NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|807643940|gb|AKC89346|]
View 

RNA-dependent RNA-polymerase, partial [Caspiy virus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
2078-2697 1.39e-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: 272.42  E-value: 1.39e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2078 NDELMKLMNLVFYICLCCPWCVHYKSLENFLSKHMDETGGYDF-------GNTTVSKVMDITLEKVWKLAlkehFNIDSD 2150
Cdd:pfam04196   20 TYEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPsryvimlGLSIYSNIPSYIAKKFEPLS----KTLRSV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2151 IELLkYVVKYTSAMFTGNGRPISCSLSTQSSTINVLEHGQMVD----KLRIFLTKSQLYTKELDFIWTCHMITNSNFEVT 2226
Cdd:pfam04196   96 YMVR-LIKRLLFTLFDQNGEPFKRSIYLGDLNDDQKGITNERLldsiTFPILSTLKELINNVYLGFYLKNKGLHENHNVM 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2227 KRLTGRTTG-ERLPRSVRSKVV------YEIIKVVGESGHAILQQLAFS-GILNTEHEFFAVLAPKAQLGGHRDLLvQET 2298
Cdd:pfam04196  175 IDLLKKILEwELKFREVRSKKLgkpvngAILVHLVSISYLADLCRHNLLrNRLENRHNFKAPITTISTLTSSKLCL-QIG 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2299 YTKLIHATSEMFSRTLLATTNDDGLTTS----HLKE-NILCSALNCIELSKKTHGAPVEDNDKLKHFYKVFCISGDNTKW 2373
Cdd:pfam04196  254 TFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGtNLEVGEDNYEHLSKAIEYIETKVKDKLYEKNKSVVLKLKPEIE 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2374 GPIHCCSFFSGMMQQLLKDHPDWSsfYKLVFLKNLYRQVEIPAgSIKKILNAFRFNNVDKKIEEMN-EFQLRNLLVETVD 2452
Cdd:pfam04196  334 EPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQYA-VERISRAILKLNPSEMISEPKDkKILAISEKHEMEA 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2453 EWNENPIIKFLIVTYLAQGKvaMRMYNHMGQGIHHATSSILTSIMGDVITHFIKLYVQRNFKGLTSHVEHaGSSDDYAKI 2532
Cdd:pfam04196  411 RWTVEDTFKTLSTSDDAISK--KNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKFLGLYLLCNY-MSKTDLLPS 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2533 IVVSGIIPKSAFEAYEKQFWPRMCRLKNIISGISRACQ-MKDSAKTLAGDAFIEFYSEFMLshRITPAVIKFIFTGLINS 2611
Cdd:pfam04196  488 DILLNLVDQKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK--RAIKLLDGSCLVNSIVH 565
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2612 SVTSPQSMAQACQVSSQQAMYNSVpLLTNFAFTVLRQQMFMNHTeYFQRTYGLITTgSLSAFGRLYLpqYSNLTCSSVAI 2691
Cdd:pfam04196  566 SDDSQTSISIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCI-YASPKKTYVTL-TVKEFNSEFF--FSGEVSSSLLR 640

                   ....*.
gi 807643940  2692 EDSETI 2697
Cdd:pfam04196  641 WLLASV 646
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
5-178 1.05e-69

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: 231.33  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940    5 VWQPLTPGMYTSWIRVCVHDFFNIGRVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNWSECTMAKdeynarahk 84
Cdd:cd21880     1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEAR--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   85 trksysevvankdiptaTNQDGLALYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNNDYKVVGVQRYGNKPVSASFN 164
Cdd:cd21880    72 -----------------LYYLSLEEYLRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLN 134
                         170
                  ....*....|....
gi 807643940  165 LMLIDGHFDALTLQ 178
Cdd:cd21880   135 LLHSGGHFDALRLK 148
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2078-2697 1.39e-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: 272.42  E-value: 1.39e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2078 NDELMKLMNLVFYICLCCPWCVHYKSLENFLSKHMDETGGYDF-------GNTTVSKVMDITLEKVWKLAlkehFNIDSD 2150
Cdd:pfam04196   20 TYEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPsryvimlGLSIYSNIPSYIAKKFEPLS----KTLRSV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2151 IELLkYVVKYTSAMFTGNGRPISCSLSTQSSTINVLEHGQMVD----KLRIFLTKSQLYTKELDFIWTCHMITNSNFEVT 2226
Cdd:pfam04196   96 YMVR-LIKRLLFTLFDQNGEPFKRSIYLGDLNDDQKGITNERLldsiTFPILSTLKELINNVYLGFYLKNKGLHENHNVM 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2227 KRLTGRTTG-ERLPRSVRSKVV------YEIIKVVGESGHAILQQLAFS-GILNTEHEFFAVLAPKAQLGGHRDLLvQET 2298
Cdd:pfam04196  175 IDLLKKILEwELKFREVRSKKLgkpvngAILVHLVSISYLADLCRHNLLrNRLENRHNFKAPITTISTLTSSKLCL-QIG 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2299 YTKLIHATSEMFSRTLLATTNDDGLTTS----HLKE-NILCSALNCIELSKKTHGAPVEDNDKLKHFYKVFCISGDNTKW 2373
Cdd:pfam04196  254 TFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGtNLEVGEDNYEHLSKAIEYIETKVKDKLYEKNKSVVLKLKPEIE 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2374 GPIHCCSFFSGMMQQLLKDHPDWSsfYKLVFLKNLYRQVEIPAgSIKKILNAFRFNNVDKKIEEMN-EFQLRNLLVETVD 2452
Cdd:pfam04196  334 EPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQYA-VERISRAILKLNPSEMISEPKDkKILAISEKHEMEA 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2453 EWNENPIIKFLIVTYLAQGKvaMRMYNHMGQGIHHATSSILTSIMGDVITHFIKLYVQRNFKGLTSHVEHaGSSDDYAKI 2532
Cdd:pfam04196  411 RWTVEDTFKTLSTSDDAISK--KNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKFLGLYLLCNY-MSKTDLLPS 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2533 IVVSGIIPKSAFEAYEKQFWPRMCRLKNIISGISRACQ-MKDSAKTLAGDAFIEFYSEFMLshRITPAVIKFIFTGLINS 2611
Cdd:pfam04196  488 DILLNLVDQKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK--RAIKLLDGSCLVNSIVH 565
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2612 SVTSPQSMAQACQVSSQQAMYNSVpLLTNFAFTVLRQQMFMNHTeYFQRTYGLITTgSLSAFGRLYLpqYSNLTCSSVAI 2691
Cdd:pfam04196  566 SDDSQTSISIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCI-YASPKKTYVTL-TVKEFNSEFF--FSGEVSSSLLR 640

                   ....*.
gi 807643940  2692 EDSETI 2697
Cdd:pfam04196  641 WLLASV 646
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
5-178 1.05e-69

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: 231.33  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940    5 VWQPLTPGMYTSWIRVCVHDFFNIGRVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNWSECTMAKdeynarahk 84
Cdd:cd21880     1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEAR--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   85 trksysevvankdiptaTNQDGLALYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNNDYKVVGVQRYGNKPVSASFN 164
Cdd:cd21880    72 -----------------LYYLSLEEYLRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLN 134
                         170
                  ....*....|....
gi 807643940  165 LMLIDGHFDALTLQ 178
Cdd:cd21880   135 LLHSGGHFDALRLK 148
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2078-2697 1.39e-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: 272.42  E-value: 1.39e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2078 NDELMKLMNLVFYICLCCPWCVHYKSLENFLSKHMDETGGYDF-------GNTTVSKVMDITLEKVWKLAlkehFNIDSD 2150
Cdd:pfam04196   20 TYEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPsryvimlGLSIYSNIPSYIAKKFEPLS----KTLRSV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2151 IELLkYVVKYTSAMFTGNGRPISCSLSTQSSTINVLEHGQMVD----KLRIFLTKSQLYTKELDFIWTCHMITNSNFEVT 2226
Cdd:pfam04196   96 YMVR-LIKRLLFTLFDQNGEPFKRSIYLGDLNDDQKGITNERLldsiTFPILSTLKELINNVYLGFYLKNKGLHENHNVM 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2227 KRLTGRTTG-ERLPRSVRSKVV------YEIIKVVGESGHAILQQLAFS-GILNTEHEFFAVLAPKAQLGGHRDLLvQET 2298
Cdd:pfam04196  175 IDLLKKILEwELKFREVRSKKLgkpvngAILVHLVSISYLADLCRHNLLrNRLENRHNFKAPITTISTLTSSKLCL-QIG 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2299 YTKLIHATSEMFSRTLLATTNDDGLTTS----HLKE-NILCSALNCIELSKKTHGAPVEDNDKLKHFYKVFCISGDNTKW 2373
Cdd:pfam04196  254 TFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGtNLEVGEDNYEHLSKAIEYIETKVKDKLYEKNKSVVLKLKPEIE 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2374 GPIHCCSFFSGMMQQLLKDHPDWSsfYKLVFLKNLYRQVEIPAgSIKKILNAFRFNNVDKKIEEMN-EFQLRNLLVETVD 2452
Cdd:pfam04196  334 EPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQYA-VERISRAILKLNPSEMISEPKDkKILAISEKHEMEA 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2453 EWNENPIIKFLIVTYLAQGKvaMRMYNHMGQGIHHATSSILTSIMGDVITHFIKLYVQRNFKGLTSHVEHaGSSDDYAKI 2532
Cdd:pfam04196  411 RWTVEDTFKTLSTSDDAISK--KNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKFLGLYLLCNY-MSKTDLLPS 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2533 IVVSGIIPKSAFEAYEKQFWPRMCRLKNIISGISRACQ-MKDSAKTLAGDAFIEFYSEFMLshRITPAVIKFIFTGLINS 2611
Cdd:pfam04196  488 DILLNLVDQKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK--RAIKLLDGSCLVNSIVH 565
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  2612 SVTSPQSMAQACQVSSQQAMYNSVpLLTNFAFTVLRQQMFMNHTeYFQRTYGLITTgSLSAFGRLYLpqYSNLTCSSVAI 2691
Cdd:pfam04196  566 SDDSQTSISIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCI-YASPKKTYVTL-TVKEFNSEFF--FSGEVSSSLLR 640

                   ....*.
gi 807643940  2692 EDSETI 2697
Cdd:pfam04196  641 WLLASV 646
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
5-178 1.05e-69

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: 231.33  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940    5 VWQPLTPGMYTSWIRVCVHDFFNIGRVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNWSECTMAKdeynarahk 84
Cdd:cd21880     1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEAR--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   85 trksysevvankdiptaTNQDGLALYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNNDYKVVGVQRYGNKPVSASFN 164
Cdd:cd21880    72 -----------------LYYLSLEEYLRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLN 134
                         170
                  ....*....|....
gi 807643940  165 LMLIDGHFDALTLQ 178
Cdd:cd21880   135 LLHSGGHFDALRLK 148
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
28-175 4.89e-20

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: 88.65  E-value: 4.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   28 IGRVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNWsectmakdeynarahktrksysEVVANKDIPTATNQDGL 107
Cdd:cd22744     2 VVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENP----------------------DLYEPAELADEDDGEDF 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807643940  108 ALYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNNDYKvvGVQRYGNKPVSASFNLMLI---DGHFDAL 175
Cdd:cd22744    60 DEYLQRMRKPGTWGGELELQALANALNVPIVVYSEDGGFL--PVSVFGPGPGPSGRPIHLLytgGNHYDAL 128
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
28-147 2.85e-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: 60.74  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   28 IGRVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNwsectmaKDEYNARAHKTRKSYSEvvankdiptatnqdgl 107
Cdd:cd22755     3 TIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKN-------PDEFRNLLRSDYESVEE---------------- 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 807643940  108 alYLNEAS--DDGYWGGSIEAQMLSKALDISIIIWSvNNDYK 147
Cdd:cd22755    60 --YLEKSRmrYDGTWATDVEIFAAATLLGVDIYVYS-KGGYK 98
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
26-175 1.12e-09

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: 59.14  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   26 FNIGRVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNWSECtmakdeynarAHKTRKSYSEVVANKDiptatnqd 105
Cdd:cd22757     1 FRVIPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEF----------SIYTHDSEGNNYKSAE-------- 62
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807643940  106 glaLYLNEASDDGYWGGSIEAQMLSKALDISIIIWsvnNDYKV-VGVQRYGNKPVSASFNLMLIDGHFDAL 175
Cdd:cd22757    63 ---EYRADMSKPGTYGTLCELVAAAELYPFHFEVY---RNGKLyASFGDPSNPVKRLKFSGDLSNGHFDVL 127
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
31-143 2.21e-09

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: 58.34  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   31 VRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNwsectmaKDEYnarahktrKSYSEVVANKDIptatnQDGLALY 110
Cdd:cd22756     5 ITGDGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRAN-------PDDF--------KPFSEAATFAED-----DEAFEDY 64
                          90       100       110
                  ....*....|....*....|....*....|...
gi 807643940  111 LNEASDDGYWGGSIEAQMLSKALDISIIIWSVN 143
Cdd:cd22756    65 LARMAKDGTYGDNLEIVAFARAYNVDVKVYQPD 97
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
31-145 1.07e-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: 50.73  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   31 VRGDGNCFFRSFALLFFGTEDQW--RTVKNTSINYARTNwsectmakdeynarahktRKSYSEVVANKDIPTATNQDgla 108
Cdd:cd22758    11 VPGDGNCFFHAVSDQLYGNGIEHshKELRQQAVNYLREN------------------PELYDGFFLSEFDEEESWEE--- 69
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 807643940  109 lYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNND 145
Cdd:cd22758    70 -YLNRMSKDGTWGDHIILQAAANLFNVRIVIISSDGS 105
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
30-175 5.77e-06

OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar proteins; Deubiquitinating enzyme OTU3 (also called OTU domain-containing protein 3) and deubiquitinating enzyme OTU4 (also called OTU domain-containing protein 4) are deubiquitinases (DUBs) or ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU3 and OTU4 may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 48.80  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   30 RVRGDGNCFFRSFallffgtedqwrtVKNTSINYARTNWSEctmaKDEyNARAHKTRKS-YSEVVANKDIPTATNQDG-- 106
Cdd:cd22746     6 PVKGDGRCLFRAV-------------ARGLALATGGRPLSE----RRE-RADADALRKAvVEEIRKRRDELFEGSLVIeg 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807643940  107 -LALYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNND-YKVVGVQRYGNKPVSA-SFNLMLIDG-HFDAL 175
Cdd:cd22746    68 dFDAYCQRMSHPDTWGGEPELLMLADVLQRPIAVYLPTPGkGGLRKIQEYGEEYLGGePIRLLYNGGnHYDLL 140
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
31-163 2.24e-04

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: 44.09  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   31 VRGDGNCFFRSFAllffgteDQWRTVKNTSINYarTNWSECTMAKDEYnaRAHKtrksysevvaNKDIPTATNQDGLAL- 109
Cdd:cd22748    11 IPPDGHCLYRAIA-------DQLKLRGGSEEPY--SYKELRKLAADYM--RAHR----------DDFLPFLTNDDGDLMt 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940  110 ------YLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNNDYKVVGVQRYGNKPVSASF 163
Cdd:cd22748    70 eeefeeYCDKIENTAEWGGQLELRALSKALKRPIHVYQAGSPPLVIGEEFDSGEPLRLSY 129
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
30-51 1.69e-03

OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU domain-containing protein that is required for the development of thoracic vertebrae in mammals. 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. Vertnin and some subfamily members do not possess the conserved catalytic residues and may not have DUB activity. VRTN gene is associated with variations in vertebral number.


Pssm-ID: 438612  Cd Length: 137  Bit Score: 41.44  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|..
gi 807643940   30 RVRGDGNCFFRSFALLFFGTED 51
Cdd:cd22791     5 RVTGDGNCLFRAASLLLFGDES 26
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
30-47 3.17e-03

Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 (also called ubiquitin thioesterase OTUB1 or OTU domain-containing ubiquitin aldehyde-binding protein 1), otubain-2 (also called ubiquitin thioesterase OTUB2 or OTU domain-containing ubiquitin aldehyde-binding protein 2), and similar proteins. They function as deubiquitylases (DUBs)/ubiquitin thioesterases (EC 3.4.19.12). OTUB1 can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates, while OTUB2 mediates the deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains. The otubain subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Members of this subfamily are classified as family C65 cysteine proteases by MEROPS.


Pssm-ID: 438586 [Multi-domain]  Cd Length: 232  Bit Score: 42.32  E-value: 3.17e-03
                          10
                  ....*....|....*...
gi 807643940   30 RVRGDGNCFFRSFALLFF 47
Cdd:cd22749    37 RVRGDGNCFYRAFAFSYL 54
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
26-145 4.78e-03

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: 40.10  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   26 FNIGRVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYartnwsectMAKDeynaRAHktrksYSEVVAnkdiptatnqD 105
Cdd:cd22796     5 LEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDY---------MEKE----RDH-----FSQFVT----------E 56
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 807643940  106 GLALYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVNND 145
Cdd:cd22796    57 DFTQYVKRKRRDRVFGNNLEIQAMSEIYNRPIEVYSYSNG 96
OTU_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
28-143 5.51e-03

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; Deubiquitinating enzyme OTU5, also called OTU domain-containing protein 6, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU5 is an inactive cysteine protease. It regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). It is required for phosphate (Pi) homeostasis. OTU5 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438618 [Multi-domain]  Cd Length: 149  Bit Score: 40.41  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   28 IGRVRGDGNCFFRSFallffgtEDQWRTVKNTSINYARTNWSEctMAKDeyNARAHKTR-KSYSEVVANKDIPtatnQDG 106
Cdd:cd22797    12 IKEIKADGHCLYRAV-------EDQLQLRGGGAPAPDYQQLRE--LAAD--YMRAHPDDfLPFLEDEDEGGDG----DEA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 807643940  107 LALYLNEASDDGYWGGSIEAQMLSKALDISIIIWSVN 143
Cdd:cd22797    77 FEAYCREVESTAAWGGQLELGALAHALRRHIKVYSAG 113
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
30-121 6.02e-03

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: 39.83  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807643940   30 RVRGDGNCFFRSFALLFFGTEDQWRTVKNTSINYARTNWSEC--TMAKDEYNArahktrksysevvankdiptatnqdgl 107
Cdd:cd22751    14 KVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPELYyeFYVPEEYDE--------------------------- 66
                          90
                  ....*....|....
gi 807643940  108 alYLNEASDDGYWG 121
Cdd:cd22751    67 --YLKKMSKDGEWG 78
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH