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Conserved domains on  [gi|13386070|ref|NP_080856|]
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ubiquitin thioesterase OTUB2 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTUB2 cd22764
Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, ...
 8-229 4.43e-145

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: 403.68  E-value: 4.43e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070   8 LISEKCDILSILRDHPENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKSREILKFKERVLQTPNDLLA 87
Cdd:cd22764   1 LISEKCDISSLLPEHPENPIYQRKLKDLSKRYASIRKTRGDGNCFYRALAFAYLESLLGNSREIQKFKETVLQSKNELLA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  88 AGFEEHKFRNFFNAFYSVVELVEKDSSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHE 167
Cdd:cd22764  81 AGFEEHRFRNLFNTFVSVVELVEADGSGSSLLKAFNDQTTSDSIVQYLRLLTSAFLQNRADFFQHFVEEGMNIKDFCTQE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386070 168 VEPMAMECDHVQITALSQALNIALQVEYVDEMDTALNHHVFPEAAIPSVYLLYKTSHYNILY 229
Cdd:cd22764 161 VEPMAMECDHIQITALSQALGIPLQVEYVDEMDTALNHHIFPEGAEPSVYLLYKTSHYNILY 222
 
Name Accession Description Interval E-value
OTUB2 cd22764
Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, ...
 8-229 4.43e-145

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: 403.68  E-value: 4.43e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070   8 LISEKCDILSILRDHPENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKSREILKFKERVLQTPNDLLA 87
Cdd:cd22764   1 LISEKCDISSLLPEHPENPIYQRKLKDLSKRYASIRKTRGDGNCFYRALAFAYLESLLGNSREIQKFKETVLQSKNELLA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  88 AGFEEHKFRNFFNAFYSVVELVEKDSSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHE 167
Cdd:cd22764  81 AGFEEHRFRNLFNTFVSVVELVEADGSGSSLLKAFNDQTTSDSIVQYLRLLTSAFLQNRADFFQHFVEEGMNIKDFCTQE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386070 168 VEPMAMECDHVQITALSQALNIALQVEYVDEMDTALNHHVFPEAAIPSVYLLYKTSHYNILY 229
Cdd:cd22764 161 VEPMAMECDHIQITALSQALGIPLQVEYVDEMDTALNHHIFPEGAEPSVYLLYKTSHYNILY 222
Peptidase_C65 pfam10275
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ...
 1-229 8.05e-103

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: 297.65  E-value: 8.05e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070     1 MSETSFNLISEKCDILSILRDHP-ENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKSREILKFKERVL 79
Cdd:pfam10275   1 EEEAQGPLVSEKGPLSALEKEYAkADPIYLQKIQDLSEKYSGIRRTRGDGNCFYRAFGFSYLELLLESKDEIDRFKARVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070    80 QTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKD--SSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEE 157
Cdd:pfam10275  81 SLKEALVALGFDEDTFEDFCDAFLELLKKVEDGvsTSESELLQAFNDQETSDYIVYFLRLLTSAYLKTHADEYEPFIDGG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386070   158 MDIKDFCTHEVEPMAMECDHVQITALSQALNIALQVEYVD--EMDTALNHHVFP-----EAAIPSVYLLYKTSHYNILY 229
Cdd:pfam10275 161 GTVEEFCQQEVEPMNKEADHLQIIALAEALGVPVRVEYLDrsAEGNTVNHHDFPgeddtEEQAPFITLLYRPGHYDILY 239
 
Name Accession Description Interval E-value
OTUB2 cd22764
Ubiquitin Thioesterase Otubain-2; Otubain-2 is also called ubiquitin thioesterase OTUB2, ...
 8-229 4.43e-145

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: 403.68  E-value: 4.43e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070   8 LISEKCDILSILRDHPENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKSREILKFKERVLQTPNDLLA 87
Cdd:cd22764   1 LISEKCDISSLLPEHPENPIYQRKLKDLSKRYASIRKTRGDGNCFYRALAFAYLESLLGNSREIQKFKETVLQSKNELLA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  88 AGFEEHKFRNFFNAFYSVVELVEKDSSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHE 167
Cdd:cd22764  81 AGFEEHRFRNLFNTFVSVVELVEADGSGSSLLKAFNDQTTSDSIVQYLRLLTSAFLQNRADFFQHFVEEGMNIKDFCTQE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386070 168 VEPMAMECDHVQITALSQALNIALQVEYVDEMDTALNHHVFPEAAIPSVYLLYKTSHYNILY 229
Cdd:cd22764 161 VEPMAMECDHIQITALSQALGIPLQVEYVDEMDTALNHHIFPEGAEPSVYLLYKTSHYNILY 222
Peptidase_C65 pfam10275
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ...
 1-229 8.05e-103

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: 297.65  E-value: 8.05e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070     1 MSETSFNLISEKCDILSILRDHP-ENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKSREILKFKERVL 79
Cdd:pfam10275   1 EEEAQGPLVSEKGPLSALEKEYAkADPIYLQKIQDLSEKYSGIRRTRGDGNCFYRAFGFSYLELLLESKDEIDRFKARVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070    80 QTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKD--SSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEE 157
Cdd:pfam10275  81 SLKEALVALGFDEDTFEDFCDAFLELLKKVEDGvsTSESELLQAFNDQETSDYIVYFLRLLTSAYLKTHADEYEPFIDGG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386070   158 MDIKDFCTHEVEPMAMECDHVQITALSQALNIALQVEYVD--EMDTALNHHVFP-----EAAIPSVYLLYKTSHYNILY 229
Cdd:pfam10275 161 GTVEEFCQQEVEPMNKEADHLQIIALAEALGVPVRVEYLDrsAEGNTVNHHDFPgeddtEEQAPFITLLYRPGHYDILY 239
OTUB1 cd22763
Ubiquitin Thioesterase Otubain-1; Otubain-1 is also called ubiquitin thioesterase OTUB1, ...
 8-229 2.33e-91

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: 267.90  E-value: 2.33e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070   8 LISEKCDILSILRDH-PENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKSREILKFKERVLQTPNDLL 86
Cdd:cd22763   1 LVSEKEDLSVLEKEYaEDDPIYQAKIKDLKKKYSYIRRTRPDGNCFYRAFGFAYLESLLDDPEELQRFKEVAAKSKDELV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  87 AAGFEEHKFRNFFNAFYSVVELVEKDSSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTH 166
Cdd:cd22763  81 SLGFPSFTIEDFHDTFMEVLEKVEKGTSVEELLEIFNDQGTSDYLVVYLRLLTSGYLQKEADFFQNFIEGGRSVKEFCSQ 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13386070 167 EVEPMAMECDHVQITALSQALNIALQVEYVD-EMDTALNHHVFPEAAIPSVYLLYKTSHYNILY 229
Cdd:cd22763 161 EVEPMYKESDHIHIIALTSALGVSVRVEYMDrGEGGTVNPHDFPEGSEPRIHLLYRPGHYDILY 224
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
 8-229 2.75e-76

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: 229.91  E-value: 2.75e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070   8 LISEKCDILSILRDHPENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLL--GKSREILKFKERVLQTPNDL 85
Cdd:cd22749   1 LVGEKEPLSALAEEYAGNPIFLQKIKELKKKYSGFRRVRGDGNCFYRAFAFSYLELLLknQDPAELERLLARLESLKNLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  86 LAAGFEEHKFRNFFNAFYSVVELVEKD----SSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEEMDIK 161
Cdd:cd22749  81 EALGFEELVFEDFYEEFLELLKKLRNSkereLTEEELLELFNDEETSNYIVVFLRLLTSAYLKTNADDYEPFLFEGMSVE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386070 162 DFCTHEVEPMAMECDHVQITALSQALNIALQVEYVDEMD-TALNHHVFPE---AAIPSVYLLYKTSHYNILY 229
Cdd:cd22749 161 EFCEREVEPMGKEADHLQITALANALGVPVRVEYLDRSAgGEVNFHEFPPedsDSLPVITLLYRPGHYDILY 232
AtOTU1-like cd22765
Arabidopsis thaliana Deubiquitinating enzyme OTU1 and similar plant proteins; This group ...
 25-229 1.37e-57

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: 182.94  E-value: 1.37e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  25 NRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKS--REILKFKERVLQTPNDLLAAGFEEHKFRNFFNAF 102
Cdd:cd22765  20 SPVFVAKIESLGETYGAIRRTRGDGNCFFRSFMFGYLEHLLETQdgAEVRRVLKRIEQCKKKLVDLGYQELVFEDAMEIL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070 103 YSVVE--LVEKDSSVS--SLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFID--EEMDIKDFCTHEVEPMAMECD 176
Cdd:cd22765 100 VEQLEsiGQGDEESISieTLLENMRDDMVSNYVVMFLRFVTSAEIQRRADFFEPFIMglSNMTVEQFCRRSVEPMGEESD 179

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13386070 177 HVQITALSQALNIALQVEYVD----------EMDTALNHHVF-----PEAAIPSVYLLYKTSHYNILY 229
Cdd:cd22765 180 HVHIVALTDALQVPIRVVYLDrsscdgagggAGGVEVNHHDFvpegcPAAGRPRVHLLYRPGHYDILY 247
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 41-228 5.20e-05

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: 41.65  E-value: 5.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  41 SIRKTKGDGNCFYRALGYSylesllgksreilkfkervlqtpndllaagfeehkfrnffnafysvvelvekdssvssllk 120
Cdd:cd22744   1 RVVDVPGDGNCLFRALAHA------------------------------------------------------------- 19

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070 121 VFNDQSSsdriVQFLRLLTSAFIRNRADFFR----HFIDEEMDIKDFCTHevepMAMEC---DHVQITALSQALNIALQV 193
Cdd:cd22744  20 LYGDQES----HRELRQEVVDYLRENPDLYEpaelADEDDGEDFDEYLQR----MRKPGtwgGELELQALANALNVPIVV 91

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13386070 194 eyVDEMDTALNHHVFPEAAIPS---VYLLYK-TSHYNIL 228
Cdd:cd22744  92 --YSEDGGFLPVSVFGPGPGPSgrpIHLLYTgGNHYDAL 128
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
 42-137 1.89e-03

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (OTUD3) is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 37.65  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386070  42 IRKTKGDGNCFYRALGysylESLLGKSREILKFKERVLQTpndllaagFEEHkfRNFFNAFysVVELVEKDSSVSSLLK- 120
Cdd:cd22770  16 LRDIPGDGNCLFRALG----DQLEGHSRNHLKHRQETVQY--------MIEH--REDFEPF--VEDDVPFDKHVANLSKp 79

                        90
                ....*....|....*...
gi 13386070 121 -VFNDQsssDRIVQFLRL 137
Cdd:cd22770  80 gTYAGN---DAIVAFARL 94
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 132-193 3.26e-03

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2, vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), fungal OTU domain-containing protein 2 (OTU2), and similar proteins. OTUD6A, OTUD6B, and Schizosaccharomyces pombe OTU2 are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. 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: 438585 [Multi-domain]  Cd Length: 144  Bit Score: 36.77  E-value: 3.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13386070 132 VQFLRLLTSAFIRNRADFFRHFI----DEEMDIKDFCTH--EVEPMAMECDHVQITALSQALNIALQV 193
Cdd:cd22748  38 YKELRKLAADYMRAHRDDFLPFLtnddGDLMTEEEFEEYcdKIENTAEWGGQLELRALSKALKRPIHV 105
OTU_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
 132-187 8.29e-03

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; Deubiquitinating enzyme OTU5, also called OTU domain-containing protein 6, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes 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. OTU5 is an inactive cysteine protease. It regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). It is required for phosphate (Pi) homeostasis. OTU5 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438618 [Multi-domain]  Cd Length: 149  Bit Score: 35.78  E-value: 8.29e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386070 132 VQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCT------HEVEPMAMECDHVQITALSQAL 187
Cdd:cd22797  42 YQQLRELAADYMRAHPDDFLPFLEDEDEGGDGDEafeaycREVESTAAWGGQLELGALAHAL 103
 
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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