Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for B9JZF5

Entry ID Method Resolution Chain Position Source
AF-B9JZF5-F1 Predicted AlphaFoldDB

No variants for B9JZF5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B9JZF5

No associated diseases with B9JZF5

3 regional properties for B9JZF5

Type Name Position InterPro Accession
domain Zinc finger, DNA glycosylase/AP lyase-type 261 - 297 IPR000214
domain Formamidopyrimidine-DNA glycosylase, catalytic domain 1 - 133 IPR012319
domain DNA glycosylase/AP lyase, H2TH DNA-binding 149 - 247 IPR015886

Functions

Description
EC Number 3.2.2.23 Hydrolyzing N-glycosyl compounds
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
class I DNA-(apurinic or apyrimidinic site) endonuclease activity Catalysis of the cleavage of an AP site 3' of the baseless site by a beta-lyase mechanism, leaving an unsaturated aldehyde, termed a 3'-(4-hydroxy-5-phospho-2-pentenal) residue, and a 5'-phosphate.
damaged DNA binding Binding to damaged DNA.
oxidized purine nucleobase lesion DNA N-glycosylase activity Catalysis of the removal of oxidized purine bases by cleaving the N-C1' glycosidic bond between the oxidized purine and the deoxyribose sugar. The reaction involves the formation of a covalent enzyme-substrate intermediate. Release of the enzyme and free base by a beta-elimination or a beta, gamma-elimination mechanism results in the cleavage of the DNA backbone 3' of the apurinic (AP) site.
zinc ion binding Binding to a zinc ion (Zn).

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
MPELPEVETV KRGLAPSMEG RRLTRLELRR TDLRFPLPVD FAARTQGRLI VSLSRRAKYL
70 80 90 100 110 120
LIDLDDGVSI VSHLGMSGSY RIEAANETGL PGQFHMARSR DEKHDHVIFH LSGPEGDPLR
130 140 150 160 170 180
VIYNDPRRFG FMDMVERRHM DRHAAFAGLG PEPVGNALDA DYLAFRFKGK AQPLKTALLD
190 200 210 220 230 240
QKVIAGLGNI YVCEALWRAH LSPETPARAL VNAEGKPVAA LEDLTQAIRT VIAEAIEAGG
250 260 270 280 290
SSLRDHIQAD GSLGYFQHSF NVYDREGEAC RTPGCTGTVE RMTQAGRSTF HCPQCQR