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Conservation of functionally important amino acid residues (FIRs). |
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| Functional Site Type (# of residues) |
Ce-GnRHR vs. human GnRHR1 |
Ce-GnRHR vs. Dm-AKHR |
Human GnRHR1 vs. Dm-AKHR |
Ce-GnRHR vs. human Rhodopsin |
Ce-GnRHR vs. human Vasopressin receptor |
|
|
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| Receptor activation (6) |
83.3% |
83.3% |
83.3% |
75.0% |
83.3% |
| Ligand binding (7) |
35.7% |
21.4% |
42.9% |
7.1% |
35.7% |
| Binding pocket formation (24) |
54.2% |
68.8% |
72.9% |
43.8% |
33.3% |
| PKC phosphorylation (2) |
50.0% |
75.0% |
50.0% |
25.0% |
50.0% |
| Gq/11 G-protein coupling (8) |
62.5% |
93.8% |
68.8% |
56.2% |
62.5% |
| Gs G-protein coupling (3) |
50.0% |
33.3% |
33.3% |
0.0% |
33.3% |
| Total similarity (FIRs only) |
56.0% |
66.0% |
66.0% |
41.0% |
44.0% |
|
|
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| Identity (all residues) |
20.8% |
26.6% |
20.4% |
12.4% |
17.9% |
| Identity + Similarity (all residues) |
36.3% |
45.2% |
37.9% |
28.5% |
34.4% |
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Shown are the amino acid similarities between the functionally important residues of Ce-GnRHR and human GnRHR1, Drosophila melanogaster AKHR (Dm-AKHR), human rhodopsin, and human vasopressin type 1a. Also shown are the overall amino acid identity/similarity for each comparison. 'Similarity' of compared amino acids was based on the BLOSUM62 matrix, a more conservative measure of similarity than that used in the ALIGN algorithm, and percentages were calculated as described in methods. | |||||
Vadakkadath Meethal et al. BMC Evolutionary Biology 2006 6:103 doi:10.1186/1471-2148-6-103 |
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