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Conserved domains on  [gi|119574889|gb|EAW54504|]
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ubiquitin specific peptidase 54, isoform CRA_c [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 10115580)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that catalyzes the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the-terminal Gly of ubiquitin, a 76-residue protein attached to proteins as an intracellular targeting signal

CATH:  2.20.210.10
EC:  3.4.19.12
Gene Ontology:  GO:0004843|GO:0016579
SCOP:  4003158

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
3-232 2.01e-12

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.


:

Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 69.05  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889    3 DAAECFENLLMRIHFHIADETK-EDICTAQHCISHQKFAMTLFEQCVCTSCGATS---DPLPFIQmvhyisttslcnqai 78
Cdd:cd02257    24 DAHEFLLFLLDKLHEELKKSSKrTSDSSSLKSLIHDLFGGKLESTIVCLECGHESvstEPELFLS--------------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889   79 CMLERREKPSPSMFgELLQN--ASTMGDLRNCPSNCGER---IRIRRVLMNAPQIITIGL---VWDSDHSDLAEDVIHSL 150
Cdd:cd02257    89 LPLPVKGLPQVSLE-DCLEKffKEEILEGDNCYKCEKKKkqeATKRLKIKKLPPVLIIHLkrfSFNEDGTKEKLNTKVSF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889  151 GTCLKLGDLFFRVTDDRAKQSELY---LVGMICYYGK-----HYSTFFFQTKIRKWMYFDDAHVKEIgpKWKDVVTKCIK 222
Cdd:cd02257   168 PLELDLSPYLSEGEKDSDSDNGSYkyeLVAVVVHSGTsadsgHYVAYVKDPSDGKWYKFNDDKVTEV--SEEEVLEFGSL 245
                         250
                  ....*....|
gi 119574889  223 GHyQPLLLLY 232
Cdd:cd02257   246 SS-SAYILFY 254
 
Name Accession Description Interval E-value
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
3-232 2.01e-12

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.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 69.05  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889    3 DAAECFENLLMRIHFHIADETK-EDICTAQHCISHQKFAMTLFEQCVCTSCGATS---DPLPFIQmvhyisttslcnqai 78
Cdd:cd02257    24 DAHEFLLFLLDKLHEELKKSSKrTSDSSSLKSLIHDLFGGKLESTIVCLECGHESvstEPELFLS--------------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889   79 CMLERREKPSPSMFgELLQN--ASTMGDLRNCPSNCGER---IRIRRVLMNAPQIITIGL---VWDSDHSDLAEDVIHSL 150
Cdd:cd02257    89 LPLPVKGLPQVSLE-DCLEKffKEEILEGDNCYKCEKKKkqeATKRLKIKKLPPVLIIHLkrfSFNEDGTKEKLNTKVSF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889  151 GTCLKLGDLFFRVTDDRAKQSELY---LVGMICYYGK-----HYSTFFFQTKIRKWMYFDDAHVKEIgpKWKDVVTKCIK 222
Cdd:cd02257   168 PLELDLSPYLSEGEKDSDSDNGSYkyeLVAVVVHSGTsadsgHYVAYVKDPSDGKWYKFNDDKVTEV--SEEEVLEFGSL 245
                         250
                  ....*....|
gi 119574889  223 GHyQPLLLLY 232
Cdd:cd02257   246 SS-SAYILFY 254
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
3-232 2.54e-10

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 63.62  E-value: 2.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889     3 DAAECFENLLMRIHfhiaDETKEDICTAQHCISHQKFAMTLFEQCVCTSCG---ATSDPLPFIQ-MVHYISTTSLCNQAI 78
Cdd:pfam00443   90 DAQEFLLFLLDGLH----EDLNGNHSTENESLITDLFRGQLKSRLKCLSCGevsETFEPFSDLSlPIPGDSAELKTASLQ 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889    79 CMLERREKPspsmfgELLQNastmGDLRNCPsNCGE------RIRIRRvlmnAPQIITIGLVWDSDHSDLAEdvihslgt 152
Cdd:pfam00443  166 ICFLQFSKL------EELDD----EEKYYCD-KCGCkqdaikQLKISR----LPPVLIIHLKRFSYNRSTWE-------- 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889   153 clKLGDLF----------FRVTDDRAKQSELY---LVGMICYYG----KHYSTFFFQTKIRKWMYFDDAHVKEIGPKwKD 215
Cdd:pfam00443  223 --KLNTEVefpleldlsrYLAEELKPKTNNLQdyrLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEE-TA 299
                          250
                   ....*....|....*..
gi 119574889   216 VVTKcikghyQPLLLLY 232
Cdd:pfam00443  300 VLSS------SAYILFY 310
 
Name Accession Description Interval E-value
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
3-232 2.01e-12

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.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 69.05  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889    3 DAAECFENLLMRIHFHIADETK-EDICTAQHCISHQKFAMTLFEQCVCTSCGATS---DPLPFIQmvhyisttslcnqai 78
Cdd:cd02257    24 DAHEFLLFLLDKLHEELKKSSKrTSDSSSLKSLIHDLFGGKLESTIVCLECGHESvstEPELFLS--------------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889   79 CMLERREKPSPSMFgELLQN--ASTMGDLRNCPSNCGER---IRIRRVLMNAPQIITIGL---VWDSDHSDLAEDVIHSL 150
Cdd:cd02257    89 LPLPVKGLPQVSLE-DCLEKffKEEILEGDNCYKCEKKKkqeATKRLKIKKLPPVLIIHLkrfSFNEDGTKEKLNTKVSF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889  151 GTCLKLGDLFFRVTDDRAKQSELY---LVGMICYYGK-----HYSTFFFQTKIRKWMYFDDAHVKEIgpKWKDVVTKCIK 222
Cdd:cd02257   168 PLELDLSPYLSEGEKDSDSDNGSYkyeLVAVVVHSGTsadsgHYVAYVKDPSDGKWYKFNDDKVTEV--SEEEVLEFGSL 245
                         250
                  ....*....|
gi 119574889  223 GHyQPLLLLY 232
Cdd:cd02257   246 SS-SAYILFY 254
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
3-232 2.54e-10

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 63.62  E-value: 2.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889     3 DAAECFENLLMRIHfhiaDETKEDICTAQHCISHQKFAMTLFEQCVCTSCG---ATSDPLPFIQ-MVHYISTTSLCNQAI 78
Cdd:pfam00443   90 DAQEFLLFLLDGLH----EDLNGNHSTENESLITDLFRGQLKSRLKCLSCGevsETFEPFSDLSlPIPGDSAELKTASLQ 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889    79 CMLERREKPspsmfgELLQNastmGDLRNCPsNCGE------RIRIRRvlmnAPQIITIGLVWDSDHSDLAEdvihslgt 152
Cdd:pfam00443  166 ICFLQFSKL------EELDD----EEKYYCD-KCGCkqdaikQLKISR----LPPVLIIHLKRFSYNRSTWE-------- 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574889   153 clKLGDLF----------FRVTDDRAKQSELY---LVGMICYYG----KHYSTFFFQTKIRKWMYFDDAHVKEIGPKwKD 215
Cdd:pfam00443  223 --KLNTEVefpleldlsrYLAEELKPKTNNLQdyrLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEE-TA 299
                          250
                   ....*....|....*..
gi 119574889   216 VVTKcikghyQPLLLLY 232
Cdd:pfam00443  300 VLSS------SAYILFY 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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