Uniprot ID | P15808 |
Uniprot Name | THY1_DICDI |
Taxonomy ID | 44689 |
Sequence |
M
G
L
D
I
Q
T
E
I
D
K
I
V
I
E
K
V
K
P
E
V
E
Y
Y
D
V
M
G
G
S
H
R
W
E
V
K
V
H
D
H
G
K
V
A
L
V
D
T
M
P
R
L
A
P
V
G
Q
T
A
D
F
S
I
C
Q
A
A
R
V
S
Y
G
A
G
T
K
K
V
T
E
D
K
G
L
I
R
Y
L
Y
R
H
Q
H
T
S
P
F
E
M
V
E
F
K
F
H
C
V
M
P
V
F
I
A
R
Q
W
I
R
H
R
T
A
N
V
N
E
Y
S
A
R
Y
S
V
L
P
D
K
F
Y
H
P
S
I
E
E
V
R
K
Q
S
T
S
N
R
Q
G
G
E
E
A
L
E
P
K
T
A
Q
E
F
L
D
Y
L
D
K
V
E
E
N
Y
K
T
Y
N
E
L
L
E
K
G
L
S
R
E
L
G
R
I
G
L
P
V
S
I
Y
T
E
W
Y
W
K
I
D
L
H
N
L
F
H
F
L
R
L
R
M
D
S
H
S
Q
K
E
I
R
D
Y
A
N
T
I
F
A
L
I
R
P
I
V
P
V
A
C
E
A
F
I
D
Y
A
F
E
S
L
K
L
T
R
L
E
I
E
A
I
R
T
G
S
P
L
N
T
T
N
K
R
E
I
E
E
F
E
E
K
K
K
L
L
F
P
N
T
Q
A
|
Cofactor |
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9WYT0}; Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers. {ECO:0000250|UniProtKB:Q9WYT0}; |
Active site |
ACT_SITE 224 224 Involved in ionization of N3 of dUMP, leading to its activation. {ECO:0000250|UniProtKB:Q9WYT0}. |
Pfam |
PF02511
|
InterPro |
IPR003669
IPR036098
|