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Conserved domains on  [gi|1239937954|ref|XP_022259168|]
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OTU domain-containing protein 4 isoform X5 [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 ...
1-72 1.94e-42

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: 150.98  E-value: 1.94e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    1 MACIHYLRENREKFEA-----------------EWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSN 63
Cdd:cd22794     42 KACVDYLRRNREKFEAfiegpfeqylknlenpkEWAGQVEISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSN 121

                   ....*....
gi 1239937954   64 GNHYDIVYP 72
Cdd:cd22794    122 GNHYDSVYP 130
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
192-250 7.46e-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: 7.46e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239937954  192 DYSIAAGLQYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKHS--PKNLKPPP 250
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTvpLKNLKPPP 63
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
447-776 7.26e-04

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  447 PSTLENISDDKcariSSPSKSKKLECPPVEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVP 526
Cdd:pfam03154  149 PSPQDNESDSD----SSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  527 AQIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPYNE 589
Cdd:pfam03154  223 STAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLTP 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  590 KGDRAIAPP---YSLCHTGEDLPKDknilrfffnlgvkaySCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPwfq 666
Cdd:pfam03154  303 QSSQSQVPPgpsPAAPGQSQQRIHT---------------PPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIP--- 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  667 EAPSAQNEgdctctdaHFPMQTEATVNGQMPqAEIGPPtfssPLVIPPSQVSESHGQLSYQADIESENSGQLLHAEYEES 746
Cdd:pfam03154  365 QLPNPQSH--------KHPPHLSGPSPFQMN-SNLPPP----PALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQP 431
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1239937954  747 ---LSGKNMFPQPSFGPNP-FLGPVPIAPPFFPH 776
Cdd:pfam03154  432 pvlTQSQSLPPPAASHPPTsGLHQVPSQSPFPQH 465
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
821-1025 4.31e-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: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  821 VSAVDEFQEARGEGTHCLPEASVGKHEGRAEQSSQTPKVDLARPSILPVAEEEAhlPTQILNRERETVPVELEPKRTIPS 900
Cdd:PRK12678    52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAA--PAARAAAAAAAEAASAPEAAQARE 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  901 LKEKSEK-----VKDPKTAADAVSGANSVESRVQRPKEESSEDENEVsnilRSGRSKQfyNQTYGGRKYKSDWGSSGRGG 975
Cdd:PRK12678   130 RRERGEAarrgaARKAGEGGEQPATEARADAAERTEEEERDERRRRG----DREDRQA--EAERGERGRREERGRDGDDR 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1239937954  976 YQHARGEESWKGQPGRSRDEGyQYHRNVRGRPYRGDRRRSGMGDGHRGQN 1025
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 ...
1-72 1.94e-42

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: 150.98  E-value: 1.94e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    1 MACIHYLRENREKFEA-----------------EWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSN 63
Cdd:cd22794     42 KACVDYLRRNREKFEAfiegpfeqylknlenpkEWAGQVEISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSN 121

                   ....*....
gi 1239937954   64 GNHYDIVYP 72
Cdd:cd22794    122 GNHYDSVYP 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
192-250 7.46e-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: 7.46e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239937954  192 DYSIAAGLQYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKHS--PKNLKPPP 250
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTvpLKNLKPPP 63
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
447-776 7.26e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  447 PSTLENISDDKcariSSPSKSKKLECPPVEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVP 526
Cdd:pfam03154  149 PSPQDNESDSD----SSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  527 AQIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPYNE 589
Cdd:pfam03154  223 STAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLTP 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  590 KGDRAIAPP---YSLCHTGEDLPKDknilrfffnlgvkaySCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPwfq 666
Cdd:pfam03154  303 QSSQSQVPPgpsPAAPGQSQQRIHT---------------PPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIP--- 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  667 EAPSAQNEgdctctdaHFPMQTEATVNGQMPqAEIGPPtfssPLVIPPSQVSESHGQLSYQADIESENSGQLLHAEYEES 746
Cdd:pfam03154  365 QLPNPQSH--------KHPPHLSGPSPFQMN-SNLPPP----PALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQP 431
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1239937954  747 ---LSGKNMFPQPSFGPNP-FLGPVPIAPPFFPH 776
Cdd:pfam03154  432 pvlTQSQSLPPPAASHPPTsGLHQVPSQSPFPQH 465
PRK12678 PRK12678
transcription termination factor Rho; Provisional
821-1025 4.31e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  821 VSAVDEFQEARGEGTHCLPEASVGKHEGRAEQSSQTPKVDLARPSILPVAEEEAhlPTQILNRERETVPVELEPKRTIPS 900
Cdd:PRK12678    52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAA--PAARAAAAAAAEAASAPEAAQARE 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  901 LKEKSEK-----VKDPKTAADAVSGANSVESRVQRPKEESSEDENEVsnilRSGRSKQfyNQTYGGRKYKSDWGSSGRGG 975
Cdd:PRK12678   130 RRERGEAarrgaARKAGEGGEQPATEARADAAERTEEEERDERRRRG----DREDRQA--EAERGERGRREERGRDGDDR 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1239937954  976 YQHARGEESWKGQPGRSRDEGyQYHRNVRGRPYRGDRRRSGMGDGHRGQN 1025
Cdd:PRK12678   204 DRRDRREQGDRREERGRRDGG-DRRGRRRRRDRRDARGDDNREDRGDRDG 252
PHA03247 PHA03247
large tegument protein UL36; Provisional
460-808 5.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  460 RISSPSKSKKLECPPveQKPAEHVSLSNPAPLLVSPEVHLTPAVPSlPATVPAWPSEPTTFGPTGVPAQIPVLSVTQTLT 539
Cdd:PHA03247  2666 RARRLGRAAQASSPP--QRPRRRAARPTVGSLTSLADPPPPPPTPE-PAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  540 TGPDSAVSQAHLTPSPVPVSIQAVNQPLMP-LPQTLSLYQDPLYPGFPYNEKGDRAIAPPYSLCHTGEDLPKDknilrff 618
Cdd:PHA03247  2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA------- 2815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  619 fnlgvkAYSCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPW------FQEAPSAQNEGDCTCTDAHFPMQteatv 692
Cdd:PHA03247  2816 ------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggdVRRRPPSRSPAAKPAAPARPPVR----- 2884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  693 ngQMPQAEIGPPTFSSPLviPPSQVSEshgQLSYQADIESENSGQLLHAEYEESLSGKNMFPQPSFGPNPFLGPVPIAPP 772
Cdd:PHA03247  2885 --RLARPAVSRSTESFAL--PPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1239937954  773 FFPHVWYGYPFQGFVenPVMRQNIVLPSDEKELDLP 808
Cdd:PHA03247  2958 AVPQPWLGALVPGRV--AVPRFRVPQPAPSREAPAS 2991
 
Name Accession Description Interval E-value
OTU_OTUD4 cd22794
OTU (ovarian tumor) domain of OTU domain-containing protein 4 and similar proteins; OTU ...
1-72 1.94e-42

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: 150.98  E-value: 1.94e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    1 MACIHYLRENREKFEA-----------------EWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSN 63
Cdd:cd22794     42 KACVDYLRRNREKFEAfiegpfeqylknlenpkEWAGQVEISALSLMYKRDFIIYQEPGKPPSNVTENGFPDKILLCFSN 121

                   ....*....
gi 1239937954   64 GNHYDIVYP 72
Cdd:cd22794    122 GNHYDSVYP 130
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
192-250 7.46e-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: 7.46e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239937954  192 DYSIAAGLQYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKHS--PKNLKPPP 250
Cdd:cd20448      1 DFSIAAGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVfvEELGKKHTvpLKNLKPPP 63
OTU_ALG13-like cd22753
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
2-72 1.05e-26

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: 106.09  E-value: 1.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    2 ACIHYLRENREKFEA-----------------EWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNG 64
Cdd:cd22753     43 ACVEYLEKNREEFEKfseisfddylerlsdpkEWGGLLELEALSLLYKVDFIVYSIPDQPPSNITNNGYPKKIMLCYSGG 122

                   ....*...
gi 1239937954   65 NHYDIVYP 72
Cdd:cd22753    123 NHYDSVYS 130
OTU_ALG13 cd22795
OTU (ovarian tumor) domain of bifunctional UDP-N-acetylglucosamine transferase and ...
2-72 8.72e-26

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: 103.35  E-value: 8.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    2 ACIHYLRENREKFEA-----------------EWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNG 64
Cdd:cd22795     43 ACVSYMRANQCNFESyvegsfekylerledpkESAGQLEISALSLIYNRDFILYRYPGKPPTYATDNGFEDKILLCCSSN 122

                   ....*...
gi 1239937954   65 NHYDIVYP 72
Cdd:cd22795    123 GHYDSVYT 130
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
200-248 6.39e-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: 6.39e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1239937954  200 QYEVGDKCQVRLDHNGKFSNADFPGVHSENGPVLV--EELGKKH--SPKNLKP 248
Cdd:cd20380      1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVfvEELGEKKtvPYENLKP 53
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
197-261 4.97e-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: 59.48  E-value: 4.97e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1239937954  197 AGLQYEVGDKCQVRLDHNGKFSNADFP--GVHSENGPVLVEELGKKH--SPKNLKP----PPSESWNTVSGKK 261
Cdd:cd20447      2 AGRQYYLGDKCQVRLEPGGKYYNAHIQevGQDSNSVTVFIEELAEKHtvPLANLKPvtqvTPVPAWNMMPNRK 74
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
2-70 2.46e-06

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: 47.55  E-value: 2.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    2 ACIHYLRENREKFE-------------------AEWVGQVEISALSLMYRKDFIIYREpNVSPSQVTenNFPEK----VL 58
Cdd:cd22771     35 KVVDYMEAHEEDFEpffeddetfedyvsrmredGTWGGNLELQAASLVYRVNIVVHQL-GQPRWEIE--NFPDKgartIH 111
                           90
                   ....*....|..
gi 1239937954   59 LCFSNGNHYDIV 70
Cdd:cd22771    112 LSYHDGEHYNSV 123
OTU cd22744
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ...
2-70 4.05e-06

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: 47.05  E-value: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    2 ACIHYLRENREKFEA-----------------------EWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEK-- 56
Cdd:cd22744     33 EVVDYLRENPDLYEPaeladeddgedfdeylqrmrkpgTWGGELELQALANALNVPIVVYSEDGGFLPVSVFGPGPGPsg 112
                           90
                   ....*....|....*.
gi 1239937954   57 --VLLCFSNGNHYDIV 70
Cdd:cd22744    113 rpIHLLYTGGNHYDAL 128
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
447-776 7.26e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  447 PSTLENISDDKcariSSPSKSKKLECPPVEQkpAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVP 526
Cdd:pfam03154  149 PSPQDNESDSD----SSAQQQILQTQPPVLQ--AQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  527 AQIPVLSVTQTLTT-------GPDSAVSQAHLTPSPVPVSIQAVNQPLM-----PLPQTL----SLYQDPLYP-GFPYNE 589
Cdd:pfam03154  223 STAAPHTLIQQTPTlhpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgqmpPMPHSLqtgpSHMQHPVPPqPFPLTP 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  590 KGDRAIAPP---YSLCHTGEDLPKDknilrfffnlgvkaySCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPwfq 666
Cdd:pfam03154  303 QSSQSQVPPgpsPAAPGQSQQRIHT---------------PPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIP--- 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  667 EAPSAQNEgdctctdaHFPMQTEATVNGQMPqAEIGPPtfssPLVIPPSQVSESHGQLSYQADIESENSGQLLHAEYEES 746
Cdd:pfam03154  365 QLPNPQSH--------KHPPHLSGPSPFQMN-SNLPPP----PALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQP 431
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1239937954  747 ---LSGKNMFPQPSFGPNP-FLGPVPIAPPFFPH 776
Cdd:pfam03154  432 pvlTQSQSLPPPAASHPPTsGLHQVPSQSPFPQH 465
OTU_CeDUB-like cd22755
OTU (ovarian tumor) domain of Caenorhabditis elegans deubiquitylating enzyme with USP/UBP and ...
5-70 3.52e-03

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: 38.78  E-value: 3.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239937954    5 HYLRENREKFEAEWVGQVEISALSLM-------YRKDF---IIYRePNVSPSQVTENNFPekVLLCFSNGNHYDIV 70
Cdd:cd22755     59 EYLEKSRMRYDGTWATDVEIFAAATLlgvdiyvYSKGGykwLLYS-PRFKLGKRNGSREA--IYLKNTNGNHFEPV 131
OTU_OTUD6-like cd22748
OTU (ovarian tumor) domain of OTU domain-containing proteins 6A, 6B, and similar proteins; ...
6-67 3.56e-03

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: 39.08  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    6 YLRENREKFE--------------------------AEWVGQVEISALSLMYRKDFIIYREPnvSPSQVTENNFPEK--V 57
Cdd:cd22748     48 YMRAHRDDFLpfltnddgdlmteeefeeycdkientAEWGGQLELRALSKALKRPIHVYQAG--SPPLVIGEEFDSGepL 125
                           90
                   ....*....|....*
gi 1239937954   58 LLCF-----SNGNHY 67
Cdd:cd22748    126 RLSYhrhayGLGEHY 140
PRK12678 PRK12678
transcription termination factor Rho; Provisional
821-1025 4.31e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  821 VSAVDEFQEARGEGTHCLPEASVGKHEGRAEQSSQTPKVDLARPSILPVAEEEAhlPTQILNRERETVPVELEPKRTIPS 900
Cdd:PRK12678    52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAA--PAARAAAAAAAEAASAPEAAQARE 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  901 LKEKSEK-----VKDPKTAADAVSGANSVESRVQRPKEESSEDENEVsnilRSGRSKQfyNQTYGGRKYKSDWGSSGRGG 975
Cdd:PRK12678   130 RRERGEAarrgaARKAGEGGEQPATEARADAAERTEEEERDERRRRG----DREDRQA--EAERGERGRREERGRDGDDR 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1239937954  976 YQHARGEESWKGQPGRSRDEGyQYHRNVRGRPYRGDRRRSGMGDGHRGQN 1025
Cdd:PRK12678   204 DRRDRREQGDRREERGRRDGG-DRRGRRRRRDRRDARGDDNREDRGDRDG 252
PHA03247 PHA03247
large tegument protein UL36; Provisional
460-808 5.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  460 RISSPSKSKKLECPPveQKPAEHVSLSNPAPLLVSPEVHLTPAVPSlPATVPAWPSEPTTFGPTGVPAQIPVLSVTQTLT 539
Cdd:PHA03247  2666 RARRLGRAAQASSPP--QRPRRRAARPTVGSLTSLADPPPPPPTPE-PAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  540 TGPDSAVSQAHLTPSPVPVSIQAVNQPLMP-LPQTLSLYQDPLYPGFPYNEKGDRAIAPPYSLCHTGEDLPKDknilrff 618
Cdd:PHA03247  2743 AVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPA------- 2815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  619 fnlgvkAYSCPMWAPHSYLYPLHQAYLAACRMYPKVSVPVYPPNPW------FQEAPSAQNEGDCTCTDAHFPMQteatv 692
Cdd:PHA03247  2816 ------AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggdVRRRPPSRSPAAKPAAPARPPVR----- 2884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954  693 ngQMPQAEIGPPTFSSPLviPPSQVSEshgQLSYQADIESENSGQLLHAEYEESLSGKNMFPQPSFGPNPFLGPVPIAPP 772
Cdd:PHA03247  2885 --RLARPAVSRSTESFAL--PPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1239937954  773 FFPHVWYGYPFQGFVenPVMRQNIVLPSDEKELDLP 808
Cdd:PHA03247  2958 AVPQPWLGALVPGRV--AVPRFRVPQPAPSREAPAS 2991
OTU_OTUD5-like cd22752
OTU (ovarian tumor) domain of OTU domain-containing protein 5 and similar proteins; OTU ...
2-72 8.53e-03

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: 37.53  E-value: 8.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239937954    2 ACIHYLRENREKF-----------------EAEWVGQVEISALSLMYRKDFIIY---REP-NVSPSQVTENNFPekVLLC 60
Cdd:cd22752     35 HCMDYMEKNRDYFsqfvtedfeeyinrkrqDGVWGNHIEIQAMSELYNRPIEVYaysTEPiNTFHEASSSDNEP--IRLS 112
                           90
                   ....*....|..
gi 1239937954   61 FSNGNHYDIVYP 72
Cdd:cd22752    113 YHGNSHYNSIVD 124
 
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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