ID Card:
Full name:
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmFO
Synonym:
Mcap0476
GI:
123535705
COG:
COG1206
UniProt:
Q2SS13
Alpha Fold Predicted Structure:
AF-Q2SS13-F1
Enzyme type:
methyltransferase
Position of modification - modification:
l :1947(1939) - m5U
Protein sequence:
MNKKVKIIGAGLAGCEAAYFLANNDIQVELYEVKTLIKNEVQKTNNFAELVCSNTFRSQSLLNAAGILKAEMRRLNSLVIKIADSCKIDGDDALAVDREDFSKKLTDVIKNHPNITIIEQNVSYIDDENDLTLIATGPLTTNELKEDIQRLIGKQKLFFMDASAPIITKDSIDFNKVYYSGRHKQGKYICCPLNEQEFNKFVDDLVNAEQVQLKEFEKSIFFKGCQPIEQLAKTSKKLLLKGPMSPNNLLDQNNQQPYAVVQLRQDDAKDSLYNMVGFQTNLKWPEQKRVFQTIPGLEKAKIVRYGVMHKNYYINSPKILNFKLQVIRKKNVFFAGQITGVEGYIESASSGIWAAINILAFINNKKIKPLPNTTILGALTNYITNSKIYSLKPMKCNLGILEQENKYQSNDKFYSYNNSKNSLENYIEQLNKILRTNI
Comments:
M. capricolum possesses two homologs of TrmFO - folate-dependent tRNA MTase. Mcap0476, renamed to RlmFO, is the only one which is active and was found to methylate U in position 1939 (E. coli numbering) in LSU rRNA. This enzyme represents the first folate-dependent flavoprotein seen to modify rRNA.
Alpha Fold Predicted Structure:
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Protein sequence:
M
N
K
K
V
K
I
I
G
A
G
L
A
G
C
E
A
A
Y
F
L
A
N
N
D
I
Q
V
E
L
Y
E
V
K
T
L
I
K
N
E
V
Q
K
T
N
N
F
A
E
L
V
C
S
N
T
F
R
S
Q
S
L
L
N
A
A
G
I
L
K
A
E
M
R
R
L
N
S
L
V
I
K
I
A
D
S
C
K
I
D
G
D
D
A
L
A
V
D
R
E
D
F
S
K
K
L
T
D
V
I
K
N
H
P
N
I
T
I
I
E
Q
N
V
S
Y
I
D
D
E
N
D
L
T
L
I
A
T
G
P
L
T
T
N
E
L
K
E
D
I
Q
R
L
I
G
K
Q
K
L
F
F
M
D
A
S
A
P
I
I
T
K
D
S
I
D
F
N
K
V
Y
Y
S
G
R
H
K
Q
G
K
Y
I
C
C
P
L
N
E
Q
E
F
N
K
F
V
D
D
L
V
N
A
E
Q
V
Q
L
K
E
F
E
K
S
I
F
F
K
G
C
Q
P
I
E
Q
L
A
K
T
S
K
K
L
L
L
K
G
P
M
S
P
N
N
L
L
D
Q
N
N
Q
Q
P
Y
A
V
V
Q
L
R
Q
D
D
A
K
D
S
L
Y
N
M
V
G
F
Q
T
N
L
K
W
P
E
Q
K
R
V
F
Q
T
I
P
G
L
E
K
A
K
I
V
R
Y
G
V
M
H
K
N
Y
Y
I
N
S
P
K
I
L
N
F
K
L
Q
V
I
R
K
K
N
V
F
F
A
G
Q
I
T
G
V
E
G
Y
I
E
S
A
S
S
G
I
W
A
A
I
N
I
L
A
F
I
N
N
K
K
I
K
P
L
P
N
T
T
I
L
G
A
L
T
N
Y
I
T
N
S
K
I
Y
S
L
K
P
M
K
C
N
L
G
I
L
E
Q
E
N
K
Y
Q
S
N
D
K
F
Y
S
Y
N
N
S
K
N
S
L
E
N
Y
I
E
Q
L
N
K
I
L
R
T
N
I
50 100 150 200 250 300 350 400 Sequence G H T B S N
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
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