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Conserved domains on  [gi|353523825|ref|NP_001238806|]
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ubiquitin carboxyl-terminal hydrolase 4 isoform c [Homo sapiens]

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 ...
139-226 3.58e-38

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: 130.36  E-value: 3.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825  139 ELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQ 218
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 353523825  219 NEDGTWPR 226
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 1.34e-32

Domain in ubiquitin-specific proteases;


:

Pssm-ID: 197831  Cd Length: 88  Bit Score: 115.92  E-value: 1.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 353523825   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
 
Name Accession Description Interval E-value
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
139-226 3.58e-38

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: 130.36  E-value: 3.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825  139 ELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQ 218
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 353523825  219 NEDGTWPR 226
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 1.34e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 115.92  E-value: 1.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 353523825   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
31-123 2.79e-27

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: 101.68  E-value: 2.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825   31 GAQWYLIDSRWFKQWKKYVGfdswdmynvgEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGc 110
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWYG- 69
                          90
                  ....*....|...
gi 353523825  111 veGQQPIVRKVVE 123
Cdd:pfam06337  70 --GGPEIKRNVVN 80
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-184 9.81e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 40.64  E-value: 9.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353523825 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLW 184
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-DFRLW 190
 
Name Accession Description Interval E-value
Ubiquitin_3 pfam14836
Ubiquitin-like domain; This ubiquitin-like domain is found in several ubiquitin ...
139-226 3.58e-38

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: 130.36  E-value: 3.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825  139 ELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQ 218
Cdd:pfam14836   1 SFKLCLPGNLQSPITKKFSKTDTIDFIEKELRKLFSIPKEKETRLWNRYSSNTRELLTDPDITVQEAGLYHGQVLLIEEK 80

                  ....*...
gi 353523825  219 NEDGTWPR 226
Cdd:pfam14836  81 NEDGNWPR 88
DUSP smart00695
Domain in ubiquitin-specific proteases;
27-125 1.34e-32

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 115.92  E-value: 1.34e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825    27 TLQRGAQWYLIDSRWFKQWKKYVGfdswdmynvGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLN 106
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVE---------GKDGKDPGPIDNSGILCSHGGPRLKEHLVEGEDYVLIPEELWNKLVR 71
                           90
                   ....*....|....*....
gi 353523825   107 WYGCVEGqqPIVRKVVEHG 125
Cdd:smart00695  72 WYGGGPG--PIPRKVVCQG 88
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
31-123 2.79e-27

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: 101.68  E-value: 2.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825   31 GAQWYLIDSRWFKQWKKYVGfdswdmynvgEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGc 110
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVK----------EPNNEPGPIDNSDLLDDESNGQLKPNLQEGVDYVIVPEEVWEFLVEWYG- 69
                          90
                  ....*....|...
gi 353523825  111 veGQQPIVRKVVE 123
Cdd:pfam06337  70 --GGPEIKRNVVN 80
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
35-184 9.81e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 40.64  E-value: 9.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 353523825  35 YLIDSRWFKqwkKYVGFDSWDmynvGEhnlFPGPIdNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGcVEGq 114
Cdd:COG5560   48 VIFAYAWYE---GMFDRASCD----GG---SPGPI-VQGPIVDFEPESLKKSLREGIDYSIISGAVWQLLVRWYG-LAG- 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 353523825 115 qPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCH--------FSKADTIATIEKEMRKLFNIPAErETRLW 184
Cdd:COG5560  115 -LITPRITVLLPSESAPEVESYPVVFKLHWLFSINGSLINLghdpvphsASSHGTLRDLSERVMNAFVDPSD-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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