ID Card:
Full name:
glutamine:preQ0-tRNA amidinotransferase or Archaeosine Synthase
Synonym:
Archaeosine synthase, Glutamine:preQ0-tRNA amidinotransferase
GI:
3024970
COG:
COG1549
UniProt:
Q58428
Alpha Fold Predicted Structure:
AF-Q58428-F1
Enzyme type:
amidinotransferase
Position of modification - modification:
t :15 - G+
Protein sequence:
MLEPIAYDIGRLCKEEDKELTPKLIDIDVIGLSQEKIFYGIMTPFRCPNSKSIYELRKSYVKADGIKMPFDTFRELTSIFKKSFIGTVKYKGNVFKYQILNFGKHVDLIELEDADLYIIADGRRLIERKELQIIPKIREKISPNSAIYSPAVFPWEIPLLAYIGVDYFDDSLAKLYASMGYKFTKNRAVKVDSFSFEELYNNNKKVYEEILEEVRIAIKNGFLRNVVEETAVSHPYLWANYRRYEPDLRNIPLSKENKIIVTTNINIPEVKKYLERLDNYEPYSNIIVLLPCSSKKPYSISQSHQKFIKAIKSAKVVVEEVILTSPYGLVPRALERLVNYDIPVTGEWSFEEIELINNCLKNFLKKVKEKFDDYIVIAHLPEHYLEILELDDIVITSKGNPTSEEALKNLTDTLKKYKELTKSKDINKKGQRIHNIQQLAEFQFGINFIPNEIFINHKGQIFTKINNKNQQIASINPKNGLLILTLSGGELLWNSGGKDINYIEVNYEIKKGSLFPPGFVDCNENISYNDEVVLIKDDTFLGIGRALMSGFEMKKAKHGALVNIRNVKS
Comments:
7-deazaguanosine derivative archaeosine (G(+) ) at tRNA position 15 is a molecular signature of Archaea. Noteworthy, the biosynthesis of this modified ribonucleotide is complex, involving the initial production of 7-cyano-7-deazaguanine (preQ(0) ). ArcTGTs are an enzyme family responsible for the biosynthesis of pre Q(0). The corresponding gene has been cloned also for Methano caldococcus jannaschii (Philips et al. 2010 ). It was shown to convert pre Q(0) to G(+)-tRNA using several nitrogen sources and to do so in an ATP dependent process.
Reaction
Substrate
SubstrateType
Position
(Anti)Codon
Modified (Anti)Codon
Amino Acid Change
Transcript Name
Transcript Region
Cellular Localization
References
preQ0:G+
RNA
tRNA
15
preQ0 - tRNA
D-loop
cytosol
20129918
Alpha Fold Predicted Structure:
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Protein sequence:
M
L
E
P
I
A
Y
D
I
G
R
L
C
K
E
E
D
K
E
L
T
P
K
L
I
D
I
D
V
I
G
L
S
Q
E
K
I
F
Y
G
I
M
T
P
F
R
C
P
N
S
K
S
I
Y
E
L
R
K
S
Y
V
K
A
D
G
I
K
M
P
F
D
T
F
R
E
L
T
S
I
F
K
K
S
F
I
G
T
V
K
Y
K
G
N
V
F
K
Y
Q
I
L
N
F
G
K
H
V
D
L
I
E
L
E
D
A
D
L
Y
I
I
A
D
G
R
R
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I
E
R
K
E
L
Q
I
I
P
K
I
R
E
K
I
S
P
N
S
A
I
Y
S
P
A
V
F
P
W
E
I
P
L
L
A
Y
I
G
V
D
Y
F
D
D
S
L
A
K
L
Y
A
S
M
G
Y
K
F
T
K
N
R
A
V
K
V
D
S
F
S
F
E
E
L
Y
N
N
N
K
K
V
Y
E
E
I
L
E
E
V
R
I
A
I
K
N
G
F
L
R
N
V
V
E
E
T
A
V
S
H
P
Y
L
W
A
N
Y
R
R
Y
E
P
D
L
R
N
I
P
L
S
K
E
N
K
I
I
V
T
T
N
I
N
I
P
E
V
K
K
Y
L
E
R
L
D
N
Y
E
P
Y
S
N
I
I
V
L
L
P
C
S
S
K
K
P
Y
S
I
S
Q
S
H
Q
K
F
I
K
A
I
K
S
A
K
V
V
V
E
E
V
I
L
T
S
P
Y
G
L
V
P
R
A
L
E
R
L
V
N
Y
D
I
P
V
T
G
E
W
S
F
E
E
I
E
L
I
N
N
C
L
K
N
F
L
K
K
V
K
E
K
F
D
D
Y
I
V
I
A
H
L
P
E
H
Y
L
E
I
L
E
L
D
D
I
V
I
T
S
K
G
N
P
T
S
E
E
A
L
K
N
L
T
D
T
L
K
K
Y
K
E
L
T
K
S
K
D
I
N
K
K
G
Q
R
I
H
N
I
Q
Q
L
A
E
F
Q
F
G
I
N
F
I
P
N
E
I
F
I
N
H
K
G
Q
I
F
T
K
I
N
N
K
N
Q
Q
I
A
S
I
N
P
K
N
G
L
L
I
L
T
L
S
G
G
E
L
L
W
N
S
G
G
K
D
I
N
Y
I
E
V
N
Y
E
I
K
K
G
S
L
F
P
P
G
F
V
D
C
N
E
N
I
S
Y
N
D
E
V
V
L
I
K
D
D
T
F
L
G
I
G
R
A
L
M
S
G
F
E
M
K
K
A
K
H
G
A
L
V
N
I
R
N
V
K
S
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
Discovery and characterization of an amidinotransferase involved in the modification of archaeal tRNA.
Phillips G, Chikwana VM, Maxwell A, El-Yacoubi B, Swairjo MA, Iwata-Reuyl D, de Crecy-Lagard V...
J Biol Chem
[details]
20129918
-