ID Card:
Full name:
tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]
GI:
2833204
Orf:
YLR405W, L8084.2
COG:
COG0042
UniProt:
Q06063
Alpha Fold Predicted Structure:
AF-Q06063-F1
Enzyme type:
dihydrouridine synthase
Position of modification - modification:
t :20a - D
t :20b - D
Protein sequence:
MHTMHIPSGDVLIPKPKLITEETDPLHIIKTRQKTHGRPVTIAGPMVRYSKLPFRQLCREYNVDIVYSPMILAREYVRNEHARISDLSTNNEDTPLIVQVGVNNVADLLKFVEMVAPYCDGIGINCGCPIKEQIREGIGCALIYNSDLLCSMVHAVKDKYGDKLRIETKIRIHEALDETVELCRKLCDAGVDWITIHGRTRRTRSSQPANLDAIKYIIENISDKNVPVIANGDCFKLSDLERITKYTGAHGVMAVRGLLSNPALFAGYTTCPWGCIEKFCYWALEFGGLPFQLAQHHLYCMLENMELKKSLLKKMMNLKNYISLIDWFNKTFEFKRYGEDGFGMGVEIPYKANSCVQRSASVVERQE
Comments:
Dihydrouridine synthases are a conserved enzyme family that is encoded by the orthologous COG0042 gene family (Kasprzak et al. 2012 ). Dihydrouridine (D) is a post-trascriptionally modified pyrimidine nucleoside. D results from the reduction of C5,6-double bondof a uridine residue in RNA transcripts (Kasprzak et al. 2012 ) that brings to the addition of two hydrogen atoms C6 and C5. With the absence of the double bond, dihydrouridine is believed to decrease region stability, promoting dynamic motion and accommodating loop structure.Indeed, Dihydrouridine (D) appears as important in the maintenance of tRNA stability
(Alexandrov et al. 2006 ). It appears acting as a quality control marker, with its absence provoking rapid tRNA decays. D is generated post-transcriptionally by Dus enzymes and it is found in different positions of tRNAs. Dus4 specifically modifies position 20a, 20b, and 20 in the D-loop of many tRNA substrates.
Reaction
Substrate
SubstrateType
Position
(Anti)Codon
Modified (Anti)Codon
Amino Acid Change
Transcript Name
Transcript Region
Cellular Localization
References
U:D
tRNA
20a
GUU
GUU
tRNAAsn GUU
D-loop
cytosol
U:D
tRNA
20a
CUC
CUC
tRNAGlu CUC
D-loop
cytosol
U:D
tRNA
20a
{CC
{CC
tRNAGly {CC
D-loop
cytosol
U:D
tRNA
20a
GUG
GUG
tRNAHis GUG
D-loop
cytosol
U:D
tRNA
20a
IAU
IAU
tRNAIle IAU
D-loop
cytosol
U:D
tRNA
20a
UAU
UAU
tRNAIle UAU
D-loop
cytosol
U:D
tRNA
20a
UAG
UAG
tRNALeu UAG
D-loop
cytosol
U:D
tRNA
20a
CGA
CGA
tRNASer CGA
D-loop
cytosol
U:D
tRNA
20a
UGA
UGA
tRNASer UGA
D-loop
cytosol
U:D
tRNA
20a
IGA
IGA
tRNASer IGA
D-loop
cytosol
U:D
tRNA
20a
GUA
GUA
tRNATyr GUA
D-loop
cytosol
U:D
tRNA
20a
UAC
UAC
tRNAVal UAC
D-loop
cytosol
U:D
tRNA
20a
CAC
CAC
tRNAVal CAC
D-loop
cytosol
U:D
tRNA
20a
IAC
IAC
tRNAVal IAC
D-loop
cytosol
U:D
tRNA
20b
UAG
UAG
tRNALeu UAG
D-loop
cytosol
U:D
tRNA
20b
CAA
CAA
tRNALeu CAA
D-loop
cytosol
U:D
tRNA
20b
UAA
UAA
tRNALeu UAA
D-loop
cytosol
U:D
tRNA
20b
GUA
GUA
tRNATyr GUA
D-loop
cytosol
Alpha Fold Predicted Structure:
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Protein sequence:
M
H
T
M
H
I
P
S
G
D
V
L
I
P
K
P
K
L
I
T
E
E
T
D
P
L
H
I
I
K
T
R
Q
K
T
H
G
R
P
V
T
I
A
G
P
M
V
R
Y
S
K
L
P
F
R
Q
L
C
R
E
Y
N
V
D
I
V
Y
S
P
M
I
L
A
R
E
Y
V
R
N
E
H
A
R
I
S
D
L
S
T
N
N
E
D
T
P
L
I
V
Q
V
G
V
N
N
V
A
D
L
L
K
F
V
E
M
V
A
P
Y
C
D
G
I
G
I
N
C
G
C
P
I
K
E
Q
I
R
E
G
I
G
C
A
L
I
Y
N
S
D
L
L
C
S
M
V
H
A
V
K
D
K
Y
G
D
K
L
R
I
E
T
K
I
R
I
H
E
A
L
D
E
T
V
E
L
C
R
K
L
C
D
A
G
V
D
W
I
T
I
H
G
R
T
R
R
T
R
S
S
Q
P
A
N
L
D
A
I
K
Y
I
I
E
N
I
S
D
K
N
V
P
V
I
A
N
G
D
C
F
K
L
S
D
L
E
R
I
T
K
Y
T
G
A
H
G
V
M
A
V
R
G
L
L
S
N
P
A
L
F
A
G
Y
T
T
C
P
W
G
C
I
E
K
F
C
Y
W
A
L
E
F
G
G
L
P
F
Q
L
A
Q
H
H
L
Y
C
M
L
E
N
M
E
L
K
K
S
L
L
K
K
M
M
N
L
K
N
Y
I
S
L
I
D
W
F
N
K
T
F
E
F
K
R
Y
G
E
D
G
F
G
M
G
V
E
I
P
Y
K
A
N
S
C
V
Q
R
S
A
S
V
V
E
R
Q
E
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
The specificities of four yeast dihydrouridine synthases for cytoplasmic tRNAs.
Xing F, Hiley SL, Hughes TR, Phizicky EM
J Biol Chem
[details]
14970222
-
A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA.
Xing F, Martzen MR, Phizicky EM
RNA
[details]
12003496
-
Molecular evolution of dihydrouridine synthases.
Kasprzak JM, Czerwoniec A, Bujnicki JM...
BMC Bioinformatics
[details]
22741570
-
Links: