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Conserved domains on  [gi|1953297908|ref|XP_038544428|]
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OTU domain-containing protein 4 isoform X4 [Canis lupus familiaris]

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 ...
 1-110 1.88e-54

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: 185.27  E-value: 1.88e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    1 MACIHYLRENREKFEAFIEGSFEEYLKRLENPQEgkivskadsesssicmeyakeWVGQVEISALSLMYRKDFIIYREPN 80
Cdd:cd22794     42 KACVDYLRRNREKFEAFIEGPFEQYLKNLENPKE---------------------WAGQVEISALSLMYKRDFIIYQEPG 100

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953297908   81 VSPSQVTENNFPEKVLLCFSNGNHYDIVYP 110
Cdd:cd22794    101 KPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 230-288 7.73e-27

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: 104.20  E-value: 7.73e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953297908  230 DYSIAAGLQYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKHS--PKNLKPPP 288
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTvpLKNLKPPP 63
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 485-814 3.47e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  485 PSTLENISDDKcariSSPSKSKKLECPPVEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVP 564
Cdd:pfam03154  149 PSPQDNESDSD----SSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  565 AQIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPYNE 627
Cdd:pfam03154  223 STAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLTP 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  628 KGDRAIAPP---YSLCHTGEDLPKDknilrfffnlgvkaySCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPwfq 704
Cdd:pfam03154  303 QSSQSQVPPgpsPAAPGQSQQRIHT---------------PPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIP--- 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  705 EAPSAQNEgdctctdaHFPMQTEATVNGQMPqAEIGPPtfssPLVIPPSQVSESHGQLSYQADIESENSGQLLHAEYEES 784
Cdd:pfam03154  365 QLPNPQSH--------KHPPHLSGPSPFQMN-SNLPPP----PALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQP 431

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1953297908  785 ---LSGKNMFPQPSFGPNP-FLGPVPIAPPFFPH 814
Cdd:pfam03154  432 pvlTQSQSLPPPAASHPPTsGLHQVPSQSPFPQH 465
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 859-1063 4.28e-03

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  859 VSAVDEFQEARGEGTHCLPEASVGKHEGRAEQSSQTPKVDLARPSILPVAEEEAhlPTQILNRERETVPVELEPKRTIPS 938
Cdd:PRK12678    52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAA--PAARAAAAAAAEAASAPEAAQARE 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  939 LKEKSEK-----VKDPKTAADAVSGANSVESRVQRPKEESSEDENEVsnilRSGRSKQfyNQTYGGRKYKSDWGSSGRGG 1013
Cdd:PRK12678   130 RRERGEAarrgaARKAGEGGEQPATEARADAAERTEEEERDERRRRG----DREDRQA--EAERGERGRREERGRDGDDR 203

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953297908 1014 YQHARGEESWKGQPGRSRDEGyQYHRNVRGRPYRGDRRRSGMGDGHRGQN 1063
Cdd:PRK12678   204 DRRDRREQGDRREERGRRDGG-DRRGRRRRRDRRDARGDDNREDRGDRDG 252
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 1-110 1.88e-54

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: 185.27  E-value: 1.88e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    1 MACIHYLRENREKFEAFIEGSFEEYLKRLENPQEgkivskadsesssicmeyakeWVGQVEISALSLMYRKDFIIYREPN 80
Cdd:cd22794     42 KACVDYLRRNREKFEAFIEGPFEQYLKNLENPKE---------------------WAGQVEISALSLMYKRDFIIYQEPG 100

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953297908   81 VSPSQVTENNFPEKVLLCFSNGNHYDIVYP 110
Cdd:cd22794    101 KPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 230-288 7.73e-27

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: 104.20  E-value: 7.73e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953297908  230 DYSIAAGLQYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKHS--PKNLKPPP 288
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTvpLKNLKPPP 63
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 485-814 3.47e-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: 44.76  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  485 PSTLENISDDKcariSSPSKSKKLECPPVEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVP 564
Cdd:pfam03154  149 PSPQDNESDSD----SSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  565 AQIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPYNE 627
Cdd:pfam03154  223 STAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLTP 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  628 KGDRAIAPP---YSLCHTGEDLPKDknilrfffnlgvkaySCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPwfq 704
Cdd:pfam03154  303 QSSQSQVPPgpsPAAPGQSQQRIHT---------------PPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIP--- 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  705 EAPSAQNEgdctctdaHFPMQTEATVNGQMPqAEIGPPtfssPLVIPPSQVSESHGQLSYQADIESENSGQLLHAEYEES 784
Cdd:pfam03154  365 QLPNPQSH--------KHPPHLSGPSPFQMN-SNLPPP----PALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQP 431

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1953297908  785 ---LSGKNMFPQPSFGPNP-FLGPVPIAPPFFPH 814
Cdd:pfam03154  432 pvlTQSQSLPPPAASHPPTsGLHQVPSQSPFPQH 465
PHA03247 PHA03247
large tegument protein UL36; Provisional
 498-846 3.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  498 RISSPSKSKKLECPPveQKPAEHVSLSNPAPLLVSPEVHLTPAVPSlPATVPAWPSEPTTFGPTGVPAQIPVLSVTQTLT 577
Cdd:PHA03247  2666 RARRLGRAAQASSPP--QRPRRRAARPTVGSLTSLADPPPPPPTPE-PAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  578 TGPDSAVSQAHLTPSPVPVSIQAVNQPLMP-LPQTLSLYQDPLYPGFPYNEKGDRAIAPPYSLCHTGEDLPKDknilrff 656
Cdd:PHA03247  2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA------- 2815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  657 fnlgvkAYSCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPW------FQEAPSAQNEGDCTCTDAHFPMQteatv 730
Cdd:PHA03247  2816 ------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggdVRRRPPSRSPAAKPAAPARPPVR----- 2884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  731 ngQMPQAEIGPPTFSSPLviPPSQVSEshgQLSYQADIESENSGQLLHAEYEESLSGKNMFPQPSFGPNPFLGPVPIAPP 810
Cdd:PHA03247  2885 --RLARPAVSRSTESFAL--PPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1953297908  811 FFPHVWYGYPFQGFVenPVMRQNIVLPSDEKELDLP 846
Cdd:PHA03247  2958 AVPQPWLGALVPGRV--AVPRFRVPQPAPSREAPAS 2991
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 859-1063 4.28e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  859 VSAVDEFQEARGEGTHCLPEASVGKHEGRAEQSSQTPKVDLARPSILPVAEEEAhlPTQILNRERETVPVELEPKRTIPS 938
Cdd:PRK12678    52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAA--PAARAAAAAAAEAASAPEAAQARE 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  939 LKEKSEK-----VKDPKTAADAVSGANSVESRVQRPKEESSEDENEVsnilRSGRSKQfyNQTYGGRKYKSDWGSSGRGG 1013
Cdd:PRK12678   130 RRERGEAarrgaARKAGEGGEQPATEARADAAERTEEEERDERRRRG----DREDRQA--EAERGERGRREERGRDGDDR 203

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953297908 1014 YQHARGEESWKGQPGRSRDEGyQYHRNVRGRPYRGDRRRSGMGDGHRGQN 1063
Cdd:PRK12678   204 DRRDRREQGDRREERGRRDGG-DRRGRRRRRDRRDARGDDNREDRGDRDG 252
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 2-77 6.90e-03

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: 37.82  E-value: 6.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953297908    2 ACIHYLRENREKFEAFIEGSFEEYLKRLENPQegkivskadsesssicmeyakEWVGQVEISALSLMYRKDFIIYR 77
Cdd:pfam02338   33 TLAEYMREHKEEFEPFLEDDETGDIIEIEQTG---------------------AWGGEIEIFALAHILRRPIIVYK 87
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
 1-110 1.88e-54

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: 185.27  E-value: 1.88e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    1 MACIHYLRENREKFEAFIEGSFEEYLKRLENPQEgkivskadsesssicmeyakeWVGQVEISALSLMYRKDFIIYREPN 80
Cdd:cd22794     42 KACVDYLRRNREKFEAFIEGPFEQYLKNLENPKE---------------------WAGQVEISALSLMYKRDFIIYQEPG 100

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953297908   81 VSPSQVTENNFPEKVLLCFSNGNHYDIVYP 110
Cdd:cd22794    101 KPPSNVTENGFPDKILLCFSNGNHYDSVYP 130
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 2-110 4.96e-36

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: 132.63  E-value: 4.96e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    2 ACIHYLRENREKFEAFIEGSFEEYLKRLENPqegkivskadsesssicmeyaKEWVGQVEISALSLMYRKDFIIYREPNV 81
Cdd:cd22795     43 ACVSYMRANQCNFESYVEGSFEKYLERLEDP---------------------KESAGQLEISALSLIYNRDFILYRYPGK 101

                           90       100
                   ....*....|....*....|....*....
gi 1953297908   82 SPSQVTENNFPEKVLLCFSNGNHYDIVYP 110
Cdd:cd22795    102 PPTYATDNGFEDKILLCCSSNGHYDSVYT 130
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
 2-110 1.82e-34

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: 128.43  E-value: 1.82e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    2 ACIHYLRENREKFEAFIEGSFEEYLKRLENPqegkivskadsesssicmeyaKEWVGQVEISALSLMYRKDFIIYREPNV 81
Cdd:cd22753     43 ACVEYLEKNREEFEKFSEISFDDYLERLSDP---------------------KEWGGLLELEALSLLYKVDFIVYSIPDQ 101

                           90       100
                   ....*....|....*....|....*....
gi 1953297908   82 SPSQVTENNFPEKVLLCFSNGNHYDIVYP 110
Cdd:cd22753    102 PPSNITNNGYPKKIMLCYSGGNHYDSVYS 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 230-288 7.73e-27

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: 104.20  E-value: 7.73e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953297908  230 DYSIAAGLQYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKHS--PKNLKPPP 288
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTvpLKNLKPPP 63
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
 238-286 7.31e-13

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: 64.14  E-value: 7.31e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953297908  238 QYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKH--SPKNLKP 286
Cdd:cd20380      1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVfvEELGEKKtvPYENLKP 53
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
 2-108 1.95e-11

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: 62.19  E-value: 1.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    2 ACIHYLRENREKFEAFIEG--SFEEYLKRlenpqegkivskadsesssicMEYAKEWVGQVEISALSLMYRKDFIIYREp 79
Cdd:cd22771     35 KVVDYMEAHEEDFEPFFEDdeTFEDYVSR---------------------MREDGTWGGNLELQAASLVYRVNIVVHQL- 92

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1953297908   80 NVSPSQVTenNFPEK----VLLCFSNGNHYDIV 108
Cdd:cd22771     93 GQPRWEIE--NFPDKgartIHLSYHDGEHYNSV 123
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 235-299 4.82e-11

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: 59.86  E-value: 4.82e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953297908  235 AGLQYEVGDKCQVRLDHNGKFSNADFP--GVHSENGPVLVEELGKKH--SPKNLKP----PPSESWNTVSGKK 299
Cdd:cd20447      2 AGRQYYLGDKCQVRLEPGGKYYNAHIQevGQDSNSVTVFIEELAEKHtvPLANLKPvtqvTPVPAWNMMPNRK 74
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
 2-108 7.22e-10

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: 57.83  E-value: 7.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    2 ACIHYLRENREKFEA------FIEGSFEEYLKRLENPqegkivskadsesssicmeyaKEWVGQVEISALSLMYRKDFII 75
Cdd:cd22744     33 EVVDYLRENPDLYEPaeladeDDGEDFDEYLQRMRKP---------------------GTWGGELELQALANALNVPIVV 91

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1953297908   76 YREPNVSPSQVTENNFPEK----VLLCFSNGNHYDIV 108
Cdd:cd22744     92 YSEDGGFLPVSVFGPGPGPsgrpIHLLYTGGNHYDAL 128
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
 2-110 7.43e-08

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: 52.17  E-value: 7.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    2 ACIHYLRENREKFEAFIEGSFEEYLKRlenpqegkivskadsesssicMEYAKEWVGQVEISALSLMYRKDFIIY---RE 78
Cdd:cd22752     35 HCMDYMEKNRDYFSQFVTEDFEEYINR---------------------KRQDGVWGNHIEIQAMSELYNRPIEVYaysTE 93

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1953297908   79 P-NVSPSQVTENNFPekVLLCFSNGNHYDIVYP 110
Cdd:cd22752     94 PiNTFHEASSSDNEP--IRLSYHGNSHYNSIVD 124
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
 6-108 2.32e-07

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: 50.64  E-value: 2.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    6 YLRENREKFEAF--------IEGSFEEYLKRLENPqegkivskadsesssicmeyaKEWVGQVEISALSLMYRKDFIIYR 77
Cdd:cd22756     37 YMRANPDDFKPFseaatfaeDDEAFEDYLARMAKD---------------------GTYGDNLEIVAFARAYNVDVKVYQ 95

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1953297908   78 E---PNVSPSQVTENNFPEKVL-LCFSNGNHYDIV 108
Cdd:cd22756     96 PdpvYVISAPEDGSPGPARRVLhIAYHNWEHYSSV 130
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
 6-105 5.04e-07

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: 50.25  E-value: 5.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    6 YLRENREKFEAFI---------EGSFEEYLKRLENPqegkivskadsesssicmeyaKEWVGQVEISALSLMYRKDFIIY 76
Cdd:cd22748     48 YMRAHRDDFLPFLtnddgdlmtEEEFEEYCDKIENT---------------------AEWGGQLELRALSKALKRPIHVY 106

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1953297908   77 REPnvSPSQVTENNFPEK--VLLCF-----SNGNHY 105
Cdd:cd22748    107 QAG--SPPLVIGEEFDSGepLRLSYhrhayGLGEHY 140
OTU_plant_OTU6-like cd22796
OTU (ovarian tumor) domain of deubiquitinating enzyme OTU6 from plants and similar proteins; ...
 2-109 1.03e-05

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: 45.88  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    2 ACIHYLRENREKFEAFIEGSFEEYLKRlenpqegkivSKADsesssicmeyaKEWVGQVEISALSLMYRKDFIIYREPNV 81
Cdd:cd22796     38 MCMDYMEKERDHFSQFVTEDFTQYVKR----------KRRD-----------RVFGNNLEIQAMSEIYNRPIEVYSYSNG 96

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1953297908   82 SP-----SQVTENNFPekVLLCFSNGNHYDIVY 109
Cdd:cd22796     97 EPinifhGSYEGDDPP--IRLSYHDGNHYNSII 127
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 485-814 3.47e-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: 44.76  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  485 PSTLENISDDKcariSSPSKSKKLECPPVEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVP 564
Cdd:pfam03154  149 PSPQDNESDSD----SSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  565 AQIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPYNE 627
Cdd:pfam03154  223 STAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLTP 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  628 KGDRAIAPP---YSLCHTGEDLPKDknilrfffnlgvkaySCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPwfq 704
Cdd:pfam03154  303 QSSQSQVPPgpsPAAPGQSQQRIHT---------------PPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIP--- 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  705 EAPSAQNEgdctctdaHFPMQTEATVNGQMPqAEIGPPtfssPLVIPPSQVSESHGQLSYQADIESENSGQLLHAEYEES 784
Cdd:pfam03154  365 QLPNPQSH--------KHPPHLSGPSPFQMN-SNLPPP----PALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQP 431

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1953297908  785 ---LSGKNMFPQPSFGPNP-FLGPVPIAPPFFPH 814
Cdd:pfam03154  432 pvlTQSQSLPPPAASHPPTsGLHQVPSQSPFPQH 465
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
 1-108 3.96e-04

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: 41.48  E-value: 3.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    1 MACIHYLRENREKFEAFI---EGSFEEYLKRLenpqegkivskadsesssiCMEYAKEWVGQVEISALSLM-------YR 70
Cdd:cd22755     33 KAIVDFLEKNPDEFRNLLrsdYESVEEYLEKS-------------------RMRYDGTWATDVEIFAAATLlgvdiyvYS 93

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1953297908   71 KDF---IIYRePNVSPSQVTENNFPekVLLCFSNGNHYDIV 108
Cdd:cd22755     94 KGGykwLLYS-PRFKLGKRNGSREA--IYLKNTNGNHFEPV 131
OTU_fungi_OTU2-like cd22762
OTU (ovarian tumor) domain of fungal OTU domain-containing protein 2 and similar proteins; ...
 6-66 3.24e-03

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: 39.13  E-value: 3.24e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953297908    6 YLRENREKFEAFI------EGSFEEYLKRLENpqegkivskadsesssicmeyAKEWVGQVEISALS 66
Cdd:cd22762     48 YIRKHPDDFEPFLfeetdeLEDIDEYCKKIEN---------------------TAEWGGELELLALA 93
PHA03247 PHA03247
large tegument protein UL36; Provisional
 498-846 3.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  498 RISSPSKSKKLECPPveQKPAEHVSLSNPAPLLVSPEVHLTPAVPSlPATVPAWPSEPTTFGPTGVPAQIPVLSVTQTLT 577
Cdd:PHA03247  2666 RARRLGRAAQASSPP--QRPRRRAARPTVGSLTSLADPPPPPPTPE-PAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  578 TGPDSAVSQAHLTPSPVPVSIQAVNQPLMP-LPQTLSLYQDPLYPGFPYNEKGDRAIAPPYSLCHTGEDLPKDknilrff 656
Cdd:PHA03247  2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA------- 2815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  657 fnlgvkAYSCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPW------FQEAPSAQNEGDCTCTDAHFPMQteatv 730
Cdd:PHA03247  2816 ------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggdVRRRPPSRSPAAKPAAPARPPVR----- 2884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  731 ngQMPQAEIGPPTFSSPLviPPSQVSEshgQLSYQADIESENSGQLLHAEYEESLSGKNMFPQPSFGPNPFLGPVPIAPP 810
Cdd:PHA03247  2885 --RLARPAVSRSTESFAL--PPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1953297908  811 FFPHVWYGYPFQGFVenPVMRQNIVLPSDEKELDLP 846
Cdd:PHA03247  2958 AVPQPWLGALVPGRV--AVPRFRVPQPAPSREAPAS 2991
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 859-1063 4.28e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  859 VSAVDEFQEARGEGTHCLPEASVGKHEGRAEQSSQTPKVDLARPSILPVAEEEAhlPTQILNRERETVPVELEPKRTIPS 938
Cdd:PRK12678    52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAA--PAARAAAAAAAEAASAPEAAQARE 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908  939 LKEKSEK-----VKDPKTAADAVSGANSVESRVQRPKEESSEDENEVsnilRSGRSKQfyNQTYGGRKYKSDWGSSGRGG 1013
Cdd:PRK12678   130 RRERGEAarrgaARKAGEGGEQPATEARADAAERTEEEERDERRRRG----DREDRQA--EAERGERGRREERGRDGDDR 203

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953297908 1014 YQHARGEESWKGQPGRSRDEGyQYHRNVRGRPYRGDRRRSGMGDGHRGQN 1063
Cdd:PRK12678   204 DRRDRREQGDRREERGRRDGG-DRRGRRRRRDRRDARGDDNREDRGDRDG 252
Otubain_C65 cd22749
Otubain subfamily of ubiquitin thioesterases; The otubain subfamily is composed of otubain-1 ...
 6-109 4.83e-03

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: 40.01  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953297908    6 YLRENREKFEAFIEG--SFEEYLKRLENPqegkivskadsesssicmeYAKEwVGQVEISALSLMYRKDF-IIYREpNVS 82
Cdd:cd22749    141 YLKTNADDYEPFLFEgmSVEEFCEREVEP-------------------MGKE-ADHLQITALANALGVPVrVEYLD-RSA 199

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1953297908   83 PSQVTENNFPE-------KVLLCFSNGnHYDIVY 109
Cdd:cd22749    200 GGEVNFHEFPPedsdslpVITLLYRPG-HYDILY 232
OTU pfam02338
OTU-like cysteine protease; This family is comprised of a group of predicted cysteine ...
 2-77 6.90e-03

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: 37.82  E-value: 6.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953297908    2 ACIHYLRENREKFEAFIEGSFEEYLKRLENPQegkivskadsesssicmeyakEWVGQVEISALSLMYRKDFIIYR 77
Cdd:pfam02338   33 TLAEYMREHKEEFEPFLEDDETGDIIEIEQTG---------------------AWGGEIEIFALAHILRRPIIVYK 87
 
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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