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Conserved domains on  [gi|1243457515|ref|NP_001342468|]
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ubiquitin carboxyl-terminal hydrolase MINDY-3 isoform e [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

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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 ...
 30-103 7.58e-17

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: 77.27  E-value: 7.58e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243457515  30 TQELLGIHEQAAVGFLTLMEALRYCKVGSYLKSPKFPIWIVGSETHLTVFFAKDMALVApeapSEQARRVFQTY 103
Cdd:pfam13898 221 ATPLKGILSRSDIGLLSLFEHYQLCQVGSRLKTPKLPIWVVCSEGHYSVLFSTNRELLS----DWKAERRFDLY 290
 
Name Accession Description Interval E-value
MINDY-3_4_CD pfam13898
Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ...
 30-103 7.58e-17

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: 77.27  E-value: 7.58e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243457515  30 TQELLGIHEQAAVGFLTLMEALRYCKVGSYLKSPKFPIWIVGSETHLTVFFAKDMALVApeapSEQARRVFQTY 103
Cdd:pfam13898 221 ATPLKGILSRSDIGLLSLFEHYQLCQVGSRLKTPKLPIWVVCSEGHYSVLFSTNRELLS----DWKAERRFDLY 290
 
Name Accession Description Interval E-value
MINDY-3_4_CD pfam13898
Deubiquitinating enzyme MINDY-3/4, conserved domain; Deubiquitinating enzymes (DUBs) remove ...
 30-103 7.58e-17

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: 77.27  E-value: 7.58e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243457515  30 TQELLGIHEQAAVGFLTLMEALRYCKVGSYLKSPKFPIWIVGSETHLTVFFAKDMALVApeapSEQARRVFQTY 103
Cdd:pfam13898 221 ATPLKGILSRSDIGLLSLFEHYQLCQVGSRLKTPKLPIWVVCSEGHYSVLFSTNRELLS----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.
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