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Conserved domains on  [gi|2462597716|ref|XP_054206246|]
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OTU domain-containing protein 4 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OTU super family cl45892
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 1-96 2.20e-56

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.


The actual alignment was detected with superfamily member cd22794:

Pssm-ID: 459237 [Multi-domain]  Cd Length: 130  Bit Score: 190.66  E-value: 2.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    1 MACIHYLRENREKFEAvtcnfkhFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEK 80
Cdd:cd22794     42 KACVDYLRRNREKFEA-------FIEGPFEQYLKNLENPKEWAGQVEISALSLMYKRDFIIYQEPGKPPSNVTENGFPDK 114

                           90
                   ....*....|....*.
gi 2462597716   81 VLLCFSNGNHYDIVYP 96
Cdd:cd22794    115 ILLCFSNGNHYDSVYP 130
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 217-276 1.22e-29

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


The actual alignment was detected with superfamily member cd20448:

Pssm-ID: 470623  Cd Length: 64  Bit Score: 112.28  E-value: 1.22e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462597716  217 DYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGIHSENGPVLV--EELGKKHTS--KNLKAPPP 276
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTVplKNLKPPPQ 64
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 485-828 4.80e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  485 TVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPavPSLPATVPAWPS--EPTTFGPTGVPAPIPVLSVTq 562
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSlaDPPPPPPTPEPAPHALVSAT- 2719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  563 TLTTGPDSAVSQAHLTPSpVPVSIQAVNQPLMPL-------PQTLSLYQDPLYPGFPCNEKGDRAIVPPY-SLCQTGEDL 634
Cdd:PHA03247  2720 PLPPGPAAARQASPALPA-APAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaSLSESRESL 2798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  635 PKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVP--------VYPHNPwFQEAPAAQNESDCTCT 706
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpslplggsVAPGGD-VRRRPPSRSPAAKPAA 2877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  707 DAHFPMQteasvngQMPQPEIGPPTFSSPLviPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKnmfPQPSFGP 786
Cdd:PHA03247  2878 PARPPVR-------RLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR---PQPPLAP 2945

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2462597716  787 NPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDE 828
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 1-96 2.20e-56

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: 190.66  E-value: 2.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    1 MACIHYLRENREKFEAvtcnfkhFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEK 80
Cdd:cd22794     42 KACVDYLRRNREKFEA-------FIEGPFEQYLKNLENPKEWAGQVEISALSLMYKRDFIIYQEPGKPPSNVTENGFPDK 114

                           90
                   ....*....|....*.
gi 2462597716   81 VLLCFSNGNHYDIVYP 96
Cdd:cd22794    115 ILLCFSNGNHYDSVYP 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 217-276 1.22e-29

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: 112.28  E-value: 1.22e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462597716  217 DYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGIHSENGPVLV--EELGKKHTS--KNLKAPPP 276
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTVplKNLKPPPQ 64
PHA03247 PHA03247
large tegument protein UL36; Provisional
 485-828 4.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  485 TVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPavPSLPATVPAWPS--EPTTFGPTGVPAPIPVLSVTq 562
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSlaDPPPPPPTPEPAPHALVSAT- 2719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  563 TLTTGPDSAVSQAHLTPSpVPVSIQAVNQPLMPL-------PQTLSLYQDPLYPGFPCNEKGDRAIVPPY-SLCQTGEDL 634
Cdd:PHA03247  2720 PLPPGPAAARQASPALPA-APAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaSLSESRESL 2798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  635 PKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVP--------VYPHNPwFQEAPAAQNESDCTCT 706
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpslplggsVAPGGD-VRRRPPSRSPAAKPAA 2877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  707 DAHFPMQteasvngQMPQPEIGPPTFSSPLviPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKnmfPQPSFGP 786
Cdd:PHA03247  2878 PARPPVR-------RLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR---PQPPLAP 2945

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2462597716  787 NPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDE 828
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 2-63 9.21e-05

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: 43.21  E-value: 9.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462597716    2 ACIHYLRENREKFEAvtcnfkhFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYR 63
Cdd:pfam02338   33 TLAEYMREHKEEFEP-------FLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRPIIVYK 87
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 472-801 1.02e-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: 46.68  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  472 PSTLENITDDkyatvSSPSKSKKLECPSPAEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGV 551
Cdd:pfam03154  149 PSPQDNESDS-----DSSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  552 PAPIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPCN 614
Cdd:pfam03154  222 QSTAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLT 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  615 EKGDRAIVPPYSLCQ------------------TGEDLPKDKNILRFFFNL-GVKAYSC----PMWAPHSYLYPLHQAYL 671
Cdd:pfam03154  302 PQSSQSQVPPGPSPAapgqsqqrihtppsqsqlQSQQPPREQPLPPAPLSMpHIKPPPTtpipQLPNPQSHKHPPHLSGP 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  672 AACRMYPKVPVPvyphnpwfqeaPAAQNESDCTC---TDAHFPMQTEASVNGQMPQPEIGPPTFSSPLVIPPSqvSESHG 748
Cdd:pfam03154  382 SPFQMNSNLPPP-----------PALKPLSSLSThhpPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPP--AASHP 448

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462597716  749 QLSYQADLESETPgqllhadyeeslsgknmFPQPSFGPNpflGPVPIAPPFFP 801
Cdd:pfam03154  449 PTSGLHQVPSQSP-----------------FPQHPFVPG---GPPPITPPSGP 481
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 1-96 2.20e-56

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: 190.66  E-value: 2.20e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    1 MACIHYLRENREKFEAvtcnfkhFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEK 80
Cdd:cd22794     42 KACVDYLRRNREKFEA-------FIEGPFEQYLKNLENPKEWAGQVEISALSLMYKRDFIIYQEPGKPPSNVTENGFPDK 114

                           90
                   ....*....|....*.
gi 2462597716   81 VLLCFSNGNHYDIVYP 96
Cdd:cd22794    115 ILLCFSNGNHYDSVYP 130
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 2-96 2.15e-37

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: 136.86  E-value: 2.15e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREKFEAvtcnfkhFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKV 81
Cdd:cd22795     43 ACVSYMRANQCNFES-------YVEGSFEKYLERLEDPKESAGQLEISALSLIYNRDFILYRYPGKPPTYATDNGFEDKI 115

                           90
                   ....*....|....*
gi 2462597716   82 LLCFSNGNHYDIVYP 96
Cdd:cd22795    116 LLCCSSNGHYDSVYT 130
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 2-96 1.10e-36

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: 134.59  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREKFEavtcnfkHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKV 81
Cdd:cd22753     43 ACVEYLEKNREEFE-------KFSEISFDDYLERLSDPKEWGGLLELEALSLLYKVDFIVYSIPDQPPSNITNNGYPKKI 115

                           90
                   ....*....|....*
gi 2462597716   82 LLCFSNGNHYDIVYP 96
Cdd:cd22753    116 MLCYSGGNHYDSVYS 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 217-276 1.22e-29

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: 112.28  E-value: 1.22e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462597716  217 DYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGIHSENGPVLV--EELGKKHTS--KNLKAPPP 276
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTVplKNLKPPPQ 64
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 2-94 2.76e-15

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


Pssm-ID: 438581 [Multi-domain]  Cd Length: 128  Bit Score: 73.24  E-value: 2.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREKFEAVtCNFKHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEK- 80
Cdd:cd22744     33 EVVDYLRENPDLYEPA-ELADEDDGEDFDEYLQRMRKPGTWGGELELQALANALNVPIVVYSEDGGFLPVSVFGPGPGPs 111

                           90
                   ....*....|....*..
gi 2462597716   81 ---VLLCFSNGNHYDIV 94
Cdd:cd22744    112 grpIHLLYTGGNHYDAL 128
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
 225-272 4.27e-15

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: 70.30  E-value: 4.27e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462597716  225 QYEVGDKCQVRLDHNGKFLNADVQGIHSENGPVLV--EELGKKHT--SKNLK 272
Cdd:cd20380      1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVfvEELGEKKTvpYENLK 52
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 2-94 3.09e-12

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: 64.50  E-value: 3.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREKFEavtcnfkHFIEG--SFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREpNVSPSQVTenNFPE 79
Cdd:cd22771     35 KVVDYMEAHEEDFE-------PFFEDdeTFEDYVSRMREDGTWGGNLELQAASLVYRVNIVVHQL-GQPRWEIE--NFPD 104

                           90
                   ....*....|....*....
gi 2462597716   80 K----VLLCFSNGNHYDIV 94
Cdd:cd22771    105 KgartIHLSYHDGEHYNSV 123
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 222-286 5.16e-12

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: 62.56  E-value: 5.16e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462597716  222 AGLQYEVGDKCQVRLDHNGKFLNADVQ--GIHSENGPVLVEELGKKHTSK--NLK----APPPESWNTVSGKK 286
Cdd:cd20447      2 AGRQYYLGDKCQVRLEPGGKYYNAHIQevGQDSNSVTVFIEELAEKHTVPlaNLKpvtqVTPVPAWNMMPNRK 74
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 6-94 4.60e-11

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: 61.42  E-value: 4.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    6 YLRENREKFEAVTCNFKHF-IEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYRE---PNVSPSQVTENNFPEKV 81
Cdd:cd22756     37 YMRANPDDFKPFSEAATFAeDDEAFEDYLARMAKDGTYGDNLEIVAFARAYNVDVKVYQPdpvYVISAPEDGSPGPARRV 116

                           90
                   ....*....|....
gi 2462597716   82 L-LCFSNGNHYDIV 94
Cdd:cd22756    117 LhIAYHNWEHYSSV 130
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
 2-91 5.75e-10

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: 58.43  E-value: 5.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREKFEAVTCNFkHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYRE-PNVSPSQVTENNFPEK 80
Cdd:cd22758     41 QAVNYLRENPELYDGFFLSE-FDEEESWEEYLNRMSKDGTWGDHIILQAAANLFNVRIVIISSdGSDETTIIEPGNSKNG 119

                           90
                   ....*....|...
gi 2462597716   81 --VLLCFSNGNHY 91
Cdd:cd22758    120 rtIYLGHIGENHY 132
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 6-91 1.01e-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: 57.96  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    6 YLRENREKFEA--VTCNFKHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPnvSPSQVTENNFPEK--V 81
Cdd:cd22748     48 YMRAHRDDFLPflTNDDGDLMTEEEFEEYCDKIENTAEWGGQLELRALSKALKRPIHVYQAG--SPPLVIGEEFDSGepL 125

                           90
                   ....*....|....*
gi 2462597716   82 LLCF-----SNGNHY 91
Cdd:cd22748    126 RLSYhrhayGLGEHY 140
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 2-96 3.59e-09

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: 55.63  E-value: 3.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREKFEavtcnfkHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIY---REP-NVSPSQVTENNF 77
Cdd:cd22752     35 HCMDYMEKNRDYFS-------QFVTEDFEEYINRKRQDGVWGNHIEIQAMSELYNRPIEVYaysTEPiNTFHEASSSDNE 107

                           90
                   ....*....|....*....
gi 2462597716   78 PekVLLCFSNGNHYDIVYP 96
Cdd:cd22752    108 P--IRLSYHGNSHYNSIVD 124
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
 2-95 1.93e-07

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: 50.89  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREkfeavtcNFKHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSP-----SQVTENN 76
Cdd:cd22796     38 MCMDYMEKERD-------HFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAMSEIYNRPIEVYSYSNGEPinifhGSYEGDD 110

                           90
                   ....*....|....*....
gi 2462597716   77 FPekVLLCFSNGNHYDIVY 95
Cdd:cd22796    111 PP--IRLSYHDGNHYNSII 127
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
 1-92 1.27e-06

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


Pssm-ID: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 48.80  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    1 MACIHYLRENREKFEAvtcnFKHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIY----REPNVSPSQVTENN 76
Cdd:cd22746     45 KAVVEEIRKRRDELFE----GSLVIEGDFDAYCQRMSHPDTWGGEPELLMLADVLQRPIAVYlptpGKGGLRKIQEYGEE 120

                           90
                   ....*....|....*...
gi 2462597716   77 FP--EKVLLCFSNGNHYD 92
Cdd:cd22746    121 YLggEPIRLLYNGGNHYD 138
PHA03247 PHA03247
large tegument protein UL36; Provisional
 485-828 4.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  485 TVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPavPSLPATVPAWPS--EPTTFGPTGVPAPIPVLSVTq 562
Cdd:PHA03247  2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPTVGSLTSlaDPPPPPPTPEPAPHALVSAT- 2719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  563 TLTTGPDSAVSQAHLTPSpVPVSIQAVNQPLMPL-------PQTLSLYQDPLYPGFPCNEKGDRAIVPPY-SLCQTGEDL 634
Cdd:PHA03247  2720 PLPPGPAAARQASPALPA-APAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaSLSESRESL 2798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  635 PKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVP--------VYPHNPwFQEAPAAQNESDCTCT 706
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPpslplggsVAPGGD-VRRRPPSRSPAAKPAA 2877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  707 DAHFPMQteasvngQMPQPEIGPPTFSSPLviPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKnmfPQPSFGP 786
Cdd:PHA03247  2878 PARPPVR-------RLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR---PQPPLAP 2945

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2462597716  787 NPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDE 828
Cdd:PHA03247  2946 TTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSRE 2987
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 6-52 7.94e-06

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: 46.45  E-value: 7.94e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2462597716    6 YLRENREKFEAVTCNfKHFIEGSFEEYLKRLENPQEWVGQVEISALS 52
Cdd:cd22762     48 YIRKHPDDFEPFLFE-ETDELEDIDEYCKKIENTAEWGGELELLALA 93
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 1-94 1.40e-05

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: 45.71  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    1 MACIHYLRENREKFEavtcNFKHFIEGSFEEYLKRLENPQ--EWVGQVEISALSLM-------YRKDF---IIYRePNVS 68
Cdd:cd22755     33 KAIVDFLEKNPDEFR----NLLRSDYESVEEYLEKSRMRYdgTWATDVEIFAAATLlgvdiyvYSKGGykwLLYS-PRFK 107

                           90       100
                   ....*....|....*....|....*.
gi 2462597716   69 PSQVTENNFPekVLLCFSNGNHYDIV 94
Cdd:cd22755    108 LGKRNGSREA--IYLKNTNGNHFEPV 131
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 2-63 9.21e-05

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: 43.21  E-value: 9.21e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462597716    2 ACIHYLRENREKFEAvtcnfkhFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYR 63
Cdd:pfam02338   33 TLAEYMREHKEEFEP-------FLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRPIIVYK 87
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 472-801 1.02e-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: 46.68  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  472 PSTLENITDDkyatvSSPSKSKKLECPSPAEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGV 551
Cdd:pfam03154  149 PSPQDNESDS-----DSSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQT 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  552 PAPIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPCN 614
Cdd:pfam03154  222 QSTAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLT 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  615 EKGDRAIVPPYSLCQ------------------TGEDLPKDKNILRFFFNL-GVKAYSC----PMWAPHSYLYPLHQAYL 671
Cdd:pfam03154  302 PQSSQSQVPPGPSPAapgqsqqrihtppsqsqlQSQQPPREQPLPPAPLSMpHIKPPPTtpipQLPNPQSHKHPPHLSGP 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  672 AACRMYPKVPVPvyphnpwfqeaPAAQNESDCTC---TDAHFPMQTEASVNGQMPQPEIGPPTFSSPLVIPPSqvSESHG 748
Cdd:pfam03154  382 SPFQMNSNLPPP-----------PALKPLSSLSThhpPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPP--AASHP 448

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462597716  749 QLSYQADLESETPgqllhadyeeslsgknmFPQPSFGPNpflGPVPIAPPFFP 801
Cdd:pfam03154  449 PTSGLHQVPSQSP-----------------FPQHPFVPG---GPPPITPPSGP 481
OTU_plant_OTU3-like cd22759
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; ...
 25-93 1.03e-04

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: 43.87  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716   25 IEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYRE----------PNVSPSQVTENNFPEK---------VLLCF 85
Cdd:cd22759     70 VEGSLDRYCRRIQRPDFWGGESELLVLSKMLKQPIIVYIPeseaknggwgSGFIPIQKYGEEFAKGtkgrkgrkpVRLLY 149


                   ....*...
gi 2462597716   86 SNGNHYDI 93
Cdd:cd22759    150 SGSNHYDL 157
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
 6-52 2.28e-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: 42.49  E-value: 2.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462597716    6 YLRENREKF-----EAVTCNFkhFIEGSFEEYLKRLENPQEWVGQVEISALS 52
Cdd:cd22761     49 YMRENKDDFlpfltNPDTGDP--LTEEEFEKYCDDVENTGAWGGQLELRALS 98
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 470-585 2.76e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.91  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  470 PEPSTLENITDDKYATVSSPSKSKKLECPSPAEQKPAehvsLSNPAPLLVSPEVHLTPavPSLPATVPAwpsePTTFGPT 549
Cdd:pfam05109  490 PSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPA----VTTPTPNATSPTLGKTS--PTSAVTTPT----PNATSPT 559

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462597716  550 -GVPAPIPVLSVTQTLTTGPDSAVSqahlTPSPVPVS 585
Cdd:pfam05109  560 pAVTTPTPNATIPTLGKTSPTSAVT----TPTPNATS 592
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
 2-95 4.05e-04

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: 41.42  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    2 ACIHYLRENREKFEAVTCNFKHFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVsPSQVTENNFPEKV 81
Cdd:cd22757     34 EVVDYVVNNWDEFSIYTHDSEGNNYKSAEEYRADMSKPGTYGTLCELVAAAELYPFHFEVYRNGKL-YASFGDPSNPVKR 112

                           90
                   ....*....|....*..
gi 2462597716   82 LLC---FSNGnHYDiVY 95
Cdd:cd22757    113 LKFsgdLSNG-HFD-VL 127
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
 6-95 4.48e-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: 43.09  E-value: 4.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716    6 YLRENREKFEAVTcnfkhFIEGSFEEYLKR-LENPQEWVGQVEISALSLMYRKDF-IIYREpNVSPSQVTENNFPE---- 79
Cdd:cd22749    141 YLKTNADDYEPFL-----FEGMSVEEFCEReVEPMGKEADHLQITALANALGVPVrVEYLD-RSAGGEVNFHEFPPedsd 214

                           90
                   ....*....|....*....
gi 2462597716   80 ---KVLLCFSNGnHYDIVY 95
Cdd:cd22749    215 slpVITLLYRPG-HYDILY 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
 468-575 4.59e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462597716  468 KRPE---PSTLENITD-DKYATVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEP 543
Cdd:PHA03247   355 RRPTwtpPSSLEDLSAgRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPAAPVPASVPTPAPTPVPASAPPPPATP 434

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462597716  544 TTF-------GPTGVPAPIPVLSVTQTLTTGPDSAVSQA 575
Cdd:PHA03247   435 LPSaepgsddGPAPPPERQPPAPATEPAPDDPDDATRKA 473
 
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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