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 Q12524

Entry ID Method Resolution Chain Position Source
AF-Q12524-F1 Predicted AlphaFoldDB

2 variants for Q12524

Variant ID(s) Position Change Description Diseaes Association Provenance
s12-442035 235 T>I No SGRP
s12-441926 271 I>M No SGRP

No associated diseases with Q12524

2 regional properties for Q12524

Type Name Position InterPro Accession
conserved_site NUDIX hydrolase, NudL, conserved site 57 - 77 IPR000059
domain NUDIX hydrolase domain 37 - 199 IPR000086

Functions

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

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

6 GO annotations of molecular function

Name Definition
8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity Catalysis of the reaction: 8-oxo-7,8-dihydrodeoxyguanosine-triphosphate (8-oxo-dGTP) + H2O = 8-oxo-7,8-dihydrodeoxyguanosine phosphate (8-oxo-dGMP) + diphosphate. 8-oxo-dGTP is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for DNA synthesis causing transversion mutations. 8-oxo-dGTPase hydrolyses 8-oxo-dGTP to its monophosphate form to prevent the misincorporation of 8-oxo-dGTP into cellular DNA.
8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity Catalysis of the reaction: 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) + H2O = 8-oxo-7,8-dihydroguanosine diphosphate (8-oxo-GDP) + phosphate. 8-oxo-7,8-dihydroguanosine triphosphate (8-oxo-GTP) is the oxidised form of the free guanine nucleotide and can act as a potent mutagenic substrate for transcription.
acetyl-CoA hydrolase activity Catalysis of the reaction: acetyl-CoA + H(2)O = acetate + CoA + H(+).
CoA pyrophosphatase activity Catalysis of the reaction: coenzyme A or its derivatives + H2O = 3',5'-ADP + 4'-phosphopantetheine.
magnesium ion binding Binding to a magnesium (Mg) ion.
manganese ion binding Binding to a manganese ion (Mn).

3 GO annotations of biological process

Name Definition
coenzyme A catabolic process The chemical reactions and pathways resulting in the breakdown of coenzyme A, 3'-phosphoadenosine-(5')diphospho(4')pantatheine, an acyl carrier in many acylation and acyl-transfer reactions in which the intermediate is a thiol ester.
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
nucleoside diphosphate metabolic process The chemical reactions and pathways involving a nucleoside diphosphate, a compound consisting of a nucleobase linked to a deoxyribose or ribose sugar esterified with diphosphate on the sugar.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q99P30 Nudt7 Peroxisomal coenzyme A diphosphatase NUDT7 Mus musculus (Mouse) PR
10 20 30 40 50 60
MILSQRRMLS SKQLIENLIR YKFHKTPYTR SSIWPFKRNS AVIILLFIGM KGELRVLLTK
70 80 90 100 110 120
RSRTLRSFSG DVSFPGGKAD YFQETFESVA RREAEEEIGL PHDPEVLHKE FGMKLDNLVM
130 140 150 160 170 180
DMPCYLSRTF LSVKPMVCFL YKDKLEKHED KYKVPLDIRK FFGKLNPGET SSLFSVPLND
190 200 210 220 230 240
LVIHLLPEAD EDVKSYQAEY FERKEYKLNW GGIKWLIMHY HFHVANNNEM PWLQTIEDLS
250 260 270 280 290 300
SSDEDGVDGG IFRFRDLWGL TCKILFDVSC IANGLMDEKL KGELGHEDLI VGLHDYGNQM
310 320 330
QPNGRSEWEI GMINGDRNLK YSDVIPEYYM KHLLECRSLW