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 A1SNJ7

Entry ID Method Resolution Chain Position Source
AF-A1SNJ7-F1 Predicted AlphaFoldDB

No variants for A1SNJ7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1SNJ7

No associated diseases with A1SNJ7

1 regional properties for A1SNJ7

Type Name Position InterPro Accession
conserved_site Adenylate kinase, conserved site 81 - 92 IPR033690

Functions

Description
EC Number 2.7.4.3 Phosphotransferases with a phosphate group as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
adenylate kinase activity Catalysis of the reaction: ATP + AMP = 2 ADP.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

2 GO annotations of biological process

Name Definition
AMP salvage The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from derivatives of it (either adenine, ADP or adenosine 3',5'-bisphosphate) without de novo synthesis.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRLIIMGPPG AGKGTQAKYI AEHFKIPAIS TGDIFRANVT EGTPLGVEAK RYMDAGEYVP
70 80 90 100 110 120
DEVTNRMVRN RIDEPDAVGG FLLDGYPRTV AQVEELDGMI RFTGHRLDAV VCLTVDQDEI
130 140 150 160 170 180
VGRLLQRAQV EGRADDTEDV IRRRQDLYLE QTAPLIEIYK QRDLVHEVDG IGEVDEVTAR
190
IFQALDVIPE S