Analysis of p.(Ala826Thr) variant, MYO7A gene, myosin VIIa protein (2215 residues)
Ortholog conservation: |
Number of sequences | AAPI* | AAPIR** | Number of divergencies | Number of mutant | Number of gaps | Conservation of A826 | Conservation - gap |
---|---|---|---|---|---|---|---|
24 | 76.99% | 69.20% | 14 details |
0 details |
0 details |
10 / 24 (41.67%) | 10 / 24 (41.67%) |
*AAPI: Alignment Average Percentage Identity
**AAPIR: Alignment Average Percentage Identity of the Region (20 residues surrounding position 826). AAPIR appears in green if it is more than 10% compared to AAPI, in red if less than 10%.
You can check the AAPIRs compared with AAPI of the whole alignment by clicking here. The help page will tell you more.
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Domain conservation: |
The residue belongs to the domain IQ 4.
814 |
| 834 |
|
|||
IQ 4 of myosin VIIa domain alignment including p.A826 residue.
Number of sequences | AAPID*** (from aa 814 to aa 834) |
AAPIR! | Number of divergencies | Number of mutant | Number of gaps | Conservation of A826 | Conservation - gap |
---|---|---|---|---|---|---|---|
1048 | 26.44% | 32.21% | 960 details |
29 | 0 | 88 / 1048 (8.40%) | 88 / 1048 (8.40%) |
If we just consider IQ domain of myosin VIIa, we can add that:
on 3 sequences, conservation is 1/3 (33.33%),
or 1/3 (33.33%) if you do not take the gaps into account.
***AAPID: Alignment Average Percentage Identity of the Domain (positions are indicated).
!AAPIR is here compared with AAPID.
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Secondary structure analysis: |
Residu A826 is predicted to belong to an α helice. Probability is 0.991.
Direct environment is as follow:
A | R | C | R | A826 | Y | L | V | R |
Observed frequencies in α helices:
A: 1.23
T: 0.9
Mutant residu is less observed in this type of structure.
3D analysis: |
Models provided and analysed by USMA must be considered as predictions, therefore be careful when interpreting the results. All efforts have been made to build structures of quality, however, they are provided with NO WARRANTY as to their accuracy with the real biological molecules studied.
Predicted wild type and mutant structures have been compared. You will find the results below. Please note that USMA's "3D engine" is unable to analyse interactions with non amino-acids molecules (e.g. ATP or Ca2+).
PDB template | Sequence identity* | Molprobity bad rotamers | Molprobity Ramachandran outliers | Molprobity Ramachandran favored |
---|---|---|---|---|
2DFS | 37 % | 21/836 - 2.5 % | 8/955 - 0.8 % | 924/955 - 96.8 % |
* between target and template
Otherwise, see detailed Molprobity output
A826 | T826 |
---|---|
distance: 3.04 Å / angle: 1.88 rad between N and ARG 823 O distance: 3.04 Å / angle: 2.63 rad between N and ALA 822 O | distance: 3.08 Å / angle: 1.90 rad between N and ARG 823 O distance: 2.84 Å / angle: 2.08 rad between OG1 and ARG 823 O distance: 3.09 Å / angle: 2.65 rad between N and ALA 822 O |
A826 | T826 |
---|---|
none | none |
A826 (wild-type) | T826 (mutant) |
---|---|
JSmol Legends: The residue at the position 826 is located in the center, labelled in yellow and surrounded by its neighboring residues (distance < 5 Å). Amino acids involved in H-bonds with the residue 826 are labelled in blue. Amino acids involved in steric clashes with the residue 826 are labelled in red.
Additional ressources: |
See accession numbers of sequences used or references.
Execution time: 10 wallclock secs ( 6.99 usr 0.02 sys + 2.30 cusr 0.69 csys = 10.00 CPU)