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 Q03F96

Entry ID Method Resolution Chain Position Source
AF-Q03F96-F1 Predicted AlphaFoldDB

No variants for Q03F96

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q03F96

No associated diseases with Q03F96

2 regional properties for Q03F96

Type Name Position InterPro Accession
active_site Thymidylate synthase, active site 178 - 206 IPR020940
domain Thymidylate synthase/dCMP hydroxymethylase domain 4 - 316 IPR023451

Functions

Description
EC Number 2.1.1.45 Methyltransferases
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.

1 GO annotations of molecular function

Name Definition
thymidylate synthase activity Catalysis of the reaction: 5,10-methylenetetrahydrofolate + dUMP = 7,8-dihydrofolate + thymidylate.

3 GO annotations of biological process

Name Definition
dTMP biosynthetic process The chemical reactions and pathways resulting in the formation of dTMP, deoxyribosylthymine monophosphate (2'-deoxyribosylthymine 5'-phosphate).
dTTP biosynthetic process The chemical reactions and pathways resulting in the formation of dTTP, deoxyribosylthymine triphosphate.
methylation The process in which a methyl group is covalently attached to a molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLEEQYLNLE RYVLENGHLK GDRTQTGTLS TFGYQMRFDL SEGFPLLTTK RVPFGLIKSE
70 80 90 100 110 120
LLWFLKGDTN IRYLLQHNNH IWDEWAFKKW VESDEYQGPD MTDFGHRSLT DPEFNELYKI
130 140 150 160 170 180
EKQRFTEQIL EDDTFSAKYG DLGNVYGSQW RAWKTSTGET IDQISNVIDM IKNNPNSRRM
190 200 210 220 230 240
IVSAWNPEDV PTSALPPCHS LFQFYVADGK LSCQLYQRSG DIFLGIPFNI ASYALLTELI
250 260 270 280 290 300
AKATGLEVGE FIHTIGDAHI YSNHLDQVKE QLERTPRPAP KLKFKQVHDS IFDYEPGDIV
310
VEGYDPHPTI KAPVAV