ID Card:
Full name:
tRNA-specific adenosine deaminase 1
Synonym:
ADAT1, YGL243W
GI:
1723979
Orf:
HRA400
COG:
COG0590
UniProt:
P53065
Alpha Fold Predicted Structure:
AF-P53065-F1
Enzyme type:
deaminase
Position of modification - modification:
t :37 - m1I
Protein sequence:
MVSCQGTRPCIVNLLTMPSEDKLGEEISTRVINEYSKLKSACRPIIRPSGIREWTILAGVAAINRDGGANKIEILSIATGVKALPDSELQRSEGKILHDCHAEILALRGANTVLLNRIQNYNPSSGDKFIQHNDEIPARFNLKENWELALYISRLPCGDASMSFLNDNCKNDDFIKIEDSDEFQYVDRSVKTILRGRLNFNRRNVVRTKPGRYDSNITLSKSCSDKLLMKQRSSVLNCLNYELFEKPVFLKYIVIPNLEDETKHHLEQSFHTRLPNLDNEIKFLNCLKPFYDDKLDEEDVPGLMCSVKLFMDDFSTEEAILNGVRNGFYTKSSKPLRKHCQSQVSRFAQWELFKKIRPEYEGISYLEFKSRQKKRSQLIIAIKNILSPDGWIPTRTDDVK
Comments:
ADAT1 is a homodimeric enzyme and shares conserved sequence motifs with other well-characterized adenosine deaminases, including mammalian mRNA deaminases (ADARs). Also, like most members of the deaminase superfamily, a Zn2+ ion is coordinated by a conserved histidine and two cysteines. The fourth ligand is an active water molecule that acts as the nucleophile. Highly conserved glutamate then aids the reactions by shuttling a proton from water to the N1 position of inosine during the deamination reaction. These motifs constitute the canonical deaminase signature (C/H)xExn PCxxC found in most nucleotide deaminases. Tad1 (ADAT1) catalyzes the A-to-I deamination which is the first step in m1I synthesis in tRNA position 37 (Paris et al. 2011 ).
Reaction
Substrate
SubstrateType
Position
(Anti)Codon
Modified (Anti)Codon
Amino Acid Change
Transcript Name
Transcript Region
Cellular Localization
References
A:I
RNA
tRNA
37
IGC
IGC
tRNAAla IGC
anticodon
Nucleus
22024020
Alpha Fold Predicted Structure:
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Protein sequence:
M
V
S
C
Q
G
T
R
P
C
I
V
N
L
L
T
M
P
S
E
D
K
L
G
E
E
I
S
T
R
V
I
N
E
Y
S
K
L
K
S
A
C
R
P
I
I
R
P
S
G
I
R
E
W
T
I
L
A
G
V
A
A
I
N
R
D
G
G
A
N
K
I
E
I
L
S
I
A
T
G
V
K
A
L
P
D
S
E
L
Q
R
S
E
G
K
I
L
H
D
C
H
A
E
I
L
A
L
R
G
A
N
T
V
L
L
N
R
I
Q
N
Y
N
P
S
S
G
D
K
F
I
Q
H
N
D
E
I
P
A
R
F
N
L
K
E
N
W
E
L
A
L
Y
I
S
R
L
P
C
G
D
A
S
M
S
F
L
N
D
N
C
K
N
D
D
F
I
K
I
E
D
S
D
E
F
Q
Y
V
D
R
S
V
K
T
I
L
R
G
R
L
N
F
N
R
R
N
V
V
R
T
K
P
G
R
Y
D
S
N
I
T
L
S
K
S
C
S
D
K
L
L
M
K
Q
R
S
S
V
L
N
C
L
N
Y
E
L
F
E
K
P
V
F
L
K
Y
I
V
I
P
N
L
E
D
E
T
K
H
H
L
E
Q
S
F
H
T
R
L
P
N
L
D
N
E
I
K
F
L
N
C
L
K
P
F
Y
D
D
K
L
D
E
E
D
V
P
G
L
M
C
S
V
K
L
F
M
D
D
F
S
T
E
E
A
I
L
N
G
V
R
N
G
F
Y
T
K
S
S
K
P
L
R
K
H
C
Q
S
Q
V
S
R
F
A
Q
W
E
L
F
K
K
I
R
P
E
Y
E
G
I
S
Y
L
E
F
K
S
R
Q
K
K
R
S
Q
L
I
I
A
I
K
N
I
L
S
P
D
G
W
I
P
T
R
T
D
D
V
K
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:
Publications:
Title
Authors
Journal
Details
PubMed Id DOI
Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2.
Gerber A, Grosjean H, Melcher T, Keller W
EMBO J
[details]
9707437
-
A-to-I and C-to-U editing within transfer RNAs.
Su AA, Randau L
Biochemistry (Mosc)
[details]
22022967
-
Determinants of tRNA editing and modification: Avoiding conundrums, affecting function.
Paris Z, Fleming IM, Alfonzo JD
Semin Cell Dev Biol
[details]
22024020
-
Links: