Table 1 |
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Variability tolerated at key residue positions within the EPK catalytic domain |
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| Residue |
G1 |
G2 |
G3 |
K |
E |
D |
N |
D |
E |
D |
| Subdomain |
I |
I |
I |
II |
III |
V1B |
V1B |
VII |
VIII |
IX |
| Number not conserved* |
52/473 |
29/473 |
135/473 |
16/482 |
19/483 |
29/493 |
23/493 |
23/496 |
34/493 |
22/493 |
| % conserved |
89% |
94% |
71% |
97% |
96% |
94% |
95% |
95% |
93% |
95% |
| Amino-acid substitution† |
A/14; S/10 |
A/5; D/4 |
A/55; S/53 |
C/4; R/3, N/3 |
A/7; D/3, R/3 |
N/17; S/5 |
(S/T)/8; (K/R)/8 |
E/6; G/5 |
D/14; N/10 |
N/7; A, G, T/3 each |
| SCOP (structure)‡ |
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| Number not conserved |
0/27 |
0/27 |
4/27 |
0/27 |
0/27 |
0/27 |
0/27 |
1/27 |
1/27 |
0/27 |
| Amino-acid substitution |
S/3, A/1 |
E/1 |
N/1 |
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The partial alignment (see Additional data files) was used to examine conservation among previously identified [52] highly conserved residues in EPK subdomains I-IX. The amino acids listed along the top of the table correspond to residues of PKA-Calpha (NP_002721): G1 = G51, G2 = G53, G3 = G56, K73, E92, D167, N172, D185, E209, D221. *The number of residues in Table 1 that differed from the consensus residue are listed first, along with the number of sequences informative at that residue. †The top two most commonly substituted amino acids at the given position and the number of occurrences of the substituted amino acid at that position. ‡The 27 EPK structural families defined in SCOP were searched for examples of EPKs with non-canonical residues at any of these ten positions. G53 is substitued three times with S (CK2, Cal, Phk) and once with A (Dap). Residue D in subdomain VII is substituted with E in titin. E in subdomain VIII is substituted with N in CK1. |
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Kostich et al. Genome Biology 2002 3:research0043.1 doi:10.1186/gb-2002-3-9-research0043 |
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