ID Card:
Protein sequence:
MASVLGSGRGSGGLSSQLKCKSKRRRRRRSKRKDKVSILSTFLAPFKHLSPGITNTEDDDTLSTSSAEVKENRNVGNLAARPPPSGDRARGGAPGAKRKRPLEEGNGGHLCKLQLVWKKLSWSVAPKNALVQLHELRPGLQYRTVSQTGPVHAPVFAVAVEVNGLTFEGTGPTKKKAKMRAAELALRSFVQFPNACQAHLAMGGGPGPGTDFTSDQADFPDTLFQEFEPPAPRPGLAGGRPGDAALLSAAYGRRRLLCRALDLVGPTPATPAAPGERNPVVLLNRLRAGLRYVCLAEPAERRARSFVMAVSVDGRTFEGSGRSKKLARGQAAQAALQELFDIQMPGHAPGRARRTPMPQEFADSISQLVTQKFREVTTDLTPMHARHKALAGIVMTKGLDARQAQVVALSSGTKCISGEHLSDQGLVVNDCHAEVVARRAFLHFLYTQLELHLSKRREDSERSIFVRLKEGGYRLRENILFHLYVSTSPCGDARLHSPYEITTDLHSSKHLVRKFRGHLRTKIESGEGTVPVRGPSAVQTWDGVLLGEQLITMSCTDKIARWNVLGLQGALLSHFVEPVYLQSIVVGSLHHTGHLARVMSHRMEGVGQLPASYRHNRPLLSGVSDAEARQPGKSPPFSMNWVVGSADLEIINATTGRRSCGGPSRLCKHVLSARWARLYGRLSTRTPSPGDTPSMYCEAKLGAHTYQSVKQQLFKAFQKAGLGTWVRKPPEQQQFLLTL
Comments:
ADAR, ADARB1, and ADARB2 are the three highly conserved members of the ADAR mammalian protein family. ADAR and ADARB1 catalyze the hydrolytic deamination of Adenosine (Nishikura 2010 ) that brings to the occurrence of Inosine (I), one of the most prevalent post-transcriptional modification in higher eukaryotes (Walkley & Li 2017 ). ADARB2 has been identified as inactive in vitro . Experiments suggests that ADARB2 may utilize its arginine rich N-terminal motif to target a selective set of substrates. It has been speculated that this motif may recognize and bind to specific stem loop structures of single stranded (ss) RNAs. Noteworthy, in vitro experiments show that ADARB2 effectively suppresses editing of 5HTC R RNA by ADAR and ADAB1 (Chen et al. 2000 )
Alpha Fold Predicted Structure:
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Protein sequence:
M
A
S
V
L
G
S
G
R
G
S
G
G
L
S
S
Q
L
K
C
K
S
K
R
R
R
R
R
R
S
K
R
K
D
K
V
S
I
L
S
T
F
L
A
P
F
K
H
L
S
P
G
I
T
N
T
E
D
D
D
T
L
S
T
S
S
A
E
V
K
E
N
R
N
V
G
N
L
A
A
R
P
P
P
S
G
D
R
A
R
G
G
A
P
G
A
K
R
K
R
P
L
E
E
G
N
G
G
H
L
C
K
L
Q
L
V
W
K
K
L
S
W
S
V
A
P
K
N
A
L
V
Q
L
H
E
L
R
P
G
L
Q
Y
R
T
V
S
Q
T
G
P
V
H
A
P
V
F
A
V
A
V
E
V
N
G
L
T
F
E
G
T
G
P
T
K
K
K
A
K
M
R
A
A
E
L
A
L
R
S
F
V
Q
F
P
N
A
C
Q
A
H
L
A
M
G
G
G
P
G
P
G
T
D
F
T
S
D
Q
A
D
F
P
D
T
L
F
Q
E
F
E
P
P
A
P
R
P
G
L
A
G
G
R
P
G
D
A
A
L
L
S
A
A
Y
G
R
R
R
L
L
C
R
A
L
D
L
V
G
P
T
P
A
T
P
A
A
P
G
E
R
N
P
V
V
L
L
N
R
L
R
A
G
L
R
Y
V
C
L
A
E
P
A
E
R
R
A
R
S
F
V
M
A
V
S
V
D
G
R
T
F
E
G
S
G
R
S
K
K
L
A
R
G
Q
A
A
Q
A
A
L
Q
E
L
F
D
I
Q
M
P
G
H
A
P
G
R
A
R
R
T
P
M
P
Q
E
F
A
D
S
I
S
Q
L
V
T
Q
K
F
R
E
V
T
T
D
L
T
P
M
H
A
R
H
K
A
L
A
G
I
V
M
T
K
G
L
D
A
R
Q
A
Q
V
V
A
L
S
S
G
T
K
C
I
S
G
E
H
L
S
D
Q
G
L
V
V
N
D
C
H
A
E
V
V
A
R
R
A
F
L
H
F
L
Y
T
Q
L
E
L
H
L
S
K
R
R
E
D
S
E
R
S
I
F
V
R
L
K
E
G
G
Y
R
L
R
E
N
I
L
F
H
L
Y
V
S
T
S
P
C
G
D
A
R
L
H
S
P
Y
E
I
T
T
D
L
H
S
S
K
H
L
V
R
K
F
R
G
H
L
R
T
K
I
E
S
G
E
G
T
V
P
V
R
G
P
S
A
V
Q
T
W
D
G
V
L
L
G
E
Q
L
I
T
M
S
C
T
D
K
I
A
R
W
N
V
L
G
L
Q
G
A
L
L
S
H
F
V
E
P
V
Y
L
Q
S
I
V
V
G
S
L
H
H
T
G
H
L
A
R
V
M
S
H
R
M
E
G
V
G
Q
L
P
A
S
Y
R
H
N
R
P
L
L
S
G
V
S
D
A
E
A
R
Q
P
G
K
S
P
P
F
S
M
N
W
V
V
G
S
A
D
L
E
I
I
N
A
T
T
G
R
R
S
C
G
G
P
S
R
L
C
K
H
V
L
S
A
R
W
A
R
L
Y
G
R
L
S
T
R
T
P
S
P
G
D
T
P
S
M
Y
C
E
A
K
L
G
A
H
T
Y
Q
S
V
K
Q
Q
L
F
K
A
F
Q
K
A
G
L
G
T
W
V
R
K
P
P
E
Q
Q
Q
F
L
L
T
L
Secondary Structure Alphabet
G: 3-turn helix (310 helix) H: α-helix I: 𝝅-helix (5 - turn helix) T: Hydrogen Bonded Turn B: β-sheet S: Bend C: Coil (residues not present in any of the above conformations) N: Not assigned
Download PDB Structures & DSSP Secondary Structures:
Diseases connected to this enzyme:
Publications: