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 A5UK79

Entry ID Method Resolution Chain Position Source
AF-A5UK79-F1 Predicted AlphaFoldDB

No variants for A5UK79

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5UK79

No associated diseases with A5UK79

2 regional properties for A5UK79

Type Name Position InterPro Accession
domain dUTPase-like 74 - 166 IPR029054
domain dUTPase, trimeric 72 - 155 IPR033704

Functions

Description
EC Number 3.5.4.30 In cyclic amidines
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

3 GO annotations of molecular function

Name Definition
dCTP deaminase (dUMP-forming) activity Catalysis of the reaction: dCTP + 2 H(2)O = diphosphate + dUMP + H(+) + NH(4)(+).
dCTP deaminase activity Catalysis of the reaction: dCTP + H2O = dUTP + NH3.
nucleotide binding Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.

2 GO annotations of biological process

Name Definition
dUMP biosynthetic process The chemical reactions and pathways resulting in the formation of dUMP, deoxyuridine monophosphate (2'-deoxyuridine 5'-phosphate).
dUTP biosynthetic process The chemical reactions and pathways resulting in the formation of dUTP, deoxyuridine (5'-)triphosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAILSDKTIK EYLEEGKIVI DPLKDEQQIQ PSSVDMRLGD EFKVFKVIRK PYIDPKDEED
70 80 90 100 110 120
IAEYMESSTV PEGEAFIIHP NEFALATTQE YVKVPDDLVA RVEGRSSMGR LGVTMHVTAG
130 140 150 160 170 180
YVDPGFEGRI TLEISNIGAM PVALYPGQRV CQLVFETMTT PAELPYGHPK RNSKYMKQLK
190
PESSRVKLDY ELKK