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 A6M378

Entry ID Method Resolution Chain Position Source
AF-A6M378-F1 Predicted AlphaFoldDB

No variants for A6M378

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6M378

No associated diseases with A6M378

2 regional properties for A6M378

Type Name Position InterPro Accession
active_site Thymidylate synthase, active site 123 - 151 IPR020940
domain Thymidylate synthase/dCMP hydroxymethylase domain 7 - 263 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
MSLYDDKYLA IANDILENGY FDNNRTGVKT YKLPHQIMQF NLEKEFPILT TKFVAFKTAV
70 80 90 100 110 120
KELLWIFKDQ SNSVKELQSQ NVKIWDEWMM EDGTIGTSYG WIVKKFDQID KLIDALKNNP
130 140 150 160 170 180
QDRRMMINLW QIPYLDSAPL YPCCFLTMWD VTDGKLNCML VQRSGDWGLG VPFNTSQYAV
190 200 210 220 230 240
LVHLLAQVTG LKPGLFTHVI NNAHIYENQV DGLKLQLTRK NDAYNAPKLW INPEITNFYD
250 260
FTPDDIKLED YKHHESIKMD VSV