ID Card:
Full name:
tRNA(His) guanylyltransferase
GI:
45270428
Orf:
YGR024c
COG:
COG4021
UniProt:
P53215
Structures:
|
|
Alpha Fold Predicted Structure:
AF-P53215-F1
Enzyme type:
guanylyltransferase
Position of modification - modification:
t :0 - G
Protein sequence:
MANSKFGYVRQFETHDVILPQCYIVVRIDGKKFHEFSKFYEFAKPNDENALKLMNACAKNLVLKYKNDIILAFGESDEYSFILKSSTTLFNRRKDKLATLFGSFFTSNYVALWAKFFPEKPLNIKHLPYFDSRCVAYPNLQTIKDYLSWRYVDTHINNLYNTTFWQLIIKCGLTPQESEKKLCGTFSNEKQEILFSECGINYNNEPEMFKKGSLVTRKGEILHINVIAQIDELFEGY
Comments:
tRNAHis guanylyltransferase, adds a guanosine residue to the 5' end of tRNAHis after transcription and RNase P cleavage. Enzymes from Thg1 family exhibit 3'-to-5' polymerase activity. A crystal structure of Mycobacterium tuberculosis and H. sapiens homologues have been solved (3OTB, 3OTD, 3OTE and 3OTC, respectively).
Reaction
Substrate
SubstrateType
Position
(Anti)Codon
Modified (Anti)Codon
Amino Acid Change
Transcript Name
Transcript Region
Cellular Localization
References
pN:pG(pN)
RNA
tRNA
0
GUG
GUG
tRNAHis GUG
acceptor-stem
Cytoplasm
21059936   
Alpha Fold Predicted Structure:
Clear Selection and Reset Camera
Clear Selection
Reset Camera
Protein sequence:
M
A
N
S
K
F
G
Y
V
R
Q
F
E
T
H
D
V
I
L
P
Q
C
Y
I
V
V
R
I
D
G
K
K
F
H
E
F
S
K
F
Y
E
F
A
K
P
N
D
E
N
A
L
K
L
M
N
A
C
A
K
N
L
V
L
K
Y
K
N
D
I
I
L
A
F
G
E
S
D
E
Y
S
F
I
L
K
S
S
T
T
L
F
N
R
R
K
D
K
L
A
T
L
F
G
S
F
F
T
S
N
Y
V
A
L
W
A
K
F
F
P
E
K
P
L
N
I
K
H
L
P
Y
F
D
S
R
C
V
A
Y
P
N
L
Q
T
I
K
D
Y
L
S
W
R
Y
V
D
T
H
I
N
N
L
Y
N
T
T
F
W
Q
L
I
I
K
C
G
L
T
P
Q
E
S
E
K
K
L
C
G
T
F
S
N
E
K
Q
E
I
L
F
S
E
C
G
I
N
Y
N
N
E
P
E
M
F
K
K
G
S
L
V
T
R
K
G
E
I
L
H
I
N
V
I
A
Q
I
D
E
L
F
E
G
Y
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
tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis.
Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM
Genes Dev
[details]
14633974
-
tRNAHis guanylyltransferase (THG1), a unique 3′-5′ nucleotidyl transferase, shares unexpected structural homology with canonical 5′-3′ DNA polymerases.
Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublié S
Proc Natl Acad Sci U S A
[details]
21059936
-
Doing it in reverse: 3'-to-5' polymerization by the Thg1 superfamily.
Jackman JE, Gott JM, Gray MW
RNA
[details]
22456265
-
Links: