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Conserved domains on  [gi|1189398108|ref|NP_001338091|]
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ubiquitin carboxyl-terminal hydrolase 15 isoform 7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUSP super family cl12116
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 24-74 4.27e-12

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


The actual alignment was detected with superfamily member smart00695:

Pssm-ID: 416436  Cd Length: 88  Bit Score: 55.83  E-value: 4.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189398108  24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKGH 74
Cdd:smart00695  2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSH 43
 
Name Accession Description Interval E-value
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-74 4.27e-12

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 55.83  E-value: 4.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189398108  24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKGH 74
Cdd:smart00695  2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSH 43
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 27-75 2.76e-10

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 51.21  E-value: 2.76e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 1189398108 27 GDTWYLVDSRWFKQWKKYVgfdswdkyqmGDQNVYPGPIDNSGLLKGHY 75
Cdd:pfam06337  1 GDKVYLISSKWLNKWKSYV----------KEPNNEPGPIDNSDLLDDES 39
 
Name Accession Description Interval E-value
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-74 4.27e-12

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 55.83  E-value: 4.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189398108  24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKGH 74
Cdd:smart00695  2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSH 43
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
 27-75 2.76e-10

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 51.21  E-value: 2.76e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 1189398108 27 GDTWYLVDSRWFKQWKKYVgfdswdkyqmGDQNVYPGPIDNSGLLKGHY 75
Cdd:pfam06337  1 GDKVYLISSKWLNKWKSYV----------KEPNNEPGPIDNSDLLDDES 39
 
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.
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