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Conserved domains on  [gi|795097409|ref|XP_011793087|]
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PREDICTED: ubiquitin thioesterase OTU1 [Colobus angolensis palliatus]

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 2.60e-95

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: 280.14  E-value: 2.60e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 148 VLTRTVVPADNSCLFTSVYYVVEGGVLNpaCAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22745    2 YLVRRVVPDDNSCLFTSISYLLEGGLLD--SAPELREIVADAILSDPDTYNEAILGKPPDEYCAWILKPDSWGGAIELSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 228 LSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPD--PDTPPLTIFSSNDDIVLVQALELADEAR 305
Cdd:cd22745   80 LSKHFGVEICVVDVQTGRVDRFGEDKGYSKRIFLLYSGIHYDALALNPSLdaPEDFDVTVFSVSDDEVLEAALELAKELK 159

                 ..
gi 795097409 306 RR 307
Cdd:cd22745  160 AK 161
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
47-121 3.49e-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: 120.39  E-value: 3.49e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795097409  47 WRLRCKAKDGTHVLQGLSSRTRVRELQSQIAAITGIAPDGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIVE 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 2.60e-95

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: 280.14  E-value: 2.60e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 148 VLTRTVVPADNSCLFTSVYYVVEGGVLNpaCAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22745    2 YLVRRVVPDDNSCLFTSISYLLEGGLLD--SAPELREIVADAILSDPDTYNEAILGKPPDEYCAWILKPDSWGGAIELSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 228 LSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPD--PDTPPLTIFSSNDDIVLVQALELADEAR 305
Cdd:cd22745   80 LSKHFGVEICVVDVQTGRVDRFGEDKGYSKRIFLLYSGIHYDALALNPSLdaPEDFDVTVFSVSDDEVLEAALELAKELK 159

                 ..
gi 795097409 306 RR 307
Cdd:cd22745  160 AK 161
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
77-347 1.37e-42

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


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 150.02  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409  77 AAITGIAPDGQRILVGYPPE-----CLDLSNGDTILEDLPIQSGDMLIVEEDQTRPKSS----PAFTKRGAS----SYVR 143
Cdd:COG5539   27 DLQTKITRIMKQLTFGRPPQrlngkCLDLSYALSQKDEVEIEKAPKLRAETNEADQEDSltplQNIPELGISsfekSVSQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 144 ETLPVLTRTVVPADNSCLFTSVYYVveggvLNPACAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWG-GA 222
Cdd:COG5539  107 QSINVLEDMPGQDDNSRLFQAERYS-----LRDASVAKLREVVSLEVLSNPDLYNPAILEIDVIAYATWIVKPDSQGdGC 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 223 IEISILSKFYQCEICVVDTQTVRIDRFGEDAgYTKRVLLIYDGIHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELAD 302
Cdd:COG5539  182 IEIAIISDQLPVRIHVVDVDKDSEDRYNSHP-YVQRISILFTGIHFDEETLAMVLWDTYVNEVLFDASDGITIEIQQLAS 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 795097409 303 EARRRRQFTDVNRFTLRCMVCQKGLTGQAEAREHAKETGHTNFGE 347
Cdd:COG5539  261 LLKNPHYYTNTASPSIKCNICGTGFVGEKDYYAHALATGHYNFGE 305
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
47-121 3.49e-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: 120.39  E-value: 3.49e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795097409  47 WRLRCKAKDGTHVLQGLSSRTRVRELQSQIAAITGIAPDGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIVE 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 2.60e-95

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: 280.14  E-value: 2.60e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 148 VLTRTVVPADNSCLFTSVYYVVEGGVLNpaCAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22745    2 YLVRRVVPDDNSCLFTSISYLLEGGLLD--SAPELREIVADAILSDPDTYNEAILGKPPDEYCAWILKPDSWGGAIELSI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 228 LSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPD--PDTPPLTIFSSNDDIVLVQALELADEAR 305
Cdd:cd22745   80 LSKHFGVEICVVDVQTGRVDRFGEDKGYSKRIFLLYSGIHYDALALNPSLdaPEDFDVTVFSVSDDEVLEAALELAKELK 159

                 ..
gi 795097409 306 RR 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 2.38e-65

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: 203.71  E-value: 2.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 148 VLTRTVVPADNSCLFTSVYYVVEGGVLNpacAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22793    2 VVVRRVIDSDNSCLFNAVGYVMEGSRKK---APELRQVIADAVLSDPFEYNEAFLGKSNKEYCEWILNPNSWGGAIELSI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 228 LSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNfPDPDTPP---LTIFS---SNDDIVLVQALELA 301
Cdd:cd22793   79 LSDHYGREIAAFDIQTKRCDVYGEGKGYTERVMLIYDGLHYDALAIA-PFPGAPEdvdVTIFPvdtGRIGAAEAKAQKLV 157

                 ....*.
gi 795097409 302 DEARRR 307
Cdd:cd22793  158 EEAHKA 163
COG5539 COG5539
Predicted cysteine protease (OTU family) [Posttranslational modification, protein turnover, ...
77-347 1.37e-42

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


Pssm-ID: 227826 [Multi-domain]  Cd Length: 306  Bit Score: 150.02  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409  77 AAITGIAPDGQRILVGYPPE-----CLDLSNGDTILEDLPIQSGDMLIVEEDQTRPKSS----PAFTKRGAS----SYVR 143
Cdd:COG5539   27 DLQTKITRIMKQLTFGRPPQrlngkCLDLSYALSQKDEVEIEKAPKLRAETNEADQEDSltplQNIPELGISsfekSVSQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 144 ETLPVLTRTVVPADNSCLFTSVYYVveggvLNPACAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWG-GA 222
Cdd:COG5539  107 QSINVLEDMPGQDDNSRLFQAERYS-----LRDASVAKLREVVSLEVLSNPDLYNPAILEIDVIAYATWIVKPDSQGdGC 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 223 IEISILSKFYQCEICVVDTQTVRIDRFGEDAgYTKRVLLIYDGIHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELAD 302
Cdd:COG5539  182 IEIAIISDQLPVRIHVVDVDKDSEDRYNSHP-YVQRISILFTGIHFDEETLAMVLWDTYVNEVLFDASDGITIEIQQLAS 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 795097409 303 EARRRRQFTDVNRFTLRCMVCQKGLTGQAEAREHAKETGHTNFGE 347
Cdd:COG5539  261 LLKNPHYYTNTASPSIKCNICGTGFVGEKDYYAHALATGHYNFGE 305
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
47-121 3.49e-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: 120.39  E-value: 3.49e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795097409  47 WRLRCKAKDGTHVLQGLSSRTRVRELQSQIAAITGIAPDGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIVE 121
Cdd:cd17059    1 MRLRVRSKGGQHVLSLLTDTSTVGELQDRIAALTGIPPSSQKILYGFPPKPLDLSDEEASLESLGIQSGDTLIVE 75
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
154-271 1.90e-17

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: 77.48  E-value: 1.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSVYYVVEGgvlNPACAPEMRRLIAQIVASDPDFYSEAIL-----GKTNQEYCDWIKRDDTWGGAIEISIL 228
Cdd:cd22744    5 VPGDGNCLFRALAHALYG---DQESHRELRQEVVDYLRENPDLYEPAELadeddGEDFDEYLQRMRKPGTWGGELELQAL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 795097409 229 SKFYQCEICVV--DTQTVRIDRFGEDAGYTKRVL-LIYDGI-HYDPL 271
Cdd:cd22744   82 ANALNVPIVVYseDGGFLPVSVFGPGPGPSGRPIhLLYTGGnHYDAL 128
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
154-271 9.04e-12

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: 61.86  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSV--YYVVEGGVLNPACApEMRRLIAQIVASDPDFYSEAILGKTNQ-----EYCDWIKRDDTWGGAIEIS 226
Cdd:cd22762   12 IKPDGHCLFAAIadQLQLRGSEINLDYK-ELRKLAAEYIRKHPDDFEPFLFEETDEledidEYCKKIENTAEWGGELELL 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 795097409 227 ILSKFYQCEICVVDTQTvRIDRFGEDAGYTKRVL-LIYD------GIHYDPL 271
Cdd:cd22762   91 ALAKAFGVPIHVVQAEG-RVIKINEEGDSDKPELwLAYYkhsyglGEHYNSL 141
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
154-262 2.44e-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: 57.96  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSVYY--VVEGGVLNPACAPEMRRLIAQ------------IVASDPDFYSEAILgktnQEYCDWIKRDDTW 219
Cdd:cd22748   11 IPPDGHCLYRAIADqlKLRGGSEEPYSYKELRKLAADymrahrddflpfLTNDDGDLMTEEEF----EEYCDKIENTAEW 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 795097409 220 GGAIEISILSKFYQCEICVVDTQTVRIdRFGEDaGYTKRVLLI 262
Cdd:cd22748   87 GGQLELRALSKALKRPIHVYQAGSPPL-VIGEE-FDSGEPLRL 127
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
149-270 1.81e-09

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: 55.24  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 149 LTRTVVPADNSCLF---------TSVYYVVeggvLNPACAPEMRRLIAQIvasdpdfysEAILGKTNQEYCDWIKRDDTW 219
Cdd:cd22753   10 LYRKHIPRDGSCLFravseqlffTQSYHQQ----VRQACVEYLEKNREEF---------EKFSEISFDDYLERLSDPKEW 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 795097409 220 GGAIEISILSKFYQCEICV---VDTQTVRIdrfgEDAGYTKRVLLIYDGI-HYDP 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 5.90e-08

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: 51.45  E-value: 5.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSV---YYVVEGGVLnpacapEMRRLIAQIVASDPDFYSEAIL-GKTNQEYCDWIKRDDTWGGAIEISILS 229
Cdd:cd21880   27 VPGDGNCFFRSIaelLFDTEDEWR------LVKNTIESYARANWDECPEARLyYLSLEEYLRDAMKDGYWGGSLEAEILS 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 795097409 230 KFYQCEI---CVVDTQTVRID-RFGEDaGYTKRVLLIYDGIHYDPL 271
Cdd:cd21880  101 KALGITIiiwVVDDSDWVTAAvRFGDG-DVSTSLNLLHSGGHFDAL 145
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
154-269 3.39e-07

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: 48.70  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSVYYVVEGgvlNPACAPEMRRLIAQIVASDPDFYSEAIL-GKTNQEYCDWIKRDDTWGGAIEISILSKFY 232
Cdd:cd22771    7 VEGDGNCLFRALADQLYG---DEERHAELRKKVVDYMEAHEEDFEPFFEdDETFEDYVSRMREDGTWGGNLELQAASLVY 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 795097409 233 QCEICV--VDTQTVRIDRFGEDAgyTKRVLLIY-DGIHYD 269
Cdd:cd22771   84 RVNIVVhqLGQPRWEIENFPDKG--ARTIHLSYhDGEHYN 121
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
154-268 1.46e-06

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: 46.88  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSV---YYvvegGVLNPACAPEMRRLIAQIVASDPDFYSEAILGKTN-----QEYCDWIKRDDTWGGAIEI 225
Cdd:cd22758   11 VPGDGNCFFHAVsdqLY----GNGIEHSHKELRQQAVNYLRENPELYDGFFLSEFDeeeswEEYLNRMSKDGTWGDHIIL 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 795097409 226 SILSKFYQCEICVVDT-QTVRIDRFGEDAGYTKRVLLI--YDGIHY 268
Cdd:cd22758   87 QAAANLFNVRIVIISSdGSDETTIIEPGNSKNGRTIYLghIGENHY 132
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
150-271 1.97e-06

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: 46.06  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 150 TRTVVPADNSCLFTSVYYVVEGGVLnpacapEMRRLIAQIVASDPDFYSEAilgktnqeycDWIKRDDTWGGAIEISILS 229
Cdd:cd22792    1 KVVPVPGDGNCFWHSLGHFLGLSAL------ELKKLLRDSLFDDPELDEEL----------DEQLEPGVYAEDEAIAAAA 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 795097409 230 KFYQCEICVVDTQTVRIDRFGEDaGYTKRVLLIYDGIHYDPL 271
Cdd:cd22792   65 KLFGVNICVHDPDEGVLYTFTPN-ESSKSIHLLLENEHFEPL 105
OTU_plant_OTU3-like cd22759
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; ...
149-271 7.16e-06

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: 45.41  E-value: 7.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 149 LTRTVVPADNSCLFTSV---YYVVEGGVLNP----ACAPEMRRLIAQIVASDP---DFYSEAILGKTNQE----YCDWIK 214
Cdd:cd22759    3 YTVVRVKGDGRCMFRALvkgLAANKGIFLSGreeeQEADELRLAVAEALCRSEerrRDYEEALIAITVEGsldrYCRRIQ 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795097409 215 RDDTWGGAIEISILSKFYQCEICVV-----------DTQTVRIDRFGED-----AGYTKR--VLLIYDG-IHYDPL 271
Cdd:cd22759   83 RPDFWGGESELLVLSKMLKQPIIVYipeseaknggwGSGFIPIQKYGEEfakgtKGRKGRkpVRLLYSGsNHYDLL 158
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
149-271 3.79e-05

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: 43.03  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 149 LTRTVVPADNSCLFTSVyyvVEGGVLNP-----------ACAPEMRRLIAQIVASDPD-FYSEAILGKTN-QEYCDWIKR 215
Cdd:cd22746    2 LRVVPVKGDGRCLFRAV---ARGLALATggrplserrerADADALRKAVVEEIRKRRDeLFEGSLVIEGDfDAYCQRMSH 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795097409 216 DDTWGGAIEISILSKFYQCEICV--VDTQTV---RIDRFGEdaGYTKR---VLLIYDGIHYDPL 271
Cdd:cd22746   79 PDTWGGEPELLMLADVLQRPIAVylPTPGKGglrKIQEYGE--EYLGGepiRLLYNGGNHYDLL 140
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
207-269 6.52e-05

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: 42.49  E-value: 6.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795097409 207 QEYCDWIKRDDTWGGAIEISILSKFYQCEICVVDTQTVRIdRFGEDAGYTKRVLLIYD------GIHYD 269
Cdd:cd22761   76 EKYCDDVENTGAWGGQLELRALSHVLKRPIEVIQAEGPPI-IIGEEFKSGKPLILTYHrhayglGEHYN 143
OTU_plant_OTU4-like cd22760
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; ...
149-272 2.53e-04

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: 40.44  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 149 LTRTVVPADNSCLFTSVYYVVEGGVLNPACAPEMRRLIAQ---------IVASDPDfySEAILGKTNQEYCDWIKRDDTW 219
Cdd:cd22760    2 YRVHGIAGDGRCLFRAVAHGECLARGKAAPDEERERELADelrtraadeLVKRREE--TEWFIEGDFDEYVARMRRPGVW 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 795097409 220 GGAIEISILSKFYQCEICV--VDTQT---VRIDRFGEDAGYTKRVLLIYDGI-HYDPLQ 272
Cdd:cd22760   80 GGEPELLMLSHVLQRPITVymADEGEgglISIAEYGQEYGKGNPIRVLFHGFgHYEALL 138
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
154-268 8.23e-04

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: 39.08  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSV---YYvvegGvlNPACAPEMRRLIAQIVASDPDFY-------SEAILGKTNQEYCDWIKRDDTWGGAI 223
Cdd:cd22756    5 ITGDGNCLFRALsdqLY----G--DPDRHLEIRAEVVEYMRANPDDFkpfseaaTFAEDDEAFEDYLARMAKDGTYGDNL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 795097409 224 EISILSKFYQCEICV--VDTQTVRIDRFGEDAGYTKRVLLI--YDGIHY 268
Cdd:cd22756   79 EIVAFARAYNVDVKVyqPDPVYVISAPEDGSPGPARRVLHIayHNWEHY 127
Ubl1_ISG15 cd01792
ubiquitin-like (Ubl) domain 1 found in interferon-stimulated gene 15 (ISG15) and similar ...
47-122 1.58e-03

ubiquitin-like (Ubl) domain 1 found in interferon-stimulated gene 15 (ISG15) and similar proteins; ISG15, also termed interferon-induced 15 kDa protein, or interferon-induced 17 kDa protein (IP17), or ubiquitin cross-reactive protein (UCRP), is an antiviral interferon-induced ubiquitin-like protein (Ubl) that upon viral infection, modifies cellular and viral proteins by mechanisms similar to ubiquitination. Although ISG15 has properties similar to those of other Ubl molecules, it is a unique member of the Ubl superfamily, whose expression and conjugation to target proteins are tightly regulated by specific signaling pathways, indicating it may have specialized functions in the immune system. ISG15 contains two tandem Ubl domains with a beta-grasp Ubl fold. This family corresponds to the first Ubl domain.


Pssm-ID: 340490  Cd Length: 75  Bit Score: 36.75  E-value: 1.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795097409  47 WRLRCKAKDGTHVLQGLSSRTRVRELQSQIAAITGIAPDGQRILVgyPPECLDLSNGDTILE-DLPIQSGDMLIVEE 122
Cdd:cd01792    1 WDLTVKMLTGNEFQVSVSPSMTVSELKAQITQKIGVPAFQQRLAV--QPSGVELQDGVRLASqGLGPSSTVLLVVKK 75
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
154-233 1.89e-03

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: 37.95  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSVYYVVEGGVLNpacAPEMRRLIAQIVASD-PDFYSEAILGKTN-----QEYCDWIKRDDTWGGAIEISI 227
Cdd:cd22757    6 IPGDGACLFRALSYLLYGTQSR---HLEVRKEVVDYVVNNwDEFSIYTHDSEGNnyksaEEYRADMSKPGTYGTLCELVA 82

                 ....*.
gi 795097409 228 LSKFYQ 233
Cdd:cd22757   83 AAELYP 88
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
154-269 2.19e-03

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: 37.53  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSVYYVVEGGvlnpacaPEMRRLIAQI----VASDPDFYSEAILGKTNqEYCDWIKRDDTWGGAIEISILS 229
Cdd:cd22752    7 MEEDGNCLFRAVADQVYGD-------QEMHDVVRKHcmdyMEKNRDYFSQFVTEDFE-EYINRKRQDGVWGNHIEIQAMS 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 795097409 230 KFYQCEICVVDTQTVRIDRFGE--DAGYTKRVLLIYDGIHYD 269
Cdd:cd22752   79 ELYNRPIEVYAYSTEPINTFHEasSSDNEPIRLSYHGNSHYN 120
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
49-120 4.38e-03

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 35.26  E-value: 4.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795097409  49 LRCKAKDG-THVLQgLSSRTRVRELQSQIAAITGIAPDGQRILV-GYPpecldLSNGDTiLEDLPIQSGDMLIV 120
Cdd:cd17039    1 ITVKTLDGkTYTVE-VDPDDTVADLKEKIEEKTGIPVEQQRLIYnGKE-----LKDDKT-LSDYGIKDGSTIHL 67
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
154-270 9.16e-03

OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains, and similar proteins; This subfamily is composed of mostly uncharacterized proteins containing an OTU domain, similar to Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and OTU domains. OTU domain-containing proteins function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 36.08  E-value: 9.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409 154 VPADNSCLFTSVYYVVEGgvlNPACAPEMRRLIAQIVASDPDFYSEaILGKTNQEYCDWIKR-----DDTWGGAIEISIL 228
Cdd:cd22755    6 IVGDGNCFFRALSYAITG---SEKYHRKIRKAIVDFLEKNPDEFRN-LLRSDYESVEEYLEKsrmryDGTWATDVEIFAA 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 795097409 229 SKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLL---IY----DGIHYDP 270
Cdd:cd22755   82 ATLLGVDIYVYSKGGYKWLLYSPRFKLGKRNGSreaIYlkntNGNHFEP 130
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
64-145 9.69e-03

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 35.34  E-value: 9.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795097409  64 SSRTRVRELQSQIAAITGIAPDGQRILVGyppeCLDLSNGDTILEDLPIQSGDMLIVEEDQTRPKSSPAFTKRGASSYVR 143
Cdd:cd01795   13 SSTTTLKELKLQIMEKFSVAPFDQHLYFN----GRELTDDSATLADLGILPGDVLYLKVDEPPDDPDDADEADVSRARVP 88

                 ..
gi 795097409 144 ET 145
Cdd:cd01795   89 EE 90
 
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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