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Conserved domains on  [gi|1734341917|ref|NP_001360742|]
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USP domain-containing protein [Caenorhabditis elegans]

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 ...
119-388 2.15e-07

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: 52.06  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 119 CFAISVCQALLACPPFVRYVKEKIAETKLDMHMKS--LVAQFA---AHSIPAAGSGDWPRVSISKLLNSIPGGFNGKCRE 193
Cdd:pfam00443  10 CYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRdlfKALQKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 194 DA--------EDWYRQLSKEFYDE-------TF-GQVSAYYKtvCHECGKCREINDKSPRVQLRCPD---LEITAANIES 254
Cdd:pfam00443  90 DAqefllfllDGLHEDLNGNHSTEneslitdLFrGQLKSRLK--CLSCGEVSETFEPFSDLSLPIPGdsaELKTASLQIC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 255 MLAVTGNEIVTWEhDGCENTTCRETTRYE-------FPDVILVSVDTFQDGNRH---IGKELEFFPTEDFSPISVNNDEP 324
Cdd:pfam00443 168 FLQFSKLEELDDE-EKYYCDKCGCKQDAIkqlkisrLPPVLIIHLKRFSYNRSTwekLNTEVEFPLELDLSRYLAEELKP 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734341917 325 D------------IFHLGGViyfrtfncfrdeSSGHYMARVYHHGNV--FLADDNRIYEqnINRPTEPANSVPYFAFY 388
Cdd:pfam00443 247 KtnnlqdyrlvavVVHSGSL------------SSGHYIAYIKAYENNrwYKFDDEKVTE--VDEETAVLSSSAYILFY 310
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
119-388 2.15e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 52.06  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 119 CFAISVCQALLACPPFVRYVKEKIAETKLDMHMKS--LVAQFA---AHSIPAAGSGDWPRVSISKLLNSIPGGFNGKCRE 193
Cdd:pfam00443  10 CYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRdlfKALQKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 194 DA--------EDWYRQLSKEFYDE-------TF-GQVSAYYKtvCHECGKCREINDKSPRVQLRCPD---LEITAANIES 254
Cdd:pfam00443  90 DAqefllfllDGLHEDLNGNHSTEneslitdLFrGQLKSRLK--CLSCGEVSETFEPFSDLSLPIPGdsaELKTASLQIC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 255 MLAVTGNEIVTWEhDGCENTTCRETTRYE-------FPDVILVSVDTFQDGNRH---IGKELEFFPTEDFSPISVNNDEP 324
Cdd:pfam00443 168 FLQFSKLEELDDE-EKYYCDKCGCKQDAIkqlkisrLPPVLIIHLKRFSYNRSTwekLNTEVEFPLELDLSRYLAEELKP 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734341917 325 D------------IFHLGGViyfrtfncfrdeSSGHYMARVYHHGNV--FLADDNRIYEqnINRPTEPANSVPYFAFY 388
Cdd:pfam00443 247 KtnnlqdyrlvavVVHSGSL------------SSGHYIAYIKAYENNrwYKFDDEKVTE--VDEETAVLSSSAYILFY 310
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
119-388 2.15e-07

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 52.06  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 119 CFAISVCQALLACPPFVRYVKEKIAETKLDMHMKS--LVAQFA---AHSIPAAGSGDWPRVSISKLLNSIPGGFNGKCRE 193
Cdd:pfam00443  10 CYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRdlfKALQKNSKSSSVSPKMFKKSLGKLNPDFSGYKQQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 194 DA--------EDWYRQLSKEFYDE-------TF-GQVSAYYKtvCHECGKCREINDKSPRVQLRCPD---LEITAANIES 254
Cdd:pfam00443  90 DAqefllfllDGLHEDLNGNHSTEneslitdLFrGQLKSRLK--CLSCGEVSETFEPFSDLSLPIPGdsaELKTASLQIC 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734341917 255 MLAVTGNEIVTWEhDGCENTTCRETTRYE-------FPDVILVSVDTFQDGNRH---IGKELEFFPTEDFSPISVNNDEP 324
Cdd:pfam00443 168 FLQFSKLEELDDE-EKYYCDKCGCKQDAIkqlkisrLPPVLIIHLKRFSYNRSTwekLNTEVEFPLELDLSRYLAEELKP 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1734341917 325 D------------IFHLGGViyfrtfncfrdeSSGHYMARVYHHGNV--FLADDNRIYEqnINRPTEPANSVPYFAFY 388
Cdd:pfam00443 247 KtnnlqdyrlvavVVHSGSL------------SSGHYIAYIKAYENNrwYKFDDEKVTE--VDEETAVLSSSAYILFY 310
 
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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