ID Card:
Full name:
tRNA (guanine(37)-N1)-methyltransferase
Synonym:
KIAA1393, TRMT5
GI:
145275187
COG:
COG2520
UniProt:
Q32P41
Alpha Fold Predicted Structure:
AF-Q32P41-F1
Enzyme type:
methyltransferase
Position of modification - modification:
t :37 - m1G
t :37 - o2yW
Protein sequence:
MVLWILWRPFGFSGRFLKLESHSITESKSLIPVAWTSLTQMLLEAPGIFLLGQRKRFSTMPETETHERETELFSPPSDVRGMTKLDRTAFKKTVNIPVLKVRKEIVSKLMRSLKRAALQRPGIRRVIEDPEDKESRLIMLDPYKIFTHDSFEKAELSVLEQLNVSPQISKYNLELTYEHFKSEEILRAVLPEGQDVTSGFSRIGHIAHLNLRDHQLSFKHLIGQVMIDKNPGITSAVNKINNIDNMYRNFQMEVLSGEQNMMTKVRENNYTYEFDFSKVYWNPRLSTEHSRITELLKPGDVLFDVFAGVGPFAIPVAKKNCTVFANDLNPESHKWLLYNCKLNKVDQKVKVFNLDGKDFLQGPVKEELMQLLGLSKERKPSVHVVMNLPAKAIEFLSAFKWLLDGQPCSSEFLPIVHCYSFSKDANPAEDVRQRAGAVLGISLEACSSVHLVRNVAPNKEMLCITFQIPASVLYKNQTRNPENHEDPPLKRQRTAEAFSDEKTQIVSNT
Comments:
The activity was studied using yeast tRNAPhe and E. coli tRNALeu. It was shown to catalyze also I->m1I reaction in position 37 in E.coli tRNAAsp hence it is predicted to participate in the formation of m1I in position 37 of human tRNAAla.
Reaction
Substrate
SubstrateType
Position
(Anti)Codon
Modified (Anti)Codon
Amino Acid Change
Transcript Name
Transcript Region
Cellular Localization
References
G:m1G
RNA
tRNA
37
#AA
#AA
tRNAPhe #AA
anticodon-loop
Mitochondrion
15248782   
G:m1G
RNA
tRNA
37
.AA
.AA
tRNALeu .AA
anticodon-loop
Mitochondrion
15248782   
Alpha Fold Predicted Structure:
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Protein sequence:
M
V
L
W
I
L
W
R
P
F
G
F
S
G
R
F
L
K
L
E
S
H
S
I
T
E
S
K
S
L
I
P
V
A
W
T
S
L
T
Q
M
L
L
E
A
P
G
I
F
L
L
G
Q
R
K
R
F
S
T
M
P
E
T
E
T
H
E
R
E
T
E
L
F
S
P
P
S
D
V
R
G
M
T
K
L
D
R
T
A
F
K
K
T
V
N
I
P
V
L
K
V
R
K
E
I
V
S
K
L
M
R
S
L
K
R
A
A
L
Q
R
P
G
I
R
R
V
I
E
D
P
E
D
K
E
S
R
L
I
M
L
D
P
Y
K
I
F
T
H
D
S
F
E
K
A
E
L
S
V
L
E
Q
L
N
V
S
P
Q
I
S
K
Y
N
L
E
L
T
Y
E
H
F
K
S
E
E
I
L
R
A
V
L
P
E
G
Q
D
V
T
S
G
F
S
R
I
G
H
I
A
H
L
N
L
R
D
H
Q
L
S
F
K
H
L
I
G
Q
V
M
I
D
K
N
P
G
I
T
S
A
V
N
K
I
N
N
I
D
N
M
Y
R
N
F
Q
M
E
V
L
S
G
E
Q
N
M
M
T
K
V
R
E
N
N
Y
T
Y
E
F
D
F
S
K
V
Y
W
N
P
R
L
S
T
E
H
S
R
I
T
E
L
L
K
P
G
D
V
L
F
D
V
F
A
G
V
G
P
F
A
I
P
V
A
K
K
N
C
T
V
F
A
N
D
L
N
P
E
S
H
K
W
L
L
Y
N
C
K
L
N
K
V
D
Q
K
V
K
V
F
N
L
D
G
K
D
F
L
Q
G
P
V
K
E
E
L
M
Q
L
L
G
L
S
K
E
R
K
P
S
V
H
V
V
M
N
L
P
A
K
A
I
E
F
L
S
A
F
K
W
L
L
D
G
Q
P
C
S
S
E
F
L
P
I
V
H
C
Y
S
F
S
K
D
A
N
P
A
E
D
V
R
Q
R
A
G
A
V
L
G
I
S
L
E
A
C
S
S
V
H
L
V
R
N
V
A
P
N
K
E
M
L
C
I
T
F
Q
I
P
A
S
V
L
Y
K
N
Q
T
R
N
P
E
N
H
E
D
P
P
L
K
R
Q
R
T
A
E
A
F
S
D
E
K
T
Q
I
V
S
N
T
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
Isolation and characterization of the human tRNA-(N1G37) methyltransferase (TRM5) and comparison to the Escherichia coli TrmD protein.
Brule H, Elliott M, Redlak M, Zehner ZE, Holmes WM
Biochemistry
[details]
15248782
-
Conservation of structure and mechanism by Trm5 enzymes.
Christian T, Gamper H, Hou YM...
RNA
[details]
23887145
-
Links: