|
|
1)
|
chain |
A |
residue |
156 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
157 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
158 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
182 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
213 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
214 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
301 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
302 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
303 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
305 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
306 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
336 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE ADP A 376
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
53-63 |
type |
prosite |
sequence |
YVGDEAQSKRG
|
description |
ACTINS_1 Actins signature 1. YVGDEAQs.KRG
|
source |
prosite : PS00406
|
|
14)
|
chain |
A |
residue |
356-364 |
type |
prosite |
sequence |
WITKQEYDE
|
description |
ACTINS_2 Actins signature 2. WITKqEYDE
|
source |
prosite : PS00432
|
|
15)
|
chain |
A |
residue |
104-116 |
type |
prosite |
sequence |
LLTEAPLNPKANR
|
description |
ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
|
source |
prosite : PS01132
|
|
16)
|
chain |
A |
residue |
1 |
type |
MOD_RES |
sequence |
D
|
description |
N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
44 |
type |
MOD_RES |
sequence |
M
|
description |
Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
47 |
type |
MOD_RES |
sequence |
M
|
description |
Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
61 |
type |
MOD_RES |
sequence |
K
|
description |
N6-malonyllysine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
A |
residue |
73 |
type |
MOD_RES |
sequence |
X
|
description |
Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
21)
|
chain |
A |
residue |
84 |
type |
MOD_RES |
sequence |
K
|
description |
N6-methyllysine => ECO:0000250|UniProtKB:P68133
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
22)
|
chain |
A |
residue |
177 |
type |
MOD_RES |
sequence |
R
|
description |
ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
|
source |
Swiss-Prot : SWS_FT_FI6
|
|