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Conserved domains on  [gi|1039768791|ref|XP_017175897|]
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OTU domain-containing protein 3 isoform X2 [Mus musculus]

Protein Classification

OTU domain-containing protein( domain architecture ID 1904167)

OTU (ovarian tumor) domain-containing protein may function as a deubiquitinase (DUBs)/ubiquitin thiolesterase that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, or may be inactive

EC:  3.4.19.12
PubMed:  10664582|23827681

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 ...
8-43 4.19e-17

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 cd22770:

Pssm-ID: 459237 [Multi-domain]  Cd Length: 145  Bit Score: 76.17  E-value: 4.19e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1039768791   8 TIRGTDKGSTRELHIAYRYGEHYDSVRRINDNSEAP 43
Cdd:cd22770   110 QIRGTEKSSSRELHISYHNGDHYSSVRKLGDNSENP 145
rne super family cl35953
ribonuclease E; Reviewed
174-254 6.14e-03

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 38.10  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768791  174 AEENHEPGDRVKQRGPSREEAGSGRRLSGNQGRNEGR--------------METSEARASP-AEESKAHKSQlpkvtNKQ 238
Cdd:PRK10811   597 EAKPERQQDRRKPRQNNRRDRNERRDTRDNRTRREGRenreenrrnrrqaqQQTAETRESQqAEVTEKARTQ-----DEQ 671
                           90
                   ....*....|....*.
gi 1039768791  239 RREQQRLEKKKRQEER 254
Cdd:PRK10811   672 QQAPRRERQRRRNDEK 687
 
Name Accession Description Interval E-value
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
8-43 4.19e-17

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


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 76.17  E-value: 4.19e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1039768791   8 TIRGTDKGSTRELHIAYRYGEHYDSVRRINDNSEAP 43
Cdd:cd22770   110 QIRGTEKSSSRELHISYHNGDHYSSVRKLGDNSENP 145
rne PRK10811
ribonuclease E; Reviewed
174-254 6.14e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 38.10  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768791  174 AEENHEPGDRVKQRGPSREEAGSGRRLSGNQGRNEGR--------------METSEARASP-AEESKAHKSQlpkvtNKQ 238
Cdd:PRK10811   597 EAKPERQQDRRKPRQNNRRDRNERRDTRDNRTRREGRenreenrrnrrqaqQQTAETRESQqAEVTEKARTQ-----DEQ 671
                           90
                   ....*....|....*.
gi 1039768791  239 RREQQRLEKKKRQEER 254
Cdd:PRK10811   672 QQAPRRERQRRRNDEK 687
 
Name Accession Description Interval E-value
OTU_OTUD3 cd22770
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; OTU ...
8-43 4.19e-17

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


Pssm-ID: 438607 [Multi-domain]  Cd Length: 145  Bit Score: 76.17  E-value: 4.19e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1039768791   8 TIRGTDKGSTRELHIAYRYGEHYDSVRRINDNSEAP 43
Cdd:cd22770   110 QIRGTEKSSSRELHISYHNGDHYSSVRKLGDNSENP 145
OTU_OTUD3-like cd22756
OTU (ovarian tumor) domain of OTU domain-containing protein 3 and similar proteins; This ...
8-34 1.30e-04

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: 41.01  E-value: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039768791   8 TIRGTDKGST----RELHIAYRYGEHYDSVR 34
Cdd:cd22756   101 VISAPEDGSPgparRVLHIAYHNWEHYSSVR 131
OTU_plant_OTU7-like cd22771
OTU (ovarian tumor) domain of Arabidopsis thaliana deubiquitinating enzyme OTU7 and similar ...
6-34 2.51e-04

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: 39.84  E-value: 2.51e-04
                          10        20
                  ....*....|....*....|....*....
gi 1039768791   6 RSTIRGTDKGSTRELHIAYRYGEHYDSVR 34
Cdd:cd22771    96 RWEIENFPDKGARTIHLSYHDGEHYNSVR 124
rne PRK10811
ribonuclease E; Reviewed
174-254 6.14e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 38.10  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768791  174 AEENHEPGDRVKQRGPSREEAGSGRRLSGNQGRNEGR--------------METSEARASP-AEESKAHKSQlpkvtNKQ 238
Cdd:PRK10811   597 EAKPERQQDRRKPRQNNRRDRNERRDTRDNRTRREGRenreenrrnrrqaqQQTAETRESQqAEVTEKARTQ-----DEQ 671
                           90
                   ....*....|....*.
gi 1039768791  239 RREQQRLEKKKRQEER 254
Cdd:PRK10811   672 QQAPRRERQRRRNDEK 687
 
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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