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 Q9RT03

Entry ID Method Resolution Chain Position Source
AF-Q9RT03-F1 Predicted AlphaFoldDB

No variants for Q9RT03

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9RT03

No associated diseases with Q9RT03

No regional properties for Q9RT03

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9RT03

Functions

Description
EC Number 2.4.2.1 Pentosyltransferases
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
adenosine deaminase activity Catalysis of the reaction: adenosine + H2O = inosine + NH3.
copper ion binding Binding to a copper (Cu) ion.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
S-methyl-5-thioadenosine phosphorylase activity Catalysis of the reaction: 5'-methylthioadenosine + phosphate = adenine + 5-methylthio-D-ribose 1-phosphate.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTAPGLPLLR APNLAVPHAF TTRAGGVSAG PYAGLNLDDR SDDPRPVAEN RARLAAALGF
70 80 90 100 110 120
AADDFARLNQ VHGVQVVHAQ APGFWEGDAL VTATPGVLLA IGTADCYPLL LADPEAGVIG
130 140 150 160 170 180
AAHAGWKGTV GRIGQRTVEQ MVNLGARPER IHAAVGPGIC GEQYEVGEDV AAQFRAAGLG
190 200 210 220 230 240
EWVLEREGRT HLDLAGANRA LLEGAGVGDL WVSGRCSTEA DFYSYRRDAG QTGRMWAVIG
250
LPRREGQTGE ARA