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Conserved domains on  [gi|392899753|ref|NP_001255320|]
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OTU domain-containing protein [Caenorhabditis elegans]

Protein Classification

OTU domain-containing protein( domain architecture ID 17785023)

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; similar to Homo sapiens OTU domain-containing proteins 6A and 6B

CATH:  1.10.10.1640|3.30.200.90|3.90.70.80
Gene Ontology:  GO:0004843
PubMed:  10664582|23827681|31884527|12704427
SCOP:  4004307

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
 117-266 3.06e-70

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2) and vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), which 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: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 212.75  E-value: 3.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 117 VKEMLAEDHMKMIDIPADGDCMYNAISHQLQEEGIEISVRKLRKRCGTYMREHSEDFRPFI--EDMANMDSDSSWATYLG 194
Cdd:cd22761    1 IKKILKERGLKIHEIPSDGDCLYNAIAHQLSLRGIETSVEELRKQTADYMRENKDDFLPFLtnPDTGDPLTEEEFEKYCD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899753 195 GVENvaeiGGVWGGELELKACSMIFEKTIVVYKQYGGRHTIGEEYSSpkDRALRVVFLRHAYSLGEHYNSTC 266
Cdd:cd22761   81 DVEN----TGAWGGQLELRALSHVLKRPIEVIQAEGPPIIIGEEFKS--GKPLILTYHRHAYGLGEHYNSVE 146
 
Name Accession Description Interval E-value
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
 117-266 3.06e-70

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2) and vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), which 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: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 212.75  E-value: 3.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 117 VKEMLAEDHMKMIDIPADGDCMYNAISHQLQEEGIEISVRKLRKRCGTYMREHSEDFRPFI--EDMANMDSDSSWATYLG 194
Cdd:cd22761    1 IKKILKERGLKIHEIPSDGDCLYNAIAHQLSLRGIETSVEELRKQTADYMRENKDDFLPFLtnPDTGDPLTEEEFEKYCD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899753 195 GVENvaeiGGVWGGELELKACSMIFEKTIVVYKQYGGRHTIGEEYSSpkDRALRVVFLRHAYSLGEHYNSTC 266
Cdd:cd22761   81 DVEN----TGAWGGQLELRALSHVLKRPIEVIQAEGPPIIIGEEFKS--GKPLILTYHRHAYGLGEHYNSVE 146
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 132-262 1.18e-44

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 146.83  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753  132 PADGDCMYNAISHQL---QEEGIEISVRKLRKRCGTYMREHSEDFRPFIEDMANMDSdsswatylggveNVAEIGGVWGG 208
Cdd:pfam02338   1 PGDGNCLYRSISHQLwgvHDVLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDI------------IEIEQTGAWGG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392899753  209 ELELKACSMIFEKTIVVYKQYGGRHTIG-EEYS----SPKDRALRVVFLRHAYSLGEHY 262
Cdd:pfam02338  69 EIEIFALAHILRRPIIVYKSEGGEELGGlKEYGiylpLGWDPSLCLVYPRHLYYLGGHY 127
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
 104-264 5.68e-08

Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 52.57  E-value: 5.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 104 KNQLSDRQMEKAAVKEMLAEDHMKMIDIPADGDCMYNAISHQLqeeGIEISV------RKLRKRCGTYMREHSEDFRPFI 177
Cdd:COG5539  149 LSNPDLYNPAILEIDVIAYATWIVKPDSQGDGCIEIAIISDQL---PVRIHVvdvdkdSEDRYNSHPYVQRISILFTGIH 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 178 EDMANMDSdSSWATYLGGVENVAEiggvWGGELELKACSMIFEKTIVVYKQYGGRHTIGEeysSPKDRALRVVFLRHAYS 257
Cdd:COG5539  226 FDEETLAM-VLWDTYVNEVLFDAS----DGITIEIQQLASLLKNPHYYTNTASPSIKCNI---CGTGFVGEKDYYAHALA 297


                 ....*..
gi 392899753 258 LGeHYNS 264
Cdd:COG5539  298 TG-HYNF 303
 
Name Accession Description Interval E-value
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
 117-266 3.06e-70

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2) and vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), which 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: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 212.75  E-value: 3.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 117 VKEMLAEDHMKMIDIPADGDCMYNAISHQLQEEGIEISVRKLRKRCGTYMREHSEDFRPFI--EDMANMDSDSSWATYLG 194
Cdd:cd22761    1 IKKILKERGLKIHEIPSDGDCLYNAIAHQLSLRGIETSVEELRKQTADYMRENKDDFLPFLtnPDTGDPLTEEEFEKYCD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899753 195 GVENvaeiGGVWGGELELKACSMIFEKTIVVYKQYGGRHTIGEEYSSpkDRALRVVFLRHAYSLGEHYNSTC 266
Cdd:cd22761   81 DVEN----TGAWGGQLELRALSHVLKRPIEVIQAEGPPIIIGEEFKS--GKPLILTYHRHAYGLGEHYNSVE 146
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 121-264 2.72e-51

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: 164.66  E-value: 2.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 121 LAEDHMKMIDIPADGDCMYNAISHQLQEEG---IEISVRKLRKRCGTYMREHSEDFRPFIEDM-ANMDSDSSWATYLGGV 196
Cdd:cd22748    1 LKPLGLRIKEIPPDGHCLYRAIADQLKLRGgseEPYSYKELRKLAADYMRAHRDDFLPFLTNDdGDLMTEEEFEEYCDKI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899753 197 ENVAEiggvWGGELELKACSMIFEKTIVVYKQYGGRHTIGEEYSSpkDRALRVVFLRHAYSLGEHYNS 264
Cdd:cd22748   81 ENTAE----WGGQLELRALSKALKRPIHVYQAGSPPLVIGEEFDS--GEPLRLSYHRHAYGLGEHYNS 142
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 132-262 1.18e-44

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian Tumour (OTU) gene in Drosophila. Members include proteins from eukaryotes, viruses and pathogenic bacterium. The conserved cysteine and histidine, and possibly the aspartate, represent the catalytic residues in this putative group of proteases.


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 146.83  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753  132 PADGDCMYNAISHQL---QEEGIEISVRKLRKRCGTYMREHSEDFRPFIEDMANMDSdsswatylggveNVAEIGGVWGG 208
Cdd:pfam02338   1 PGDGNCLYRSISHQLwgvHDVLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDI------------IEIEQTGAWGG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392899753  209 ELELKACSMIFEKTIVVYKQYGGRHTIG-EEYS----SPKDRALRVVFLRHAYSLGEHY 262
Cdd:pfam02338  69 EIEIFALAHILRRPIIVYKSEGGEELGGlKEYGiylpLGWDPSLCLVYPRHLYYLGGHY 127
OTU_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
 130-265 4.88e-42

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: 140.94  E-value: 4.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 130 DIPADGDCMYNAISHQLQ---EEGIEISVRKLRKRCGTYMREHSEDFRPFIEDMANMDS-DSSWATYLGGVENVAeiggV 205
Cdd:cd22797   14 EIKADGHCLYRAVEDQLQlrgGGAPAPDYQQLRELAADYMRAHPDDFLPFLEDEDEGGDgDEAFEAYCREVESTA----A 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 206 WGGELELKACSMIFEKTIVVYKQYGGRHTIGEEYSSPkDRALRVVFLRHAYSLGEHYNST 265
Cdd:cd22797   90 WGGQLELGALAHALRRHIKVYSAGMPDVEMGEEYAGT-GPPLRLCYHRHAFGLGEHYNSV 148
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 121-265 2.50e-37

OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; This subfamily includes Schizosaccharomyces pombe and Saccharomyces cerevisiae OTU domain-containing protein 2 (OTU2) and similar proteins. S. pombe OTU2 is a ubiquitin thioesterase/hydrolase (EC 3.4.19.12) that can remove conjugated ubiquitin from protein substrates and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Fungal OTU2 bbelongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438599 [Multi-domain]  Cd Length: 142  Bit Score: 128.50  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 121 LAEDHMKMIDIPADGDCMYNAISHQLQEEGIEI--SVRKLRKRCGTYMREHSEDFRPFIedMANMDSDSSWATYLGGVEN 198
Cdd:cd22762    2 LEELGLEEHDIKPDGHCLFAAIADQLQLRGSEInlDYKELRKLAAEYIRKHPDDFEPFL--FEETDELEDIDEYCKKIEN 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899753 199 VAEiggvWGGELELKACSMIFEKTIVVYkQYGGRHTIGEEYSSPKDRALRVVFLRHAYSLGEHYNST 265
Cdd:cd22762   80 TAE----WGGELELLALAKAFGVPIHVV-QAEGRVIKINEEGDSDKPELWLAYYKHSYGLGEHYNSL 141
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 127-264 2.74e-27

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: 102.13  E-value: 2.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 127 KMIDIPADGDCMYNAISHQLQeeGIEISVRKLRKRCGTYMREHSEDFRPfiEDMANMDSDSSWATYLGGVENvaeiGGVW 206
Cdd:cd22744    1 RVVDVPGDGNCLFRALAHALY--GDQESHRELRQEVVDYLRENPDLYEP--AELADEDDGEDFDEYLQRMRK----PGTW 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899753 207 GGELELKACSMIFEKTIVVYkQYGGRHTIGEEYSSPKDRALRVVFLrhAYSLGEHYNS 264
Cdd:cd22744   73 GGELELQALANALNVPIVVY-SEDGGFLPVSVFGPGPGPSGRPIHL--LYTGGNHYDA 127
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 130-264 4.01e-27

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: 101.48  E-value: 4.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 130 DIPADGDCMYNAISHQLqeEGIEISVRKLRKRCGTYMREHSEDFRPFIEDmanmdsDSSWATYlggVENVAEIgGVWGGE 209
Cdd:cd22771    6 DVEGDGNCLFRALADQL--YGDEERHAELRKKVVDYMEAHEEDFEPFFED------DETFEDY---VSRMRED-GTWGGN 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392899753 210 LELKACSMIFEKTIVVYkQYGGRHTIGEEYSSPKDRALRVvflrhAYSLGEHYNS 264
Cdd:cd22771   74 LELQAASLVYRVNIVVH-QLGQPRWEIENFPDKGARTIHL-----SYHDGEHYNS 122
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 129-264 1.09e-26

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This subfamily includes bilaterial OTU domain-containing protein 3 (OTUD3), Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, and similar proteins. 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. OTU7 is a DUB that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. 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: 438593 [Multi-domain]  Cd Length: 131  Bit Score: 100.71  E-value: 1.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 129 IDIPADGDCMYNAISHQLqeEGIEISVRKLRKRCGTYMREHSEDFRPFIEDMANMDSDSSWATYLggvENVAEiGGVWGG 208
Cdd:cd22756    3 KDITGDGNCLFRALSDQL--YGDPDRHLEIRAEVVEYMRANPDDFKPFSEAATFAEDDEAFEDYL---ARMAK-DGTYGD 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392899753 209 ELELKACSMIFEKTIVVYkQYGGRHTIGEEYSSPKDRALRVVFLrhAYSLGEHYNS 264
Cdd:cd22756   77 NLEIVAFARAYNVDVKVY-QPDPVYVISAPEDGSPGPARRVLHI--AYHNWEHYSS 129
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 121-265 2.02e-26

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438595 [Multi-domain]  Cd Length: 135  Bit Score: 100.04  E-value: 2.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 121 LAEDHMKMIDIPADGDCMYNAISHQLQEEGIEISVRKLRKRCGTYMREHSEDFRPFieDMANMDSDSSWATYLggveNVA 200
Cdd:cd22758    1 AKENGFEIRDVPGDGNCFFHAVSDQLYGNGIEHSHKELRQQAVNYLRENPELYDGF--FLSEFDEEESWEEYL----NRM 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392899753 201 EIGGVWGGELELKACSMIFEKTIVVYKQYGGRHTIgeEYSSPKDRALRVVFLrhAYSLGEHYNST 265
Cdd:cd22758   75 SKDGTWGDHIILQAAANLFNVRIVIISSDGSDETT--IIEPGNSKNGRTIYL--GHIGENHYVSL 135
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 131-267 2.23e-13

OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, is a deubiquitinase that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. OTUD4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 65.47  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 131 IPADGDCMYNAISHQL---QEEGIEIsvrklRKRCGTYMREHSEDFRPFIEdmanmdsdSSWATYLGGVENVAEiggvWG 207
Cdd:cd22794   15 IAKDGSCLFRAVAEQVfhtQSRHLEV-----RKACVDYLRRNREKFEAFIE--------GPFEQYLKNLENPKE----WA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899753 208 GELELKACSMIFEKTIVVYKQyggrhtIGEEYSSPKDRALR-VVFLrhAYSLGEHYNSTCP 267
Cdd:cd22794   78 GQVEISALSLMYKRDFIIYQE------PGKPPSNVTENGFPdKILL--CFSNGNHYDSVYP 130
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
 126-264 3.12e-12

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: 62.69  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 126 MKMIDIPADGDCMYNAISHQLqeEGIEISVRKLRKRCGTYMREHSEDFRPFIEDmanmdsDSSWATYlggVENVAEiGGV 205
Cdd:cd22770   14 LKLRDIPGDGNCLFRALGDQL--EGHSRNHLKHRQETVQYMIEHREDFEPFVED------DVPFDKH---VANLSK-PGT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 206 WGGELELKACSMIFEKTIVVYKQYGGRHTI-GEEYSSPKDralrvvfLRHAYSLGEHYNS 264
Cdd:cd22770   82 YAGNDAIVAFARLHQVNVVIHQLNAPLWQIrGTEKSSSRE-------LHISYHNGDHYSS 134
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 131-264 1.52e-10

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 and similar proteins; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is alco called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). This subfamily also contains OTU domain-containing protein 4 (OTUD4), also called HIV-1-induced protein HIN-1, a DUB that specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein upon phosphorylation, triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. 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: 438590 [Multi-domain]  Cd Length: 130  Bit Score: 57.55  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 131 IPADGDCMYNAISHQL---QEEGIEIsvrklRKRCGTYMREHSEDFRPFIEDmanmdsdsSWATYLGGVENVAEiggvWG 207
Cdd:cd22753   15 IPRDGSCLFRAVSEQLfftQSYHQQV-----RQACVEYLEKNREEFEKFSEI--------SFDDYLERLSDPKE----WG 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392899753 208 GELELKACSMIFEKTIVVYKQYGGRHTIGEEYSSPKdralrVVFLrhAYSLGEHYNS 264
Cdd:cd22753   78 GLLELEALSLLYKVDFIVYSIPDQPPSNITNNGYPK-----KIML--CYSGGNHYDS 127
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
 121-264 2.24e-10

OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This subfamily contains Arabidopsis thaliana deubiquitinating enzymes OTU8, OTU9, OTU10, OTU11, and OTU12, and similar proteins from plants and other eukaryotes. OTU8-OTU12 are 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: 438588 [Multi-domain]  Cd Length: 134  Bit Score: 57.17  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 121 LAEDHMKMIDIPADGDCMYNAISHQL---QEEGieisvRKLRKRCGTYMREHSEDFRPFIEDManmdsdsswaTYLGGVE 197
Cdd:cd22751    5 LDLYGLVERKVEGDGNCQFRALSDQLfgtQDHH-----AEVRELVVKQLRAHPELYYEFYVPE----------EYDEYLK 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392899753 198 NVAEiGGVWGGELELKACSMIFEKTIVVYKQYGGRHTIgeEY-SSPKDRALRVVFLrhAYSLGEHYNS 264
Cdd:cd22751   70 KMSK-DGEWGDELTLQAAADAFGVKIHVITSFEDNWFL--EIePRGLVRSKRVLFL--SYWAEVHYNS 132
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 127-263 3.67e-10

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: 56.50  E-value: 3.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 127 KMIDIPADGDCMYNAISHQLQeeGIEISVRKLRKRCGTYMREHSEDFRPFIedmanMDSDSSWATYL---GGVENvaeig 203
Cdd:cd22755    2 KTIKIVGDGNCFFRALSYAIT--GSEKYHRKIRKAIVDFLEKNPDEFRNLL-----RSDYESVEEYLeksRMRYD----- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392899753 204 GVWGGELELKACSMIFEKTIVVYKQYGGR-HTIGEEYSSPKDRALR-VVFLRHAYslGEHYN 263
Cdd:cd22755   70 GTWATDVEIFAAATLLGVDIYVYSKGGYKwLLYSPRFKLGKRNGSReAIYLKNTN--GNHFE 129
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
 129-263 9.43e-10

OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The VP80 protein is a capsid-associated structural protein that was first identified as P87 in Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus (OpMNPV); its homologs are found only in NPV genomes. The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) VP80 protein is essential for the formation of both budded virus (BV) and occlusion-derived virus (ODV). It has also been shown to interact with the virus-triggered, nuclear F-actin cytoskeleton. P87/VP80 contains an N-terminal OTU domain. 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. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438594 [Multi-domain]  Cd Length: 128  Bit Score: 55.29  E-value: 9.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 129 IDIPADGDCMYNAISHQLqeEGIEISVRKLRKRCGTYMREHSEDFRPFIedmanMDSDSSwaTYLGGVENVAEIG--GVW 206
Cdd:cd22757    4 IPIPGDGACLFRALSYLL--YGTQSRHLEVRKEVVDYVVNNWDEFSIYT-----HDSEGN--NYKSAEEYRADMSkpGTY 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899753 207 GGELELKACSMIFEKTIVVYKQyggrhtiGEEYSSPKDRALRVVFLRHAYSLGE-HYN 263
Cdd:cd22757   75 GTLCELVAAAELYPFHFEVYRN-------GKLYASFGDPSNPVKRLKFSGDLSNgHFD 125
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 134-232 3.58e-09

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also called asparagine-linked glycosylation 13 homolog, glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13 homolog. It displays both glycosyltransferase (EC 2.4.1.141) and deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) activities. With ALG14, it forms a UDP-N-acetylglucosamine transferase that catalyzes the second step of eukaryotic N-linked glycosylation in the endoplasmic reticulum. ALG13 variants cause a form of early infantile epileptic encephalopathy known as EIEE36 refractory seizures, neurodevelopmental impairment, and poor prognosis; given the essential role of ALG13 in glycosylation, it is also considered a congenital disorder of glycosylation (CDG). ALG13 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438616 [Multi-domain]  Cd Length: 130  Bit Score: 53.66  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 134 DGDCMYNAISHQL---QEEGIEIsvrklRKRCGTYMREHSEDFRPFIEdmanmdsdSSWATYLGGVENVAEiggvWGGEL 210
Cdd:cd22795   18 DASCLFRAVSEQLflcQIHHLEI-----RKACVSYMRANQCNFESYVE--------GSFEKYLERLEDPKE----SAGQL 80

                         90       100
                 ....*....|....*....|..
gi 392899753 211 ELKACSMIFEKTIVVYKqYGGR 232
Cdd:cd22795   81 EISALSLIYNRDFILYR-YPGK 101
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 126-264 1.86e-08

OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU domain-containing protein 5 (OTUD5), also called deubiquitinating enzyme A (DUBA), is a phosphorylation-dependent deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can hydrolyze 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, and may function as negative regulator of the innate immune system. It limits type I interferon production in macrophages and suppresses interleukin-17A production in T cells. OTUD5 also functions in an apoptotic signaling cascade by mediating the sequential activation of PDCD5 (programmed cell death 5) and p53 in response to genotoxic stress. In Drosophila, OTUD5/DUBA is essential for spermatogenesis. This subfamily also includes Arabidopsis thaliana OTU domain-containing protein 6, also called deubiquitinating enzyme OTU6 or otubain-like deubiquitinase 1 (OTLD1), which binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It also includes plant OTU6.


Pssm-ID: 438589 [Multi-domain]  Cd Length: 124  Bit Score: 51.78  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 126 MKMIDIPADGDCMYNAISHQLQeeGIEISVRKLRKRCGTYMREHSEDFRPFIEDmanmdsdsSWATYlggvenVAEI--G 203
Cdd:cd22752    2 FIIKEMEEDGNCLFRAVADQVY--GDQEMHDVVRKHCMDYMEKNRDYFSQFVTE--------DFEEY------INRKrqD 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392899753 204 GVWGGELELKACSMIFEKTIVVYKQYGGRHTIGEEYSSPKDRALRVvflrhAYSLGEHYNS 264
Cdd:cd22752   66 GVWGNHIEIQAMSELYNRPIEVYAYSTEPINTFHEASSSDNEPIRL-----SYHGNSHYNS 121
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
 104-264 5.68e-08

Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 52.57  E-value: 5.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 104 KNQLSDRQMEKAAVKEMLAEDHMKMIDIPADGDCMYNAISHQLqeeGIEISV------RKLRKRCGTYMREHSEDFRPFI 177
Cdd:COG5539  149 LSNPDLYNPAILEIDVIAYATWIVKPDSQGDGCIEIAIISDQL---PVRIHVvdvdkdSEDRYNSHPYVQRISILFTGIH 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 178 EDMANMDSdSSWATYLGGVENVAEiggvWGGELELKACSMIFEKTIVVYKQYGGRHTIGEeysSPKDRALRVVFLRHAYS 257
Cdd:COG5539  226 FDEETLAM-VLWDTYVNEVLFDAS----DGITIEIQQLASLLKNPHYYTNTASPSIKCNI---CGTGFVGEKDYYAHALA 297


                 ....*..
gi 392899753 258 LGeHYNS 264
Cdd:COG5539  298 TG-HYNF 303
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
 131-243 6.58e-07

OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU domain-containing protein 1 (OTUD1), also called DUBA-7 in humans, is a deubiquitinating enzyme/ubiquitinyl hydrolase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin; this specificity is facilitated by the C-terminal Ub-interacting motif (UIM) of OTUD1. It interacts and promotes the deubiquitination of myeloid cell leukemia 1 (MCL1), a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumorigenesis. OTUD1 also deubiquitinates IFN regulatory factor 3 (IRF3) and attenuates its function; IRF3 is critical for the transcription of type I IFNs in defensing virus and promoting inflammatory responses. Loss-of-function mutations of OTUD1 associated with multiple autoimmune diseases including systemic lupus erythematosus (SLE), rheumatoid arthritis (RA), ulcerative colitis (UC) and Hashimoto's thyroiditis (HT). OTUD1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438584 [Multi-domain]  Cd Length: 149  Bit Score: 47.88  E-value: 6.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 131 IPADGDCMYNAISHQLQeeGIEISVRKLRKRCGTYMREHSEDFRPFIEDmanmDSDSSWATylggvenvAEIGGVWGGEL 210
Cdd:cd22747   26 IIPDGNCLYRAVSKAVY--GDQALHRELREQTVHYIADHLDEFNPIIEG----DVGEFLIK--------AAQDGAWAGYP 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 392899753 211 ELKACSMIFEktIVVYKQYGGR----------HTIGEEYSSPK 243
Cdd:cd22747   92 ELLAMGQMLN--VNIRLTTGGSlesptvstmvHYLGPEDSGKP 132
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
 133-264 2.23e-06

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), 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. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438617 [Multi-domain]  Cd Length: 128  Bit Score: 45.88  E-value: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 133 ADGDCMYNAISHQL---QEEGIEIsvrklRKRCGTYMREHSEDFRPFIedmanmdsDSSWATYLGGVENvaeiGGVWGGE 209
Cdd:cd22796   12 GDGNCLFRAVADQVygdQEMHDEV-----REMCMDYMEKERDHFSQFV--------TEDFTQYVKRKRR----DRVFGNN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392899753 210 LELKACSMIFEKTIVVYkQYGGRHTIG---EEYSSPKdralrvVFLRHAYSLGEHYNS 264
Cdd:cd22796   75 LEIQAMSEIYNRPIEVY-SYSNGEPINifhGSYEGDD------PPIRLSYHDGNHYNS 125
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
 131-262 4.13e-06

OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar proteins; Deubiquitinating enzyme OTU3 (also called OTU domain-containing protein 3) and deubiquitinating enzyme OTU4 (also called OTU domain-containing protein 4) are deubiquitinases (DUBs) or 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. OTU3 and OTU4 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: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 45.34  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 131 IPADGDCMYNAISH--QLQEEGIEISVR-------KLRKRCGTYMREHSEDFRPFIedmanMDSDSSWATYLGGVENVae 201
Cdd:cd22746    7 VKGDGRCLFRAVARglALATGGRPLSERreradadALRKAVVEEIRKRRDELFEGS-----LVIEGDFDAYCQRMSHP-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899753 202 igGVWGGELELKACSMIFEKTIVVY----KQYGGRH--TIGEEYSspKDRALRVvflrhAYSLGEHY 262
Cdd:cd22746   80 --DTWGGEPELLMLADVLQRPIAVYlptpGKGGLRKiqEYGEEYL--GGEPIRL-----LYNGGNHY 137
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
 129-263 3.09e-05

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. 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: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 42.21  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 129 IDIPADGDCMYNAISHQLQEEGIEisvrkLRKRCGTYMReHSEDFRPFIEDMANmdsdsswatylggvenvaeiGGVWGG 208
Cdd:cd22792    3 VPVPGDGNCFWHSLGHFLGLSALE-----LKKLLRDSLF-DDPELDEELDEQLE--------------------PGVYAE 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392899753 209 ELELKACSMIFEKTIVVYKQYGGRhtigeEYSSPKDRALRVVFLRHAyslGEHYN 263
Cdd:cd22792   57 DEAIAAAAKLFGVNICVHDPDEGV-----LYTFTPNESSKSIHLLLE---NEHFE 103
OTU_plant_OTU4-like cd22760
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; ...
 129-262 5.90e-03

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; Deubiquitinating enzyme OTU4, also called OTU domain-containing protein 4, 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. OTU4 may play an important regulatory role at the level of protein turnover by preventing degradation. OTU4 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438597 [Multi-domain]  Cd Length: 138  Bit Score: 36.20  E-value: 5.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392899753 129 IDIPADGDCMYNAISH--QLQEEGIEISVRK-------LRKR-CGTYM--REHSE-----DFRPFIEDMANMdsdsswat 191
Cdd:cd22760    5 HGIAGDGRCLFRAVAHgeCLARGKAAPDEERereladeLRTRaADELVkrREETEwfiegDFDEYVARMRRP-------- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392899753 192 ylggvenvaeigGVWGGELELKACSMIFEKTIVVYKQ---YGGRHTI---GEEYssPKDRALRVVFlrHAYSlgeHY 262
Cdd:cd22760   77 ------------GVWGGEPELLMLSHVLQRPITVYMAdegEGGLISIaeyGQEY--GKGNPIRVLF--HGFG---HY 134
 
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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