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Conserved domains on  [gi|808355133|ref|NP_001293465|]
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OTU domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
79-238 2.38e-67

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


:

Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 219.71  E-value: 2.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  79 IGRVVKEFDNNDQKDAHEYLTELLSCVDDIMQVV-------PDEIKHLDPLNSIRYKTERSFICFNCGHEEKSSDCGWIL 151
Cdd:cd02673   21 IGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNrtnvppsNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 152 PLSISNNDYGIIELLESNFKTTLETNKICSSCSCENAVSSERIANFPECLILNPMRY-ERTSISDYRKDNRQITVPLTLD 230
Cdd:cd02673  101 DVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSERIMTFPECLSINLKRYkLRIATSDYLKKNEEIMKKYCGT 180

                 ....*...
gi 808355133 231 LTRFGAFA 238
Cdd:cd02673  181 DAKYSLVA 188
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
347-467 3.85e-38

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: 137.39  E-value: 3.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRN--DIAIVDKYCHKTDHKTYVQQV--EGDGWWATNVEICVM 422
Cdd:cd22755    2 KTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKnpDEFRNLLRSDYESVEEYLEKSrmRYDGTWATDVEIFAA 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808355133 423 ANLLNVNIYTFLSDG--WICTSPQNSSTSRS---GSFYLENKD-CHYEPVL 467
Cdd:cd22755   82 ATLLGVDIYVYSKGGykWLLYSPRFKLGKRNgsrEAIYLKNTNgNHFEPVV 132
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
496-606 1.35e-30

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


The actual alignment was detected with superfamily member cd02673:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 245  Bit Score: 119.94  E-value: 1.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 496 FKKRKP--DDDASRKPRNLSESERRRQPPRDAEDNGNHYKKMNANTD--------------QIAKYRLFAAICHIGEFPD 559
Cdd:cd02673  119 FKTWSPieKDCSSCKCESAISSERIMTFPECLSINLKRYKLRIATSDylkkneeimkkycgTDAKYSLVAVICHLGESPY 198
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 808355133 560 RGHYLALTRDLYNPSKWLDCSDAVVRDISSGDVIKDASSSGYLLFYD 606
Cdd:cd02673  199 DGHYIAYTKELYNGSSWLYCSDDEIRPVSKNDVSTNARSSGYLIFYD 245
 
Name Accession Description Interval E-value
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
79-238 2.38e-67

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 219.71  E-value: 2.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  79 IGRVVKEFDNNDQKDAHEYLTELLSCVDDIMQVV-------PDEIKHLDPLNSIRYKTERSFICFNCGHEEKSSDCGWIL 151
Cdd:cd02673   21 IGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNrtnvppsNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 152 PLSISNNDYGIIELLESNFKTTLETNKICSSCSCENAVSSERIANFPECLILNPMRY-ERTSISDYRKDNRQITVPLTLD 230
Cdd:cd02673  101 DVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSERIMTFPECLSINLKRYkLRIATSDYLKKNEEIMKKYCGT 180

                 ....*...
gi 808355133 231 LTRFGAFA 238
Cdd:cd02673  181 DAKYSLVA 188
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
347-467 3.85e-38

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: 137.39  E-value: 3.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRN--DIAIVDKYCHKTDHKTYVQQV--EGDGWWATNVEICVM 422
Cdd:cd22755    2 KTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKnpDEFRNLLRSDYESVEEYLEKSrmRYDGTWATDVEIFAA 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808355133 423 ANLLNVNIYTFLSDG--WICTSPQNSSTSRS---GSFYLENKD-CHYEPVL 467
Cdd:cd22755   82 ATLLGVDIYVYSKGGykWLLYSPRFKLGKRNgsrEAIYLKNTNgNHFEPVV 132
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
496-606 1.35e-30

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 119.94  E-value: 1.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 496 FKKRKP--DDDASRKPRNLSESERRRQPPRDAEDNGNHYKKMNANTD--------------QIAKYRLFAAICHIGEFPD 559
Cdd:cd02673  119 FKTWSPieKDCSSCKCESAISSERIMTFPECLSINLKRYKLRIATSDylkkneeimkkycgTDAKYSLVAVICHLGESPY 198
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 808355133 560 RGHYLALTRDLYNPSKWLDCSDAVVRDISSGDVIKDASSSGYLLFYD 606
Cdd:cd02673  199 DGHYIAYTKELYNGSSWLYCSDDEIRPVSKNDVSTNARSSGYLIFYD 245
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-246 5.08e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 70.16  E-value: 5.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133    1 MQALSSCPSLVSRFemlhrLRHGNYLECPSYDLRPKFAvfESCLRMMVKLSDRMENPHLKEYRLPSFsetelantrlkIG 80
Cdd:pfam00443  16 LQSLFSIPPFRDYL-----LRISPLSEDSRYNKDINLL--CALRDLFKALQKNSKSSSVSPKMFKKS-----------LG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133   81 RVVKEFDNNDQKDAHEYLTELLSCVDDIMQVVPDEIKHLDPLNSIRYKTERSFICFNCGHEEKSSDCGWILPLSISNND- 159
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSa 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  160 -----YGIIELLESNFKTTLETNKICSSCSCENAVSSE---RIANFPECLILNPMRYERTSISdYRKDNRQITVPLTLDL 231
Cdd:pfam00443 158 elktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIkqlKISRLPPVLIIHLKRFSYNRST-WEKLNTEVEFPLELDL 236
                         250
                  ....*....|....*
gi 808355133  232 TRFGAFASLEQDENR 246
Cdd:pfam00443 237 SRYLAEELKPKTNNL 251
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
536-605 1.39e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 56.68  E-value: 1.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  536 NANTDQIAKYRLFAAICHIGEfPDRGHYLALTRDlYNPSKWLDCSDAVVRDISSGDVIKdaSSSGYLLFY 605
Cdd:pfam00443 245 KPKTNNLQDYRLVAVVVHSGS-LSSGHYIAYIKA-YENNRWYKFDDEKVTEVDEETAVL--SSSAYILFY 310
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
353-470 1.68e-08

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


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 53.22  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  353 SDGNCFYRAISWCL-----TGSQKYHKALRIATANYLRNdiaivdkycHK--------TDHKTYVQQVEGDGWWATNVEI 419
Cdd:pfam02338   2 GDGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMRE---------HKeefepfleDDETGDIIEIEQTGAWGGEIEI 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808355133  420 CVMANLLNVNIYTFLSdgwicTSPQNSSTSRSGSFYLEnkdCHYEPVLSLK 470
Cdd:pfam02338  73 FALAHILRRPIIVYKS-----EGGEELGGLKEYGIYLP---LGWDPSLCLV 115
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
535-607 3.11e-06

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 49.03  E-value: 3.11e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355133 535 MNANTDQIAK------YRLFAAICHIGEFpDRGHYLALTRDlyNPsKWLDCSDAVVRDISSGDVIKDASSSGYLLFYDR 607
Cdd:COG5533  209 LPVKHDQILNivketyYDLVGFVLHQGSL-EGGHYIAYVKK--GG-KWEKANDSDVTPVSEEEAINEKAKNAYLYFYER 283
 
Name Accession Description Interval E-value
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
79-238 2.38e-67

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 219.71  E-value: 2.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  79 IGRVVKEFDNNDQKDAHEYLTELLSCVDDIMQVV-------PDEIKHLDPLNSIRYKTERSFICFNCGHEEKSSDCGWIL 151
Cdd:cd02673   21 IGKINTEFDNDDQQDAHEFLLTLLEAIDDIMQVNrtnvppsNIEIKRLNPLEAFKYTIESSYVCIGCSFEENVSDVGNFL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 152 PLSISNNDYGIIELLESNFKTTLETNKICSSCSCENAVSSERIANFPECLILNPMRY-ERTSISDYRKDNRQITVPLTLD 230
Cdd:cd02673  101 DVSMIDNKLDIDELLISNFKTWSPIEKDCSSCKCESAISSERIMTFPECLSINLKRYkLRIATSDYLKKNEEIMKKYCGT 180

                 ....*...
gi 808355133 231 LTRFGAFA 238
Cdd:cd02673  181 DAKYSLVA 188
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
347-467 3.85e-38

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: 137.39  E-value: 3.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRN--DIAIVDKYCHKTDHKTYVQQV--EGDGWWATNVEICVM 422
Cdd:cd22755    2 KTIKIVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKnpDEFRNLLRSDYESVEEYLEKSrmRYDGTWATDVEIFAA 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808355133 423 ANLLNVNIYTFLSDG--WICTSPQNSSTSRS---GSFYLENKD-CHYEPVL 467
Cdd:cd22755   82 ATLLGVDIYVYSKGGykWLLYSPRFKLGKRNgsrEAIYLKNTNgNHFEPVV 132
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
496-606 1.35e-30

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 119.94  E-value: 1.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 496 FKKRKP--DDDASRKPRNLSESERRRQPPRDAEDNGNHYKKMNANTD--------------QIAKYRLFAAICHIGEFPD 559
Cdd:cd02673  119 FKTWSPieKDCSSCKCESAISSERIMTFPECLSINLKRYKLRIATSDylkkneeimkkycgTDAKYSLVAVICHLGESPY 198
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 808355133 560 RGHYLALTRDLYNPSKWLDCSDAVVRDISSGDVIKDASSSGYLLFYD 606
Cdd:cd02673  199 DGHYIAYTKELYNGSSWLYCSDDEIRPVSKNDVSTNARSSGYLIFYD 245
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
89-249 2.13e-20

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 91.01  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  89 NDQKDAHEYLTELLSCVDDIMQVVPDEIKHLDPLNSI-----RYKTERSFICFNCGHEEKSSDCGWILPLSISNNDYG-- 161
Cdd:cd02257   20 SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLihdlfGGKLESTIVCLECGHESVSTEPELFLSLPLPVKGLPqv 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 162 -IIELLESNFKTTLETNKICSSCSCE---NAVSSERIANFPECLILNPMRYERTSISDYRKDNRQITVPLTLDLTRFGAF 237
Cdd:cd02257  100 sLEDCLEKFFKEEILEGDNCYKCEKKkkqEATKRLKIKKLPPVLIIHLKRFSFNEDGTKEKLNTKVSFPLELDLSPYLSE 179
                        170
                 ....*....|..
gi 808355133 238 ASLEQDENRNSV 249
Cdd:cd02257  180 GEKDSDSDNGSY 191
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
347-466 1.32e-18

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: 82.10  E-value: 1.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRND-----IAIVDKYCHKTDHKTYVQQVEGDGWWATNVEICV 421
Cdd:cd22744    1 RVVDVPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENpdlyePAELADEDDGEDFDEYLQRMRKPGTWGGELELQA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 808355133 422 MANLLNVNIYTFLSDGWICTSP--QNSSTSRSGSFYLE-NKDCHYEPV 466
Cdd:cd22744   81 LANALNVPIVVYSEDGGFLPVSvfGPGPGPSGRPIHLLyTGGNHYDAL 128
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
347-430 2.36e-13

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: 66.81  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRNdiaivdkycHKTDHK----------TYVQQVEGDGWWATN 416
Cdd:cd22771    3 RIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEA---------HEEDFEpffeddetfeDYVSRMREDGTWGGN 73
                         90
                 ....*....|....
gi 808355133 417 VEICVMANLLNVNI 430
Cdd:cd22771   74 LELQAASLVYRVNI 87
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
1-246 5.08e-13

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 70.16  E-value: 5.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133    1 MQALSSCPSLVSRFemlhrLRHGNYLECPSYDLRPKFAvfESCLRMMVKLSDRMENPHLKEYRLPSFsetelantrlkIG 80
Cdd:pfam00443  16 LQSLFSIPPFRDYL-----LRISPLSEDSRYNKDINLL--CALRDLFKALQKNSKSSSVSPKMFKKS-----------LG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133   81 RVVKEFDNNDQKDAHEYLTELLSCVDDIMQVVPDEIKHLDPLNSIRYKTERSFICFNCGHEEKSSDCGWILPLSISNND- 159
Cdd:pfam00443  78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSa 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  160 -----YGIIELLESNFKTTLETNKICSSCSCENAVSSE---RIANFPECLILNPMRYERTSISdYRKDNRQITVPLTLDL 231
Cdd:pfam00443 158 elktaSLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIkqlKISRLPPVLIIHLKRFSYNRST-WEKLNTEVEFPLELDL 236
                         250
                  ....*....|....*
gi 808355133  232 TRFGAFASLEQDENR 246
Cdd:pfam00443 237 SRYLAEELKPKTNNL 251
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
347-463 5.93e-13

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: 66.14  E-value: 5.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCL--TGSQKYHKALRIATANYLRN----DIAIVDKYCHKTDH-KTYVQQVEGDGWWATNVEI 419
Cdd:cd22758    7 EIRDVPGDGNCFFHAVSDQLygNGIEHSHKELRQQAVNYLREnpelYDGFFLSEFDEEESwEEYLNRMSKDGTWGDHIIL 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 808355133 420 CVMANLLNVNIYTFLSDGWICT---SPQNSSTSRsgSFYLENKD-CHY 463
Cdd:cd22758   87 QAAANLFNVRIVIISSDGSDETtiiEPGNSKNGR--TIYLGHIGeNHY 132
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
534-605 1.06e-12

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 68.28  E-value: 1.06e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355133 534 KMNANTDQIAKYRLFAAICHIGEFPDRGHYLALTRDlYNPSKWLDCSDAVVRDISSGDVIKD--ASSSGYLLFY 605
Cdd:cd02257  182 KDSDSDNGSYKYELVAVVVHSGTSADSGHYVAYVKD-PSDGKWYKFNDDKVTEVSEEEVLEFgsLSSSAYILFY 254
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
354-468 3.51e-11

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: 61.02  E-value: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 354 DGNCFYRAISWCLTGSQKYHKALRIATANYLRNDIAIVDKYChKTDHKTYVQQVEGDGWWATNVEICVMANLLNVNIYTF 433
Cdd:cd22753   18 DGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFS-EISFDDYLERLSDPKEWGGLLELEALSLLYKVDFIVY 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 808355133 434 lsdgwicTSPQNSSTSRSGSFYLE------NKDCHYEPVLS 468
Cdd:cd22753   97 -------SIPDQPPSNITNNGYPKkimlcySGGNHYDSVYS 130
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
351-448 2.92e-09

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: 55.97  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 351 IESDGNCFYRAISWCLTGSQKYHKALRIATANYLRNDI----AIVDkychkTDHKTYVQQVEGDGWWATNVEICVMANLL 426
Cdd:cd22747   26 IIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLdefnPIIE-----GDVGEFLIKAAQDGAWAGYPELLAMGQML 100
                         90       100
                 ....*....|....*....|..
gi 808355133 427 NVNIYtfLSDGWICTSPQNSST 448
Cdd:cd22747  101 NVNIR--LTTGGSLESPTVSTM 120
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
347-437 3.43e-09

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: 55.65  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCL-----TGSQKYHKALRIATANYLRND--------IAIVDKYCHKTDHKTYVQQVEGDGWW 413
Cdd:cd22748    7 RIKEIPPDGHCLYRAIADQLklrggSEEPYSYKELRKLAADYMRAHrddflpflTNDDGDLMTEEEFEEYCDKIENTAEW 86
                         90       100
                 ....*....|....*....|....
gi 808355133 414 ATNVEICVMANLLNVNIYTFLSDG 437
Cdd:cd22748   87 GGQLELRALSKALKRPIHVYQAGS 110
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
347-430 4.92e-09

OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This subfamily includes bilaterial OTU domain-containing protein 3 (OTUD3), Arabidopsis thaliana deubiquitinating enzyme OTU7, also called OTU domain-containing protein 7, and similar proteins. OTUD3 is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. It is an acetylation-dependent deubiquitinase that restricts innate antiviral immune signaling. It directly hydrolyzes lysine 63 (Lys63)-linked polyubiquitination of MAVS (mitochondrial antiviral-signaling protein) and shuts off innate antiviral immune response. OTUD3 can elicit tumor-suppressing or tumor-promoting activities in a cell- and tissue-dependent manner. It is a DUB for PTEN (phosphatase and tension homologue deleted on chromosome 10); the OTUD3-PTEN signaling axis plays a critical role in suppression of breast tumorigenesis. OTUD3 is also a DUB for glucose-regulated protein GRP78, stabilizing it and promoting lung tumorigenesis. OTU7 is a DUB that shows a preference for 'Lys-63' over 'Lys-48' over 'Met-1'-linked ubiquitin (UB) tetramers as substrates. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438593 [Multi-domain]  Cd Length: 131  Bit Score: 54.87  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLR-------NDIAIVDKYCHKTDHKTYVQQVEGDGWWATNVEI 419
Cdd:cd22756    1 YAKDITGDGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRanpddfkPFSEAATFAEDDEAFEDYLARMAKDGTYGDNLEI 80
                         90
                 ....*....|.
gi 808355133 420 CVMANLLNVNI 430
Cdd:cd22756   81 VAFARAYNVDV 91
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
536-605 1.39e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 56.68  E-value: 1.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  536 NANTDQIAKYRLFAAICHIGEfPDRGHYLALTRDlYNPSKWLDCSDAVVRDISSGDVIKdaSSSGYLLFY 605
Cdd:pfam00443 245 KPKTNNLQDYRLVAVVVHSGS-LSSGHYIAYIKA-YENNRWYKFDDEKVTEVDEETAVL--SSSAYILFY 310
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
353-470 1.68e-08

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


Pssm-ID: 426728 [Multi-domain]  Cd Length: 127  Bit Score: 53.22  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  353 SDGNCFYRAISWCL-----TGSQKYHKALRIATANYLRNdiaivdkycHK--------TDHKTYVQQVEGDGWWATNVEI 419
Cdd:pfam02338   2 GDGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMRE---------HKeefepfleDDETGDIIEIEQTGAWGGEIEI 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808355133  420 CVMANLLNVNIYTFLSdgwicTSPQNSSTSRSGSFYLEnkdCHYEPVLSLK 470
Cdd:pfam02338  73 FALAHILRRPIIVYKS-----EGGEELGGLKEYGIYLP---LGWDPSLCLV 115
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
542-605 2.78e-08

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 54.60  E-value: 2.78e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355133 542 IAKYRLFAAICHIGEFpDRGHYLALTRDlYNPSKWLDCSDAVVRDISSGDVIkdaSSSGYLLFY 605
Cdd:cd02674  171 PFKYDLYAVVNHYGSL-NGGHYTAYCKN-NETNDWYKFDDSRVTKVSESSVV---SSSAYILFY 229
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
351-441 3.47e-08

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: 52.54  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 351 IESDGNCFYRAISWCLTGSQKYHKALRIATANYLRNDIAIVDKYCHKTDHKTYVQQVEGDGWWATNVEICVMANLLNVNI 430
Cdd:cd22751   15 VEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPELYYEFYVPEEYDEYLKKMSKDGEWGDELTLQAAADAFGVKI 94
                         90
                 ....*....|...
gi 808355133 431 Y--TFLSDGWICT 441
Cdd:cd22751   95 HviTSFEDNWFLE 107
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
87-230 5.44e-08

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 53.91  E-value: 5.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  87 DNNDQKDAHEYLTELLSCVDDImqvvpdeikhldPLNSIRYKTERSFICFNCGHEEK-SSDCGWILPLSISNNDYGIIEL 165
Cdd:cd02662   30 EFLEQQDAHELFQVLLETLEQL------------LKFPFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSGSGTT 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355133 166 LESNFKTTLETNKI----CSSCSCenavsseRIANFPECLILNPMRYERTSISDYRKDNRQITVPLTLD 230
Cdd:cd02662   98 LEHCLDDFLSTEIIddykCDRCQT-------VIVRLPQILCIHLSRSVFDGRGTSTKNSCKVSFPERLP 159
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
527-605 5.70e-08

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 55.07  E-value: 5.70e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355133 527 DNGNHYKKMNANTDQIAKYRLFAAICHIGEFpDRGHYLALTRdlYNPSKWLDCSDAVVRDISSGDVIKdasSSGYLLFY 605
Cdd:cd02660  255 SSSIGDTQDSNSLDPDYTYDLFAVVVHKGTL-DTGHYTAYCR--QGDGQWFKFDDAMITRVSEEEVLK---SQAYLLFY 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
1-230 8.71e-08

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 54.25  E-value: 8.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133   1 MQALSSCPSLVSRFEMLhrlRHGNYLEC--PSYDLRPKFAvfesclrmmvKLSDRM-ENPHLKEYRLPSfSETE----LA 73
Cdd:cd02658   15 LQVLFSIPSFQWRYDDL---ENKFPSDVvdPANDLNCQLI----------KLADGLlSGRYSKPASLKS-ENDPyqvgIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  74 NTRLK--IGRVVKEFDNNDQKDAHEYLTELLSCVDDIMQVVPDeikhLDPLNSIRYKTERSFICFNCGHEEKSSDCGWIL 151
Cdd:cd02658   81 PSMFKalIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLG----LNPNDLFKFMIEDRLECLSCKKVKYTSELSEIL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 152 PLSISNNDYGIIEL---------LESNFKTTLETNKI---CSSCSCE-NAVSSERIANFPECLILNPMRYERTSISDYRK 218
Cdd:cd02658  157 SLPVPKDEATEKEEgelvyepvpLEDCLKAYFAPETIedfCSTCKEKtTATKTTGFKTFPDYLVINMKRFQLLENWVPKK 236
                        250
                 ....*....|..
gi 808355133 219 DNRQITVPLTLD 230
Cdd:cd02658  237 LDVPIDVPEELG 248
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
345-432 1.82e-07

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: 50.30  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 345 PGRVKGiesDGNCFYRAISWCLTGSQKYHKALRIATanylrndiaIVDKYCHKTDHKTYVQQ----VEGDGWWATNVEIC 420
Cdd:cd22791    3 PLRVTG---DGNCLFRAASLLLFGDESLHLELRLRT---------VLELVLNSEFYEAIYEAeikaTCKPGSYSGIWHIY 70
                         90
                 ....*....|..
gi 808355133 421 VMANLLNVNIYT 432
Cdd:cd22791   71 ALSSVLQRPIFS 82
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
347-466 1.18e-06

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: 47.93  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRNDIAIVDKYCHKtDHKTYVQQVEGDGWWATNVEICVMANLL 426
Cdd:cd22752    3 IIKEMEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYFSQFVTE-DFEEYINRKRQDGVWGNHIEIQAMSELY 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 808355133 427 NVNIYTFLSDgwicTSPQNSstsrsgsfYLENKDCHYEPV 466
Cdd:cd22752   82 NRPIEVYAYS----TEPINT--------FHEASSSDNEPI 109
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
347-433 2.32e-06

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: 47.20  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRNDIAIVDKYCHKTDHKTYVQQVE------GDGWWATNVEIC 420
Cdd:cd22757    2 RVIPIPGDGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYTHDSEGNNYKSAEEyradmsKPGTYGTLCELV 81
                         90
                 ....*....|...
gi 808355133 421 VMANLLNVNIYTF 433
Cdd:cd22757   82 AAAELYPFHFEVY 94
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
535-607 3.11e-06

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 49.03  E-value: 3.11e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355133 535 MNANTDQIAK------YRLFAAICHIGEFpDRGHYLALTRDlyNPsKWLDCSDAVVRDISSGDVIKDASSSGYLLFYDR 607
Cdd:COG5533  209 LPVKHDQILNivketyYDLVGFVLHQGSL-EGGHYIAYVKK--GG-KWEKANDSDVTPVSEEEAINEKAKNAYLYFYER 283
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
535-605 8.17e-06

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 48.04  E-value: 8.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355133 535 MNANTDQIAKYRLFAAICHIGEFPDRGHYLALTRDLynPSKWLDCSDAVVRDISSGDVIkdaSSSGYLLFY 605
Cdd:cd02661  238 MSQPNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSS--NGKWYNMDDSKVSPVSIETVL---SQKAYILFY 303
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
85-240 1.24e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 47.42  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  85 EFDNNDQKDAHEYLTELLSCVD---------DIMQVVPDEIKhldplNSIRYKTErsfiCFNCGHEEKSSDCGWILPLSI 155
Cdd:cd02668   82 GLDTGQQQDAQEFSKLFLSLLEaklsksknpDLKNIVQDLFR-----GEYSYVTQ----CSKCGRESSLPSKFYELELQL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 156 SNN---DYGIIELLeSNFKTTLETNKICSSC-SCENAVSSERIANFPECLILNPMRYERTSISDYRKD-NRQITVPLTLD 230
Cdd:cd02668  153 KGHktlEECIDEFL-KEEQLTGDNQYFCESCnSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKlNASISFPEILD 231
                        170
                 ....*....|
gi 808355133 231 LTRFGAFASL 240
Cdd:cd02668  232 MGEYLAESDE 241
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
89-239 1.77e-05

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 46.51  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  89 NDQKDAHEYLTELLSCVDDImqvvpdeikhLDPLNSIRYKteRSFICFNCGHEEKSSDCGWILPLSISNNDYG-----II 163
Cdd:cd02674   20 ADQQDAQEFLLFLLDGLHSI----------IVDLFQGQLK--SRLTCLTCGKTSTTFEPFTYLSLPIPSGSGDapkvtLE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 164 ELLESNFKT-TLETNKICSSCSCE---NAVSSERIANFPECLILNPMRYERTSISdYRKDNRQITVPLT-LDLTRFGAFA 238
Cdd:cd02674   88 DCLRLFTKEeTLDGDNAWKCPKCKkkrKATKKLTISRLPKVLIIHLKRFSFSRGS-TRKLTTPVTFPLNdLDLTPYVDTR 166

                 .
gi 808355133 239 S 239
Cdd:cd02674  167 S 167
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
354-467 2.00e-05

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 43.75  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 354 DGNCFYRAISwCLTGSQkyHKALRIATANYLRNDIAIvdkychktdHKTYVQQVEgDGWWATNVEICVMANLLNVNIYTF 433
Cdd:cd22792    8 DGNCFWHSLG-HFLGLS--ALELKKLLRDSLFDDPEL---------DEELDEQLE-PGVYAEDEAIAAAAKLFGVNICVH 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 808355133 434 -LSDGWICTSPQNSStSRSGSFYLENKdcHYEPVL 467
Cdd:cd22792   75 dPDEGVLYTFTPNES-SKSIHLLLENE--HFEPLV 106
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
538-605 8.08e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 44.99  E-value: 8.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355133 538 NTDQIakYRLFAAICHIGEFPDRGHYLALTRDLYnpsKWLDCSDAVVRDISSGDV-----IKDASSSGYLLFY 605
Cdd:cd02663  232 NPDRL--YELVAVVVHIGGGPNHGHYVSIVKSHG---GWLLFDDETVEKIDENAVeeffgDSPNQATAYVLFY 299
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
87-262 8.57e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 44.94  E-value: 8.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  87 DNNDQKDAHEYLTELLSCVDDIMQ--VVPDEIKhldplNSIRYKTERSFICFNCGHEEKSSDCGWILPLSISNNDyGIIE 164
Cdd:cd02659   82 NTFEQHDVQEFFRVLFDKLEEKLKgtGQEGLIK-----NLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKK-NLEE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 165 LLESNFKT-TLE-TNKI-CSSCsCE--NAVSSERIANFPECLILNPMRYERTSISDYR-KDNRQITVPLTLDLTRFgafa 238
Cdd:cd02659  156 SLDAYVQGeTLEgDNKYfCEKC-GKkvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRiKINDRFEFPLELDMEPY---- 230
                        170       180
                 ....*....|....*....|....
gi 808355133 239 sLEQDENRNSVSFGSCGKDSIKYR 262
Cdd:cd02659  231 -TEKGLAKKEGDSEKKDSESYIYE 253
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
354-442 2.62e-04

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: 41.43  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 354 DGNCFYRAISWCLTGSQKYHKALRIATANYLRN--DIAIVDKYCHKT-DHktYVQQVEGDGWWATNVEICVMANLLNVNI 430
Cdd:cd21880   30 DGNCFFRSIAELLFDTEDEWRLVKNTIESYARAnwDECPEARLYYLSlEE--YLRDAMKDGYWGGSLEAEILSKALGITI 107
                         90
                 ....*....|...
gi 808355133 431 YTFLSDG-WICTS 442
Cdd:cd21880  108 IIWVVDDsDWVTA 120
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
543-605 2.86e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 43.08  E-value: 2.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355133 543 AKYRLFAAICHIGEFPDRGHYLALTR-DLYNPSKWLDCSDAVVRDISSGDVIKDassSGYLLFY 605
Cdd:cd02658  250 GKYELIAFISHKGTSVHSGHYVAHIKkEIDGEGKWVLFNDEKVVASQDPPEMKK---LGYIYFY 310
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
347-437 3.32e-04

OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; This subfamily includes Schizosaccharomyces pombe and Saccharomyces cerevisiae OTU domain-containing protein 2 (OTU2) and similar proteins. S. pombe OTU2 is a ubiquitin thioesterase/hydrolase (EC 3.4.19.12) that can remove conjugated ubiquitin from protein substrates and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Fungal OTU2 bbelongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438599 [Multi-domain]  Cd Length: 142  Bit Score: 41.06  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLT--GSQKY--HKALRIATANYLR--------------NDIAIVDKYCHKtdhktyvqqVE 408
Cdd:cd22762    8 EEHDIKPDGHCLFAAIADQLQlrGSEINldYKELRKLAAEYIRkhpddfepflfeetDELEDIDEYCKK---------IE 78
                         90       100
                 ....*....|....*....|....*....
gi 808355133 409 GDGWWATNVEICVMANLLNVNIYTFLSDG 437
Cdd:cd22762   79 NTAEWGGELELLALAKAFGVPIHVVQAEG 107
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
91-250 6.72e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 42.36  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133  91 QKDAHEYLTELL-----SCVDDImqvvpDEIKHLDPLNSIRYKT-----ERSFICFNCGHEEKSSDCGWILPLSISNNDY 160
Cdd:cd02660   88 QQDAHEFFQFLLdqlhtHYGGDK-----NEANDESHCNCIIHQTfsgslQSSVTCQRCGGVSTTVDPFLDLSLDIPNKST 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 161 GIIELLESNFKTTL----------------ETNKICSSC-SCENAVSSERIANFPECLILNPMRYERTSISDYRKDNRQI 223
Cdd:cd02660  163 PSWALGESGVSGTPtlsdcldrftrpeklgDFAYKCSGCgSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKTSRKIDTYV 242
                        170       180
                 ....*....|....*....|....*..
gi 808355133 224 TVPLTLDLTRFGAFASLEQDENRNSVS 250
Cdd:cd02660  243 QFPLELNMTPYTSSSIGDTQDSNSLDP 269
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
347-430 7.77e-04

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: 40.18  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIESDGNCFYRAISWCLT--GSQKYHKALRIATANYLRndiaivdkyCHK-------TDHKT-----------YVQQ 406
Cdd:cd22761   11 KIHEIPSDGDCLYNAIAHQLSlrGIETSVEELRKQTADYMR---------ENKddflpflTNPDTgdplteeefekYCDD 81
                         90       100
                 ....*....|....*....|....
gi 808355133 407 VEGDGWWATNVEICVMANLLNVNI 430
Cdd:cd22761   82 VENTGAWGGQLELRALSHVLKRPI 105
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
349-423 1.88e-03

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: 38.89  E-value: 1.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808355133 349 KGIESDGNCFYRAISWCLTGSQKYHKALRIATANYLRNDIAIVDKYChKTDHKTYVQQVEGDGWWATNVEICVMA 423
Cdd:cd22794   13 KQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFI-EGPFEQYLKNLENPKEWAGQVEISALS 86
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
544-606 2.09e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 40.04  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 544 KYRLFAAICHIGeFPDRGHYLALTR-------------------DLYNPSKWLDCSDAVVRDISSGDVIkdASSSGYLLF 604
Cdd:cd02662  162 LYRLRAVVVHYG-SHSSGHYVCYRRkplfskdkepgsfvrmregPSSTSHPWWRISDTTVKEVSESEVL--EQKSAYMLF 238

                 ..
gi 808355133 605 YD 606
Cdd:cd02662  239 YE 240
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
545-605 2.56e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 40.26  E-value: 2.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355133 545 YRLFAAICHIGEFPDRGHYLALTRdlynpskWLDCSDAVVRDISSGDVIKDAS------SSGYLLFY 605
Cdd:cd02671  272 YRLFAVVMHSGATISSGHYTAYVR-------WLLFDDSEVKVTEEKDFLEALSpntsstSTPYLLFY 331
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
544-605 3.16e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 39.68  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 544 KYRLFAAICHIGEFpDRGHYLALTRD--------------------LYNPSKWLDCSDAVVRDISSGDVIKdasSSGYLL 603
Cdd:cd02667  201 LYRLYGVVEHSGTM-RSGHYVAYVKVrppqqrlsdltkskpaadeaGPGSGQWYYISDSDVREVSLEEVLK---SEAYLL 276

                 ..
gi 808355133 604 FY 605
Cdd:cd02667  277 FY 278
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
347-433 4.62e-03

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


Pssm-ID: 438617 [Multi-domain]  Cd Length: 128  Bit Score: 37.40  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355133 347 RVKGIE-----SDGNCFYRAISWCLTGSQKYHKALRIATANYLRNDIAIVDKYCHKtDHKTYVQQVEGDGWWATNVEICV 421
Cdd:cd22796    1 KKKGLEirrmdGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTE-DFTQYVKRKRRDRVFGNNLEIQA 79
                         90
                 ....*....|..
gi 808355133 422 MANLLNVNIYTF 433
Cdd:cd22796   80 MSEIYNRPIEVY 91
 
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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