General rule information
[?]
Accession |
PRU01221 |
Dates |
27-SEP-2018 (Created) 22-NOV-2019 (Last updated, Version 2) |
Function |
The cysteine and histidine rich TRIAD domain architecture is highly conserved and found only in eukaryotes. The three fingers that define the TRIAD supradomain always appear in the same order RING1-IBR-RING2. All characterized proteins containing the TRIAD supradomain have been found to possess E3 ligase activity. |
Propagated annotation
[?]
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3> or <FTGroup:4> or <FTGroup:5> or <FTGroup:6> or <FTGroup:7>
GO:0046872; Molecular function: metal ion binding.
end case
case <Feature:PS51873:178=C>
GO:0000209; Biological process: protein polyubiquitination.
GO:0061630; Molecular function: ubiquitin protein ligase activity.
GO:0032436; Biological process: positive regulation of proteasomal ubiquitin-dependent protein catabolic process.
GO:0031624; Molecular function: ubiquitin conjugating enzyme binding.
GO:0000151; Cellular component: ubiquitin ligase complex.
end case
case <FTGroup:1> or <FTGroup:2> or <FTGroup:3> or <FTGroup:4> or <FTGroup:5> or <FTGroup:6> or <FTGroup:7>
end case
case <Feature:PS51873:178=C>
end case
From: PS51873 |
Key
|
|
From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
ZN_FING
|
|
5
|
|
56
|
|
RING-type #
|
|
|
|
|
|
|
ZN_FING
|
|
75
|
|
138
|
|
IBR-type
|
|
|
|
|
|
|
ZN_FING
|
|
165
|
|
194
|
|
RING-type #; atypical
|
|
|
|
|
|
|
REGION
|
|
from
|
|
to
|
|
TRIAD supradomain
|
|
|
|
|
|
|
ACT_SITE
|
|
178
|
|
178
|
|
|
|
|
|
C
|
|
|
METAL
|
|
5
|
|
5
|
|
Zinc #1
|
|
|
|
C
|
|
1
|
METAL
|
|
8
|
|
8
|
|
Zinc #1
|
|
|
|
C
|
|
1
|
METAL
|
|
23
|
|
23
|
|
Zinc #2
|
|
|
|
C
|
|
2
|
METAL
|
|
25
|
|
25
|
|
Zinc #2; via pros nitrogen
|
|
|
|
H
|
|
2
|
METAL
|
|
28
|
|
28
|
|
Zinc #1
|
|
|
|
C
|
|
1
|
METAL
|
|
31
|
|
31
|
|
Zinc #1
|
|
|
|
C
|
|
1
|
METAL
|
|
51
|
|
51
|
|
Zinc #2
|
|
|
|
C
|
|
2
|
METAL
|
|
56
|
|
56
|
|
Zinc #2
|
|
|
|
C
|
|
2
|
METAL
|
|
95
|
|
95
|
|
Zinc #3
|
|
|
|
C
|
|
3
|
METAL
|
|
100
|
|
100
|
|
Zinc #3
|
|
|
|
C
|
|
3
|
METAL
|
|
117
|
|
117
|
|
Zinc #3
|
|
|
|
C
|
|
3
|
METAL
|
|
120
|
|
120
|
|
Zinc #3
|
|
|
|
C
|
|
3
|
METAL
|
|
125
|
|
125
|
|
Zinc #4
|
|
|
|
C
|
|
4
|
METAL
|
|
128
|
|
128
|
|
Zinc #4
|
|
|
|
C
|
|
4
|
METAL
|
|
133
|
|
133
|
|
Zinc #4; via tele nitrogen
|
|
|
|
H
|
|
4
|
METAL
|
|
138
|
|
138
|
|
Zinc #4
|
|
|
|
C
|
|
4
|
METAL
|
|
165
|
|
165
|
|
Zinc #5
|
|
|
|
C
|
|
5
|
METAL
|
|
168
|
|
168
|
|
Zinc #5
|
|
|
|
C
|
|
5
|
METAL
|
|
183
|
|
183
|
|
Zinc #5
|
|
|
|
C
|
|
5
|
METAL
|
|
186
|
|
186
|
|
Zinc #5
|
|
|
|
C
|
|
5
|
case <Feature:PS51873:202-209=C-x*-H>
METAL
|
|
191
|
|
191
|
|
Zinc #6
|
|
|
|
C
|
|
6
|
METAL
|
|
194
|
|
194
|
|
Zinc #6
|
|
|
|
C
|
|
6
|
METAL
|
|
202
|
|
202
|
|
Zinc #6
|
|
|
|
C
|
|
6
|
METAL
|
|
209
|
|
209
|
|
Zinc #6; via tele nitrogen
|
|
|
|
H
|
|
6
|
else
METAL
|
|
191
|
|
191
|
|
Zinc #6
|
|
|
|
C
|
|
7
|
METAL
|
|
194
|
|
194
|
|
Zinc #6
|
|
|
|
C
|
|
7
|
METAL
|
|
202
|
|
202
|
|
Zinc #6; via tele nitrogen
|
|
|
|
H
|
|
7
|
METAL
|
|
209
|
|
209
|
|
Zinc #6
|
|
|
|
C
|
|
7
|
end case
Additional information
[?]
Size range |
190-285 amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Example |
Q924T7 (RNF31_MOUSE) |
Scope |
Eukaryota
Viruses; Mimivirus |
Comments |
None |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see
prosite_license.html.
UniProtKB rule member sequences
[?]