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Conserved domains on  [gi|1904824923|gb|QNS29864|]
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RNA-dependent RNA polymerase [Kasokero virus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Bunya_RdRp super family cl20265
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2090-2707 3.88e-76

Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome consisting of 3 ssRNA segments (called L, M and S). The nucleocapsid protein is encode on the small (S) genomic RNA. The L segment codes for an RNA polymerase. This family contains the RNA dependent RNA polymerase on the L segment.


The actual alignment was detected with superfamily member pfam04196:

Pssm-ID: 282102  Cd Length: 739  Bit Score: 271.27  E-value: 3.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2090 ILKLSNLIFLICLSCPWCVQYKTFEAIMMRNVA----EAPGFNLPKSSTSLRELHPDSIIFLMVRDSCLDVSESDSILCT 2165
Cdd:pfam04196   23 VMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSlleiFDPSRYVIMLGLSIYSNIPSYIAKKFEPLSKTLRSVYMVRLIK 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2166 KYCMCLFTVNELPYTSAMNSHGE----FMYKSPNEQLIGRVKGIMAATGLDDSRSDFKWTVCLIANSNFEVARKITGRSN 2241
Cdd:pfam04196  103 RLLFTLFDQNGEPFKRSIYLGDLnddqKGITNERLLDSITFPILSTLKELINNVYLGFYLKNKGLHENHNVMIDLLKKIL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2242 G-ERLPRSVRSK-VIYEI-----VKLVDSTEMAILQQLAFS-YILDPNHRFFAVLAPKAQLGGHRDLLvQETGTKVVHAA 2313
Cdd:pfam04196  183 EwELKFREVRSKkLGKPVngailVHLVSISYLADLCRHNLLrNRLENRHNFKAPITTISTLTSSKLCL-QIGTFAVIKAL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2314 TEMFSRTLLSTTKDDGLTN----THLKETILNCGLEAINQF-KVIHGKEVSKDTGQYYFYKVCCISGDNTKWGPIHCCSI 2388
Cdd:pfam04196  262 QSNFSKNWLEKTSRKLRNInptfVEDKGTNLEVGEDNYEHLsKAIEYIETKVKDKLYEKNKSVVLKLKPEIEEPMDMMKK 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2389 FSGMMQQLLKDYDDWTsfYKLTFLKNLLRQVEIPaASVKKILNSFRYKNKD-IKVDQLTEAELRDEMANRLSTWDGNNVI 2467
Cdd:pfam04196  342 EFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY-AVERISRAILKLNPSEmISEPKDKKILAISEKHEMEARWTVEDTF 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2468 KFLVENYISKGKMaiNSYNHMGQGIHHATSSVLTSIMAEINERLIVNFCNQRLPDLQVTVTHaGSSDDYAKCIVLSGVLT 2547
Cdd:pfam04196  419 KTLSTSDDAISKK--NQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKFLGLYLLCNY-MSKTDLLPSDILLNLVD 495
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2548 ESAMENYEEAFWPTMCNLKNYLSGFNRACQ-MKDSAKTLVSDCFFEFYSEFMMsqRITPAVIKFILTGLINSSVTSPLSL 2626
Cdd:pfam04196  496 QKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK--RAIKLLDGSCLVNSIVHSDDSQTSI 573
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2627 VQACQVSSQQALFNSVpLITNIAFTVFRQQMFFNHTeYFTRTYGPITMgSLSPFGRLYVpkFSGLISSSIAIEDAEEVIK 2706
Cdd:pfam04196  574 SIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCI-YASPKKTYVTL-TVKEFNSEFF--FSGEVSSSLLRWLLASVSD 648

                   .
gi 1904824923 2707 S 2707
Cdd:pfam04196  649 C 649
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
8-156 1.83e-71

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: 236.73  E-value: 1.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923    8 VWEELYEGSYSNVNKFQFNNYFDVDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEVMEMDRRYQSPEAY 87
Cdd:cd21880      1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLYYLSLEEY 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904824923   88 IEDLMNDQYWGGSVEAEILSKALNMTIHIWVSGDGVWVNNARRWGAEQIHASLNLIHVhGGHFNLLLPK 156
Cdd:cd21880     81 LRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLNLLHS-GGHFDALRLK 148
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2090-2707 3.88e-76

Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome consisting of 3 ssRNA segments (called L, M and S). The nucleocapsid protein is encode on the small (S) genomic RNA. The L segment codes for an RNA polymerase. This family contains the RNA dependent RNA polymerase on the L segment.


Pssm-ID: 282102  Cd Length: 739  Bit Score: 271.27  E-value: 3.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2090 ILKLSNLIFLICLSCPWCVQYKTFEAIMMRNVA----EAPGFNLPKSSTSLRELHPDSIIFLMVRDSCLDVSESDSILCT 2165
Cdd:pfam04196   23 VMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSlleiFDPSRYVIMLGLSIYSNIPSYIAKKFEPLSKTLRSVYMVRLIK 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2166 KYCMCLFTVNELPYTSAMNSHGE----FMYKSPNEQLIGRVKGIMAATGLDDSRSDFKWTVCLIANSNFEVARKITGRSN 2241
Cdd:pfam04196  103 RLLFTLFDQNGEPFKRSIYLGDLnddqKGITNERLLDSITFPILSTLKELINNVYLGFYLKNKGLHENHNVMIDLLKKIL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2242 G-ERLPRSVRSK-VIYEI-----VKLVDSTEMAILQQLAFS-YILDPNHRFFAVLAPKAQLGGHRDLLvQETGTKVVHAA 2313
Cdd:pfam04196  183 EwELKFREVRSKkLGKPVngailVHLVSISYLADLCRHNLLrNRLENRHNFKAPITTISTLTSSKLCL-QIGTFAVIKAL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2314 TEMFSRTLLSTTKDDGLTN----THLKETILNCGLEAINQF-KVIHGKEVSKDTGQYYFYKVCCISGDNTKWGPIHCCSI 2388
Cdd:pfam04196  262 QSNFSKNWLEKTSRKLRNInptfVEDKGTNLEVGEDNYEHLsKAIEYIETKVKDKLYEKNKSVVLKLKPEIEEPMDMMKK 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2389 FSGMMQQLLKDYDDWTsfYKLTFLKNLLRQVEIPaASVKKILNSFRYKNKD-IKVDQLTEAELRDEMANRLSTWDGNNVI 2467
Cdd:pfam04196  342 EFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY-AVERISRAILKLNPSEmISEPKDKKILAISEKHEMEARWTVEDTF 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2468 KFLVENYISKGKMaiNSYNHMGQGIHHATSSVLTSIMAEINERLIVNFCNQRLPDLQVTVTHaGSSDDYAKCIVLSGVLT 2547
Cdd:pfam04196  419 KTLSTSDDAISKK--NQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKFLGLYLLCNY-MSKTDLLPSDILLNLVD 495
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2548 ESAMENYEEAFWPTMCNLKNYLSGFNRACQ-MKDSAKTLVSDCFFEFYSEFMMsqRITPAVIKFILTGLINSSVTSPLSL 2626
Cdd:pfam04196  496 QKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK--RAIKLLDGSCLVNSIVHSDDSQTSI 573
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2627 VQACQVSSQQALFNSVpLITNIAFTVFRQQMFFNHTeYFTRTYGPITMgSLSPFGRLYVpkFSGLISSSIAIEDAEEVIK 2706
Cdd:pfam04196  574 SIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCI-YASPKKTYVTL-TVKEFNSEFF--FSGEVSSSLLRWLLASVSD 648

                   .
gi 1904824923 2707 S 2707
Cdd:pfam04196  649 C 649
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
8-156 1.83e-71

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: 236.73  E-value: 1.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923    8 VWEELYEGSYSNVNKFQFNNYFDVDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEVMEMDRRYQSPEAY 87
Cdd:cd21880      1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLYYLSLEEY 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904824923   88 IEDLMNDQYWGGSVEAEILSKALNMTIHIWVSGDGVWVNNARRWGAEQIHASLNLIHVhGGHFNLLLPK 156
Cdd:cd21880     81 LRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLNLLHS-GGHFDALRLK 148
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
35-150 4.27e-08

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


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 54.38  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   35 PGDGTCFFSSVSKYIFNTTEMWK-----TVKSTCANYARAHWQEVMEMdrrYQSPEA-YIEDLMNDQYWGGSVEAEILSK 108
Cdd:pfam02338    1 PGDGNCLYRSISHQLWGVHDVLRkmlvqELRETLAEYMREHKEEFEPF---LEDDETgDIIEIEQTGAWGGEIEIFALAH 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1904824923  109 ALNMTIHIWVSGDGV--------WVNNARRWGAEQIHASLNLIHVHGGHF 150
Cdd:pfam02338   78 ILRRPIIVYKSEGGEelgglkeyGIYLPLGWDPSLCLVYPRHLYYLGGHY 127
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2090-2707 3.88e-76

Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome consisting of 3 ssRNA segments (called L, M and S). The nucleocapsid protein is encode on the small (S) genomic RNA. The L segment codes for an RNA polymerase. This family contains the RNA dependent RNA polymerase on the L segment.


Pssm-ID: 282102  Cd Length: 739  Bit Score: 271.27  E-value: 3.88e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2090 ILKLSNLIFLICLSCPWCVQYKTFEAIMMRNVA----EAPGFNLPKSSTSLRELHPDSIIFLMVRDSCLDVSESDSILCT 2165
Cdd:pfam04196   23 VMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSlleiFDPSRYVIMLGLSIYSNIPSYIAKKFEPLSKTLRSVYMVRLIK 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2166 KYCMCLFTVNELPYTSAMNSHGE----FMYKSPNEQLIGRVKGIMAATGLDDSRSDFKWTVCLIANSNFEVARKITGRSN 2241
Cdd:pfam04196  103 RLLFTLFDQNGEPFKRSIYLGDLnddqKGITNERLLDSITFPILSTLKELINNVYLGFYLKNKGLHENHNVMIDLLKKIL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2242 G-ERLPRSVRSK-VIYEI-----VKLVDSTEMAILQQLAFS-YILDPNHRFFAVLAPKAQLGGHRDLLvQETGTKVVHAA 2313
Cdd:pfam04196  183 EwELKFREVRSKkLGKPVngailVHLVSISYLADLCRHNLLrNRLENRHNFKAPITTISTLTSSKLCL-QIGTFAVIKAL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2314 TEMFSRTLLSTTKDDGLTN----THLKETILNCGLEAINQF-KVIHGKEVSKDTGQYYFYKVCCISGDNTKWGPIHCCSI 2388
Cdd:pfam04196  262 QSNFSKNWLEKTSRKLRNInptfVEDKGTNLEVGEDNYEHLsKAIEYIETKVKDKLYEKNKSVVLKLKPEIEEPMDMMKK 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2389 FSGMMQQLLKDYDDWTsfYKLTFLKNLLRQVEIPaASVKKILNSFRYKNKD-IKVDQLTEAELRDEMANRLSTWDGNNVI 2467
Cdd:pfam04196  342 EFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY-AVERISRAILKLNPSEmISEPKDKKILAISEKHEMEARWTVEDTF 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2468 KFLVENYISKGKMaiNSYNHMGQGIHHATSSVLTSIMAEINERLIVNFCNQRLPDLQVTVTHaGSSDDYAKCIVLSGVLT 2547
Cdd:pfam04196  419 KTLSTSDDAISKK--NQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKFLGLYLLCNY-MSKTDLLPSDILLNLVD 495
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2548 ESAMENYEEAFWPTMCNLKNYLSGFNRACQ-MKDSAKTLVSDCFFEFYSEFMMsqRITPAVIKFILTGLINSSVTSPLSL 2626
Cdd:pfam04196  496 QKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK--RAIKLLDGSCLVNSIVHSDDSQTSI 573
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923 2627 VQACQVSSQQALFNSVpLITNIAFTVFRQQMFFNHTeYFTRTYGPITMgSLSPFGRLYVpkFSGLISSSIAIEDAEEVIK 2706
Cdd:pfam04196  574 SIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCI-YASPKKTYVTL-TVKEFNSEFF--FSGEVSSSLLRWLLASVSD 648

                   .
gi 1904824923 2707 S 2707
Cdd:pfam04196  649 C 649
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
8-156 1.83e-71

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: 236.73  E-value: 1.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923    8 VWEELYEGSYSNVNKFQFNNYFDVDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEVMEMDRRYQSPEAY 87
Cdd:cd21880      1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLYYLSLEEY 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904824923   88 IEDLMNDQYWGGSVEAEILSKALNMTIHIWVSGDGVWVNNARRWGAEQIHASLNLIHVhGGHFNLLLPK 156
Cdd:cd21880     81 LRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLNLLHS-GGHFDALRLK 148
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
31-153 4.96e-21

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: 91.34  E-value: 4.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   31 VDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEVMEMDRRYQ----SPEAYIEDLMNDQYWGGSVEAEIL 106
Cdd:cd22744      2 VVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPAELADEddgeDFDEYLQRMRKPGTWGGELELQAL 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1904824923  107 SKALNMTIHIWVSGDGVW----VNNARRWGAEQIHaslnLIHVHGGHFNLL 153
Cdd:cd22744     82 ANALNVPIVVYSEDGGFLpvsvFGPGPGPSGRPIH----LLYTGGNHYDAL 128
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
29-120 1.04e-12

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: 67.61  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   29 FDVDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEV-----MEMDRRYQSPEAYIEDLMNDQYWGGSVEA 103
Cdd:cd22757      1 FRVIPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFsiythDSEGNNYKSAEEYRADMSKPGTYGTLCEL 80
                           90
                   ....*....|....*..
gi 1904824923  104 EILSKALNMTIHIWVSG 120
Cdd:cd22757     81 VAAAELYPFHFEVYRNG 97
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
31-154 8.86e-10

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


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 59.58  E-value: 8.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   31 VDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEVMEMDR-RYQSPEAYIEDLM--NDQYWGGSVEAEILS 107
Cdd:cd22755      3 TIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLRsDYESVEEYLEKSRmrYDGTWATDVEIFAAA 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1904824923  108 KALNMTIHIWVSGDGVWV-------NNARRWGAEQIHaslnLIHVHGGHFNLLL 154
Cdd:cd22755     83 TLLGVDIYVYSKGGYKWLlysprfkLGKRNGSREAIY----LKNTNGNHFEPVV 132
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
29-151 1.29e-08

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; Deubiquitinating enzyme OTU6, also called OTU domain-containing protein 6 or otubain-like deubiquitinase 1 (OTLD1), is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU6 binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. OTU6 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438617 [Multi-domain]  Cd Length: 128  Bit Score: 55.89  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   29 FDVDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYarahwqevMEMDRRYQSP------EAYIEDLMNDQYWGGSVE 102
Cdd:cd22796      5 LEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDY--------MEKERDHFSQfvtedfTQYVKRKRRDRVFGNNLE 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1904824923  103 AEILSKALNMTIHIWVSGDGVWVNNARRwGAEQIHASLNLIHVHGGHFN 151
Cdd:cd22796     77 IQAMSEIYNRPIEVYSYSNGEPINIFHG-SYEGDDPPIRLSYHDGNHYN 124
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
35-155 1.68e-08

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: 55.63  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   35 PGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEVMEMDRryQSPEAYIEDLMNDQYWGGSVEAEILSKALNMTI 114
Cdd:cd22753     16 PRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFSE--ISFDDYLERLSDPKEWGGLLELEALSLLYKVDF 93
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1904824923  115 HIWVSGDGVWVNNARRWGAEQIHaslnLIHVHGGHFNLLLP 155
Cdd:cd22753     94 IVYSIPDQPPSNITNNGYPKKIM----LCYSGGNHYDSVYS 130
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
35-150 4.27e-08

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


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 54.38  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   35 PGDGTCFFSSVSKYIFNTTEMWK-----TVKSTCANYARAHWQEVMEMdrrYQSPEA-YIEDLMNDQYWGGSVEAEILSK 108
Cdd:pfam02338    1 PGDGNCLYRSISHQLWGVHDVLRkmlvqELRETLAEYMREHKEEFEPF---LEDDETgDIIEIEQTGAWGGEIEIFALAH 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1904824923  109 ALNMTIHIWVSGDGV--------WVNNARRWGAEQIHASLNLIHVHGGHF 150
Cdd:pfam02338   78 ILRRPIIVYKSEGGEelgglkeyGIYLPLGWDPSLCLVYPRHLYYLGGHY 127
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
29-150 3.66e-07

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: 51.89  E-value: 3.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   29 FDVDEMPGDGTCFFSSVSKYIFNTTEMW--KTVKSTCANYARAH---WQE-VMEMDRRYQSPEAYIEDLMNDQYWGGSVE 102
Cdd:cd22758      6 FEIRDVPGDGNCFFHAVSDQLYGNGIEHshKELRQQAVNYLRENpelYDGfFLSEFDEEESWEEYLNRMSKDGTWGDHII 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1904824923  103 AEILSKALNMTIHIWVSGDGVWVNNARRWGAEQIhASLNLIHVHGGHF 150
Cdd:cd22758     86 LQAAANLFNVRIVIISSDGSDETTIIEPGNSKNG-RTIYLGHIGENHY 132
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
33-151 4.63e-07

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: 51.79  E-value: 4.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   33 EMPGDGTCFFSSVS---KYIFNTTEMW--KTVKSTCANYARAHWQE----VMEMDRRYQSP---EAYIEDLMNDQYWGGS 100
Cdd:cd22748     10 EIPPDGHCLYRAIAdqlKLRGGSEEPYsyKELRKLAADYMRAHRDDflpfLTNDDGDLMTEeefEEYCDKIENTAEWGGQ 89
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1904824923  101 VEAEILSKALNMTIHIWVSGDGVWVnnarrWGAEQIHAS-LNL-IHVH----GGHFN 151
Cdd:cd22748     90 LELRALSKALKRPIHVYQAGSPPLV-----IGEEFDSGEpLRLsYHRHayglGEHYN 141
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
33-115 1.12e-06

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: 51.33  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   33 EMPGDGTCFFSSVSkYIFNTTEMWKTVK--STCANYARAH---WQEVM-EMdrryqSPEAYIEDLMNDQYWGGSVEAEIL 106
Cdd:cd22745      7 VVPDDNSCLFTSIS-YLLEGGLLDSAPElrEIVADAILSDpdtYNEAIlGK-----PPDEYCAWILKPDSWGGAIELSIL 80

                   ....*....
gi 1904824923  107 SKALNMTIH 115
Cdd:cd22745     81 SKHFGVEIC 89
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
33-153 1.49e-06

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: 50.30  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   33 EMPGDGTCFFSSVS---KYIFNTTEM-WKTVKSTCANYARAH--------WQEVMEMdrryQSPEAYIEDLMNDQYWGGS 100
Cdd:cd22762     11 DIKPDGHCLFAAIAdqlQLRGSEINLdYKELRKLAAEYIRKHpddfepflFEETDEL----EDIDEYCKKIENTAEWGGE 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1904824923  101 VEAEILSKALNMTIHIWVSGDGVWVNNArrwGAEQIHASLNLI-HVH----GGHFNLL 153
Cdd:cd22762     87 LELLALAKAFGVPIHVVQAEGRVIKINE---EGDSDKPELWLAyYKHsyglGEHYNSL 141
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
33-151 1.82e-06

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: 49.86  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   33 EMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAH---WQEVMEMDRRYqspEAYIEDLMNDQYWGGSVEAEILSKA 109
Cdd:cd22771      6 DVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHeedFEPFFEDDETF---EDYVSRMREDGTWGGNLELQAASLV 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1904824923  110 LNMTIHIWVSGDGVW-VNNARRWGAEQIHASLnlihvHGG-HFN 151
Cdd:cd22771     83 YRVNIVVHQLGQPRWeIENFPDKGARTIHLSY-----HDGeHYN 121
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
33-125 1.03e-05

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: 47.55  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   33 EMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAH------WQEVM---EMDRRYqspEAYIEDLMNDQYWGGSVEA 103
Cdd:cd22756      4 DITGDGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANpddfkpFSEAAtfaEDDEAF---EDYLARMAKDGTYGDNLEI 80
                           90       100
                   ....*....|....*....|..
gi 1904824923  104 EILSKALNMTIHIWvSGDGVWV 125
Cdd:cd22756     81 VAFARAYNVDVKVY-QPDPVYV 101
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
29-119 1.69e-05

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: 46.77  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   29 FDVDEMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYarahwqevMEMDRRYQSP------EAYIEDLMNDQYWGGSVE 102
Cdd:cd22752      2 FIIKEMEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDY--------MEKNRDYFSQfvtedfEEYINRKRQDGVWGNHIE 73
                           90
                   ....*....|....*..
gi 1904824923  103 AEILSKALNMTIHIWVS 119
Cdd:cd22752     74 IQAMSELYNRPIEVYAY 90
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
33-126 2.82e-05

OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This subfamily contains Arabidopsis thaliana deubiquitinating enzymes OTU8, OTU9, OTU10, OTU11, and OTU12, and similar proteins from plants and other eukaryotes. OTU8-OTU12 are deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438588 [Multi-domain]  Cd Length: 134  Bit Score: 46.38  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   33 EMPGDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHWQEVMEM--DRRYqspEAYIEDLMNDQYWGGSVEAEILSKAL 110
Cdd:cd22751     14 KVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPELYYEFyvPEEY---DEYLKKMSKDGEWGDELTLQAAADAF 90
                           90
                   ....*....|....*.
gi 1904824923  111 NMTIHIWVSGDGVWVN 126
Cdd:cd22751     91 GVKIHVITSFEDNWFL 106
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
36-107 3.28e-05

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


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 46.21  E-value: 3.28e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1904824923   36 GDGTCFFSSVSKYIFNTTEMWKTVKSTCANYARAHwQEVMEMdrRYQSP-EAYIEDLMNDQYWGGSVEAEILS 107
Cdd:cd22794     17 KDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRN-REKFEA--FIEGPfEQYLKNLENPKEWAGQVEISALS 86
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
35-156 2.02e-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: 43.37  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904824923   35 PGDGTCFFSSVSKYI-FNTTEMwktvKSTCanyarahwqevmeMDRRYQSPEAYIE--DLMNDQYWGgsvEAEIL---SK 108
Cdd:cd22792      6 PGDGNCFWHSLGHFLgLSALEL----KKLL-------------RDSLFDDPELDEEldEQLEPGVYA---EDEAIaaaAK 65
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1904824923  109 ALNMTIHIWVSGDGVWVNNarrwGAEQIHASLNLIHVhGGHFNLLLPK 156
Cdd:cd22792     66 LFGVNICVHDPDEGVLYTF----TPNESSKSIHLLLE-NEHFEPLVPK 108
 
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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