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Conserved domains on  [gi|365733608|ref|NP_001242962|]
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OTU domain-containing protein 4 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
25-154 2.22e-91

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: 288.12  E-value: 2.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   25 MDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQV 104
Cdd:cd22794     1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 365733608  105 EISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYP 154
Cdd:cd22794    81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
273-333 3.79e-24

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: 445840  Cd Length: 64  Bit Score: 96.49  E-value: 3.79e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 365733608  273 DYSIAAGLQYEVGDKChQVRLDHNGKLSNADIHGVHSENG--LVLSEELGKKHT--PKNLKPPPP 333
Cdd:cd20448     1 DFSIAAGMQYSVGDKC-KVRLDHNGKFYNAHIQEVSPENGpvVVFVEELGKKHTvpLKNLKPPPQ 64
PHA03247 super family cl33720
large tegument protein UL36; Provisional
543-872 6.32e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  543 SSPSKSKKECPSP-VEQKPAEHIPLSNPAPLLVSPEVHLT----PAVPSLPATVPAWPSEPTTFGP------------TG 605
Cdd:PHA03247 2629 PSPSPAANEPDPHpPPTVPPPERPRDDPAPGRVSRPRRARrlgrAAQASSPPQRPRRRAARPTVGSltsladppppppTP 2708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  606 VPAQIPILSVTQTTGPDAAVSQAHLTPSPVPVSIQAVNQPLMPL-------PQTMSLYQDPLYPGFPCSEKGDRAIAPPY 678
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  679 -SLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYMAACRMYPKVPVPVY-PQNTW------FQEAPPA 750
Cdd:PHA03247 2789 aSLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlPLGGSvapggdVRRRPPS 2868
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  751 QSESDCPCTDAHyslhPEASVNGQmPQAEMGPPAFASPlviPPSQVSEGHGQLSYQPELESENPGQLLHAEYEESLSgkn 830
Cdd:PHA03247 2869 RSPAAKPAAPAR----PPVRRLAR-PAVSRSTESFALP---PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP--- 2937
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 365733608  831 mYPQQSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFVENPVMR 872
Cdd:PHA03247 2938 -RPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
25-154 2.22e-91

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: 288.12  E-value: 2.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   25 MDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQV 104
Cdd:cd22794     1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 365733608  105 EISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYP 154
Cdd:cd22794    81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
273-333 3.79e-24

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: 96.49  E-value: 3.79e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 365733608  273 DYSIAAGLQYEVGDKChQVRLDHNGKLSNADIHGVHSENG--LVLSEELGKKHT--PKNLKPPPP 333
Cdd:cd20448     1 DFSIAAGMQYSVGDKC-KVRLDHNGKFYNAHIQEVSPENGpvVVFVEELGKKHTvpLKNLKPPPQ 64
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
42-121 3.27e-14

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian tumor (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: 70.17  E-value: 3.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608    42 DGSCLFRAVAEQV-----LHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKD 116
Cdd:pfam02338    3 DGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                   ....*
gi 365733608   117 FVIYQ 121
Cdd:pfam02338   83 IIVYK 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
543-872 6.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  543 SSPSKSKKECPSP-VEQKPAEHIPLSNPAPLLVSPEVHLT----PAVPSLPATVPAWPSEPTTFGP------------TG 605
Cdd:PHA03247 2629 PSPSPAANEPDPHpPPTVPPPERPRDDPAPGRVSRPRRARrlgrAAQASSPPQRPRRRAARPTVGSltsladppppppTP 2708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  606 VPAQIPILSVTQTTGPDAAVSQAHLTPSPVPVSIQAVNQPLMPL-------PQTMSLYQDPLYPGFPCSEKGDRAIAPPY 678
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  679 -SLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYMAACRMYPKVPVPVY-PQNTW------FQEAPPA 750
Cdd:PHA03247 2789 aSLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlPLGGSvapggdVRRRPPS 2868
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  751 QSESDCPCTDAHyslhPEASVNGQmPQAEMGPPAFASPlviPPSQVSEGHGQLSYQPELESENPGQLLHAEYEESLSgkn 830
Cdd:PHA03247 2869 RSPAAKPAAPAR----PPVRRLAR-PAVSRSTESFALP---PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP--- 2937
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 365733608  831 mYPQQSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFVENPVMR 872
Cdd:PHA03247 2938 -RPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
25-154 2.22e-91

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: 288.12  E-value: 2.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   25 MDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQV 104
Cdd:cd22794     1 MDEYLRSLGLYRKQIAKDGSCLFRAVAEQVFHTQSRHLEVRKACVDYLRRNREKFEAFIEGPFEQYLKNLENPKEWAGQV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 365733608  105 EISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYP 154
Cdd:cd22794    81 EISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
25-154 1.06e-66

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: 220.11  E-value: 1.06e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   25 MDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQV 104
Cdd:cd22753     1 IDEYLDSLGLYRKHIPRDGSCLFRAVSEQLFFTQSYHQQVRQACVEYLEKNREEFEKFSEISFDDYLERLSDPKEWGGLL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 365733608  105 EISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYP 154
Cdd:cd22753    81 ELEALSLLYKVDFIVYSIPDQPPSNITNNGYPKKIMLCYSGGNHYDSVYS 130
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
25-154 5.55e-61

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: 203.89  E-value: 5.55e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   25 MDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQV 104
Cdd:cd22795     1 MDEYLGSLGLYRKLTAKDASCLFRAVSEQLFLCQIHHLEIRKACVSYMRANQCNFESYVEGSFEKYLERLEDPKESAGQL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 365733608  105 EISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYP 154
Cdd:cd22795    81 EISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSNGHYDSVYT 130
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
33-152 2.08e-32

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: 122.28  E-value: 2.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   33 GLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEG--SFEEYLKRLENPQEWVGQVEISALS 110
Cdd:cd22771     1 GLRIRDVEGDGNCLFRALADQLYGDEERHAELRKKVVDYMEAHEEDFEPFFEDdeTFEDYVSRMREDGTWGGNLELQAAS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 365733608  111 LMYRKDFVIYQEPnvSPSHVTEnNFPEK----VLLCFSNGNHYDIV 152
Cdd:cd22771    81 LVYRVNIVVHQLG--QPRWEIE-NFPDKgartIHLSYHDGEHYNSV 123
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
39-152 4.39e-29

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: 112.91  E-value: 4.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   39 VAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEA------FIEGSFEEYLKRLENPQEWVGQVEISALSLM 112
Cdd:cd22744     5 VPGDGNCLFRALAHALYGDQESHRELRQEVVDYLRENPDLYEPaeladeDDGEDFDEYLQRMRKPGTWGGELELQALANA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 365733608  113 YRKDFVIYQE----PNVSPSHVTENNFPEKVLLCFSNGNHYDIV 152
Cdd:cd22744    85 LNVPIVVYSEdggfLPVSVFGPGPGPSGRPIHLLYTGGNHYDAL 128
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
42-152 8.49e-25

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: 100.71  E-value: 8.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   42 DGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAF--------IEGSFEEYLKRLENPQEWVGQVEISALSLMY 113
Cdd:cd22756     8 DGNCLFRALSDQLYGDPDRHLEIRAEVVEYMRANPDDFKPFseaatfaeDDEAFEDYLARMAKDGTYGDNLEIVAFARAY 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 365733608  114 RKDFVIYQE---PNVSPSHVTENNFPEKVL-LCFSNGNHYDIV 152
Cdd:cd22756    88 NVDVKVYQPdpvYVISAPEDGSPGPARRVLhIAYHNWEHYSSV 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
273-333 3.79e-24

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: 96.49  E-value: 3.79e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 365733608  273 DYSIAAGLQYEVGDKChQVRLDHNGKLSNADIHGVHSENG--LVLSEELGKKHT--PKNLKPPPP 333
Cdd:cd20448     1 DFSIAAGMQYSVGDKC-KVRLDHNGKFYNAHIQEVSPENGpvVVFVEELGKKHTvpLKNLKPPPQ 64
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
33-154 4.28e-24

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: 98.39  E-value: 4.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   33 GLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLM 112
Cdd:cd22752     1 GFIIKEMEEDGNCLFRAVADQVYGDQEMHDVVRKHCMDYMEKNRDYFSQFVTEDFEEYINRKRQDGVWGNHIEIQAMSEL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 365733608  113 YRKDFVIYQ---EP-NVSPSHVTENNFPekVLLCFSNGNHYDIVYP 154
Cdd:cd22752    81 YNRPIEVYAystEPiNTFHEASSSDNEP--IRLSYHGNSHYNSIVD 124
OTU_232R-like cd22758
OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase ...
29-149 1.88e-22

OTU (ovarian tumor) domain of Invertebrate iridescent virus putative ubiquitin thioesterase 232R and similar proteins; This subfamily contains putative ubiquitin thioesterases 232R from Invertebrate iridescent virus and L96 from Tipula iridescent virus (TIV), Dictyostelium discoideum OTU domain-containing protein DDB_G0284757, and similar proteins. L96 may be involved in TIV genomic DNA packaging in a manner related to the Gag polyproteins of the mammalian viruses. Proteins in this subfamily contain an OTU domain. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. They belong to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438595 [Multi-domain]  Cd Length: 135  Bit Score: 94.26  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   29 LRKLGLYRKLVAKDGSCLFRAVAEQV--LHSQSRHVEVRMACIRYLRENREKFEAF------IEGSFEEYLKRLENPQEW 100
Cdd:cd22758     1 AKENGFEIRDVPGDGNCFFHAVSDQLygNGIEHSHKELRQQAVNYLRENPELYDGFflsefdEEESWEEYLNRMSKDGTW 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 365733608  101 VGQVEISALSLMYRKDFVIYQE-PNVSPSHVTENNFPEK--VLLCFSNGNHY 149
Cdd:cd22758    81 GDHIILQAAANLFNVRIVIISSdGSDETTIIEPGNSKNGrtIYLGHIGENHY 132
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
30-153 1.50e-21

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: 91.33  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   30 RKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISAL 109
Cdd:cd22796     1 KKKGLEIRRMDGDGNCLFRAVADQVYGDQEMHDEVREMCMDYMEKERDHFSQFVTEDFTQYVKRKRRDRVFGNNLEIQAM 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 365733608  110 SLMYRKDFVIYQEPNVSP-----SHVTENNFPekVLLCFSNGNHYDIVY 153
Cdd:cd22796    81 SEIYNRPIEVYSYSNGEPinifhGSYEGDDPP--IRLSYHDGNHYNSII 127
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
29-149 1.81e-21

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: 91.47  E-value: 1.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   29 LRKLGLYRKLVAKDGSCLFRAVAEQVLH-----SQSRHVEVRMACIRYLRENREKFEAFI---------EGSFEEYLKRL 94
Cdd:cd22748     1 LKPLGLRIKEIPPDGHCLYRAIADQLKLrggseEPYSYKELRKLAADYMRAHRDDFLPFLtnddgdlmtEEEFEEYCDKI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 365733608   95 ENPQEWVGQVEISALSLMYRKDFVIYQ--EPNVSpshVTENNFPEKVL-LCF-----SNGNHY 149
Cdd:cd22748    81 ENTAEWGGQLELRALSKALKRPIHVYQagSPPLV---IGEEFDSGEPLrLSYhrhayGLGEHY 140
OTU_plant_OTU9-like cd22751
OTU (ovarian tumor) domain of plant deubiquitinating enzyme OTU9 and similar proteins; This ...
29-153 1.84e-19

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: 85.67  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   29 LRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENRE-KFEAFIEGSFEEYLKRLENPQEW------- 100
Cdd:cd22751     5 LDLYGLVERKVEGDGNCQFRALSDQLFGTQDHHAEVRELVVKQLRAHPElYYEFYVPEEYDEYLKKMSKDGEWgdeltlq 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 365733608  101 ----VGQVEISALSlMYRKDFVIYQEPnvspshvTENNFPEKVL-LCFSNGNHYDIVY 153
Cdd:cd22751    85 aaadAFGVKIHVIT-SFEDNWFLEIEP-------RGLVRSKRVLfLSYWAEVHYNSIY 134
OTU_OTUD1 cd22747
OTU (ovarian tumor) domain of OTU domain-containing protein 1 and similar proteins; OTU ...
26-153 3.90e-16

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


Pssm-ID: 438584  Cd Length: 149  Bit Score: 76.39  E-value: 3.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   26 DAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVE 105
Cdd:cd22747    13 DKYLRERNKYRFHIIPDGNCLYRAVSKAVYGDQALHRELREQTVHYIADHLDEFNPIIEGDVGEFLIKAAQDGAWAGYPE 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 365733608  106 ISALSLMYRKDfvIY-------QEPNVSPS-HV--TENNFPEKVLLCF-SNGnHYDIVY 153
Cdd:cd22747    93 LLAMGQMLNVN--IRlttggslESPTVSTMvHYlgPEDSGKPSIWLSWlSNG-HYDAVF 148
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
29-110 4.34e-16

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: 76.11  E-value: 4.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   29 LRKLGLYRKLVAKDGSCLFRAVAEQ--VLHSQSR--HVEVRMACIRYLRENREKFEAFI------EGSFEEYLKRLENPQ 98
Cdd:cd22762     2 LEELGLEEHDIKPDGHCLFAAIADQlqLRGSEINldYKELRKLAAEYIRKHPDDFEPFLfeetdeLEDIDEYCKKIENTA 81
                          90
                  ....*....|..
gi 365733608   99 EWVGQVEISALS 110
Cdd:cd22762    82 EWGGELELLALA 93
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
39-152 4.61e-16

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


Pssm-ID: 438592 [Multi-domain]  Cd Length: 132  Bit Score: 75.76  E-value: 4.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   39 VAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFI---EGSFEEYLKRLENPQ--EWVGQVEISALSLMY 113
Cdd:cd22755     6 IVGDGNCFFRALSYAITGSEKYHRKIRKAIVDFLEKNPDEFRNLLrsdYESVEEYLEKSRMRYdgTWATDVEIFAAATLL 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 365733608  114 RKDFVIYQEPNV-----SPSHVTENNFPEK--VLLCFSNGNHYDIV 152
Cdd:cd22755    86 GVDIYVYSKGGYkwllySPRFKLGKRNGSReaIYLKNTNGNHFEPV 131
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
29-163 3.57e-15

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


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 73.47  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   29 LRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEG--SFEEYLKRLENPQEWVGQVEI 106
Cdd:cd22770     9 LQALGLKLRDIPGDGNCLFRALGDQLEGHSRNHLKHRQETVQYMIEHREDFEPFVEDdvPFDKHVANLSKPGTYAGNDAI 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 365733608  107 SALSLMYRKDFVIYQePNVSPSHVTENNFPEKVLLCFS--NGNHYDIVYPItyKDSSAM 163
Cdd:cd22770    89 VAFARLHQVNVVIHQ-LNAPLWQIRGTEKSSSRELHISyhNGDHYSSVRKL--GDNSEN 144
OTU_P87_VP80-like cd22757
OTU (ovarian tumor) domain of nucleopolyhedrovirus P87/VP80 protein and similar proteins; The ...
42-153 3.63e-15

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: 73.01  E-value: 3.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   42 DGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFI---EGSF----EEYLKRLENPQEWVGQVEISALSLMYR 114
Cdd:cd22757     9 DGACLFRALSYLLYGTQSRHLEVRKEVVDYVVNNWDEFSIYThdsEGNNyksaEEYRADMSKPGTYGTLCELVAAAELYP 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 365733608  115 KDFVIYQEPNVsPSHVTENNFPEKVLLC---FSNGnHYDiVY 153
Cdd:cd22757    89 FHFEVYRNGKL-YASFGDPSNPVKRLKFsgdLSNG-HFD-VL 127
OTU_OTUD6 cd22761
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A and 6B and similar proteins; ...
29-150 4.32e-15

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


Pssm-ID: 438598 [Multi-domain]  Cd Length: 146  Bit Score: 73.30  E-value: 4.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   29 LRKLGLYRKLVAKDGSCLFRAVAEQVlhsQSRHVEVRMACIR-----YLRENREKFEAFI----------EGSFEEYLKR 93
Cdd:cd22761     5 LKERGLKIHEIPSDGDCLYNAIAHQL---SLRGIETSVEELRkqtadYMRENKDDFLPFLtnpdtgdpltEEEFEKYCDD 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 365733608   94 LENPQEWVGQVEISALSLMYRKDFVIYQEpnVSPSHVT--ENNFPEKVLLC-----FSNGNHYD 150
Cdd:cd22761    82 VENTGAWGGQLELRALSHVLKRPIEVIQA--EGPPIIIgeEFKSGKPLILTyhrhaYGLGEHYN 143
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
42-121 3.27e-14

OTU-like cysteine protease; This family is comprised of a group of predicted cysteine proteases, homologous to the Ovarian tumor (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: 70.17  E-value: 3.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608    42 DGSCLFRAVAEQV-----LHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKD 116
Cdd:pfam02338    3 DGNCLYRSISHQLwgvhdVLRKMLVQELRETLAEYMREHKEEFEPFLEDDETGDIIEIEQTGAWGGEIEIFALAHILRRP 82

                   ....*
gi 365733608   117 FVIYQ 121
Cdd:pfam02338   83 IIVYK 87
OTU_plant_OTU5-like cd22797
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; ...
29-120 4.34e-13

OTU (ovarian tumor) domain of deubiquitinating enzyme OTU5 from plants and similar proteins; Deubiquitinating enzyme OTU5, also called OTU domain-containing protein 6, is a deubiquitinase (DUB) or ubiquitin thiolesterase (EC 3.4.19.12) that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. OTU5 is an inactive cysteine protease. It regulates gene expression by contributing to chromatin organization and DNA methylation patterns (e.g. H3K4me3 and H3K27me3). It is required for phosphate (Pi) homeostasis. OTU5 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438618 [Multi-domain]  Cd Length: 149  Bit Score: 67.75  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   29 LRKLGLYRKLVAKDGSCLFRAVAEQ-----VLHSQSRHVEVRMACIRYLRENREKFEAFIEG---------SFEEYLKRL 94
Cdd:cd22797     5 LAPLGLAIKEIKADGHCLYRAVEDQlqlrgGGAPAPDYQQLRELAADYMRAHPDDFLPFLEDedeggdgdeAFEAYCREV 84
                          90       100
                  ....*....|....*....|....*.
gi 365733608   95 ENPQEWVGQVEISALSLMYRKDFVIY 120
Cdd:cd22797    85 ESTAAWGGQLELGALAHALRRHIKVY 110
OTU_plant_OTU3_4-like cd22746
OTU (ovarian tumor) domain of deubiquitinating enzymes OTU3 and OTU4 from plants, and similar ...
42-150 6.45e-13

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


Pssm-ID: 438583 [Multi-domain]  Cd Length: 141  Bit Score: 66.91  E-value: 6.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   42 DGSCLFRAVAEQVLHSQ-----SRHVEV------RMACIRYLRENREKFEA---FIEGSFEEYLKRLENPQEWVGQVEIS 107
Cdd:cd22746    10 DGRCLFRAVARGLALATggrplSERRERadadalRKAVVEEIRKRRDELFEgslVIEGDFDAYCQRMSHPDTWGGEPELL 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 365733608  108 ALSLMYRKDFVIY--QEPNVSPSHV----TENNFPEKVLLCFSNGNHYD 150
Cdd:cd22746    90 MLADVLQRPIAVYlpTPGKGGLRKIqeygEEYLGGEPIRLLYNGGNHYD 138
OTU_plant_OTU1_2-like cd22793
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU1 and OTU2 from plants and similar ...
36-150 6.28e-11

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


Pssm-ID: 438614  Cd Length: 163  Bit Score: 61.96  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   36 RKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKF-EAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYR 114
Cdd:cd22793     5 RRVIDSDNSCLFNAVGYVMEGSRKKAPELRQVIADAVLSDPFEYnEAFLGKSNKEYCEWILNPNSWGGAIELSILSDHYG 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 365733608  115 KDFVIYqepNVSPSHV----TENNFPEKVLLCFsNGNHYD 150
Cdd:cd22793    85 REIAAF---DIQTKRCdvygEGKGYTERVMLIY-DGLHYD 120
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
281-330 2.86e-10

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: 56.44  E-value: 2.86e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 365733608  281 QYEVGDKChQVRLDHNGKLSNADIHGVHSENG--LVLSEELGKKHT-P-KNLKP 330
Cdd:cd20380     1 QFKPGDKC-QVELDSPGKVYEAHIQEISPDKGpvTVFVEELGEKKTvPyENLKP 53
OTU_plant_OTU3-like cd22759
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU3 from plants and similar proteins; ...
39-151 5.86e-10

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: 58.89  E-value: 5.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   39 VAKDGSCLFRAVAEQVLHSQSRHV----------EVRMA-----CiRYLRENREKFEAFI----EGSFEEYLKRLENPQE 99
Cdd:cd22759     8 VKGDGRCMFRALVKGLAANKGIFLsgreeeqeadELRLAvaealC-RSEERRRDYEEALIaitvEGSLDRYCRRIQRPDF 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 365733608  100 WVGQVEISALSLMYRKDFVIYQepnvsPSHVTENN---------------FPEK---------VLLCFSNGNHYDI 151
Cdd:cd22759    87 WGGESELLVLSKMLKQPIIVYI-----PESEAKNGgwgsgfipiqkygeeFAKGtkgrkgrkpVRLLYSGSNHYDL 157
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
278-343 1.87e-09

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: 55.24  E-value: 1.87e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 365733608  278 AGLQYEVGDKChQVRLDHNGKLSNADIH--GVHSENGLVLSEELGKKHTPK--NLKP----PPPESWNTVSGKK 343
Cdd:cd20447     2 AGRQYYLGDKC-QVRLEPGGKYYNAHIQevGQDSNSVTVFIEELAEKHTVPlaNLKPvtqvTPVPAWNMMPNRK 74
OTU_OTU1 cd22745
OTU (ovarian tumor) domain of ubiquitin thioesterase OTU1 and similar proteins; Ubiquitin ...
34-153 8.81e-09

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


Pssm-ID: 438582  Cd Length: 161  Bit Score: 55.57  E-value: 8.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   34 LYRKLVAKDGSCLFRAVAEQVLHSQSRHV-EVRMACIRYLRENREKF-EAFIEGSFEEYLKRLENPQEWVGQVEISALSL 111
Cdd:cd22745     3 LVRRVVPDDNSCLFTSISYLLEGGLLDSApELREIVADAILSDPDTYnEAILGKPPDEYCAWILKPDSWGGAIELSILSK 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 365733608  112 MYRKDFVIYqepNVSPSHVT----ENNFPEKVLLCFSnGNHYDIVY 153
Cdd:cd22745    83 HFGVEICVV---DVQTGRVDrfgeDKGYSKRIFLLYS-GIHYDALA 124
OTU_plant_OTU4-like cd22760
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU4 from plants and similar proteins; ...
39-110 1.01e-08

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


Pssm-ID: 438597 [Multi-domain]  Cd Length: 138  Bit Score: 55.08  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   39 VAKDGSCLFRAVA---------------EQVLHSQsrhvEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQ 103
Cdd:cd22760     7 IAGDGRCLFRAVAhgeclargkaapdeeRERELAD----ELRTRAADELVKRREETEWFIEGDFDEYVARMRRPGVWGGE 82

                  ....*..
gi 365733608  104 VEISALS 110
Cdd:cd22760    83 PELLMLS 89
OTU_RNAP_L_virus cd21880
OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase ...
36-113 3.46e-07

OTU (ovarian tumor) domain of viral RNA-directed RNA polymerase L; RNA-directed RNA polymerase L is also called protein L, large structural protein, replicase, transcriptase, or ubiquitin thioesterase. It displays RNA-directed RNA polymerase (EC 2.7.7.48), deubiquitinase (DUB)/ubiquitin thiolesterase (EC 3.4.19.12), and deISGylating activities. It is a viral homolog of ovarian tumor protease (vOTU) that has been implicated in the downregulation of type I interferon immune response by removing post-translational modifying proteins ubiquitin (Ub) and the Ub-like interferon-simulated gene 15 (ISG15) from host cellular proteins. The attachment of Ub and ISG15 to cellular proteins mediates important innate antiviral responses, and their removal inhibits these antiviral pathways. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438580  Cd Length: 148  Bit Score: 50.68  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   36 RKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKF-EAFIEG-SFEEYLKRLENPQEWVGQVEISALSLMY 113
Cdd:cd21880    24 IERVPGDGNCFFRSIAELLFDTEDEWRLVKNTIESYARANWDECpEARLYYlSLEEYLRDAMKDGYWGGSLEAEILSKAL 103
OTU_VRTN cd22791
OTU (ovarian tumor) domain of vertnin and similar proteins; Vertnin (VRTN) is an OTU ...
42-129 2.09e-06

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: 48.37  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   42 DGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREkfeaFIEGSFEEYLKRLENPQEWVGQVEISAL-SLMYRKDFVIY 120
Cdd:cd22791     9 DGNCLFRAASLLLFGDESLHLELRLRTVLELVLNSE----FYEAIYEAEIKATCKPGSYSGIWHIYALsSVLQRPIFSVY 84

                  ....*....
gi 365733608  121 QEPNVSPSH 129
Cdd:cd22791    85 PEVGNQKIR 93
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
65-153 9.81e-06

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: 48.10  E-value: 9.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   65 RMACIRYLRENREKFEAFIEG--SFEEYLKR-LENPQEWVGQVEISALS--------LMYrkdfvIYQEPNVSPSHVT-- 131
Cdd:cd22749   135 RLLTSAYLKTNADDYEPFLFEgmSVEEFCEReVEPMGKEADHLQITALAnalgvpvrVEY-----LDRSAGGEVNFHEfp 209
                          90       100
                  ....*....|....*....|....
gi 365733608  132 --ENNFPEKVLLCFSNGnHYDIVY 153
Cdd:cd22749   210 peDSDSLPVITLLYRPG-HYDILY 232
PHA03247 PHA03247
large tegument protein UL36; Provisional
543-872 6.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  543 SSPSKSKKECPSP-VEQKPAEHIPLSNPAPLLVSPEVHLT----PAVPSLPATVPAWPSEPTTFGP------------TG 605
Cdd:PHA03247 2629 PSPSPAANEPDPHpPPTVPPPERPRDDPAPGRVSRPRRARrlgrAAQASSPPQRPRRRAARPTVGSltsladppppppTP 2708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  606 VPAQIPILSVTQTTGPDAAVSQAHLTPSPVPVSIQAVNQPLMPL-------PQTMSLYQDPLYPGFPCSEKGDRAIAPPY 678
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  679 -SLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYMAACRMYPKVPVPVY-PQNTW------FQEAPPA 750
Cdd:PHA03247 2789 aSLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlPLGGSvapggdVRRRPPS 2868
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  751 QSESDCPCTDAHyslhPEASVNGQmPQAEMGPPAFASPlviPPSQVSEGHGQLSYQPELESENPGQLLHAEYEESLSgkn 830
Cdd:PHA03247 2869 RSPAAKPAAPAR----PPVRRLAR-PAVSRSTESFALP---PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP--- 2937
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 365733608  831 mYPQQSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFVENPVMR 872
Cdd:PHA03247 2938 -RPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFR 2978
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
42-155 1.10e-04

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: 42.59  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608   42 DGSCLFRAVAEqvlHSQSRHVEVRMACIRYLRENrekfeafieGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFVIYQ 121
Cdd:cd22792     8 DGNCFWHSLGH---FLGLSALELKKLLRDSLFDD---------PELDEELDEQLEPGVYAEDEAIAAAAKLFGVNICVHD 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 365733608  122 EPNVSPSHVTENNFPEKVLLCFSNgNHYDIVYPI 155
Cdd:cd22792    76 PDEGVLYTFTPNESSKSIHLLLEN-EHFEPLVPK 108
PHA03379 PHA03379
EBNA-3A; Provisional
543-864 2.16e-04

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 45.43  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  543 SSPSKSKKECPSPVEQKPAEHIPLSNPAPLLVSPevhLTPAVPSLPATVPA-----------WPSEPTTFGPTGVPAQIP 611
Cdd:PHA03379  511 ASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERP---VCPAPPLIAMQGPGetsgivrvrerWRPAPWTPNPPRSPSQMS 587
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  612 ILSVTQTTGPDAAVSQAhltpspvPVSIQAVNQPLMPLPQTMSLYQDP---LYPGFPCSEKGDRAIAPpyslcqtgedlp 688
Cdd:PHA03379  588 VRDRLARLRAEAQPYQA-------SVEVQPPQLTQVSPQQPMEYPLEPeqqMFPGSPFSQVADVMRAG------------ 648
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  689 kdknilrfffnlgvkaySCPMWAPHSYLYPLHQ-----AYMAACR--MYPKVPVPVyPQNTWFqeappaqsesDCPCTDa 761
Cdd:PHA03379  649 -----------------GVPAMQPQYFDLPLQQpisqgAPLAPLRasMGPVPPVPA-TQPQYF----------DIPLTE- 699
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  762 hySLHPEASVNGQMPQAEMGPPafasplVIPPSQVSEGhgqlsyQPELESENPGQLLHAEYEESLSGK--NMYPQQSFGP 839
Cdd:PHA03379  700 --PINQGASAAHFLPQQPMEGP------LVPERWMFQG------ATLSQSVRPGVAQSQYFDLPLTQPinHGAPAAHFLH 765
                         330       340
                  ....*....|....*....|....*
gi 365733608  840 NPflgpvPIAPPFFPHVWygyPFQG 864
Cdd:PHA03379  766 QP-----PMEGPWVPEQW---MFQG 782
Peptidase_C65 pfam10275
Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly ...
64-154 2.34e-03

Peptidase C65 Otubain; This family of proteins conserved from plants to humans is a highly specific ubiquitin iso-peptidase that removes ubiquitin from proteins. The modification of cellular proteins by ubiquitin (Ub) is an important event that underlies protein stability and function in eukaryote being a dynamic and reversible process. Otubain carries several key conserved domains: (i) the OTU (ovarian tumor domain) in which there is an active cysteine protease triad (ii) a nuclear localization signal, (iii) a Ub interaction motif (UIM)-like motif phi-xx-A-xxxs-xx-Ac (where phi indicates an aromatic amino acid, x indicates any amino acid and Ac indicates an acidic amino acid), (iv) a Ub-associated (UBA)-like domain and (v) the LxxLL motif.


Pssm-ID: 431191 [Multi-domain]  Cd Length: 240  Bit Score: 40.73  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608    64 VRMACIRYLRENREKFEAFIEG--SFEEYLKR-LENPQEWVGQVEISALS--LMYRKDfVIYQEPNVSPSHVTENNFPEK 138
Cdd:pfam10275  138 LRLLTSAYLKTHADEYEPFIDGggTVEEFCQQeVEPMNKEADHLQIIALAeaLGVPVR-VEYLDRSAEGNTVNHHDFPGE 216
                           90       100
                   ....*....|....*....|....*
gi 365733608   139 ---------VLLCFSNGnHYDIVYP 154
Cdd:pfam10275  217 ddteeqapfITLLYRPG-HYDILYK 240
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
553-638 2.97e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 365733608  553 PSPVEQKPAEHIPLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPttfgptgVPAQIPILSVTQTTGPDAAVSQAHLTP 632
Cdd:PRK14951  407 PAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPP-------AQAAPETVAIPVRVAPEPAVASAAPAP 479

                  ....*.
gi 365733608  633 SPVPVS 638
Cdd:PRK14951  480 AAAPAA 485
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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