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Conserved domains on  [gi|568966691|ref|XP_006513291|]
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ubiquitin carboxyl-terminal hydrolase 15 isoform X6 [Mus musculus]

Protein Classification

DUSP and Ubiquitin_3 domain-containing protein( domain architecture ID 10653632)

DUSP and Ubiquitin_3 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
135-222 2.79e-48

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


:

Pssm-ID: 405518  Cd Length: 88  Bit Score: 155.02  E-value: 2.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691  135 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFNIPDEKEARLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 214
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 568966691  215 NEDGTWPR 222
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-121 5.85e-31

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 110.53  E-value: 5.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691    24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 103
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 568966691   104 YTLMEGqePIARKVVEQG 121
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
 
Name Accession Description Interval E-value
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
135-222 2.79e-48

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


Pssm-ID: 405518  Cd Length: 88  Bit Score: 155.02  E-value: 2.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691  135 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFNIPDEKEARLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 214
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 568966691  215 NEDGTWPR 222
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-121 5.85e-31

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 110.53  E-value: 5.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691    24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 103
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 568966691   104 YTLMEGqePIARKVVEQG 121
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
27-119 2.78e-23

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: 90.50  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691   27 GDTWYLVDSRWFKQWKKYVGfdswdkyqmgDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYtl 106
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWY-- 68
                          90
                  ....*....|...
gi 568966691  107 mEGQEPIARKVVE 119
Cdd:pfam06337  69 -GGGPEIKRNVVN 80
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-180 1.64e-03

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 39.87  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560   29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560   98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                        170
                 ....*....|....*.
gi 568966691 165 IRKIFNIPDEkEARLW 180
Cdd:COG5560  176 VMNAFVDPSD-DFRLW 190
 
Name Accession Description Interval E-value
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
135-222 2.79e-48

Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin carboxyl-terminal hydrolases and in gametogenetin-binding protein.


Pssm-ID: 405518  Cd Length: 88  Bit Score: 155.02  E-value: 2.79e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691  135 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFNIPDEKEARLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 214
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 568966691  215 NEDGTWPR 222
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
24-121 5.85e-31

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 110.53  E-value: 5.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691    24 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 103
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 568966691   104 YTLMEGqePIARKVVEQG 121
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
27-119 2.78e-23

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: 90.50  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691   27 GDTWYLVDSRWFKQWKKYVGfdswdkyqmgDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYtl 106
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWY-- 68
                          90
                  ....*....|...
gi 568966691  107 mEGQEPIARKVVE 119
Cdd:pfam06337  69 -GGGPEIKRNVVN 80
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
12-180 1.64e-03

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 39.87  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691  12 QRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLIDELDYIL 91
Cdd:COG5560   29 QEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966691  92 LPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADTIDTIEKE 164
Cdd:COG5560   98 ISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGTLRDLSER 175
                        170
                 ....*....|....*.
gi 568966691 165 IRKIFNIPDEkEARLW 180
Cdd:COG5560  176 VMNAFVDPSD-DFRLW 190
 
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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