Summary: Ubiquitin carboxyl-terminal hydrolase, family 1
Ubiquitin carboxyl-terminal hydrolase, family 1 Provide feedback
No Pfam abstract.
Internal database links
|SCOOP:||CBP4 ORF6C DUF2524|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001578
This group of cysteine peptidases belong to the MEROPS peptidase family C12 (ubiquitin C-terminal hydrolase family, clan CA). Families within the CA clan are loosely termed papain-like as protein fold of the peptidase unit resembles that of papain, the type example for clan CA. The type example is the human ubiquitin C-terminal hydrolase UCH-L1.
Ubiquitin is highly conserved, commonly found conjugated to proteins in eukaryotic cells, where it may act as a marker for rapid degradation, or it may have a chaperone function in protein assembly [PUBMED:7845226]. The ubiquitin is released by cleavage from the bound protein by a protease [PUBMED:7845226]. A number of deubiquitinising proteases are known: all are activated by thiol compounds [PUBMED:7845226, PUBMED:3015923], and inhibited by thiol-blocking agents and ubiquitin aldehyde [PUBMED:7845226, PUBMED:3031653], and as such have the properties of cysteine proteases [PUBMED:7845226].
The deubiquitinsing proteases can be split into 2 size ranges (20-30 kDa and 100-200 kDa, INTERPRO) [PUBMED:7845226]: this group are the 20-30 kDa peptides which includes the yeast yuh1. Yeast yuh1 protease is known to be active only against small ubiquitin conjugates, being inactive against conjugated beta-galactosidase [PUBMED:7845226]. A mammalian homologue, UCH (ubiquitin conjugate hydrolase), is one of the most abundant proteins in the brain [PUBMED:7845226]. Only one conserved cysteine can be identified, along with two conserved histidines. The spacing between the cysteine and the second histidine is thought to be more representative of the cysteine/histidine spacing of a cysteine protease catalytic dyad [PUBMED:7845226].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||intracellular (GO:0005622)|
|Molecular function||ubiquitin-specific protease activity (GO:0004843)|
|Biological process||ubiquitin-dependent protein catabolic process (GO:0006511)|
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This example describes an architecture with one
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EGFdomains, and finally a single
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This clan includes peptidases with the papain-like fold.
The clan contains the following 60 members:Acetyltransf_2 Amidase_5 Amidase_6 BtrH_N CHAP DUF1175 DUF1287 DUF1460 DUF2272 DUF3335 DUF553 EDR1 Guanylate_cyc_2 LRAT NLPC_P60 OTU Peptidase_C1 Peptidase_C10 Peptidase_C101 Peptidase_C12 Peptidase_C16 Peptidase_C1_2 Peptidase_C2 Peptidase_C21 Peptidase_C23 Peptidase_C27 Peptidase_C28 Peptidase_C31 Peptidase_C32 Peptidase_C33 Peptidase_C34 Peptidase_C36 Peptidase_C39 Peptidase_C39_2 Peptidase_C42 Peptidase_C47 Peptidase_C48 Peptidase_C5 Peptidase_C54 Peptidase_C58 Peptidase_C6 Peptidase_C65 Peptidase_C7 Peptidase_C70 Peptidase_C71 Peptidase_C78 Peptidase_C8 Peptidase_C9 Peptidase_C92 Peptidase_C93 Peptidase_C97 Peptidase_C98 Phytochelatin Rad4 Transglut_core Transglut_core2 Transglut_core3 UCH UCH_1 Viral_protease
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||406|
|Number in full:||2192|
|Average length of the domain:||194.10 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||64.78 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Peptidase_C12 domain has been found. There are 34 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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