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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376366  144 NILFLQWKVKLPPQKEVITSDELLTHLGNCLLSIKPqekseglqLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYT 223
Cdd:pfam04424   1 NVLLLRGKIELLPDRETISLEDLLELLADYLLDNNP--------LNYEQNISDALSLLPKLQTGLDVNPRFTGVTSFEDT 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124376366  224 PECSIFDLLGIPLYHGWLVDPQSPEAVSAVGKLSYNQL 261
Cdd:pfam04424  73 PELALFDLLNIPLVHGWLVDPQDPEAYEAVGALSYNEL 110

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376366  144 NILFLQWKVKLPPQKEVITSDELLTHLGNCLLSIKPqekseglqLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYT 223
Cdd:pfam04424   1 NVLLLRGKIELLPDRETISLEDLLELLADYLLDNNP--------LNYEQNISDALSLLPKLQTGLDVNPRFTGVTSFEDT 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124376366  224 PECSIFDLLGIPLYHGWLVDPQSPEAVSAVGKLSYNQL 261
Cdd:pfam04424  73 PELALFDLLNIPLVHGWLVDPQDPEAYEAVGALSYNEL 110

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376366  144 NILFLQWKVKLPPQKEVITSDELLTHLGNCLLSIKPqekseglqLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYT 223
Cdd:pfam04424   1 NVLLLRGKIELLPDRETISLEDLLELLADYLLDNNP--------LNYEQNISDALSLLPKLQTGLDVNPRFTGVTSFEDT 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 124376366  224 PECSIFDLLGIPLYHGWLVDPQSPEAVSAVGKLSYNQL 261
Cdd:pfam04424  73 PELALFDLLNIPLVHGWLVDPQDPEAYEAVGALSYNEL 110