NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1827368866|gb|QIS88061|]
View 

MAG: RNA-dependent RNA polymerase, partial [Taggert 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 ...
2003-2500 6.44e-60

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: 221.96  E-value: 6.44e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2003 VSFTKEEICirMKEKRFIETYSNEIMSCMNMIFFLTLTAPWCVHYKSLEAFFIKNPNLANLDQPDKEpnsQILEMTVSNM 2082
Cdd:pfam04196    1 LNKVRCLRL--VKAPELFWKATYEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPSRY---VIMLGLSIYS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2083 VWRlvSHILKEdEDKSFLSERTVKKY---VEYLITAFTINGFPLSESLNTYGDEHTVQG--EEQIL--QQLKGMLSRLGL 2155
Cdd:pfam04196   76 NIP--SYIAKK-FEPLSKTLRSVYMVrliKRLLFTLFDQNGEPFKRSIYLGDLNDDQKGitNERLLdsITFPILSTLKEL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2156 KGGRHEFLWTVHLIANSNFEVTKKLTGRQTG-ERLPRSVRSKVV------YEVIKMVGETGMAILQQLAFT-CALNTDHR 2227
Cdd:pfam04196  153 INNVYLGFYLKNKGLHENHNVMIDLLKKILEwELKFREVRSKKLgkpvngAILVHLVSISYLADLCRHNLLrNRLENRHN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2228 FFAVLAPKAQLGGCRDLLvQETGTKLIHATTEMFSRTLLSTTNDDGLTNS----HLKENILNTGLEAI-QTMRITHGKPV 2302
Cdd:pfam04196  233 FKAPITTISTLTSSKLCL-QIGTFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGTNLEVGEDNYeHLSKAIEYIET 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2303 ESFKGLVNFYRVMCISGDNTKWGPIHCCSLFSGMMQQLLKDVPDWCqfYKLTFIKNLCRQVEIPsASIKKILNSLRYHVS 2382
Cdd:pfam04196  312 KVKDKLYEKNKSVVLKLKPEIEEPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY-AVERISRAILKLNPS 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2383 DAVEIEAQTERELRQLLLSNLNIWEHNKIIQFLVKTYLSKgeMAMNSYNHMGQGIHHATSSILTSTFAVTFEELARDFFM 2462
Cdd:pfam04196  389 EMISEPKDKKILAISEKHEMEARWTVEDTFKTLSTSDDAI--SKKNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPK 466
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1827368866 2463 ECYPELTLKLDHaGSSDDYAKCLVLSGVVSASTFKNYD 2500
Cdd:pfam04196  467 EKFLGLYLLCNY-MSKTDLLPSDILLNLVDQKYYGRYD 503
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
8-157 7.38e-56

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: 191.27  E-value: 7.38e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866    8 DWHLLLAGYYYSPIDIEVEDVFEIVNQPMDGNCLYHSLACGMIEEqqPDSYKLIKEQVREAAGLFWNTTEETKTTGEDLK 87
Cdd:cd21880      1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDT--EDEWRLVKNTIESYARANWDECPEARLYYLSLE 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   88 EYLARIMKPNEWGSSLEVNFFSQKAKVTVYIWHEDANKHCDYVVRYGEDSVFESINIIHRRNHYDYLKPK 157
Cdd:cd21880     79 EYLRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLNLLHSGGHFDALRLK 148
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2003-2500 6.44e-60

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: 221.96  E-value: 6.44e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2003 VSFTKEEICirMKEKRFIETYSNEIMSCMNMIFFLTLTAPWCVHYKSLEAFFIKNPNLANLDQPDKEpnsQILEMTVSNM 2082
Cdd:pfam04196    1 LNKVRCLRL--VKAPELFWKATYEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPSRY---VIMLGLSIYS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2083 VWRlvSHILKEdEDKSFLSERTVKKY---VEYLITAFTINGFPLSESLNTYGDEHTVQG--EEQIL--QQLKGMLSRLGL 2155
Cdd:pfam04196   76 NIP--SYIAKK-FEPLSKTLRSVYMVrliKRLLFTLFDQNGEPFKRSIYLGDLNDDQKGitNERLLdsITFPILSTLKEL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2156 KGGRHEFLWTVHLIANSNFEVTKKLTGRQTG-ERLPRSVRSKVV------YEVIKMVGETGMAILQQLAFT-CALNTDHR 2227
Cdd:pfam04196  153 INNVYLGFYLKNKGLHENHNVMIDLLKKILEwELKFREVRSKKLgkpvngAILVHLVSISYLADLCRHNLLrNRLENRHN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2228 FFAVLAPKAQLGGCRDLLvQETGTKLIHATTEMFSRTLLSTTNDDGLTNS----HLKENILNTGLEAI-QTMRITHGKPV 2302
Cdd:pfam04196  233 FKAPITTISTLTSSKLCL-QIGTFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGTNLEVGEDNYeHLSKAIEYIET 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2303 ESFKGLVNFYRVMCISGDNTKWGPIHCCSLFSGMMQQLLKDVPDWCqfYKLTFIKNLCRQVEIPsASIKKILNSLRYHVS 2382
Cdd:pfam04196  312 KVKDKLYEKNKSVVLKLKPEIEEPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY-AVERISRAILKLNPS 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2383 DAVEIEAQTERELRQLLLSNLNIWEHNKIIQFLVKTYLSKgeMAMNSYNHMGQGIHHATSSILTSTFAVTFEELARDFFM 2462
Cdd:pfam04196  389 EMISEPKDKKILAISEKHEMEARWTVEDTFKTLSTSDDAI--SKKNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPK 466
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1827368866 2463 ECYPELTLKLDHaGSSDDYAKCLVLSGVVSASTFKNYD 2500
Cdd:pfam04196  467 EKFLGLYLLCNY-MSKTDLLPSDILLNLVDQKYYGRYD 503
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
8-157 7.38e-56

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: 191.27  E-value: 7.38e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866    8 DWHLLLAGYYYSPIDIEVEDVFEIVNQPMDGNCLYHSLACGMIEEqqPDSYKLIKEQVREAAGLFWNTTEETKTTGEDLK 87
Cdd:cd21880      1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDT--EDEWRLVKNTIESYARANWDECPEARLYYLSLE 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   88 EYLARIMKPNEWGSSLEVNFFSQKAKVTVYIWHEDANKHCDYVVRYGEDSVFESINIIHRRNHYDYLKPK 157
Cdd:cd21880     79 EYLRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLNLLHSGGHFDALRLK 148
 
Name Accession Description Interval E-value
Bunya_RdRp pfam04196
Bunyavirus RNA dependent RNA polymerase; The bunyaviruses are enveloped viruses with a genome ...
2003-2500 6.44e-60

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: 221.96  E-value: 6.44e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2003 VSFTKEEICirMKEKRFIETYSNEIMSCMNMIFFLTLTAPWCVHYKSLEAFFIKNPNLANLDQPDKEpnsQILEMTVSNM 2082
Cdd:pfam04196    1 LNKVRCLRL--VKAPELFWKATYEVMYAVNPIFYCTLTVKQILNFSSLLALLVTKPSLLEIFDPSRY---VIMLGLSIYS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2083 VWRlvSHILKEdEDKSFLSERTVKKY---VEYLITAFTINGFPLSESLNTYGDEHTVQG--EEQIL--QQLKGMLSRLGL 2155
Cdd:pfam04196   76 NIP--SYIAKK-FEPLSKTLRSVYMVrliKRLLFTLFDQNGEPFKRSIYLGDLNDDQKGitNERLLdsITFPILSTLKEL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2156 KGGRHEFLWTVHLIANSNFEVTKKLTGRQTG-ERLPRSVRSKVV------YEVIKMVGETGMAILQQLAFT-CALNTDHR 2227
Cdd:pfam04196  153 INNVYLGFYLKNKGLHENHNVMIDLLKKILEwELKFREVRSKKLgkpvngAILVHLVSISYLADLCRHNLLrNRLENRHN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2228 FFAVLAPKAQLGGCRDLLvQETGTKLIHATTEMFSRTLLSTTNDDGLTNS----HLKENILNTGLEAI-QTMRITHGKPV 2302
Cdd:pfam04196  233 FKAPITTISTLTSSKLCL-QIGTFAVIKALQSNFSKNWLEKTSRKLRNINptfvEDKGTNLEVGEDNYeHLSKAIEYIET 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2303 ESFKGLVNFYRVMCISGDNTKWGPIHCCSLFSGMMQQLLKDVPDWCqfYKLTFIKNLCRQVEIPsASIKKILNSLRYHVS 2382
Cdd:pfam04196  312 KVKDKLYEKNKSVVLKLKPEIEEPMDMMKKEFCMHQCLNKGQQTEG--DREIFVLNLEERMCQY-AVERISRAILKLNPS 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866 2383 DAVEIEAQTERELRQLLLSNLNIWEHNKIIQFLVKTYLSKgeMAMNSYNHMGQGIHHATSSILTSTFAVTFEELARDFFM 2462
Cdd:pfam04196  389 EMISEPKDKKILAISEKHEMEARWTVEDTFKTLSTSDDAI--SKKNQLMHVSADMSKWSASDLTYKYFFLIALLPILYPK 466
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1827368866 2463 ECYPELTLKLDHaGSSDDYAKCLVLSGVVSASTFKNYD 2500
Cdd:pfam04196  467 EKFLGLYLLCNY-MSKTDLLPSDILLNLVDQKYYGRYD 503
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
8-157 7.38e-56

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: 191.27  E-value: 7.38e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866    8 DWHLLLAGYYYSPIDIEVEDVFEIVNQPMDGNCLYHSLACGMIEEqqPDSYKLIKEQVREAAGLFWNTTEETKTTGEDLK 87
Cdd:cd21880      1 VWEEVGEGQYVSNPRFNLRDYFEIERVPGDGNCFFRSIAELLFDT--EDEWRLVKNTIESYARANWDECPEARLYYLSLE 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   88 EYLARIMKPNEWGSSLEVNFFSQKAKVTVYIWHEDANKHCDYVVRYGEDSVFESINIIHRRNHYDYLKPK 157
Cdd:cd21880     79 EYLRDAMKDGYWGGSLEAEILSKALGITIIIWVVDDSDWVTAAVRFGDGDVSTSLNLLHSGGHFDALRLK 148
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
30-154 2.85e-16

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


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 77.48  E-value: 2.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   30 EIVNQPMDGNCLYHSLACGMIEEQqpDSYKLIKEQV----REAAGLFWNTTEETKTTGEDLKEYLARIMKPNEWGSSLEV 105
Cdd:cd22744      1 RVVDVPGDGNCLFRALAHALYGDQ--ESHRELRQEVvdylRENPDLYEPAELADEDDGEDFDEYLQRMRKPGTWGGELEL 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1827368866  106 NFFSQKAKVTVYIWHEDANKHCDYVVRYGEDSVFESINIIHR-RNHYDYL 154
Cdd:cd22744     79 QALANALNVPIVVYSEDGGFLPVSVFGPGPGPSGRPIHLLYTgGNHYDAL 128
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
35-157 1.25e-07

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: 51.84  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   35 PMDGNCLYHSLAC--GMieeqqpdSYKLIKEQVREAAglfwntteetkTTGEDLKEYLARIMKPNEWGSSLEVNFFSQKA 112
Cdd:cd22792      6 PGDGNCFWHSLGHflGL-------SALELKKLLRDSL-----------FDDPELDEELDEQLEPGVYAEDEAIAAAAKLF 67
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1827368866  113 KVTVYIWHEDANKhcdyVVRYGEDSVFESINIIHRRNHYDYLKPK 157
Cdd:cd22792     68 GVNICVHDPDEGV----LYTFTPNESSKSIHLLLENEHFEPLVPK 108
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
37-151 1.18e-06

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: 49.87  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   37 DGNCLYHSLAcgmieEQ---QPDSYKLIKEQV----REAAGLFWNTTEETKTTGED--LKEYLARIMKPNEWGSSLEVNF 107
Cdd:cd22756      8 DGNCLFRALS-----DQlygDPDRHLEIRAEVveymRANPDDFKPFSEAATFAEDDeaFEDYLARMAKDGTYGDNLEIVA 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1827368866  108 FSQKAKVTVYIWHEDANkhcdYVVRYGEDSVFES----INII-HRRNHY 151
Cdd:cd22756     83 FARAYNVDVKVYQPDPV----YVISAPEDGSPGParrvLHIAyHNWEHY 127
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
29-151 1.38e-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: 49.96  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   29 FEIVNQPMDGNCLYHSLACGMIEEQQPDSYKLIKEQV----REAAGLFWNTTEETKTTGEDLKEYLARIMKPNEWGSSLE 104
Cdd:cd22758      6 FEIRDVPGDGNCFFHAVSDQLYGNGIEHSHKELRQQAvnylRENPELYDGFFLSEFDEEESWEEYLNRMSKDGTWGDHII 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827368866  105 VNFFSQKAKVTVYIWHEDANKHcdyvvrygeDSVFESINIIHRR---------NHY 151
Cdd:cd22758     86 LQAAANLFNVRIVIISSDGSDE---------TTIIEPGNSKNGRtiylghigeNHY 132
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
85-154 5.19e-03

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


Pssm-ID: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 39.56  E-value: 5.19e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827368866   85 DLKEYLARIMKPNEWGSSLEVNFFSQ--KAKVTVYIWHEDAN--KHcdyVVRYGEDSV-FESINII-HRRNHYDYL 154
Cdd:cd22746     68 DFDAYCQRMSHPDTWGGEPELLMLADvlQRPIAVYLPTPGKGglRK---IQEYGEEYLgGEPIRLLyNGGNHYDLL 140
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
28-151 7.52e-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: 39.08  E-value: 7.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827368866   28 VFEIvnqPMDGNCLYHSLACGM---IEEQQPDSYKlikeQVREAAG-----------LFWNTTEETKTTGEDLKEYLARI 93
Cdd:cd22748      8 IKEI---PPDGHCLYRAIADQLklrGGSEEPYSYK----ELRKLAAdymrahrddflPFLTNDDGDLMTEEEFEEYCDKI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827368866   94 MKPNEWGSSLEVNFFSQKAKVTVYIWHEDANkhcdyVVRYGEDsvFESINII----HRR-----NHY 151
Cdd:cd22748     81 ENTAEWGGQLELRALSKALKRPIHVYQAGSP-----PLVIGEE--FDSGEPLrlsyHRHayglgEHY 140
 
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