Table 2. Alignment of the first five E. tenella homologue kinase proteins to the mouse p38α MAPK.

Proteins	Eukaryotic protein kinase catalytic domain
	Subdomains
Homologues	I GXGX[FY]GXV	II VAXK53	VIb HRDLKPXN	VII D168FGLAR	VIII T180XY182TXXYXAPE
NM_00116850 Mus musculus p38α MAPK	GSGAY GSV	V AVKK	HRDLKPSN	DFG L A R	T *G Y * VATRW YR A P E
ETH_00035055	GKG AY GVV	V ALKK	HRDMKPSN	DFG L A R	T *D Y * VATRW YR A P E
ETH_00005380	GTGSY GHV	V AIKK	HRDLKPAN	DFG L A R	T *GHVVTRW YR A PE
ETH_00004180	GSGAY GCV	V AVKK	HRDLKPSN	DFG L A R	T *D Y * VVTRW YRPPE
ETH_00028175	GNGSFGVV	V AIKK	HRDVKPQN	DFGSAK	VAY *ICSRFYR A P E
ETH_00004310	GEGTY GVV	CALKK	HRDLKPQN	DFG L A R	T *HE VVTLW YR A PD

* AA phosphorylated.

The first five E. tenella homologue kinase proteins with the lowest e values (Table 1) are aligned to the mouse p38α MAPK. The main motifs of subdomains of the eukaryotic protein kinase catalytic domain of the mammalian p38α MAPK are aligned to the five parasite kinases. In bold, the common amino acids are shown; in italic are amino acids found at a high frequency among proteins analyzed. The amino acids K53 and D168 (numbered in Mus musculus) are both required for catalytic activity. The amino acids T180 and Y182 (numbered in Mus musculus) are exposed at the surface of the inactivated p38α MAPK and phosphorylated by MAP kinases kinases leading to the activation of the p38α MAPK.