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 Q3IF68

Entry ID Method Resolution Chain Position Source
AF-Q3IF68-F1 Predicted AlphaFoldDB

No variants for Q3IF68

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3IF68

No associated diseases with Q3IF68

1 regional properties for Q3IF68

Type Name Position InterPro Accession
domain Adenosine deaminase domain 7 - 328 IPR001365

Functions

Description
EC Number 3.5.4.4 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
2'-deoxyadenosine deaminase activity Catalysis of the reaction: 2'-deoxyadenosine + H2O = deoxyinosine + NH3.
adenosine deaminase activity Catalysis of the reaction: adenosine + H2O = inosine + NH3.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
nucleotide metabolic process The chemical reactions and pathways involving a nucleotide, a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic nucleotides (nucleoside cyclic phosphates).
purine ribonucleoside monophosphate biosynthetic process The chemical reactions and pathways resulting in the formation of purine ribonucleoside monophosphate, a compound consisting of a purine base linked to a ribose sugar esterified with phosphate on the sugar.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MINRKLPLLD IHRHLDGNVR AQTILELGRQ FNITLPADNV AALIPHVQVI DPEPNLMAFL
70 80 90 100 110 120
QKLDWGVTVL GDYDACRRIA IENIEDAQAQ GLDYVELRFS PYYMAQSQGL HPQGVVEAVI
130 140 150 160 170 180
DGIKSATKGA NVKANLIGIL SRTYGVKVCQ QELDALLAFK DDLVAVDLAG DEIGFPGELF
190 200 210 220 230 240
VEHFKQVHDA YLAATIHAGE ALGAPSIWQA INELGASRIG HGVKAIEDIE LMNYLRDKRI
250 260 270 280 290 300
GIESCLTSNI QTSTVNDLAQ HPLKQFLDHG ILACINTDDP AVEGIEIEHE YLVAAPQAGL
310 320 330
SQADIEKAQA NALEIAYLSY SDKKALLTMA STR