Q2NY21

PR
Gene name
ung
Protein name
Uracil-DNA glycosylase
Names
UDG
Species
Xanthomonas oryzae pv oryzae (strain MAFF 311018)
KEGG Pathway
xom:XOO4051
EC number
3.2.2.27: Hydrolyzing N-glycosyl compounds
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

157-241 (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 Q2NY21

Entry ID Method Resolution Chain Position Source
AF-Q2NY21-F1 Predicted AlphaFoldDB

No variants for Q2NY21

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2NY21

No associated diseases with Q2NY21

1 regional properties for Q2NY21

Type Name Position InterPro Accession
conserved_site Spider toxin CSTX, Knottin scaffold conserved site 48 - 74 IPR011142

Functions

Description
EC Number 3.2.2.27 Hydrolyzing N-glycosyl compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

1 GO annotations of molecular function

Name Definition
uracil DNA N-glycosylase activity Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.

1 GO annotations of biological process

Name Definition
base-excision repair In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTEVEARIQL EPSWKAKVGD WLLCSQMQEL SAFLRQRKAV GARVFPPGPQ IFAAFDATPF
70 80 90 100 110 120
DQVKVVILGQ DPYHGEGQAH GLCFSVLPGV PVPPSLLNIY KEIQDDLGIA RPDHGYLMPW
130 140 150 160 170 180
ARQGVLLLNA VLTVEQGRAG AHQNKGWEGF TDHVVETLNR EREGLVFLLW GSYAQSKGRV
190 200 210 220 230 240
IDQARHRVFK APHPSPLSAH RGFLGCQHFS KTNAHLQRRG ISPIDWSLPP RNELDTTSAG
A