ID Card:
Full name:
rRNA methyltransferase, mitochondrial
Synonym:
Pet56
GI:
1346886
Orf:
YOR201C
COG:
COG0566
UniProt:
P25270
Alpha Fold Predicted Structure:
AF-P25270-F1
Enzyme type:
methyltransferase
Position of modification - modification:
l :2270(2251) - Gm
Protein sequence:
MTSLTNAVFKRYLAVTPSAHQALKTRIKKKSSSFDKFFPQQSNSRKKQWETLNEDKASWFKRKYAHVHAREQDRAADPYGKKKAHVEKLKEIKNQAKLNQKSHKSKFQNKDIALKLMNDNPIFEYVYGTNSVYAALLNPSRNCHSRLLYHGTIPSKFLQIVDELKVTTELVDKHRLNLLTNYGVHNNIALETKPLQPVEIAYLGDMDTSSAALSIHELGFNNENIPHELPYGTKTDAKKFPLGLYLDEITDPHNIGAIIRSAYFLGVDFIVMSRRNCSPLTPVVSKTSSGALELLPIFYVDKPLEFFTKSQEMGGWTFITSHLANATSEKYTVGKTISMHDLNGLCNELPVVLVVGNESQGVRTNLKMRSDFFVEIPFGGIEKGNRAPEPIVDSLNVSVATALLIDNILTCK
Comments:
Mrm1 methylates the universally conserved G2270 in the so-called A-loop (hairpin 92) of the peptidyltransferase center (domain V) of 21S mito rRNA, equivalent to conserved Gm2251 in E. coli 23S rRNA and catalyzed by E. coli RlmB. The purified recombinant Mrm1 enzyme works in vitro on transcripts of both mitochondrial 21S rRNA and E. coli 23S rRNA. AdoMet is the donor of methyl group. In cytoplasmic S. cerevisiae rRNA, the analogous conserved Gm position 2618 (2251 E.coli numbering) is catalyzed at by a C/D box RNP (Nop1), guided by snoR67.
Alpha Fold Predicted Structure:
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Protein sequence:
M
T
S
L
T
N
A
V
F
K
R
Y
L
A
V
T
P
S
A
H
Q
A
L
K
T
R
I
K
K
K
S
S
S
F
D
K
F
F
P
Q
Q
S
N
S
R
K
K
Q
W
E
T
L
N
E
D
K
A
S
W
F
K
R
K
Y
A
H
V
H
A
R
E
Q
D
R
A
A
D
P
Y
G
K
K
K
A
H
V
E
K
L
K
E
I
K
N
Q
A
K
L
N
Q
K
S
H
K
S
K
F
Q
N
K
D
I
A
L
K
L
M
N
D
N
P
I
F
E
Y
V
Y
G
T
N
S
V
Y
A
A
L
L
N
P
S
R
N
C
H
S
R
L
L
Y
H
G
T
I
P
S
K
F
L
Q
I
V
D
E
L
K
V
T
T
E
L
V
D
K
H
R
L
N
L
L
T
N
Y
G
V
H
N
N
I
A
L
E
T
K
P
L
Q
P
V
E
I
A
Y
L
G
D
M
D
T
S
S
A
A
L
S
I
H
E
L
G
F
N
N
E
N
I
P
H
E
L
P
Y
G
T
K
T
D
A
K
K
F
P
L
G
L
Y
L
D
E
I
T
D
P
H
N
I
G
A
I
I
R
S
A
Y
F
L
G
V
D
F
I
V
M
S
R
R
N
C
S
P
L
T
P
V
V
S
K
T
S
S
G
A
L
E
L
L
P
I
F
Y
V
D
K
P
L
E
F
F
T
K
S
Q
E
M
G
G
W
T
F
I
T
S
H
L
A
N
A
T
S
E
K
Y
T
V
G
K
T
I
S
M
H
D
L
N
G
L
C
N
E
L
P
V
V
L
V
V
G
N
E
S
Q
G
V
R
T
N
L
K
M
R
S
D
F
F
V
E
I
P
F
G
G
I
E
K
G
N
R
A
P
E
P
I
V
D
S
L
N
V
S
V
A
T
A
L
L
I
D
N
I
L
T
C
K
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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