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 A0QJ19

Entry ID Method Resolution Chain Position Source
AF-A0QJ19-F1 Predicted AlphaFoldDB

No variants for A0QJ19

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0QJ19

No associated diseases with A0QJ19

3 regional properties for A0QJ19

Type Name Position InterPro Accession
domain Oxidoreductase FAD/NAD(P)-binding 97 - 187 IPR001433
domain FAD-binding domain, ferredoxin reductase-type 2 - 89 IPR017927
domain Dihydroorotate dehydrogenase, electron transfer subunit, iron-sulphur cluster binding domain 203 - 237 IPR019480

Functions

Description
EC Number 2.7.4.22 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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
UMP kinase activity Catalysis of the reaction: ATP + UMP = ADP + UDP.

2 GO annotations of biological process

Name Definition
'de novo' CTP biosynthetic process The chemical reactions and pathways resulting in the formation of cytidine 5'-triphosphate (CTP) from simpler components.
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
MTESREPHVA GSAAPRPEPA NGLASGQPSS RARYSRVLLK LGGEMFGGGQ VGLDPDVVAQ
70 80 90 100 110 120
VARQIAEVVR GGVQVAVVIG GGNFFRGAQL QQRGMERTRS DYMGMLGTVM NSLALQDFLE
130 140 150 160 170 180
KEGIVTRVQT AITMGQVAEP YLPLRAVRHL EKGRVVIFGA GMGLPYFSTD TTAAQRALEI
190 200 210 220 230 240
GAEVVLMAKA VDGVFSADPR QYPEAELITA ISHREVIDRG LRVADATAFS LCMDNGMPIL
250 260
VFNLLTNGNI ARAVAGEKIG TLVTT