|
|
1)
|
chain |
B |
residue |
39 |
type |
catalytic |
sequence |
E
|
description |
41
|
source |
MCSA : MCSA1
|
|
2)
|
chain |
B |
residue |
76 |
type |
catalytic |
sequence |
Y
|
description |
41
|
source |
MCSA : MCSA1
|
|
3)
|
chain |
B |
residue |
78 |
type |
catalytic |
sequence |
E
|
description |
41
|
source |
MCSA : MCSA1
|
|
4)
|
chain |
B |
residue |
134 |
type |
catalytic |
sequence |
H
|
description |
41
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
B |
residue |
168 |
type |
catalytic |
sequence |
D
|
description |
41
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
B |
residue |
212 |
type |
catalytic |
sequence |
D
|
description |
41
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
B |
residue |
252 |
type |
catalytic |
sequence |
H
|
description |
41
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
A |
residue |
53-63 |
type |
prosite |
sequence |
YVGDEAQSKRG
|
description |
ACTINS_1 Actins signature 1. YVGDEAQs.KRG
|
source |
prosite : PS00406
|
|
9)
|
chain |
A |
residue |
356-364 |
type |
prosite |
sequence |
WITKQEYDE
|
description |
ACTINS_2 Actins signature 2. WITKqEYDE
|
source |
prosite : PS00432
|
|
10)
|
chain |
B |
residue |
167-174 |
type |
prosite |
sequence |
GDFNADCS
|
description |
DNASE_I_2 Deoxyribonuclease I signature 2. GDFNAdCS
|
source |
prosite : PS00918
|
|
11)
|
chain |
B |
residue |
130-150 |
type |
prosite |
sequence |
IVALHSAPSDAVAEINSLYDV
|
description |
DNASE_I_1 Deoxyribonuclease I signature 1. IVALHSAPsdavaEINsLyDV
|
source |
prosite : PS00919
|
|
12)
|
chain |
A |
residue |
104-116 |
type |
prosite |
sequence |
LLTEAPLNPKANR
|
description |
ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
|
source |
prosite : PS01132
|
|
13)
|
chain |
C |
residue |
33 |
type |
MOD_RES |
sequence |
R
|
description |
Asymmetric dimethylarginine => ECO:0000250|UniProtKB:Q8K1I7
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
14)
|
chain |
B |
residue |
134 |
type |
ACT_SITE |
sequence |
H
|
description |
ACT_SITE => ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:4976790
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
15)
|
chain |
A |
residue |
47 |
type |
ACT_SITE |
sequence |
M
|
description |
ACT_SITE => ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:4976790
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
16)
|
chain |
B |
residue |
13 |
type |
SITE |
sequence |
E
|
description |
Involved in actin-binding => ECO:0000269|PubMed:2395459
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
17)
|
chain |
B |
residue |
67 |
type |
SITE |
sequence |
V
|
description |
Involved in actin-binding => ECO:0000269|PubMed:2395459
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
18)
|
chain |
B |
residue |
65 |
type |
SITE |
sequence |
Y
|
description |
Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
19)
|
chain |
B |
residue |
18 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1748997, ECO:0000269|PubMed:3560229
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
20)
|
chain |
A |
residue |
177 |
type |
MOD_RES |
sequence |
R
|
description |
ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096
|
source |
Swiss-Prot : SWS_FT_FI6
|
|