OTU (ovarian tumor) domain-containing protein may function as a deubiquitinase (DUBs)/ubiquitin thiolesterase that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, or may be inactive
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
85-345
0e+00
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation.
The actual alignment was detected with superfamily member cd22798:
Pssm-ID: 459237 Cd Length: 261 Bit Score: 506.26 E-value: 0e+00
OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called ...
85-345
0e+00
OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called FAM105A, is an OTU-class pseudo-deubiquitinase with a disrupted catalytic triad and undetectable cleavage activity for any diubiquitin linkage. It may play a role in endoplasmic reticulum (ER)-organelle communication. Otulinl belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).
Pssm-ID: 438619 Cd Length: 261 Bit Score: 506.26 E-value: 0e+00
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in ...
78-345
4.83e-138
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in vertebrates. The key residues as found in SwissProt:Q96BN8 are Asp126, Cys129, His339 and Asn341.
Pssm-ID: 465075 Cd Length: 265 Bit Score: 392.45 E-value: 4.83e-138
OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called ...
85-345
0e+00
OTU (ovarian tumor) domain of inactive ubiquitin thioesterase Otulinl; Otulinl, also called FAM105A, is an OTU-class pseudo-deubiquitinase with a disrupted catalytic triad and undetectable cleavage activity for any diubiquitin linkage. It may play a role in endoplasmic reticulum (ER)-organelle communication. Otulinl belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).
Pssm-ID: 438619 Cd Length: 261 Bit Score: 506.26 E-value: 0e+00
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in ...
78-345
4.83e-138
Peptidase family C101; This is a family of cysteine-peptidases that is conserved in vertebrates. The key residues as found in SwissProt:Q96BN8 are Asp126, Cys129, His339 and Asn341.
Pssm-ID: 465075 Cd Length: 265 Bit Score: 392.45 E-value: 4.83e-138
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin family; Otulin family includes ...
88-345
8.75e-124
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin family; Otulin family includes otulin and otulinl. Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulinl, also called FAM105A, is an OTU-class pseudo-deubiquitinase with a disrupted catalytic triad and undetectable cleavage activity for any diubiquitin linkage. It may play a role in endoplasmic reticulum (ER)-organelle communication. Otulin and otulinl belong to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).
Pssm-ID: 438611 Cd Length: 258 Bit Score: 356.15 E-value: 8.75e-124
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also ...
78-345
1.87e-96
OTU (ovarian tumor) domain of ubiquitin thioesterase otulin and similar proteins; Otulin, also called FAM105B, deubiquitinating enzyme otulin, OTU domain-containing deubiquitinase with linear linkage specificity, or ubiquitin thioesterase Gumby, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. It acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. Otulin belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in some cases an aspartate, as the catalytic dyad (or triad).
Pssm-ID: 438620 Cd Length: 266 Bit Score: 287.03 E-value: 1.87e-96
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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