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Conserved domains on  [gi|1070640876|ref|YP_009304993|]
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RNA-dependent RNA polymerase [Wenzhou Tick 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 ...
2065-2725 1.23e-72

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: 260.87  E-value: 1.23e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2065 LSFIREEIEVKTLEkAFLESFdHDIMLTINLIFALSLCCPWSIHYKSFELLLSQESSPLADDDQQREHLELLKTLGPCel 2144
Cdd:pfam04196    1 LNKVRCLRLVKAPE-LFWKAT-YEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPSRYVIMLGLSIYSN-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2145 IVDYLKAELDQLKNPEAARTTVEMLYRYCCAIFIANDEPIKSVLNLRDVVVT-SHVEDSAL--STTRSLLAKY-GLEKTD 2220
Cdd:pfam04196   77 IPSYIAKKFEPLSKTLRSVYMVRLIKRLLFTLFDQNGEPFKRSIYLGDLNDDqKGITNERLldSITFPILSTLkELINNV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2221 LDFKWTMNLIANSNFEVTKRLTGRT-EGEKLPRSVRSK-VIY-----EMIKLVKSTGMAILQQHAFS-YILNSGHRFFAV 2292
Cdd:pfam04196  157 YLGFYLKNKGLHENHNVMIDLLKKIlEWELKFREVRSKkLGKpvngaILVHLVSISYLADLCRHNLLrNRLENRHNFKAP 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2293 LAPKAQLGGHRDLLvQEIMTKIVHAATETFSRALLSTTMDDGLTNQ----HLKESILQTAYDQLQMSSHSHGKHLSSLGG 2368
Cdd:pfam04196  237 ITTISTLTSSKLCL-QIGTFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGTNLEVGEDNYEHLSKAIEYIETKVKD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2369 GVRYFSRTFCISGDRTKWGPIHCTSFFSGMMQQLLQDTPDWSsfFKLVMLKNLYRQVEIPsgAIKRL-LNSFRYRAQPTL 2447
Cdd:pfam04196  316 KLYEKNKSVVLKLKPEIEEPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY--AVERIsRAILKLNPSEMI 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2448 PLEQLTEDQIRQLMLDSIDIWEGNHMMQFLVQVYLSKGKMALecYNHMGQGIHHATSSVMTSCMAVLTEELIVSYFQTHM 2527
Cdd:pfam04196  392 SEPKDKKILAISEKHEMEARWTVEDTFKTLSTSDDAISKKNQ--LMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2528 PELSTTVRHaGSSDDYAKVITVAGNLPNSLFERYDERFWHHACRLQNSMVGLARGCQ-MKDSAKTLIGDAMCEFYSEFML 2606
Cdd:pfam04196  470 LGLYLLCNY-MSKTDLLPSDILLNLVDQKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2607 fhRVTPAVIKFILTGLINSSVTSPQSMVQACQVSSQQAMYNSVpLLTNICFTVFRQQMFANHTElFQRKYGPIVHGLpSA 2686
Cdd:pfam04196  549 --RAIKLLDGSCLVNSIVHSDDSQTSISIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCIY-ASPKKTYVTLTV-KE 623
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1070640876 2687 FGRLYLpmFSNLTSSTIAVEDAESIaLDLESAI---DLASRL 2725
Cdd:pfam04196  624 FNSEFF--FSGEVSSSLLRWLLASV-SDCAAEGlsdDLASLS 662
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
20-167 3.18e-59

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: 201.67  E-value: 3.18e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   20 RCKEI-EQCLGMSMITNLESLFEMQDVPADGDCFFYCVSLHLSGGSLKVDRIKGIITSFALRNWEDIYEARLFYGTPEAY 98
Cdd:cd21880      1 VWEEVgEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLYYLSLEEY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   99 IADLYSPGYWGGSVEAEILNKAYGMPIIIWSSTD-GIYSTDVRIWTRKYdgMPEMNLIAAGRHFQYLRLR 167
Cdd:cd21880     81 LRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDsDWVTAAVRFGDGDV--STSLNLLHSGGHFDALRLK 148
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2065-2725 1.23e-72

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: 260.87  E-value: 1.23e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2065 LSFIREEIEVKTLEkAFLESFdHDIMLTINLIFALSLCCPWSIHYKSFELLLSQESSPLADDDQQREHLELLKTLGPCel 2144
Cdd:pfam04196    1 LNKVRCLRLVKAPE-LFWKAT-YEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPSRYVIMLGLSIYSN-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2145 IVDYLKAELDQLKNPEAARTTVEMLYRYCCAIFIANDEPIKSVLNLRDVVVT-SHVEDSAL--STTRSLLAKY-GLEKTD 2220
Cdd:pfam04196   77 IPSYIAKKFEPLSKTLRSVYMVRLIKRLLFTLFDQNGEPFKRSIYLGDLNDDqKGITNERLldSITFPILSTLkELINNV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2221 LDFKWTMNLIANSNFEVTKRLTGRT-EGEKLPRSVRSK-VIY-----EMIKLVKSTGMAILQQHAFS-YILNSGHRFFAV 2292
Cdd:pfam04196  157 YLGFYLKNKGLHENHNVMIDLLKKIlEWELKFREVRSKkLGKpvngaILVHLVSISYLADLCRHNLLrNRLENRHNFKAP 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2293 LAPKAQLGGHRDLLvQEIMTKIVHAATETFSRALLSTTMDDGLTNQ----HLKESILQTAYDQLQMSSHSHGKHLSSLGG 2368
Cdd:pfam04196  237 ITTISTLTSSKLCL-QIGTFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGTNLEVGEDNYEHLSKAIEYIETKVKD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2369 GVRYFSRTFCISGDRTKWGPIHCTSFFSGMMQQLLQDTPDWSsfFKLVMLKNLYRQVEIPsgAIKRL-LNSFRYRAQPTL 2447
Cdd:pfam04196  316 KLYEKNKSVVLKLKPEIEEPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY--AVERIsRAILKLNPSEMI 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2448 PLEQLTEDQIRQLMLDSIDIWEGNHMMQFLVQVYLSKGKMALecYNHMGQGIHHATSSVMTSCMAVLTEELIVSYFQTHM 2527
Cdd:pfam04196  392 SEPKDKKILAISEKHEMEARWTVEDTFKTLSTSDDAISKKNQ--LMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2528 PELSTTVRHaGSSDDYAKVITVAGNLPNSLFERYDERFWHHACRLQNSMVGLARGCQ-MKDSAKTLIGDAMCEFYSEFML 2606
Cdd:pfam04196  470 LGLYLLCNY-MSKTDLLPSDILLNLVDQKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2607 fhRVTPAVIKFILTGLINSSVTSPQSMVQACQVSSQQAMYNSVpLLTNICFTVFRQQMFANHTElFQRKYGPIVHGLpSA 2686
Cdd:pfam04196  549 --RAIKLLDGSCLVNSIVHSDDSQTSISIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCIY-ASPKKTYVTLTV-KE 623
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1070640876 2687 FGRLYLpmFSNLTSSTIAVEDAESIaLDLESAI---DLASRL 2725
Cdd:pfam04196  624 FNSEFF--FSGEVSSSLLRWLLASV-SDCAAEGlsdDLASLS 662
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
20-167 3.18e-59

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: 201.67  E-value: 3.18e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   20 RCKEI-EQCLGMSMITNLESLFEMQDVPADGDCFFYCVSLHLSGGSLKVDRIKGIITSFALRNWEDIYEARLFYGTPEAY 98
Cdd:cd21880      1 VWEEVgEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLYYLSLEEY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   99 IADLYSPGYWGGSVEAEILNKAYGMPIIIWSSTD-GIYSTDVRIWTRKYdgMPEMNLIAAGRHFQYLRLR 167
Cdd:cd21880     81 LRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDsDWVTAAVRFGDGDV--STSLNLLHSGGHFDALRLK 148
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2065-2725 1.23e-72

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: 260.87  E-value: 1.23e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2065 LSFIREEIEVKTLEkAFLESFdHDIMLTINLIFALSLCCPWSIHYKSFELLLSQESSPLADDDQQREHLELLKTLGPCel 2144
Cdd:pfam04196    1 LNKVRCLRLVKAPE-LFWKAT-YEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPSRYVIMLGLSIYSN-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2145 IVDYLKAELDQLKNPEAARTTVEMLYRYCCAIFIANDEPIKSVLNLRDVVVT-SHVEDSAL--STTRSLLAKY-GLEKTD 2220
Cdd:pfam04196   77 IPSYIAKKFEPLSKTLRSVYMVRLIKRLLFTLFDQNGEPFKRSIYLGDLNDDqKGITNERLldSITFPILSTLkELINNV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2221 LDFKWTMNLIANSNFEVTKRLTGRT-EGEKLPRSVRSK-VIY-----EMIKLVKSTGMAILQQHAFS-YILNSGHRFFAV 2292
Cdd:pfam04196  157 YLGFYLKNKGLHENHNVMIDLLKKIlEWELKFREVRSKkLGKpvngaILVHLVSISYLADLCRHNLLrNRLENRHNFKAP 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2293 LAPKAQLGGHRDLLvQEIMTKIVHAATETFSRALLSTTMDDGLTNQ----HLKESILQTAYDQLQMSSHSHGKHLSSLGG 2368
Cdd:pfam04196  237 ITTISTLTSSKLCL-QIGTFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGTNLEVGEDNYEHLSKAIEYIETKVKD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2369 GVRYFSRTFCISGDRTKWGPIHCTSFFSGMMQQLLQDTPDWSsfFKLVMLKNLYRQVEIPsgAIKRL-LNSFRYRAQPTL 2447
Cdd:pfam04196  316 KLYEKNKSVVLKLKPEIEEPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY--AVERIsRAILKLNPSEMI 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2448 PLEQLTEDQIRQLMLDSIDIWEGNHMMQFLVQVYLSKGKMALecYNHMGQGIHHATSSVMTSCMAVLTEELIVSYFQTHM 2527
Cdd:pfam04196  392 SEPKDKKILAISEKHEMEARWTVEDTFKTLSTSDDAISKKNQ--LMHVSADMSKWSASDLTYKYFFLIALLPILYPKEKF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2528 PELSTTVRHaGSSDDYAKVITVAGNLPNSLFERYDERFWHHACRLQNSMVGLARGCQ-MKDSAKTLIGDAMCEFYSEFML 2606
Cdd:pfam04196  470 LGLYLLCNY-MSKTDLLPSDILLNLVDQKYYGRYDIIFWMTNGLNKNFVEVKRNWLQgNLNYTSSLVHSCAMEVYKEFLK 548
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876 2607 fhRVTPAVIKFILTGLINSSVTSPQSMVQACQVSSQQAMYNSVpLLTNICFTVFRQQMFANHTElFQRKYGPIVHGLpSA 2686
Cdd:pfam04196  549 --RAIKLLDGSCLVNSIVHSDDSQTSISIPCHVDDKQADFKSV-LVANSAFRSKELIFKYLCIY-ASPKKTYVTLTV-KE 623
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1070640876 2687 FGRLYLpmFSNLTSSTIAVEDAESIaLDLESAI---DLASRL 2725
Cdd:pfam04196  624 FNSEFF--FSGEVSSSLLRWLLASV-SDCAAEGlsdDLASLS 662
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
20-167 3.18e-59

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: 201.67  E-value: 3.18e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   20 RCKEI-EQCLGMSMITNLESLFEMQDVPADGDCFFYCVSLHLSGGSLKVDRIKGIITSFALRNWEDIYEARLFYGTPEAY 98
Cdd:cd21880      1 VWEEVgEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECPEARLYYLSLEEY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   99 IADLYSPGYWGGSVEAEILNKAYGMPIIIWSSTD-GIYSTDVRIWTRKYdgMPEMNLIAAGRHFQYLRLR 167
Cdd:cd21880     81 LRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDsDWVTAAVRFGDGDV--STSLNLLHSGGHFDALRLK 148
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
41-139 4.92e-15

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


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 74.39  E-value: 4.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   41 EMQDVPADGDCFFYCVSLHLSGGSLKVDRIKGIITSFALRNWEDIYEARLFYGTP----EAYIADLYSPGYWGGSVEAEI 116
Cdd:cd22744      1 RVVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPAELADEDDgedfDEYLQRMRKPGTWGGELELQA 80
                           90       100
                   ....*....|....*....|...
gi 1070640876  117 LNKAYGMPIIIWSSTDGIYSTDV 139
Cdd:cd22744     81 LANALNVPIVVYSEDGGFLPVSV 103
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
40-145 8.86e-08

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: 53.81  E-value: 8.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   40 FEMQDVPADGDCFFYCVSLHLSGGSLKVD--RIKGIITSFaLRNWEDIYE-----ARLFYGTPEAYIADLYSPGYWGGSV 112
Cdd:cd22758      6 FEIRDVPGDGNCFFHAVSDQLYGNGIEHShkELRQQAVNY-LRENPELYDgfflsEFDEEESWEEYLNRMSKDGTWGDHI 84
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1070640876  113 E----AEILNkaygMPIIIWSSTDGIYSTDVRIWTRK 145
Cdd:cd22758     85 IlqaaANLFN----VRIVIISSDGSDETTIIEPGNSK 117
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
44-127 1.88e-07

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: 52.59  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   44 DVPADGDCFFYCVSLHLSGGSLKVDRIKGIITSFALRNWEDiYEARL------FYGTPEAYIADLYSPGYWGGSVEAEIL 117
Cdd:cd22757      5 PIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDE-FSIYThdsegnNYKSAEEYRADMSKPGTYGTLCELVAA 83
                           90
                   ....*....|
gi 1070640876  118 NKAYGMPIII 127
Cdd:cd22757     84 AELYPFHFEV 93
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
40-130 1.47e-03

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: 41.78  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   40 FEMQDVPADGDCFFYCVS--LHLSGGSLKVDRIKGI--ITSFALRNWEDIYEARLFYGTP--------EAYIADLYSPGY 107
Cdd:cd22748      6 LRIKEIPPDGHCLYRAIAdqLKLRGGSEEPYSYKELrkLAADYMRAHRDDFLPFLTNDDGdlmteeefEEYCDKIENTAE 85
                           90       100
                   ....*....|....*....|...
gi 1070640876  108 WGGSVEAEILNKAYGMPIIIWSS 130
Cdd:cd22748     86 WGGQLELRALSKALKRPIHVYQA 108
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
36-125 2.94e-03

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: 41.06  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   36 LESL-FEMQDVPADGDCFFYCVS--LHLSGGSLKVD--RIKGIITSFALRNWEDiYEARLFYGTPE-----AYIADLYSP 105
Cdd:cd22762      2 LEELgLEEHDIKPDGHCLFAAIAdqLQLRGSEINLDykELRKLAAEYIRKHPDD-FEPFLFEETDEledidEYCKKIENT 80
                           90       100
                   ....*....|....*....|
gi 1070640876  106 GYWGGSVEAEILNKAYGMPI 125
Cdd:cd22762     81 AEWGGELELLALAKAFGVPI 100
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
43-132 5.38e-03

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: 39.83  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070640876   43 QDVPADGDCFFYCVSLHLSGGSLKVDRIKGIITSFALRNwEDIYEARLFyGTPEAYIADLYSPGYWGGSVEAEILNKAYG 122
Cdd:cd22753     13 KHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKN-REEFEKFSE-ISFDDYLERLSDPKEWGGLLELEALSLLYK 90
                           90
                   ....*....|
gi 1070640876  123 MPIIIWSSTD 132
Cdd:cd22753     91 VDFIVYSIPD 100
 
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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