NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|357380852]
View 

Chain B, Ubiquitin Carboxyl-terminal Hydrolase 15

Protein Classification

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

DUSP and Ubiquitin_3 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
132-219 8.34e-50

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: 157.33  E-value: 8.34e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852  132 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETRLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 211
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 357380852  212 NEDGTWPR 219
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
21-118 4.27e-31

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 109.37  E-value: 4.27e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852    21 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 100
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 357380852   101 YTLMEGqePIARKVVEQG 118
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 ...
132-219 8.34e-50

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: 157.33  E-value: 8.34e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852  132 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETRLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 211
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 357380852  212 NEDGTWPR 219
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
21-118 4.27e-31

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 109.37  E-value: 4.27e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852    21 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 100
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 357380852   101 YTLMEGqePIARKVVEQG 118
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
24-116 3.38e-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: 88.96  E-value: 3.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852   24 GDTWYLVDSRWFKQWKKYVGfdswdkyqmgDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYtl 103
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWY-- 68
                          90
                  ....*....|...
gi 357380852  104 mEGQEPIARKVVE 116
Cdd:pfam06337  69 -GGGPEIKRNVVN 80
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
2-177 1.54e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 42.18  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852   2 AAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLI 81
Cdd:COG5560   22 ASLPLMMQEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852  82 DELDYILLPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADT 154
Cdd:COG5560   91 EGIDYSIISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGT 168
                        170       180
                 ....*....|....*....|...
gi 357380852 155 IDTIEKEIRKIFSIPDEkETRLW 177
Cdd:COG5560  169 LRDLSERVMNAFVDPSD-DFRLW 190
 
Name Accession Description Interval E-value
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
132-219 8.34e-50

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: 157.33  E-value: 8.34e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852  132 ELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETRLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQK 211
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 357380852  212 NEDGTWPR 219
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
21-118 4.27e-31

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 109.37  E-value: 4.27e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852    21 LRKGDTWYLVDSRWFKQWKKYVGfdswdkyqmGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSW 100
Cdd:smart00695   2 LEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVRW 72
                           90
                   ....*....|....*...
gi 357380852   101 YTLMEGqePIARKVVEQG 118
Cdd:smart00695  73 YGGGPG--PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
24-116 3.38e-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: 88.96  E-value: 3.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852   24 GDTWYLVDSRWFKQWKKYVGfdswdkyqmgDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYtl 103
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWY-- 68
                          90
                  ....*....|...
gi 357380852  104 mEGQEPIARKVVE 116
Cdd:pfam06337  69 -GGGPEIKRNVVN 80
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
2-177 1.54e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 42.18  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852   2 AAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKqwkKYVGFDSWDkyqmGDqnvYPGPIdNSGLLKDGDAQSLKEHLI 81
Cdd:COG5560   22 ASLPLMMQEELIDEKPAESSKQCEYAVIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357380852  82 DELDYILLPTEGWNKLVSWYTLMEGQEPiaRKVV----EQGMFVKHCKVEVYLTELKLCENGNMN---NVVTRRFSKADT 154
Cdd:COG5560   91 EGIDYSIISGAVWQLLVRWYGLAGLITP--RITVllpsESAPEVESYPVVFKLHWLFSINGSLINlghDPVPHSASSHGT 168
                        170       180
                 ....*....|....*....|...
gi 357380852 155 IDTIEKEIRKIFSIPDEkETRLW 177
Cdd:COG5560  169 LRDLSERVMNAFVDPSD-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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH