NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907142964|ref|XP_036018398|]
View 

ubiquitin carboxyl-terminal hydrolase MINDY-3 isoform X8 [Mus musculus]

Protein Classification

MINDY deubiquitinase family protein( domain architecture ID 141790)

MINDY (motif interacting with Ub-containing novel deubiquitinating enzyme) deubiquitinase family protein is a DUF4205 domain-containing protein; similar to Homo sapiens ubiquitin carboxyl-terminal hydrolase MINDY-3 that can remove 'Lys-48'-linked conjugated ubiquitin from proteins

EC:  3.4.19.12
Gene Ontology:  GO:1990380|GO:0004843|GO:0016787
PubMed:  27292798

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-3_4_CD super family cl20500
Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ...
1-142 4.47e-40

Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitination. This entry includes MINDY-3/4. They belong to the MINDY (motif interacting with Ub-containing novel DUB) family (peptidase family C121), whose members are deubiquitinating enzymes releasing Lys48-linked ubiquitin. This is a conserved domain found in deubiquitinating enzymes, MINDY-3 and MINDY-4.


The actual alignment was detected with superfamily member pfam13898:

Pssm-ID: 464029  Cd Length: 345  Bit Score: 141.21  E-value: 4.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142964   1 MWGNKFGVLLFLYSVLLTKGIENIKNSIEDANEPLIDpvyGHG--SQSLINLLLTGHAVSNVWDG----DRECSGMQLL- 73
Cdd:pfam13898 149 EEEGGPGVILFLYSAILSRGIERVREDMDSPTSHLIG---AHGycTQELVNLLLTGRASPNVFNGvvelDDGDGYATPLk 225
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142964  74 GIHEQAAVGFLTLMEALRYCKVGSYLKSPKFPIWIVGSETHLTVFFAKDMALVApeapSEQARRVFQTY 142
Cdd:pfam13898 226 GILSRSDIGLLSLFEHYQLCQVGSRLKTPKLPIWVVCSEGHYSVLFSTNRELLS----DWKAERRFDLY 290
 
Name Accession Description Interval E-value
MINDY-3_4_CD pfam13898
Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ...
1-142 4.47e-40

Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitination. This entry includes MINDY-3/4. They belong to the MINDY (motif interacting with Ub-containing novel DUB) family (peptidase family C121), whose members are deubiquitinating enzymes releasing Lys48-linked ubiquitin. This is a conserved domain found in deubiquitinating enzymes, MINDY-3 and MINDY-4.


Pssm-ID: 464029  Cd Length: 345  Bit Score: 141.21  E-value: 4.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142964   1 MWGNKFGVLLFLYSVLLTKGIENIKNSIEDANEPLIDpvyGHG--SQSLINLLLTGHAVSNVWDG----DRECSGMQLL- 73
Cdd:pfam13898 149 EEEGGPGVILFLYSAILSRGIERVREDMDSPTSHLIG---AHGycTQELVNLLLTGRASPNVFNGvvelDDGDGYATPLk 225
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142964  74 GIHEQAAVGFLTLMEALRYCKVGSYLKSPKFPIWIVGSETHLTVFFAKDMALVApeapSEQARRVFQTY 142
Cdd:pfam13898 226 GILSRSDIGLLSLFEHYQLCQVGSRLKTPKLPIWVVCSEGHYSVLFSTNRELLS----DWKAERRFDLY 290
 
Name Accession Description Interval E-value
MINDY-3_4_CD pfam13898
Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ...
1-142 4.47e-40

Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitination. This entry includes MINDY-3/4. They belong to the MINDY (motif interacting with Ub-containing novel DUB) family (peptidase family C121), whose members are deubiquitinating enzymes releasing Lys48-linked ubiquitin. This is a conserved domain found in deubiquitinating enzymes, MINDY-3 and MINDY-4.


Pssm-ID: 464029  Cd Length: 345  Bit Score: 141.21  E-value: 4.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142964   1 MWGNKFGVLLFLYSVLLTKGIENIKNSIEDANEPLIDpvyGHG--SQSLINLLLTGHAVSNVWDG----DRECSGMQLL- 73
Cdd:pfam13898 149 EEEGGPGVILFLYSAILSRGIERVREDMDSPTSHLIG---AHGycTQELVNLLLTGRASPNVFNGvvelDDGDGYATPLk 225
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142964  74 GIHEQAAVGFLTLMEALRYCKVGSYLKSPKFPIWIVGSETHLTVFFAKDMALVApeapSEQARRVFQTY 142
Cdd:pfam13898 226 GILSRSDIGLLSLFEHYQLCQVGSRLKTPKLPIWVVCSEGHYSVLFSTNRELLS----DWKAERRFDLY 290
 
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