|
|
1)
|
chain |
A |
residue |
50 |
type |
|
sequence |
Y
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
50 |
type |
|
sequence |
Y
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
51 |
type |
|
sequence |
G
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
52 |
type |
|
sequence |
F
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
79 |
type |
|
sequence |
G
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
80 |
type |
|
sequence |
T
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
81 |
type |
|
sequence |
G
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
115 |
type |
|
sequence |
Q
|
description |
binding site for residue SAU A 301
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
78 |
type |
|
sequence |
S
|
description |
binding site for residue MLI A 302
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
79 |
type |
|
sequence |
G
|
description |
binding site for residue MLI A 302
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
80 |
type |
|
sequence |
T
|
description |
binding site for residue MLI A 302
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
81 |
type |
|
sequence |
G
|
description |
binding site for residue MLI A 302
|
source |
: AC2
|
|
13)
|
chain |
A |
residue |
82 |
type |
|
sequence |
X
|
description |
binding site for residue MLI A 302
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
83 |
type |
|
sequence |
T
|
description |
binding site for residue MLI A 302
|
source |
: AC2
|
|
15)
|
chain |
A |
residue |
115 |
type |
|
sequence |
Q
|
description |
binding site for residue MLI A 302
|
source |
: AC2
|
|
16)
|
chain |
A |
residue |
180-188 |
type |
prosite |
sequence |
VLDEADEML
|
description |
DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL
|
source |
prosite : PS00039
|
|
17)
|
chain |
A |
residue |
76 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
A |
residue |
118 |
type |
MOD_RES |
sequence |
X
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
174 |
type |
MOD_RES |
sequence |
X
|
description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
158 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
A |
residue |
193 |
type |
MOD_RES |
sequence |
X
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P60843
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
22)
|
chain |
A |
residue |
238 |
type |
MOD_RES |
sequence |
X
|
description |
N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P60843
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
23)
|
chain |
A |
residue |
146 |
type |
CROSSLNK |
sequence |
X
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
24)
|
chain |
A |
residue |
225 |
type |
CROSSLNK |
sequence |
X
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
25)
|
chain |
A |
residue |
238 |
type |
CROSSLNK |
sequence |
X
|
description |
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
|
source |
Swiss-Prot : SWS_FT_FI7
|
|