NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1827633752|dbj|BBJ21309|]
View 

cysteine protease [Cryphonectria nitschkei chrysovirus 1]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
691-786 2.69e-04

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 cd22792:

Pssm-ID: 459237 [Multi-domain]  Cd Length: 108  Bit Score: 41.05  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827633752 691 KAIDVPGDGKCGLHAVVQDLQSHGLLMQRdggrvlRLLDKSTNAPTFHSP-------------EEIAGAVLKLGLGLDV- 756
Cdd:cd22792     1 KVVPVPGDGNCFWHSLGHFLGLSALELKK------LLRDSLFDDPELDEEldeqlepgvyaedEAIAAAAKLFGVNICVh 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1827633752 757 -VADGIVHSY-GNNDGHRILLQLKDHHYMPIV 786
Cdd:cd22792    75 dPDEGVLYTFtPNESSKSIHLLLENEHFEPLV 106
 
Name Accession Description Interval E-value
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
691-786 2.69e-04

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 41.05  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827633752 691 KAIDVPGDGKCGLHAVVQDLQSHGLLMQRdggrvlRLLDKSTNAPTFHSP-------------EEIAGAVLKLGLGLDV- 756
Cdd:cd22792     1 KVVPVPGDGNCFWHSLGHFLGLSALELKK------LLRDSLFDDPELDEEldeqlepgvyaedEAIAAAAKLFGVNICVh 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1827633752 757 -VADGIVHSY-GNNDGHRILLQLKDHHYMPIV 786
Cdd:cd22792    75 dPDEGVLYTFtPNESSKSIHLLLENEHFEPLV 106
 
Name Accession Description Interval E-value
OTU_RDRP-like cd22792
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ...
691-786 2.69e-04

OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad.


Pssm-ID: 438613 [Multi-domain]  Cd Length: 108  Bit Score: 41.05  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827633752 691 KAIDVPGDGKCGLHAVVQDLQSHGLLMQRdggrvlRLLDKSTNAPTFHSP-------------EEIAGAVLKLGLGLDV- 756
Cdd:cd22792     1 KVVPVPGDGNCFWHSLGHFLGLSALELKK------LLRDSLFDDPELDEEldeqlepgvyaedEAIAAAAKLFGVNICVh 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1827633752 757 -VADGIVHSY-GNNDGHRILLQLKDHHYMPIV 786
Cdd:cd22792    75 dPDEGVLYTFtPNESSKSIHLLLENEHFEPLV 106
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH