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Conserved domains on  [gi|634826793|ref|XP_007951329|]
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ubiquitin thioesterase OTU1 [Orycteropus afer afer]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
148-307 1.39e-91

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) 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. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.


:

Pssm-ID: 438582  Cd Length: 161  Bit Score: 270.51  E-value: 1.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 148 VLTRFSVPADNSCLFTSVYYVVEGGVLNpaCAPEMRHFIAQIVAGDPEFYSAAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22745    2 YLVRRVVPDDNSCLFTSISYLLEGGLLD--SAPELREIVADAILSDPDTYNEAILGKPPDEYCAWILKPDSWGGAIELSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 228 LSKYYQCEICVVDTQTVRIDRFGEDAGYNKRVLLIYDGVHYDPLQRNFPD--PDTPPLTIFSSNDDIVLVQALELADEAR 305
Cdd:cd22745   80 LSKHFGVEICVVDVQTGRVDRFGEDKGYSKRIFLLYSGIHYDALALNPSLdaPEDFDVTVFSVSDDEVLEAALELAKELK 159

                 ..
gi 634826793 306 RK 307
Cdd:cd22745  160 AK 161
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
47-121 1.51e-34

ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain.


:

Pssm-ID: 340579  Cd Length: 75  Bit Score: 121.55  E-value: 1.51e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634826793  47 WRLRCKAKDGTHVLQGLSSRTRVRELQGQIAAITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIVE 121
Cdd:cd17059    1 MRLRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKILYGFPPKPLDLSDEEASLESLGIQSGDTLIVE 75
 
Name Accession Description Interval E-value
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
148-307 1.39e-91

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) 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. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.


Pssm-ID: 438582  Cd Length: 161  Bit Score: 270.51  E-value: 1.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 148 VLTRFSVPADNSCLFTSVYYVVEGGVLNpaCAPEMRHFIAQIVAGDPEFYSAAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22745    2 YLVRRVVPDDNSCLFTSISYLLEGGLLD--SAPELREIVADAILSDPDTYNEAILGKPPDEYCAWILKPDSWGGAIELSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 228 LSKYYQCEICVVDTQTVRIDRFGEDAGYNKRVLLIYDGVHYDPLQRNFPD--PDTPPLTIFSSNDDIVLVQALELADEAR 305
Cdd:cd22745   80 LSKHFGVEICVVDVQTGRVDRFGEDKGYSKRIFLLYSGIHYDALALNPSLdaPEDFDVTVFSVSDDEVLEAALELAKELK 159

                 ..
gi 634826793 306 RK 307
Cdd:cd22745  160 AK 161
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
91-347 4.09e-37

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


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 135.38  E-value: 4.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793  91 VGYPPE-----CLDLSNGDTILEDLPIQSGDMLIVEEDQTRHKTS----PTFAKHG----APSYYRETLPVLTRFSVPAD 157
Cdd:COG5539   41 FGRPPQrlngkCLDLSYALSQKDEVEIEKAPKLRAETNEADQEDSltplQNIPELGissfEKSVSQQSINVLEDMPGQDD 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 158 NSCLFTSVYYVveggvLNPACAPEMRHFIAQIVAGDPEFYSAAILGKTNQEYCDWIKRDDTWG-GAIEISILSKYYQCEI 236
Cdd:COG5539  121 NSRLFQAERYS-----LRDASVAKLREVVSLEVLSNPDLYNPAILEIDVIAYATWIVKPDSQGdGCIEIAIISDQLPVRI 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 237 CVVDTQTVRIDRFGEDAgYNKRVLLIYDGVHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEARRKRQFTDVNRF 316
Cdd:COG5539  196 HVVDVDKDSEDRYNSHP-YVQRISILFTGIHFDEETLAMVLWDTYVNEVLFDASDGITIEIQQLASLLKNPHYYTNTASP 274
                        250       260       270
                 ....*....|....*....|....*....|.
gi 634826793 317 TLRCMICQKGLTGQAEARDHAKETGHTNFGE 347
Cdd:COG5539  275 SIKCNICGTGFVGEKDYYAHALATGHYNFGE 305
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
47-121 1.51e-34

ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain.


Pssm-ID: 340579  Cd Length: 75  Bit Score: 121.55  E-value: 1.51e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634826793  47 WRLRCKAKDGTHVLQGLSSRTRVRELQGQIAAITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIVE 121
Cdd:cd17059    1 MRLRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKILYGFPPKPLDLSDEEASLESLGIQSGDTLIVE 75
 
Name Accession Description Interval E-value
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
148-307 1.39e-91

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) 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. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.


Pssm-ID: 438582  Cd Length: 161  Bit Score: 270.51  E-value: 1.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 148 VLTRFSVPADNSCLFTSVYYVVEGGVLNpaCAPEMRHFIAQIVAGDPEFYSAAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22745    2 YLVRRVVPDDNSCLFTSISYLLEGGLLD--SAPELREIVADAILSDPDTYNEAILGKPPDEYCAWILKPDSWGGAIELSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 228 LSKYYQCEICVVDTQTVRIDRFGEDAGYNKRVLLIYDGVHYDPLQRNFPD--PDTPPLTIFSSNDDIVLVQALELADEAR 305
Cdd:cd22745   80 LSKHFGVEICVVDVQTGRVDRFGEDKGYSKRIFLLYSGIHYDALALNPSLdaPEDFDVTVFSVSDDEVLEAALELAKELK 159

                 ..
gi 634826793 306 RK 307
Cdd:cd22745  160 AK 161
OTU_plant_OTU1_2-like cd22793
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar ...
148-307 3.38e-60

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar proteins; Deubiquitinating enzyme OTU2, also called OTU domain-containing protein 2, 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. OTU2 exhibited equivalent binding affinities for K48- and K63-linked ubiquitin chains and no cleavage activity toward linear UB chains. It may also be involved in endoplasmic-reticulum-associated protein degradation (ERAD). OTU2 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438614  Cd Length: 163  Bit Score: 190.61  E-value: 3.38e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 148 VLTRFSVPADNSCLFTSVYYVVEGGVLNpacAPEMRHFIAQIVAGDPEFYSAAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22793    2 VVVRRVIDSDNSCLFNAVGYVMEGSRKK---APELRQVIADAVLSDPFEYNEAFLGKSNKEYCEWILNPNSWGGAIELSI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 228 LSKYYQCEICVVDTQTVRIDRFGEDAGYNKRVLLIYDGVHYDPLQRNfPDPDTPP---LTIFS---SNDDIVLVQALELA 301
Cdd:cd22793   79 LSDHYGREIAAFDIQTKRCDVYGEGKGYTERVMLIYDGLHYDALAIA-PFPGAPEdvdVTIFPvdtGRIGAAEAKAQKLV 157

                 ....*.
gi 634826793 302 DEARRK 307
Cdd:cd22793  158 EEAHKA 163
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
91-347 4.09e-37

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


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 135.38  E-value: 4.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793  91 VGYPPE-----CLDLSNGDTILEDLPIQSGDMLIVEEDQTRHKTS----PTFAKHG----APSYYRETLPVLTRFSVPAD 157
Cdd:COG5539   41 FGRPPQrlngkCLDLSYALSQKDEVEIEKAPKLRAETNEADQEDSltplQNIPELGissfEKSVSQQSINVLEDMPGQDD 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 158 NSCLFTSVYYVveggvLNPACAPEMRHFIAQIVAGDPEFYSAAILGKTNQEYCDWIKRDDTWG-GAIEISILSKYYQCEI 236
Cdd:COG5539  121 NSRLFQAERYS-----LRDASVAKLREVVSLEVLSNPDLYNPAILEIDVIAYATWIVKPDSQGdGCIEIAIISDQLPVRI 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 237 CVVDTQTVRIDRFGEDAgYNKRVLLIYDGVHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEARRKRQFTDVNRF 316
Cdd:COG5539  196 HVVDVDKDSEDRYNSHP-YVQRISILFTGIHFDEETLAMVLWDTYVNEVLFDASDGITIEIQQLASLLKNPHYYTNTASP 274
                        250       260       270
                 ....*....|....*....|....*....|.
gi 634826793 317 TLRCMICQKGLTGQAEARDHAKETGHTNFGE 347
Cdd:COG5539  275 SIKCNICGTGFVGEKDYYAHALATGHYNFGE 305
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
47-121 1.51e-34

ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain.


Pssm-ID: 340579  Cd Length: 75  Bit Score: 121.55  E-value: 1.51e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634826793  47 WRLRCKAKDGTHVLQGLSSRTRVRELQGQIAAITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIVE 121
Cdd:cd17059    1 MRLRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKILYGFPPKPLDLSDEEASLESLGIQSGDTLIVE 75
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
150-271 2.42e-15

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: 71.70  E-value: 2.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 150 TRFSVPADNSCLFTSVYYVVEGgvlNPACAPEMRHFIAQIVAGDPEFYSAAIL-----GKTNQEYCDWIKRDDTWGGAIE 224
Cdd:cd22744    1 RVVDVPGDGNCLFRALAHALYG---DQESHRELRQEVVDYLRENPDLYEPAELadeddGEDFDEYLQRMRKPGTWGGELE 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 634826793 225 ISILSKYYQCEICVV--DTQTVRIDRFGEDAGYNKRVL-LIYDGV-HYDPL 271
Cdd:cd22744   78 LQALANALNVPIVVYseDGGFLPVSVFGPGPGPSGRPIhLLYTGGnHYDAL 128
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
149-271 7.67e-11

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: 59.55  E-value: 7.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 149 LTRFSVPADNSCLFTSV--YYVVEGGVLNPACApEMRHFIAQIVAGDPEFYSAAILGKTNQ-----EYCDWIKRDDTWGG 221
Cdd:cd22762    7 LEEHDIKPDGHCLFAAIadQLQLRGSEINLDYK-ELRKLAAEYIRKHPDDFEPFLFEETDEledidEYCKKIENTAEWGG 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 634826793 222 AIEISILSKYYQCEICVVDTQTvRIDRFGEDAGYNKRVL-LIYD------GVHYDPL 271
Cdd:cd22762   86 ELELLALAKAFGVPIHVVQAEG-RVIKINEEGDSDKPELwLAYYkhsyglGEHYNSL 141
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
149-262 1.84e-10

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: 58.34  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 149 LTRFSVPADNSCLFTSV-------------YYVVEggvLNPACAPEMR----HFIAQIVAGDPEFYSAAILgktnQEYCD 211
Cdd:cd22748    6 LRIKEIPPDGHCLYRAIadqlklrggseepYSYKE---LRKLAADYMRahrdDFLPFLTNDDGDLMTEEEF----EEYCD 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 634826793 212 WIKRDDTWGGAIEISILSKYYQCEICVVDTQTVRIdRFGEDaGYNKRVLLI 262
Cdd:cd22748   79 KIENTAEWGGQLELRALSKALKRPIHVYQAGSPPL-VIGEE-FDSGEPLRL 127
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
149-270 3.06e-07

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: 48.69  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 149 LTRFSVPADNSCLF---------TSVYYVVeggvLNPACAPEMRHFIAQIVAGDPEFYSaailgktnqEYCDWIKRDDTW 219
Cdd:cd22753   10 LYRKHIPRDGSCLFravseqlffTQSYHQQ----VRQACVEYLEKNREEFEKFSEISFD---------DYLERLSDPKEW 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 634826793 220 GGAIEISILSKYYQCEICV---VDTQTVRIdrfgEDAGYNKRVLLIYD-GVHYDP 270
Cdd:cd22753   77 GGLLELEALSLLYKVDFIVysiPDQPPSNI----TNNGYPKKIMLCYSgGNHYDS 127
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
154-271 5.23e-07

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: 48.75  E-value: 5.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 154 VPADNSCLFTSV----------YYVVEGGVLNPAcapeMRHFiaqivagdPEFYSAAILGKTNQEYCDWIKRDDTWGGAI 223
Cdd:cd21880   27 VPGDGNCFFRSIaellfdtedeWRLVKNTIESYA----RANW--------DECPEARLYYLSLEEYLRDAMKDGYWGGSL 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 634826793 224 EISILSKYYQCEI---CVVDTQTVRID-RFGEDaGYNKRVLLIYDGVHYDPL 271
Cdd:cd21880   95 EAEILSKALGITIiiwVVDDSDWVTAAvRFGDG-DVSTSLNLLHSGGHFDAL 145
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
149-269 2.14e-06

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: 46.72  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 149 LTRFSVPADNSCLFTSV-YYVVEGGV------LNPACAPEMRH-------FIAQIVAGDP----EFysaailgktnQEYC 210
Cdd:cd22761   10 LKIHEIPSDGDCLYNAIaHQLSLRGIetsveeLRKQTADYMREnkddflpFLTNPDTGDPlteeEF----------EKYC 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 634826793 211 DWIKRDDTWGGAIEISILSKYYQCEICVVDTQTVRIdRFGEDAGYNKRVLLIYD------GVHYD 269
Cdd:cd22761   80 DDVENTGAWGGQLELRALSHVLKRPIEVIQAEGPPI-IIGEEFKSGKPLILTYHrhayglGEHYN 143
OTU_plant_OTU3-like cd22759
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; ...
149-271 1.61e-05

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; Deubiquitinating enzyme OTU3, also called OTU domain-containing protein 3, 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. OTU3 may play an important regulatory role at the level of protein turnover by preventing degradation. OTU3 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438596  Cd Length: 159  Bit Score: 44.64  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 149 LTRFSVPADNSCLFTSV---YYVVEGGVLNP----ACAPEMRHFIAQIVAGDPE----FYSAAILGKTNQ---EYCDWIK 214
Cdd:cd22759    3 YTVVRVKGDGRCMFRALvkgLAANKGIFLSGreeeQEADELRLAVAEALCRSEErrrdYEEALIAITVEGsldRYCRRIQ 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 634826793 215 RDDTWGGAIEISILSKYYQCEICVV-----------DTQTVRIDRFGED-----AGYNKR--VLLIYDG-VHYDPL 271
Cdd:cd22759   83 RPDFWGGESELLVLSKMLKQPIIVYipeseaknggwGSGFIPIQKYGEEfakgtKGRKGRkpVRLLYSGsNHYDLL 158
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
149-269 1.81e-05

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: 43.70  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 149 LTRFSVPADNSCLFTSVYYVVEGgvlNPACAPEMRHFIAQIVAGDPEFYSAAIL-GKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22771    2 LRIRDVEGDGNCLFRALADQLYG---DEERHAELRKKVVDYMEAHEEDFEPFFEdDETFEDYVSRMREDGTWGGNLELQA 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 634826793 228 LSKYYQCEICV--VDTQTVRIDRFGEDAGynKRVLLIY-DGVHYD 269
Cdd:cd22771   79 ASLVYRVNIVVhqLGQPRWEIENFPDKGA--RTIHLSYhDGEHYN 121
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
150-271 1.94e-04

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: 40.28  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 150 TRFSVPADNSCLFTSVYYVVEGGVLnpacapEMRhfiaqIVAGDPEFYSAAILGKTNQeycdwIKRDDTWGGAIEISILS 229
Cdd:cd22792    1 KVVPVPGDGNCFWHSLGHFLGLSAL------ELK-----KLLRDSLFDDPELDEELDE-----QLEPGVYAEDEAIAAAA 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 634826793 230 KYYQCEICVVDTQTVRIDRFGEDaGYNKRVLLIYDGVHYDPL 271
Cdd:cd22792   65 KLFGVNICVHDPDEGVLYTFTPN-ESSKSIHLLLENEHFEPL 105
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
154-268 4.76e-04

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: 39.56  E-value: 4.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 154 VPADNSCLFTSV---YYvvegGVLNPACAPEMRHFIAQIVAGDPEFY-----SAAILGKTNQEYCDWIKRDDTWGGAIEI 225
Cdd:cd22758   11 VPGDGNCFFHAVsdqLY----GNGIEHSHKELRQQAVNYLRENPELYdgfflSEFDEEESWEEYLNRMSKDGTWGDHIIL 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 634826793 226 SILSKYYQCEICVVDT-QTVRIDRFGEDAGYNKRVLLI--YDGVHY 268
Cdd:cd22758   87 QAAANLFNVRIVIISSdGSDETTIIEPGNSKNGRTIYLghIGENHY 132
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
149-271 8.27e-04

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: 39.17  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 149 LTRFSVPADNSCLFTSVyyvVEGGVLNP-----------ACAPEMRHFIAQIVAGDP-EFYSAAILGKTN-QEYCDWIKR 215
Cdd:cd22746    2 LRVVPVKGDGRCLFRAV---ARGLALATggrplserrerADADALRKAVVEEIRKRRdELFEGSLVIEGDfDAYCQRMSH 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634826793 216 DDTWGGAIEISILSKYYQCEICV--VDTQTV---RIDRFGEdaGYNKR---VLLIYDGVHYDPL 271
Cdd:cd22746   79 PDTWGGEPELLMLADVLQRPIAVylPTPGKGglrKIQEYGE--EYLGGepiRLLYNGGNHYDLL 140
OTU_plant_OTU4-like cd22760
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; ...
154-272 1.91e-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: 38.13  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634826793 154 VPADNSCLFTSVYYVVEGGVLNPACAPEMRHFIAQ-------------------IVAGDPEfysaailgktnqEYCDWIK 214
Cdd:cd22760    7 IAGDGRCLFRAVAHGECLARGKAAPDEERERELADelrtraadelvkrreetewFIEGDFD------------EYVARMR 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 634826793 215 RDDTWGGAIEISILSKYYQCEICV--VDTQT---VRIDRFGEDAGYNKRVLLIYDGV-HYDPLQ 272
Cdd:cd22760   75 RPGVWGGEPELLMLSHVLQRPITVymADEGEgglISIAEYGQEYGKGNPIRVLFHGFgHYEALL 138
 
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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