Summary: Ubiquitin-specific peptidase-like, SUMO isopeptidase
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Ubiquitin-specific peptidase-like, SUMO isopeptidase Provide feedback
Peptidase_C98 is a small family of SUMO - small ubiquitin-related modifier - isopeptidases found in eukaryotes. Reversible attachment of SUMO is an essential protein modification in all eukaryotic cells, The family neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase, and the invariant residues required for SUMO binding and cleavage, in UniProtKB:Q5W0Q7 are Cys-236, His-456 and Asp-472, all of which are fully conserved in the family. Member proteins are low-abundance proteins that colocalise with coilin in Cajal bodies. Peptidase_C98 depletion does not affect global sumoylation, but causes striking coilin mis-localisation and impairs cell proliferation, functions that are not dependent on the catalytic activity. Thus, Peptidase_C98 represents a third type of SUMO protease, with essential functions in Cajal body biology.
Schulz S, Chachami G, Kozaczkiewicz L, Winter U, Stankovic-Valentin N, Haas P, Hofmann K, Urlaub H, Ovaa H, Wittbrodt J, Meulmeester E, Melchior F;, EMBO Rep. 2012; [Epub ahead of print]: Ubiquitin-specific protease-like 1 (USPL1) is a SUMO isopeptidase with essential, non-catalytic functions. PUBMED:22878415 EPMC:22878415
Internal database links
|Similarity to PfamA using HHSearch:||UCH|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR028890
Peptidase C98 is a small family of SUMO - small ubiquitin-related modifier - isopeptidases found in eukaryotes. Reversible attachment of SUMO is an essential protein modification in all eukaryotic cells. SUMO-specific isopeptidase USPL1 neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase. The invariant residues required for SUMO binding and cleavage, in SWISSPROT are Cys-236, His-456 and Asp-472, all of which are fully conserved in the family. Member proteins are low-abundance proteins that colocalise with coilin in Cajal bodies. Peptidase C98 depletion does not affect global sumoylation, but causes striking coilin mis-localisation and impairs cell proliferation, functions that are not dependent on the catalytic activity. Thus, Peptidase C98 represents a third type of SUMO protease, with essential functions in Cajal body biology [PUBMED:22878415].
This entry represents the catalytic domain.
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|Molecular function||SUMO-specific isopeptidase activity (GO:0070140)|
|SUMO binding (GO:0032183)|
- the number of sequences which exhibit this architecture
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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 65 members:Acetyltransf_2 Amidase_5 Amidase_6 BtrH_N CHAP DUF1175 DUF1287 DUF1460 DUF2026 DUF2272 DUF3335 DUF553 EDR1 Guanylate_cyc_2 Herpes_teg_N LRAT Mac-1 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 Tox-PLDMTX Transglut_core Transglut_core2 Transglut_core3 Transglut_prok UCH UCH_1 Viral_protease
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Curation and family details
|Author:||Rawlings N, Coggill P|
|Number in seed:||24|
|Number in full:||81|
|Average length of the domain:||239.40 aa|
|Average identity of full alignment:||54 %|
|Average coverage of the sequence by the domain:||26.61 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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