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Conserved domains on  [gi|2024407817|ref|XP_015132203|]
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OTU domain-containing protein 4 isoform X2 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 27-156 1.38e-93

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


:

Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 293.89  E-value: 1.38e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   27 MDCYLRSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQV 106
Cdd:cd22794      1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024407817  107 EISALSLMYKKDFIIYREPNASPSHVTENGFSDKVLLCFSNGNHYDIVYP 156
Cdd:cd22794     81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 277-340 1.05e-36

Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410519  Cd Length: 64  Bit Score: 132.32  E-value: 1.05e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024407817  277 DFSIAAGMQYSIGDKCKVRLDHNGKFYNAHIQEVCSENGPVVVFVEELGAKHSVSLKSLKPLPQ 340
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVFVEELGKKHTVPLKNLKPPPQ 64
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 521-776 1.43e-04

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.22  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  521 DKESNSRQihlsqkLEPNSSERNSQDESCPKASSPLEQVKTDSPAvAEQKLTEcLPSVTPTPS-PVFSEVHLPPTVPSVP 599
Cdd:PTZ00449   526 DKEGEEGE------HEDSKESDEPKEGGKPGETKEGEVGKKPGPA-KEHKPSK-IPTLSKKPEfPKDPKHPKDPEEPKKP 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  600 AiVPAWPSEPTTYGPAGIP--AQIPASSLMPAPATGPDSIVSQAQTLNPY-----------QDPLYPGFPLSEKGERAIA 666
Cdd:PTZ00449   598 K-RPRSAQRPTRPKSPKLPelLDIPKSPKRPESPKSPKRPPPPQRPSSPErpegpkiikspKPPKSPKPPFDPKFKEKFY 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  667 PSYSLCSSGEDLPKDKNILRFFFNLGVKAySCPMWAPHSYLYPlhqaylaacRMYPnmslPVYPHNPWFQEAPPTQIENE 746
Cdd:PTZ00449   677 DDYLDAAAKSKETKTTVVLDESFESILKE-TLPETPGTPFTTP---------RPLP----PKLPRDEEFPFEPIGDPDAE 742

                          250       260       270
                   ....*....|....*....|....*....|
gi 2024407817  747 TVQPNRHFAIPSETRSNGQMSQVDSRSPSL 776
Cdd:PTZ00449   743 QPDDIEFFTPPEEERTFFHETPADTPLPDI 772
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 921-1103 3.11e-04

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  921 APKETSARAPQLEQTCTSASPAKQATAGLQNRSTQIQGVERQTAVPNTTLPLAEPPKNELKNTAHGRKDKTDKVRDSKGA 1000
Cdd:PRK12678    97 AAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817 1001 GNLQTENRAQRVREESSEDENEVSDMLRSGRSKQFYNQTYGGGRRPRMEWGYSSRGGYQFPRNEEAWKGPPGRSRDEGNQ 1080
Cdd:PRK12678   177 DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                          170       180
                   ....*....|....*....|....
gi 2024407817 1081 YQRNFRGRPYR-NDRRRATLGDNQ 1103
Cdd:PRK12678   257 GRGGRRGRRFRdRDRRGRRGGDGG 280
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 27-156 1.38e-93

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


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 293.89  E-value: 1.38e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   27 MDCYLRSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQV 106
Cdd:cd22794      1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024407817  107 EISALSLMYKKDFIIYREPNASPSHVTENGFSDKVLLCFSNGNHYDIVYP 156
Cdd:cd22794     81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 277-340 1.05e-36

Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410519  Cd Length: 64  Bit Score: 132.32  E-value: 1.05e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024407817  277 DFSIAAGMQYSIGDKCKVRLDHNGKFYNAHIQEVCSENGPVVVFVEELGAKHSVSLKSLKPLPQ 340
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVFVEELGKKHTVPLKNLKPPPQ 64
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 44-123 2.72e-15

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


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 73.64  E-value: 2.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   44 DGSCLFRAVAEQV-----LHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQVEISALSLMYKKD 118
Cdd:pfam02338    3 DGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82


                   ....*
gi 2024407817  119 FIIYR 123
Cdd:pfam02338   83 IIVYK 87
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 521-776 1.43e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.22  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  521 DKESNSRQihlsqkLEPNSSERNSQDESCPKASSPLEQVKTDSPAvAEQKLTEcLPSVTPTPS-PVFSEVHLPPTVPSVP 599
Cdd:PTZ00449   526 DKEGEEGE------HEDSKESDEPKEGGKPGETKEGEVGKKPGPA-KEHKPSK-IPTLSKKPEfPKDPKHPKDPEEPKKP 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  600 AiVPAWPSEPTTYGPAGIP--AQIPASSLMPAPATGPDSIVSQAQTLNPY-----------QDPLYPGFPLSEKGERAIA 666
Cdd:PTZ00449   598 K-RPRSAQRPTRPKSPKLPelLDIPKSPKRPESPKSPKRPPPPQRPSSPErpegpkiikspKPPKSPKPPFDPKFKEKFY 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  667 PSYSLCSSGEDLPKDKNILRFFFNLGVKAySCPMWAPHSYLYPlhqaylaacRMYPnmslPVYPHNPWFQEAPPTQIENE 746
Cdd:PTZ00449   677 DDYLDAAAKSKETKTTVVLDESFESILKE-TLPETPGTPFTTP---------RPLP----PKLPRDEEFPFEPIGDPDAE 742

                          250       260       270
                   ....*....|....*....|....*....|
gi 2024407817  747 TVQPNRHFAIPSETRSNGQMSQVDSRSPSL 776
Cdd:PTZ00449   743 QPDDIEFFTPPEEERTFFHETPADTPLPDI 772
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 921-1103 3.11e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  921 APKETSARAPQLEQTCTSASPAKQATAGLQNRSTQIQGVERQTAVPNTTLPLAEPPKNELKNTAHGRKDKTDKVRDSKGA 1000
Cdd:PRK12678    97 AAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817 1001 GNLQTENRAQRVREESSEDENEVSDMLRSGRSKQFYNQTYGGGRRPRMEWGYSSRGGYQFPRNEEAWKGPPGRSRDEGNQ 1080
Cdd:PRK12678   177 DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                          170       180
                   ....*....|....*....|....
gi 2024407817 1081 YQRNFRGRPYR-NDRRRATLGDNQ 1103
Cdd:PRK12678   257 GRGGRRGRRFRdRDRRGRRGGDGG 280
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 285-342 3.69e-04

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 39.56  E-value: 3.69e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024407817   285 QYSIGDKCKVRLDhNGKFYNAHIQEVCSENGpVVVFVEELGAKHSVSLKSLKPLPQAS 342
Cdd:smart00333    2 TFKVGDKVAARWE-DGEWYRARIVKVDGEQL-YEVFFIDYGNEEVVPPSDLRQLPEEL 57
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 476-650 9.26e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  476 EQAFPALSNNQSVSQAATRTVDNPKKVSSNEKRSSKWTA--EVEEQKDKESNSRQIHLSQKLEPNSSERNSQDEScPKAS 553
Cdd:pfam03154   71 EEAPSPLKSAKRQREKGASDTEEPERATAKKSKTQEISRpnSPSEGEGESSDGRSVNDEGSSDPKDIDQDNRSTS-PSIP 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  554 SPLEQvKTDSPAVAEQKLTECLPSVTPTPSPVfsevhLPPTVPSVPAIVPAWPSEPTTYGPAGIPAQIPASSLMPA---P 630
Cdd:pfam03154  150 SPQDN-ESDSDSSAQQQILQTQPPVLQAQSGA-----ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNqtqS 223

                          170       180
                   ....*....|....*....|
gi 2024407817  631 ATGPDSIVSQAQTLNPYQDP 650
Cdd:pfam03154  224 TAAPHTLIQQTPTLHPQRLP 243
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 27-156 1.38e-93

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


Pssm-ID: 438615 [Multi-domain]  Cd Length: 130  Bit Score: 293.89  E-value: 1.38e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   27 MDCYLRSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQV 106
Cdd:cd22794      1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024407817  107 EISALSLMYKKDFIIYREPNASPSHVTENGFSDKVLLCFSNGNHYDIVYP 156
Cdd:cd22794     81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 27-156 3.10e-63

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: 210.48  E-value: 3.10e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   27 MDCYLRSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQV 106
Cdd:cd22753      1 IDEYLDSLGLYRKHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFSEISFDDYLERLSDPKEWGGLL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024407817  107 EISALSLMYKKDFIIYREPNASPSHVTENGFSDKVLLCFSNGNHYDIVYP 156
Cdd:cd22753     81 ELEALSLLYKVDFIVYSIPDQPPSNITNNGYPKKIMLCYSGGNHYDSVYS 130
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 27-156 3.49e-59

OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13; Bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 is also 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). ALG13 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438616 [Multi-domain]  Cd Length: 130  Bit Score: 198.88  E-value: 3.49e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   27 MDCYLRSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQV 106
Cdd:cd22795      1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024407817  107 EISALSLMYKKDFIIYREPNASPSHVTENGFSDKVLLCFSNGNHYDIVYP 156
Cdd:cd22795     81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVYT 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 277-340 1.05e-36

Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410519  Cd Length: 64  Bit Score: 132.32  E-value: 1.05e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024407817  277 DFSIAAGMQYSIGDKCKVRLDHNGKFYNAHIQEVCSENGPVVVFVEELGAKHSVSLKSLKPLPQ 340
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVFVEELGKKHTVPLKNLKPPPQ 64
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 35-154 1.14e-31

OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar proteins; Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. DUBs catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. OTU7 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438608 [Multi-domain]  Cd Length: 124  Bit Score: 119.97  E-value: 1.14e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   35 GLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEG--PFEEYLKCLENPQEWVGQVEISALS 112
Cdd:cd22771      1 GLRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFEDdeTFEDYVSRMREDGTWGGNLELQAAS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2024407817  113 LMYKKDFIIYREPnaSPSHVTENgFSDK----VLLCFSNGNHYDIV 154
Cdd:cd22771     81 LVYRVNIVVHQLG--QPRWEIEN-FPDKgartIHLSYHDGEHYNSV 123
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 37-154 1.26e-28

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: 111.76  E-value: 1.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   37 YRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEA------FIEGPFEEYLKCLENPQEWVGQVEISA 110
Cdd:cd22744      1 RVVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPaeladeDDGEDFDEYLQRMRKPGTWGGELELQA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2024407817  111 LSLMYKKDFIIYRE-PNASPSHVTENGFSDK---VLLCFSNGNHYDIV 154
Cdd:cd22744     81 LANALNVPIVVYSEdGGFLPVSVFGPGPGPSgrpIHLLYTGGNHYDAL 128
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 282-354 1.00e-25

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410518  Cd Length: 80  Bit Score: 101.47  E-value: 1.00e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024407817  282 AGMQYSIGDKCKVRLDHNGKFYNAHIQEVCSENGPVVVFVEELGAKHSVSLKSLKPLPQASPMEGWNTVPGKK 354
Cdd:cd20447      2 AGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRK 74
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 37-154 2.38e-24

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: 99.56  E-value: 2.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   37 YRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAF--------IEGPFEEYLKCLENPQEWVGQVEI 108
Cdd:cd22756      1 YAKDITGDGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANPDDFKPFseaatfaeDDEAFEDYLARMAKDGTYGDNLEI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024407817  109 SALSLMYKKDFIIYRePNA----SPSHVTENGFSDKVL-LCFSNGNHYDIV 154
Cdd:cd22756     81 VAFARAYNVDVKVYQ-PDPvyviSAPEDGSPGPARRVLhIAYHNWEHYSSV 130
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
 32-155 5.85e-23

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: 95.57  E-value: 5.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   32 RSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQVEISAL 111
Cdd:cd22796      1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2024407817  112 SLMYKKDFIIYREPNASPSHVTENGFSDK---VLLCFSNGNHYDIVY 155
Cdd:cd22796     81 SEIYNRPIEVYSYSNGEPINIFHGSYEGDdppIRLSYHDGNHYNSII 127
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
 285-338 1.28e-22

Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The TDRD13 family includes TDRD13 and OTU domain-containing protein 4 (OTUD4). TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410451  Cd Length: 54  Bit Score: 91.87  E-value: 1.28e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024407817  285 QYSIGDKCKVRLDHNGKFYNAHIQEVCSENGPVVVFVEELGAKHSVSLKSLKPL 338
Cdd:cd20380      1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVFVEELGEKKTVPYENLKPL 54
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 31-151 1.93e-22

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: 94.55  E-value: 1.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   31 LRSQGLYRKKVAKDGSCLFRAVAEQVLH-----SQSRHIDVRMACVDYLRKHREKFEAFI---------EGPFEEYLKCL 96
Cdd:cd22748      1 LKPLGLRIKEIPPDGHCLYRAIADQLKLrggseEPYSYKELRKLAADYMRAHRDDFLPFLtnddgdlmtEEEFEEYCDKI 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024407817   97 ENPQEWVGQVEISALSLMYKKDFIIYrepNASPSHVT--ENGFSDKVL-LCF-----SNGNHY 151
Cdd:cd22748     81 ENTAEWGGQLELRALSKALKRPIHVY---QAGSPPLVigEEFDSGEPLrLSYhrhayGLGEHY 140
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 35-156 3.41e-22

OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU domain-containing protein 5 (OTUD5), also called deubiquitinating enzyme A (DUBA), is a phosphorylation-dependent deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can hydrolyze 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, and may function as negative regulator of the innate immune system. It limits type I interferon production in macrophages and suppresses interleukin-17A production in T cells. OTUD5 also functions in an apoptotic signaling cascade by mediating the sequential activation of PDCD5 (programmed cell death 5) and p53 in response to genotoxic stress. In Drosophila, OTUD5/DUBA is essential for spermatogenesis. This subfamily also includes Arabidopsis thaliana OTU domain-containing protein 6, also called deubiquitinating enzyme OTU6 or otubain-like deubiquitinase 1 (OTLD1), which binds chromatin and has enzymatic histone deubiquitinase activity specific for the H2B histone. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It also includes plant OTU6.


Pssm-ID: 438589 [Multi-domain]  Cd Length: 124  Bit Score: 93.00  E-value: 3.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   35 GLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQVEISALSLM 114
Cdd:cd22752      1 GFIIKEMEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYFSQFVTEDFEEYINRKRQDGVWGNHIEIQAMSEL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024407817  115 YKKDFIIY---REPNASpSHVTENGFSDKVLLCFSNGNHYDIVYP 156
Cdd:cd22752     81 YNRPIEVYaysTEPINT-FHEASSSDNEPIRLSYHGNSHYNSIVD 124
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 31-151 4.93e-22

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: 93.10  E-value: 4.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   31 LRSQGLYRKKVAKDGSCLFRAVAEQV--LHSQSRHIDVRMACVDYLRKHREKFEAF------IEGPFEEYLKCLENPQEW 102
Cdd:cd22758      1 AKENGFEIRDVPGDGNCFFHAVSDQLygNGIEHSHKELRQQAVNYLRENPELYDGFflsefdEEESWEEYLNRMSKDGTW 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024407817  103 VGQVEISALSLMYKKDFIIYRE-PNASPSHVTENGFSDK--VLLCFSNGNHY 151
Cdd:cd22758     81 GDHIILQAAANLFNVRIVIISSdGSDETTIIEPGNSKNGrtIYLGHIGENHY 132
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
 31-155 6.22e-20

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: 86.83  E-value: 6.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   31 LRSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHRE-KFEAFIEGPFEEYLKCLENPQEW------- 102
Cdd:cd22751      5 LDLYGLVERKVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPElYYEFYVPEEYDEYLKKMSKDGEWgdeltlq 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024407817  103 ----VGQVEISALSLMYKKDFIIYrEPnaspshvTENGFSDKVL-LCFSNGNHYDIVY 155
Cdd:cd22751     85 aaadAFGVKIHVITSFEDNWFLEI-EP-------RGLVRSKRVLfLSYWAEVHYNSIY 134
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 31-112 7.35e-17

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: 78.42  E-value: 7.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   31 LRSQGLYRKKVAKDGSCLFRAVAEQVlhsQSRHID-------VRMACVDYLRKHREKFEAFI------EGPFEEYLKCLE 97
Cdd:cd22762      2 LEELGLEEHDIKPDGHCLFAAIADQL---QLRGSEinldykeLRKLAAEYIRKHPDDFEPFLfeetdeLEDIDEYCKKIE 78

                           90
                   ....*....|....*
gi 2024407817   98 NPQEWVGQVEISALS 112
Cdd:cd22762     79 NTAEWGGELELLALA 93
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
 28-155 1.66e-16

OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU domain-containing protein 1 (OTUD1), also called DUBA-7 in humans, is a deubiquitinating enzyme/ubiquitinyl hydrolase (EC 3.4.19.12) that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin; this specificity is facilitated by the C-terminal Ub-interacting motif (UIM) of OTUD1. It interacts and promotes the deubiquitination of myeloid cell leukemia 1 (MCL1), a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumorigenesis. OTUD1 also deubiquitinates IFN regulatory factor 3 (IRF3) and attenuates its function; IRF3 is critical for the transcription of type I IFNs in defensing virus and promoting inflammatory responses. Loss-of-function mutations of OTUD1 associated with multiple autoimmune diseases including systemic lupus erythematosus (SLE), rheumatoid arthritis (RA), ulcerative colitis (UC) and Hashimoto's thyroiditis (HT). OTUD1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438584 [Multi-domain]  Cd Length: 149  Bit Score: 77.54  E-value: 1.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   28 DCYLRSQGLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQVE 107
Cdd:cd22747     13 DKYLRERNKYRFHIIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLDEFNPIIEGDVGEFLIKAAQDGAWAGYPE 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024407817  108 ISALSLMYKKDfiIYREPNASPSHVT----------ENGFSDKVLLCF-SNGnHYDIVY 155
Cdd:cd22747     93 LLAMGQMLNVN--IRLTTGGSLESPTvstmvhylgpEDSGKPSIWLSWlSNG-HYDAVF 148
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
 35-157 2.32e-16

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU domain-containing protein 3 (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. It belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 76.94  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   35 GLYRKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFIEG--PFEEYLKCLENPQEWVGQVEISALS 112
Cdd:cd22770     13 GLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDdvPFDKHVANLSKPGTYAGNDAIVAFA 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2024407817  113 LMYKKDFIIYrEPNASPSHV--TENGFSDKVLLCFSNGNHYDIVYPI 157
Cdd:cd22770     93 RLHQVNVVIH-QLNAPLWQIrgTEKSSSRELHISYHNGDHYSSVRKL 138
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 39-154 3.17e-16

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: 76.15  E-value: 3.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   39 KKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAFI---EGPFEEYLKCLENPQ--EWVGQVEISALSL 113
Cdd:cd22755      4 IKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLrsdYESVEEYLEKSRMRYdgTWATDVEIFAAAT 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2024407817  114 MYKKDFIIYREPNA-----SPSHVTENGFSDK--VLLCFSNGNHYDIV 154
Cdd:cd22755     84 LLGVDIYVYSKGGYkwllySPRFKLGKRNGSReaIYLKNTNGNHFEPV 131
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
 31-152 1.75e-15

OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; This subfamily is composed of mammalian OTU domain-containing protein 6A (OTUD6A, also called DUBA-2) and vertebrate OTU domain-containing protein 6B (OTUD6B, also called DUBA-5), which are deubiquitinating enzymes/ubiquitinyl hydrolases (EC 3.4.19.12). OTUD6A hydrolyzes 'Lys-27'-, 'Lys-29'-, and 'Lys-33'-linked polyubiquitin chains, and may also be able to hydrolyze 'Lys-11'-linked ubiquitin chains. It deubiquitylates and stabilizes dynamin-related protein 1 (Drp1), a cytosolic protein responsible for mitochondrial fission and is essential in the initiation and development of several human diseases including cancer, thereby facilitating tumorigenesis. OTUD6B is a functional deubiquitinase in in vitro enzyme assays. It may play a role in the ubiquitin-dependent regulation of protein synthesis downstream of mTORC1, and may modify the ubiquitination of the protein synthesis initiation complex to repress translation. Biallelic variants in OTUD6B cause an intellectual disability syndrome that is associated with seizures and dysmorphic features. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 74.46  E-value: 1.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   31 LRSQGLYRKKVAKDGSCLFRAVAEQvLHSQSRHIDV---RMACVDYLRKHREKFEAFIEGP----------FEEYLKCLE 97
Cdd:cd22761      5 LKERGLKIHEIPSDGDCLYNAIAHQ-LSLRGIETSVeelRKQTADYMRENKDDFLPFLTNPdtgdplteeeFEKYCDDVE 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024407817   98 NPQEWVGQVEISALSLMYKKDF-IIYREpnaSPSHVTENGFSDK--VLLC-----FSNGNHYD 152
Cdd:cd22761     84 NTGAWGGQLELRALSHVLKRPIeVIQAE---GPPIIIGEEFKSGkpLILTyhrhaYGLGEHYN 143
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 44-123 2.72e-15

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


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 73.64  E-value: 2.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   44 DGSCLFRAVAEQV-----LHSQSRHIDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVGQVEISALSLMYKKD 118
Cdd:pfam02338    3 DGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82


                   ....*
gi 2024407817  119 FIIYR 123
Cdd:pfam02338   83 IIVYK 87
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
 38-152 1.48e-13

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: 68.83  E-value: 1.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   38 RKKVAKDGSCLFRAVAEQVLHSQ-----SRHIDV------RMACVDYLRKHREKFEA---FIEGPFEEYLKCLENPQEWV 103
Cdd:cd22746      4 VVPVKGDGRCLFRAVARGLALATggrplSERRERadadalRKAVVEEIRKRRDELFEgslVIEGDFDAYCQRMSHPDTWG 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024407817  104 GQVEISALSLMYKKDFIIY-REPNAS-PSHVTENG--FSDK--VLLCFSNGNHYD 152
Cdd:cd22746     84 GEPELLMLADVLQRPIAVYlPTPGKGgLRKIQEYGeeYLGGepIRLLYNGGNHYD 138
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
 44-155 9.32e-13

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: 66.07  E-value: 9.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   44 DGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKFEAF-------IEGPFEEYLKCLENPQEWVGQVEISALSLMYK 116
Cdd:cd22757      9 DGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYthdsegnNYKSAEEYRADMSKPGTYGTLCELVAAAELYP 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024407817  117 KDFIIYREPNAsPSHVTENGFSDKVLLC---FSNGnHYDiVY 155
Cdd:cd22757     89 FHFEVYRNGKL-YASFGDPSNPVKRLKFsgdLSNG-HFD-VL 127
OTU_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
 31-122 3.18e-12

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: 65.44  E-value: 3.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   31 LRSQGLYRKKVAKDGSCLFRAVAEQ-----VLHSQSRHIDVRMACVDYLRKHREKFEAFIEGP---------FEEYLKCL 96
Cdd:cd22797      5 LAPLGLAIKEIKADGHCLYRAVEDQlqlrgGGAPAPDYQQLRELAADYMRAHPDDFLPFLEDEdeggdgdeaFEAYCREV 84

                           90       100
                   ....*....|....*....|....*.
gi 2024407817   97 ENPQEWVGQVEISALSLMYKKDFIIY 122
Cdd:cd22797     85 ESTAAWGGQLELGALAHALRRHIKVY 110
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
 36-155 1.53e-09

OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin thioesterase (EC 3.4.19.12) OTU1 is also called OTU domain-containing protein 1 in yeast, while human OTU1 is also called HIV-1-induced protease 7 (HIN7), DUBA-8, or OTU domain-containing protein 2 (OTUD2). OTU1 is a deubiquitinase (DUB) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU1 has been implicated in the ER-associated degradation (ERAD) pathway. In yeast, it counteracts the activity of Ufd2 by deubiquitinating Ufd2 substrates; Ufd2 is a E4 ubiquitin ligase that interacts with Cdc48, an AAA ATPase that plays a central role in the ERAD pathway by chaperoning proteins to the proteasome for destruction. OTU1 also functions as a substrate-processing factor of valosin-containing protein (VCP, the mammalian counterpart of yeast Cdc48) that is required for the retrotranslocation of the ERAD pathway. OTU1 has been shown to preferentially hydrolyze polyubiquitin chains with Lys48 linkages. It contains ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU (ovarian tumor) domain. This model represents the OTU domain that interacts with ubiquitin and possesses catalytic activity. OTU1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. This family also contains plant OTU1 and OTU2.


Pssm-ID: 438582  Cd Length: 161  Bit Score: 57.88  E-value: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   36 LYRKKVAKDGSCLFRAVAEqVLH--SQSRHIDVRMACVDYLRKHREKF-EAFIEGPFEEYLKCLENPQEWVGQVEISALS 112
Cdd:cd22745      3 LVRRVVPDDNSCLFTSISY-LLEggLLDSAPELREIVADAILSDPDTYnEAILGKPPDEYCAWILKPDSWGGAIELSILS 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024407817  113 LMYK--------KDFIIYR--EpnaspshvtENGFSDKVLLCFSnGNHYDIVY 155
Cdd:cd22745     82 KHFGveicvvdvQTGRVDRfgE---------DKGYSKRIFLLYS-GIHYDALA 124
OTU_plant_OTU1_2-like cd22793
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar ...
 38-152 1.74e-09

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar proteins; Deubiquitinating enzyme OTU2, also called OTU domain-containing protein 2, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU2 exhibited equivalent binding affinities for K48- and K63-linked ubiquitin chains and no cleavage activity toward linear UB chains. It may also be involved in endoplasmic-reticulum-associated protein degradation (ERAD). OTU2 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438614  Cd Length: 163  Bit Score: 57.72  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   38 RKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKF-EAFIEGPFEEYLKCLENPQEWVGQVEISALSLMYK 116
Cdd:cd22793      5 RRVIDSDNSCLFNAVGYVMEGSRKKAPELRQVIADAVLSDPFEYnEAFLGKSNKEYCEWILNPNSWGGAIELSILSDHYG 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2024407817  117 KDFI----------IYREpnaspshvtENGFSDKVLLCFsNGNHYD 152
Cdd:cd22793     85 REIAafdiqtkrcdVYGE---------GKGYTERVMLIY-DGLHYD 120
OTU_plant_OTU4-like cd22760
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; ...
 40-152 1.78e-09

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


Pssm-ID: 438597 [Multi-domain]  Cd Length: 138  Bit Score: 57.00  E-value: 1.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   40 KVAKDGSCLFRAVA---------------EQVLHSQsrhiDVRMACVDYLRKHREKFEAFIEGPFEEYLKCLENPQEWVG 104
Cdd:cd22760      6 GIAGDGRCLFRAVAhgeclargkaapdeeRERELAD----ELRTRAADELVKRREETEWFIEGDFDEYVARMRRPGVWGG 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024407817  105 QVEISALSLMYKKDFIIY-REPNASP-----SHVTENGFSDKVLLCFSNGNHYD 152
Cdd:cd22760     82 EPELLMLSHVLQRPITVYmADEGEGGlisiaEYGQEYGKGNPIRVLFHGFGHYE 135
OTU_plant_OTU3-like cd22759
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; ...
 40-153 1.84e-09

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


Pssm-ID: 438596  Cd Length: 159  Bit Score: 57.74  E-value: 1.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   40 KVAKDGSCLFRAVAEQVLHSQSRHI----------DVRMACVDYL----RKHREKFEAFI----EGPFEEYLKCLENPQE 101
Cdd:cd22759      7 RVKGDGRCMFRALVKGLAANKGIFLsgreeeqeadELRLAVAEALcrseERRRDYEEALIaitvEGSLDRYCRRIQRPDF 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024407817  102 WVGQVEISALSLMYKKDFIIYREPNASPSHVTENGFS-------------------DKVLLCFSNGNHYDI 153
Cdd:cd22759     87 WGGESELLVLSKMLKQPIIVYIPESEAKNGGWGSGFIpiqkygeefakgtkgrkgrKPVRLLYSGSNHYDL 157
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
 38-157 1.28e-07

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: 52.22  E-value: 1.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   38 RKKVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREKF-EA--FIEGPfEEYLKCLENPQEWVGQVEISALSLM 114
Cdd:cd21880     24 IERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECpEArlYYLSL-EEYLRDAMKDGYWGGSLEAEILSKA 102

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024407817  115 YKKDFIIYREpnASPSHVT------ENGFSDKVLLCFsNGNHYDIVYPI 157
Cdd:cd21880    103 LGITIIIWVV--DDSDWVTaavrfgDGDVSTSLNLLH-SGGHFDALRLK 148
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
 40-112 2.46e-05

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: 45.29  E-value: 2.46e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024407817   40 KVAKDGSCLFRAVAEQVLHSQSRHIDVRMACVDYLRKHREkfeaFIEGPFEEYLKCLENPQEWVGQVEISALS 112
Cdd:cd22791      5 RVTGDGNCLFRAASLLLFGDESLHLELRLRTVLELVLNSE----FYEAIYEAEIKATCKPGSYSGIWHIYALS 73
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 521-776 1.43e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.22  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  521 DKESNSRQihlsqkLEPNSSERNSQDESCPKASSPLEQVKTDSPAvAEQKLTEcLPSVTPTPS-PVFSEVHLPPTVPSVP 599
Cdd:PTZ00449   526 DKEGEEGE------HEDSKESDEPKEGGKPGETKEGEVGKKPGPA-KEHKPSK-IPTLSKKPEfPKDPKHPKDPEEPKKP 597

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  600 AiVPAWPSEPTTYGPAGIP--AQIPASSLMPAPATGPDSIVSQAQTLNPY-----------QDPLYPGFPLSEKGERAIA 666
Cdd:PTZ00449   598 K-RPRSAQRPTRPKSPKLPelLDIPKSPKRPESPKSPKRPPPPQRPSSPErpegpkiikspKPPKSPKPPFDPKFKEKFY 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  667 PSYSLCSSGEDLPKDKNILRFFFNLGVKAySCPMWAPHSYLYPlhqaylaacRMYPnmslPVYPHNPWFQEAPPTQIENE 746
Cdd:PTZ00449   677 DDYLDAAAKSKETKTTVVLDESFESILKE-TLPETPGTPFTTP---------RPLP----PKLPRDEEFPFEPIGDPDAE 742

                          250       260       270
                   ....*....|....*....|....*....|
gi 2024407817  747 TVQPNRHFAIPSETRSNGQMSQVDSRSPSL 776
Cdd:PTZ00449   743 QPDDIEFFTPPEEERTFFHETPADTPLPDI 772
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
 67-155 1.97e-04

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: 44.25  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   67 RMACVDYLRKHREKFEAFIEG--PFEEYL-KCLENPQEWVGQVEISALSLMYKKDFIIY---REPNASPSHVT----ENG 136
Cdd:cd22749    135 RLLTSAYLKTNADDYEPFLFEgmSVEEFCeREVEPMGKEADHLQITALANALGVPVRVEyldRSAGGEVNFHEfppeDSD 214

                           90
                   ....*....|....*....
gi 2024407817  137 FSDKVLLCFSNGnHYDIVY 155
Cdd:cd22749    215 SLPVITLLYRPG-HYDILY 232
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 921-1103 3.11e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  921 APKETSARAPQLEQTCTSASPAKQATAGLQNRSTQIQGVERQTAVPNTTLPLAEPPKNELKNTAHGRKDKTDKVRDSKGA 1000
Cdd:PRK12678    97 AAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817 1001 GNLQTENRAQRVREESSEDENEVSDMLRSGRSKQFYNQTYGGGRRPRMEWGYSSRGGYQFPRNEEAWKGPPGRSRDEGNQ 1080
Cdd:PRK12678   177 DREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGE 256

                          170       180
                   ....*....|....*....|....
gi 2024407817 1081 YQRNFRGRPYR-NDRRRATLGDNQ 1103
Cdd:PRK12678   257 GRGGRRGRRFRdRDRRGRRGGDGG 280
PHA03247 PHA03247
large tegument protein UL36; Provisional
 537-663 3.65e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  537 PNSSERNSQDESCPKASSPLEQVKTD-----SPAVAEQKLTECLPSVTPTP--SPVFSEVHLPPTVPSVPAIVPAWPSEP 609
Cdd:PHA03247   362 PSSLEDLSAGRHHPKRASLPTRKRRSarhaaTPFARGPGGDDQTRPAAPVPasVPTPAPTPVPASAPPPPATPLPSAEPG 441

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024407817  610 TTYGPAGIPAQIPASSLMPAPATGPDSIVSQA-QTLNPYQDPLYPGFPLSEKGER 663
Cdd:PHA03247   442 SDDGPAPPPERQPPAPATEPAPDDPDDATRKAlDALRERRPPEPPGADLAELLGR 496
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 285-342 3.69e-04

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 39.56  E-value: 3.69e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024407817   285 QYSIGDKCKVRLDhNGKFYNAHIQEVCSENGpVVVFVEELGAKHSVSLKSLKPLPQAS 342
Cdd:smart00333    2 TFKVGDKVAARWE-DGEWYRARIVKVDGEQL-YEVFFIDYGNEEVVPPSDLRQLPEEL 57
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 913-1105 4.69e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.12  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  913 AGASSECSAPKETSARAPQLEQTCTSASPAKQATAGLQNRSTQIQGVERQTAVPNTTLPLAEPPKNELKNTAHGRKD--K 990
Cdd:PRK12678    64 AAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGaaR 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  991 TDKVRDSKGAGNLQTENRAQRVREESSEDENEVSDMLRSGRSKqfynqtyGGGRRPRMEwgySSRGGYQFPRNEEAWKGp 1070
Cdd:PRK12678   144 KAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAE-------RGERGRREE---RGRDGDDRDRRDRREQG- 212

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2024407817 1071 pGRSRDEGNQYQRNFRGRPYRNDRRRATLGDNQRG 1105
Cdd:PRK12678   213 -DRREERGRRDGGDRRGRRRRRDRRDARGDDNRED 246
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 289-338 6.89e-04

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410549  Cd Length: 50  Bit Score: 38.39  E-value: 6.89e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024407817  289 GDKCKVRLDHNGKFYNAHIQEVCSENGPVVVFVEELGAKHSVSLKSLKPL 338
Cdd:cd21182      1 GDKCLAPYSDDGKYYEATIEEITEESDTATVVFDGYGNSEEVPLSDLKPL 50
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
 286-339 8.22e-04

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. Overexpression of SPF30 causes apoptosis. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 38.44  E-value: 8.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024407817  286 YSIGDKCKVRLDHNGKFYNAHIQEVcSENGPVVVFVEELGAKHSVSLKSLKPLP 339
Cdd:cd20399      1 WKVGDKCMAVWSEDGQYYEATIEEI-SEDGTCTVTFDGYGNTEVTPLSQLKPRE 53
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 476-650 9.26e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  476 EQAFPALSNNQSVSQAATRTVDNPKKVSSNEKRSSKWTA--EVEEQKDKESNSRQIHLSQKLEPNSSERNSQDEScPKAS 553
Cdd:pfam03154   71 EEAPSPLKSAKRQREKGASDTEEPERATAKKSKTQEISRpnSPSEGEGESSDGRSVNDEGSSDPKDIDQDNRSTS-PSIP 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817  554 SPLEQvKTDSPAVAEQKLTECLPSVTPTPSPVfsevhLPPTVPSVPAIVPAWPSEPTTYGPAGIPAQIPASSLMPA---P 630
Cdd:pfam03154  150 SPQDN-ESDSDSSAQQQILQTQPPVLQAQSGA-----ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNqtqS 223

                          170       180
                   ....*....|....*....|
gi 2024407817  631 ATGPDSIVSQAQTLNPYQDP 650
Cdd:pfam03154  224 TAAPHTLIQQTPTLHPQRLP 243
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 288-338 1.13e-03

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 37.88  E-value: 1.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024407817  288 IGDKCKVRLDHNGKFYNAHIQEVCSENGPVVVFVeELGAKHSVSLKSLKPL 338
Cdd:cd20379      1 VGDLCAAKYEEDGKWYRARVLEVLSNDKVEVFFV-DYGNTETVPLSDLRPL 50
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
 38-157 2.30e-03

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: 38.74  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024407817   38 RKKVAKDGSCLFRAVAEqvlHSQSRHIDVRMACVDYLRKHrekfeafiEGPFEEYLKCLEnPQEWVGQVEISALSLMYKK 117
Cdd:cd22792      2 VVPVPGDGNCFWHSLGH---FLGLSALELKKLLRDSLFDD--------PELDEELDEQLE-PGVYAEDEAIAAAAKLFGV 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2024407817  118 DFIIYrEPNASPSHV-TENGFSDKVLLCFSNgNHYDIVYPI 157
Cdd:cd22792     70 NICVH-DPDEGVLYTfTPNESSKSIHLLLEN-EHFEPLVPK 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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