to the DNA portion of a nucleosome.
protein heterodimerization activity Binding to a nonidentical protein to form a heterodimer.
single-stranded DNA 3'-5' exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a single-stranded DNA molecule.
single-stranded DNA binding Binding to single-stranded DNA.

3 GO annotations of biological process

Name Definition
chromatin remodeling A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication.
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.
leading strand elongation The process in which an existing DNA strand is extended continuously in a 5' to 3' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Leading strand elongation proceeds in the same direction as the replication fork.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPPKGWRKDA QGNYPTTSYM KEQENVTMQD LLFPRSVIMA LAKEVPEMQQ QQVQVQAAEK
70 80 90 100 110 120
GEPVEKTPAK KLVVTKDASM ALQHSATVFV NHLLMYAREL AKEQDRRSCN VDDILNALEH
130 140 150 160 170 180
MGHPGLKPLV ANRLDDYQEA LEWKKQLKAQ LQILNGEAEE EPNELGTYDH DNETDDEEIR
190
DEPEKKLKVE P