NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530365048|ref|XP_005245382|]
View 

ubiquitin carboxyl-terminal hydrolase MINDY-1 isoform X7 [Homo sapiens]

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

EC:  3.4.19.12
Gene Ontology:  GO:0004843|GO:1990380

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2-120 3.27e-56

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: 177.73  E-value: 3.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365048    2 NILFLQWKVKLPPQKEVITSDELMAHLGNCLLSIKPqekseglqLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYT 81
Cdd:pfam04424   1 NVLLLRGKIELLPDRETISLEDLLELLADYLLDNNP--------LNYEQNISDALSLLPKLQTGLDVNPRFTGVTSFEDT 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530365048   82 PECSVFDLLGIPLYHGWLVDPqQSPEAVRAVGKLSYNQL 120
Cdd:pfam04424  73 PELALFDLLNIPLVHGWLVDP-QDPEAYEAVGALSYNEL 110
 
Name Accession Description Interval E-value
MINDY_DUB pfam04424
MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as ...
 2-120 3.27e-56

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: 177.73  E-value: 3.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365048    2 NILFLQWKVKLPPQKEVITSDELMAHLGNCLLSIKPqekseglqLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYT 81
Cdd:pfam04424   1 NVLLLRGKIELLPDRETISLEDLLELLADYLLDNNP--------LNYEQNISDALSLLPKLQTGLDVNPRFTGVTSFEDT 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530365048   82 PECSVFDLLGIPLYHGWLVDPqQSPEAVRAVGKLSYNQL 120
Cdd:pfam04424  73 PELALFDLLNIPLVHGWLVDP-QDPEAYEAVGALSYNEL 110
 
Name Accession Description Interval E-value
MINDY_DUB pfam04424
MINDY deubiquitinase; This entry represents a group of deubiquitinating (DUB) enzymes known as ...
 2-120 3.27e-56

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: 177.73  E-value: 3.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365048    2 NILFLQWKVKLPPQKEVITSDELMAHLGNCLLSIKPqekseglqLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYT 81
Cdd:pfam04424   1 NVLLLRGKIELLPDRETISLEDLLELLADYLLDNNP--------LNYEQNISDALSLLPKLQTGLDVNPRFTGVTSFEDT 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530365048   82 PECSVFDLLGIPLYHGWLVDPqQSPEAVRAVGKLSYNQL 120
Cdd:pfam04424  73 PELALFDLLNIPLVHGWLVDP-QDPEAYEAVGALSYNEL 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH