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 A1AVP9

Entry ID Method Resolution Chain Position Source
AF-A1AVP9-F1 Predicted AlphaFoldDB

No variants for A1AVP9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1AVP9

No associated diseases with A1AVP9

1 regional properties for A1AVP9

Type Name Position InterPro Accession
domain Thymidylate kinase-like domain 9 - 198 IPR039430

Functions

Description
EC Number 2.7.4.9 Phosphotransferases with a phosphate group as acceptor
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

2 GO annotations of molecular function

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

3 GO annotations of biological process

Name Definition
dTDP biosynthetic process The chemical reactions and pathways resulting in the formation of dTDP, deoxyribosylthymine diphosphate (2'-deoxyribosylthymine5'-diphosphate).
dTTP biosynthetic process The chemical reactions and pathways resulting in the formation of dTTP, deoxyribosylthymine triphosphate.
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
MQRGKFITID GVEGSGKSTQ IDFICDYLVT KKINVILTRE PGGTELGEKI RTLLLSTDIQ
70 80 90 100 110 120
SIHGDTELLL LFAARNEHIR TKIIPSLEKG DWVLSDRFTD ASYAYQGGGR GLSIERITQL
130 140 150 160 170 180
EKWVLQDFTP DVTLLLDVSV ALGMSRVESR GRKDRIELET NDFFKRVRNS YIERSKQFPK
190 200
RIKLIDASKT LEQTAQQIKI ILQVL