uncharacterized protein Dmel_CG4968 [Drosophila melanogaster]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| OTUB1 | cd22763 | Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, ... |
32-260 | 2.84e-142 | ||||
Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, or ubiquitin-specific-processing protease OTUB1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates. It is also capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. In addition, OTUB1 inhibits the DNA damage response independently of its catalytic activity by blocking ubiquitin transfer onto protein substrates via sequestration of E2 ubiquitin-conjugating enzymes. It also regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. OTUB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS. : Pssm-ID: 438600 Cd Length: 224 Bit Score: 398.10 E-value: 2.84e-142
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| Name | Accession | Description | Interval | E-value | |||||
| OTUB1 | cd22763 | Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, ... |
32-260 | 2.84e-142 | |||||
Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, or ubiquitin-specific-processing protease OTUB1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates. It is also capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. In addition, OTUB1 inhibits the DNA damage response independently of its catalytic activity by blocking ubiquitin transfer onto protein substrates via sequestration of E2 ubiquitin-conjugating enzymes. It also regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. OTUB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS. Pssm-ID: 438600 Cd Length: 224 Bit Score: 398.10 E-value: 2.84e-142
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| Peptidase_C65 | pfam10275 | Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ... |
25-261 | 9.30e-110 | |||||
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly specific ubiquitin iso-peptidase that removes ubiquitin from proteins. The modification of cellular proteins by ubiquitin (Ub) is an important event that underlies protein stability and function in eukaryote being a dynamic and reversible process. Otubain carries several key conserved domains: (i) the OTU (ovarian tumour domain) in which there is an active cysteine protease triad (ii) a nuclear localization signal, (iii) a Ub interaction motif (UIM)-like motif phi-xx-A-xxxs-xx-Ac (where phi indicates an aromatic amino acid, x indicates any amino acid and Ac indicates an acidic amino acid), (iv) a Ub-associated (UBA)-like domain and (v) the LxxLL motif. Pssm-ID: 431191 [Multi-domain] Cd Length: 240 Bit Score: 316.53 E-value: 9.30e-110
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| COG5539 | COG5539 | Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ... |
46-260 | 4.99e-05 | |||||
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227826 [Multi-domain] Cd Length: 306 Bit Score: 43.71 E-value: 4.99e-05
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| Name | Accession | Description | Interval | E-value | |||||
| OTUB1 | cd22763 | Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, ... |
32-260 | 2.84e-142 | |||||
Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, or ubiquitin-specific-processing protease OTUB1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates. It is also capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. In addition, OTUB1 inhibits the DNA damage response independently of its catalytic activity by blocking ubiquitin transfer onto protein substrates via sequestration of E2 ubiquitin-conjugating enzymes. It also regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. OTUB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS. Pssm-ID: 438600 Cd Length: 224 Bit Score: 398.10 E-value: 2.84e-142
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| Peptidase_C65 | pfam10275 | Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ... |
25-261 | 9.30e-110 | |||||
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly specific ubiquitin iso-peptidase that removes ubiquitin from proteins. The modification of cellular proteins by ubiquitin (Ub) is an important event that underlies protein stability and function in eukaryote being a dynamic and reversible process. Otubain carries several key conserved domains: (i) the OTU (ovarian tumour domain) in which there is an active cysteine protease triad (ii) a nuclear localization signal, (iii) a Ub interaction motif (UIM)-like motif phi-xx-A-xxxs-xx-Ac (where phi indicates an aromatic amino acid, x indicates any amino acid and Ac indicates an acidic amino acid), (iv) a Ub-associated (UBA)-like domain and (v) the LxxLL motif. Pssm-ID: 431191 [Multi-domain] Cd Length: 240 Bit Score: 316.53 E-value: 9.30e-110
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| Otubain_C65 | cd22749 | Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ... |
32-260 | 7.19e-89 | |||||
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 (also called ubiquitin thioesterase OTUB1 or OTU domain-containing ubiquitin aldehyde-binding protein 1), otubain-2 (also called ubiquitin thioesterase OTUB2 or OTU domain-containing ubiquitin aldehyde-binding protein 2), and similar proteins. They function as deubiquitylases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12). OTUB1 can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates, while OTUB2 mediates the deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. The otubain subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Members of this subfamily are classified as family C65 cysteine proteases by MEROPS. Pssm-ID: 438586 [Multi-domain] Cd Length: 232 Bit Score: 263.04 E-value: 7.19e-89
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| AtOTU1-like | cd22765 | Arabidopsis thaliana Deubiquitinating enzyme OTU1 and similar plant proteins; This group ... |
31-260 | 2.34e-77 | |||||
Arabidopsis thaliana Deubiquitinating enzyme OTU1 and similar plant proteins; This group contains plant otibain-like proteins including Oryza sativa Japonica group otubain-like deubiquitinase and Arabidopsis thaliana deubiquitinating enzyme OTU1 (AtOTU1), also called OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1 or OTU domain-containing protein 1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that mediates the deubiquitination of protein substrates and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. AtOTU1 shows a preference for Met-1 and 'Lys-48' over 'Lys-63'-linked ubiquitin tetramers as substrates. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS. Pssm-ID: 438602 Cd Length: 247 Bit Score: 234.56 E-value: 2.34e-77
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| OTUB2 | cd22764 | Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, ... |
32-260 | 4.36e-77 | |||||
Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, deubiquitinating enzyme OTUB2, OTU domain-containing ubiquitin aldehyde-binding protein 2, or ubiquitin-specific-processing protease OTUB2. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that mediates the deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. OTUB2 plays a role in DNA double-strand break (DSB) response (DDR); it enhances RNF8-mediated ubiquitination in an early phase of the DDR and promotes faster DSB repair but suppresses homologous recombination. It also functions as a cancer stemness and metastasis-promoting factor that deubiquitinates and activates the transcriptional regulators YAP/TAZ, which play important roles in development, physiology, and tumorigenesis and are negatively controlled by the Hippo pathway. OTUB2 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS. Pssm-ID: 438601 Cd Length: 222 Bit Score: 232.66 E-value: 4.36e-77
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| COG5539 | COG5539 | Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ... |
46-260 | 4.99e-05 | |||||
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227826 [Multi-domain] Cd Length: 306 Bit Score: 43.71 E-value: 4.99e-05
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| OTU | cd22744 | OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ... |
66-259 | 2.07e-04 | |||||
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. Pssm-ID: 438581 [Multi-domain] Cd Length: 128 Bit Score: 40.11 E-value: 2.07e-04
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| OTU_plant_OTU7-like | cd22771 | OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ... |
66-81 | 2.79e-03 | |||||
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar proteins; Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. DUBs 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. OTU7 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Pssm-ID: 438608 [Multi-domain] Cd Length: 124 Bit Score: 36.76 E-value: 2.79e-03
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| OTU_CeDUB-like | cd22755 | OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ... |
64-82 | 2.87e-03 | |||||
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains, and similar proteins; This subfamily is composed of mostly uncharacterized proteins containing an OTU domain, similar to Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains. OTU domain-containing proteins 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Pssm-ID: 438592 [Multi-domain] Cd Length: 132 Bit Score: 36.85 E-value: 2.87e-03
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| OTU_RNAP_L_virus | cd21880 | OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ... |
66-104 | 7.66e-03 | |||||
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase L is also called protein L, large structural protein, replicase, transcriptase, or ubiquitin thioesterase. It displays RNA-directed RNA polymerase (EC 2.7.7.48), deubiquitinase (DUB)/ubiquitin thiolesterase (EC 3.4.19.12), and deISGylating activities. It is a viral homolog of ovarian tumor protease (vOTU) that has been implicated in the downregulation of type I interferon immune response by removing post-translational modifying proteins ubiquitin (Ub) and the Ub-like interferon-simulated gene 15 (ISG15) from host cellular proteins. The attachment of Ub and ISG15 to cellular proteins mediates important innate antiviral responses, and their removal inhibits these antiviral pathways. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Pssm-ID: 438580 Cd Length: 148 Bit Score: 36.04 E-value: 7.66e-03
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| Blast search parameters | ||||
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