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Conserved domains on  [gi|15217866|ref|NP_176696|]
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Ubiquitin carboxyl-terminal hydrolase family protein [Arabidopsis thaliana]

Protein Classification

ubiquitin carboxyl-terminal hydrolase family protein( domain architecture ID 913)

ubiquitin carboxyl-terminal hydrolase family protein is a C19 family peptidase that may deubiquitinate polyubiquitinated target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
46-202 5.03e-11

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


The actual alignment was detected with superfamily member pfam00443:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 310  Bit Score: 61.69  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217866    46 PEANNIFDLFVYILENLPPWNPYFEVYELANKICNRCKMDLEY----PGLFENLTFEKFVQIIRIS--LKMPCDKEGCGK 119
Cdd:pfam00443 113 ENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDsaelKTASLQICFLQFSKLEELDdeEKYYCDKCGCKQ 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217866   120 RNYVQRMINKLPTVFTIALE--------WEHNETEGEIFDttsvlatEIDVSVIY---QYEGDSAFTKYRLVSMVC---- 184
Cdd:pfam00443 193 DAIKQLKISRLPPVLIIHLKrfsynrstWEKLNTEVEFPL-------ELDLSRYLaeeLKPKTNNLQDYRLVAVVVhsgs 265
                         170       180
                  ....*....|....*....|
gi 15217866   185 SDGDRYNC--VAYEDNRWVR 202
Cdd:pfam00443 266 LSSGHYIAyiKAYENNRWYK 285
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
46-202 5.03e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 61.69  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217866    46 PEANNIFDLFVYILENLPPWNPYFEVYELANKICNRCKMDLEY----PGLFENLTFEKFVQIIRIS--LKMPCDKEGCGK 119
Cdd:pfam00443 113 ENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDsaelKTASLQICFLQFSKLEELDdeEKYYCDKCGCKQ 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217866   120 RNYVQRMINKLPTVFTIALE--------WEHNETEGEIFDttsvlatEIDVSVIY---QYEGDSAFTKYRLVSMVC---- 184
Cdd:pfam00443 193 DAIKQLKISRLPPVLIIHLKrfsynrstWEKLNTEVEFPL-------ELDLSRYLaeeLKPKTNNLQDYRLVAVVVhsgs 265
                         170       180
                  ....*....|....*....|
gi 15217866   185 SDGDRYNC--VAYEDNRWVR 202
Cdd:pfam00443 266 LSSGHYIAyiKAYENNRWYK 285
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
46-202 5.03e-11

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 61.69  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217866    46 PEANNIFDLFVYILENLPPWNPYFEVYELANKICNRCKMDLEY----PGLFENLTFEKFVQIIRIS--LKMPCDKEGCGK 119
Cdd:pfam00443 113 ENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDsaelKTASLQICFLQFSKLEELDdeEKYYCDKCGCKQ 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217866   120 RNYVQRMINKLPTVFTIALE--------WEHNETEGEIFDttsvlatEIDVSVIY---QYEGDSAFTKYRLVSMVC---- 184
Cdd:pfam00443 193 DAIKQLKISRLPPVLIIHLKrfsynrstWEKLNTEVEFPL-------ELDLSRYLaeeLKPKTNNLQDYRLVAVVVhsgs 265
                         170       180
                  ....*....|....*....|
gi 15217866   185 SDGDRYNC--VAYEDNRWVR 202
Cdd:pfam00443 266 LSSGHYIAyiKAYENNRWYK 285
 
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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