ubiquitin carboxyl-terminal hydrolase MINDY-1 isoform X2 [Mus musculus]
Protein Classification
MINDY family deubiquitinase( domain architecture ID 10516731)
MINDY family deubiquitinase similar to Homo sapiens ubiquitin carboxyl-terminal hydrolase MINDY-1 that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| MINDY_DUB | pfam04424 | MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as ... |
1-64 | 1.20e-39 | ||
MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as the MINDY family (MIU-containing novel DUB). Ubiquitin (Ub) is released one molecule at a time from the distal end of proteins with Lys48-linked polyubiquitin chains. Long polyubiquitin chains are preferred. The catalytic Cys and His residues have been identified by site-directed mutagenesis, as has the Gln that participates in formation of the oxyanion hole during catalysis. Despite the structural similarity to papain-like cysteine peptidases, a residue corresponding to the Asn that orientates the imidazolium ring of the catalytic His has not been identified. Members of the MINDY family of DUBs contain an MIU (motif interacting with Ub) motif, which is a helical motif that binds mono-Ub. : Pssm-ID: 461303 Cd Length: 110 Bit Score: 133.44 E-value: 1.20e-39
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| Name | Accession | Description | Interval | E-value | ||
| MINDY_DUB | pfam04424 | MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as ... |
1-64 | 1.20e-39 | ||
MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as the MINDY family (MIU-containing novel DUB). Ubiquitin (Ub) is released one molecule at a time from the distal end of proteins with Lys48-linked polyubiquitin chains. Long polyubiquitin chains are preferred. The catalytic Cys and His residues have been identified by site-directed mutagenesis, as has the Gln that participates in formation of the oxyanion hole during catalysis. Despite the structural similarity to papain-like cysteine peptidases, a residue corresponding to the Asn that orientates the imidazolium ring of the catalytic His has not been identified. Members of the MINDY family of DUBs contain an MIU (motif interacting with Ub) motif, which is a helical motif that binds mono-Ub. Pssm-ID: 461303 Cd Length: 110 Bit Score: 133.44 E-value: 1.20e-39
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| Name | Accession | Description | Interval | E-value | ||
| MINDY_DUB | pfam04424 | MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as ... |
1-64 | 1.20e-39 | ||
MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as the MINDY family (MIU-containing novel DUB). Ubiquitin (Ub) is released one molecule at a time from the distal end of proteins with Lys48-linked polyubiquitin chains. Long polyubiquitin chains are preferred. The catalytic Cys and His residues have been identified by site-directed mutagenesis, as has the Gln that participates in formation of the oxyanion hole during catalysis. Despite the structural similarity to papain-like cysteine peptidases, a residue corresponding to the Asn that orientates the imidazolium ring of the catalytic His has not been identified. Members of the MINDY family of DUBs contain an MIU (motif interacting with Ub) motif, which is a helical motif that binds mono-Ub. Pssm-ID: 461303 Cd Length: 110 Bit Score: 133.44 E-value: 1.20e-39
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