CATH Superfamily 2.60.40.790
The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 89: Co-chaperone p23
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 1 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Hsp90 protein binding GO:0051879
Interacting selectively and non-covalently with Hsp90 proteins, any of a group of heat shock proteins around 90kDa in size.
|
6 | C0H473 (/IPI) C0H473 (/IPI) C0H473 (/IPI) C0H473 (/IPI) C0H473 (/IPI) C0H473 (/IPI) |
There are 2 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Negative regulation of ATPase activity GO:0032780
Any process that stops or reduces the rate of ATP hydrolysis by an ATPase.
|
6 | C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) |
|
Chaperone-mediated protein complex assembly GO:0051131
The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
|
6 | C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) C0H473 (/IDA) |
There are 0 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
