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Conserved domains on  [gi|1063728716|ref|NP_001318617|]
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ubiquitin-specific protease 8 [Arabidopsis thaliana]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 1000871)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins

CATH:  3.90.70.10
EC:  3.4.19.12
Gene Ontology:  GO:0016579|GO:0046872|GO:0003723

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBP12 super family cl35019
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
101-868 3.18e-141

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5560:

Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 438.93  E-value: 3.18e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 101 DFALVSSDMWLQALKWY-HDDKNTEKGVKSFSAGGVDRGDVYPVQLRLSVLQETNS---------LAVKICKKDNSVECF 170
Cdd:COG5560    94 DYSIISGAVWQLLVRWYgLAGLITPRITVLLPSESAPEVESYPVVFKLHWLFSINGslinlghdpVPHSASSHGTLRDLS 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 171 RRACKIFSLDSEQLRIWDISGQTTLFFESDVSNSKDCQQQADQEILLELQIYGLSDsiklkeskkEDGSTQQTNGITNgM 250
Cdd:COG5560   174 ERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELF---------EDRSVLLLSKITR-N 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 251 NGGTVFRFGRSNSLSFLGKAGeagtlgLTGLQNLGNTCFMNSSLQCLAHTPKLVDFFLG-EYSKEINLDNPLGMKGEIAL 329
Cdd:COG5560   244 PDWLVDSIVDDHNRSINKEAG------TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdEYEESINEENPLGMHGSVAS 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 330 AFGDLLRSLWAPGASTVAPRTFKAKLARFAPQFSGFNQHDSQELLAFLLDGLHEDLNRVKNKPYVEAKD---GDGRPDAE 406
Cdd:COG5560   318 AYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlspGDDVVVKK 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 407 VADEYWRNHVARNDSIIVDVCQGQYKSTLVCPICKKVSVMFDPFMYLSLPLPCTSMRTMDLTVMSADGSslPIPLTVNVP 486
Cdd:COG5560   398 KAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGR--RQPLKIELD 475
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 487 KFGKFEDLhKALVTACS--LPEEEtLLVTEVYNNRIIRFLEEPTDSLT-LIRDGDKLVVYrlkKDANNSPLIVYMHQKLE 563
Cdd:COG5560   476 ASSTIRGL-KKLVDAEYgkLGCFE-IKVMCIYYGGNYNMLEPADKVLLqDIPQTDFVYLY---ETNDNGIEVPVVHLRIE 550
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 564 EQFISGkssptwKAFGIPLvsrlcdvengsdvenLYLKLLSSfkmptEFFTENLENPTEEEATDKTDTDgttsvedtnsT 643
Cdd:COG5560   551 KGYKSK------RLFGDPF---------------LQLNVLIK-----ASIYDKLVKEFEELLVLVEMKK----------T 594
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 644 DVKETTESLP------DPVLRLYLTDDRGNSIEAEMLKEKPVNKSKRLNVLARWPVKELDVydtcLLSSLPEVSKSGTKR 717
Cdd:COG5560   595 DVDLVSEQVRllreesSPSSWLKLETEIDTKREEQVEEEGQMNFNDAVVISCEWEEKRYLS----LFSYDPLWTIREIGA 670
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 718 PQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKNKLEAYVDFPLDNLDL 797
Cdd:COG5560   671 AERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDL 750
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063728716 798 SSYISYKNGQTTYrYMLYAISNHYGSMGGGHYTAYVHHGGD-RWYDFDDSHVHQISQEKIKTSAAYVLFYKR 868
Cdd:COG5560   751 SGVEYMVDDPRLI-YDLYAVDNHYGGLSGGHYTAYARNFANnGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
101-868 3.18e-141

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 438.93  E-value: 3.18e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 101 DFALVSSDMWLQALKWY-HDDKNTEKGVKSFSAGGVDRGDVYPVQLRLSVLQETNS---------LAVKICKKDNSVECF 170
Cdd:COG5560    94 DYSIISGAVWQLLVRWYgLAGLITPRITVLLPSESAPEVESYPVVFKLHWLFSINGslinlghdpVPHSASSHGTLRDLS 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 171 RRACKIFSLDSEQLRIWDISGQTTLFFESDVSNSKDCQQQADQEILLELQIYGLSDsiklkeskkEDGSTQQTNGITNgM 250
Cdd:COG5560   174 ERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELF---------EDRSVLLLSKITR-N 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 251 NGGTVFRFGRSNSLSFLGKAGeagtlgLTGLQNLGNTCFMNSSLQCLAHTPKLVDFFLG-EYSKEINLDNPLGMKGEIAL 329
Cdd:COG5560   244 PDWLVDSIVDDHNRSINKEAG------TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdEYEESINEENPLGMHGSVAS 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 330 AFGDLLRSLWAPGASTVAPRTFKAKLARFAPQFSGFNQHDSQELLAFLLDGLHEDLNRVKNKPYVEAKD---GDGRPDAE 406
Cdd:COG5560   318 AYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlspGDDVVVKK 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 407 VADEYWRNHVARNDSIIVDVCQGQYKSTLVCPICKKVSVMFDPFMYLSLPLPCTSMRTMDLTVMSADGSslPIPLTVNVP 486
Cdd:COG5560   398 KAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGR--RQPLKIELD 475
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 487 KFGKFEDLhKALVTACS--LPEEEtLLVTEVYNNRIIRFLEEPTDSLT-LIRDGDKLVVYrlkKDANNSPLIVYMHQKLE 563
Cdd:COG5560   476 ASSTIRGL-KKLVDAEYgkLGCFE-IKVMCIYYGGNYNMLEPADKVLLqDIPQTDFVYLY---ETNDNGIEVPVVHLRIE 550
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 564 EQFISGkssptwKAFGIPLvsrlcdvengsdvenLYLKLLSSfkmptEFFTENLENPTEEEATDKTDTDgttsvedtnsT 643
Cdd:COG5560   551 KGYKSK------RLFGDPF---------------LQLNVLIK-----ASIYDKLVKEFEELLVLVEMKK----------T 594
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 644 DVKETTESLP------DPVLRLYLTDDRGNSIEAEMLKEKPVNKSKRLNVLARWPVKELDVydtcLLSSLPEVSKSGTKR 717
Cdd:COG5560   595 DVDLVSEQVRllreesSPSSWLKLETEIDTKREEQVEEEGQMNFNDAVVISCEWEEKRYLS----LFSYDPLWTIREIGA 670
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 718 PQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKNKLEAYVDFPLDNLDL 797
Cdd:COG5560   671 AERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDL 750
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063728716 798 SSYISYKNGQTTYrYMLYAISNHYGSMGGGHYTAYVHHGGD-RWYDFDDSHVHQISQEKIKTSAAYVLFYKR 868
Cdd:COG5560   751 SGVEYMVDDPRLI-YDLYAVDNHYGGLSGGHYTAYARNFANnGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
697-867 4.70e-60

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 203.67  E-value: 4.70e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 697 DVYDTCLLSSLPEVSKSGtkrPQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSY 776
Cdd:cd02674    62 TTFEPFTYLSLPIPSGSG---DAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 777 SRFMKNKLEAYVDFPLDNLDLSSYISYKNGQTTYRYMLYAISNHYGSMGGGHYTAYVHHG-GDRWYDFDDSHVHQISQEK 855
Cdd:cd02674   139 SRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNeTNDWYKFDDSRVTKVSESS 218
                         170
                  ....*....|..
gi 1063728716 856 IKTSAAYVLFYK 867
Cdd:cd02674   219 VVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
716-866 2.42e-49

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 176.86  E-value: 2.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 716 KRPQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKNKLEAYVDFPLDnL 795
Cdd:pfam00443 156 SAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-L 234
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063728716 796 DLSSYIS---YKNGQTTYRYMLYAISNHYGSMGGGHYTAYV-HHGGDRWYDFDDSHVHQISQEK-IKTSAAYVLFY 866
Cdd:pfam00443 235 DLSRYLAeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIkAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
101-868 3.18e-141

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 438.93  E-value: 3.18e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 101 DFALVSSDMWLQALKWY-HDDKNTEKGVKSFSAGGVDRGDVYPVQLRLSVLQETNS---------LAVKICKKDNSVECF 170
Cdd:COG5560    94 DYSIISGAVWQLLVRWYgLAGLITPRITVLLPSESAPEVESYPVVFKLHWLFSINGslinlghdpVPHSASSHGTLRDLS 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 171 RRACKIFSLDSEQLRIWDISGQTTLFFESDVSNSKDCQQQADQEILLELQIYGLSDsiklkeskkEDGSTQQTNGITNgM 250
Cdd:COG5560   174 ERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELF---------EDRSVLLLSKITR-N 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 251 NGGTVFRFGRSNSLSFLGKAGeagtlgLTGLQNLGNTCFMNSSLQCLAHTPKLVDFFLG-EYSKEINLDNPLGMKGEIAL 329
Cdd:COG5560   244 PDWLVDSIVDDHNRSINKEAG------TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSdEYEESINEENPLGMHGSVAS 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 330 AFGDLLRSLWAPGASTVAPRTFKAKLARFAPQFSGFNQHDSQELLAFLLDGLHEDLNRVKNKPYVEAKD---GDGRPDAE 406
Cdd:COG5560   318 AYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDlspGDDVVVKK 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 407 VADEYWRNHVARNDSIIVDVCQGQYKSTLVCPICKKVSVMFDPFMYLSLPLPCTSMRTMDLTVMSADGSslPIPLTVNVP 486
Cdd:COG5560   398 KAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTLPLPVSMVWKHTIVVFPESGR--RQPLKIELD 475
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 487 KFGKFEDLhKALVTACS--LPEEEtLLVTEVYNNRIIRFLEEPTDSLT-LIRDGDKLVVYrlkKDANNSPLIVYMHQKLE 563
Cdd:COG5560   476 ASSTIRGL-KKLVDAEYgkLGCFE-IKVMCIYYGGNYNMLEPADKVLLqDIPQTDFVYLY---ETNDNGIEVPVVHLRIE 550
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 564 EQFISGkssptwKAFGIPLvsrlcdvengsdvenLYLKLLSSfkmptEFFTENLENPTEEEATDKTDTDgttsvedtnsT 643
Cdd:COG5560   551 KGYKSK------RLFGDPF---------------LQLNVLIK-----ASIYDKLVKEFEELLVLVEMKK----------T 594
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 644 DVKETTESLP------DPVLRLYLTDDRGNSIEAEMLKEKPVNKSKRLNVLARWPVKELDVydtcLLSSLPEVSKSGTKR 717
Cdd:COG5560   595 DVDLVSEQVRllreesSPSSWLKLETEIDTKREEQVEEEGQMNFNDAVVISCEWEEKRYLS----LFSYDPLWTIREIGA 670
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 718 PQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKNKLEAYVDFPLDNLDL 797
Cdd:COG5560   671 AERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDL 750
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063728716 798 SSYISYKNGQTTYrYMLYAISNHYGSMGGGHYTAYVHHGGD-RWYDFDDSHVHQISQEKIKTSAAYVLFYKR 868
Cdd:COG5560   751 SGVEYMVDDPRLI-YDLYAVDNHYGGLSGGHYTAYARNFANnGWYLFDDSRITEVDPEDSVTSSAYVLFYRR 821
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
697-867 4.70e-60

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 203.67  E-value: 4.70e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 697 DVYDTCLLSSLPEVSKSGtkrPQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSY 776
Cdd:cd02674    62 TTFEPFTYLSLPIPSGSG---DAPKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSF 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 777 SRFMKNKLEAYVDFPLDNLDLSSYISYKNGQTTYRYMLYAISNHYGSMGGGHYTAYVHHG-GDRWYDFDDSHVHQISQEK 855
Cdd:cd02674   139 SRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNeTNDWYKFDDSRVTKVSESS 218
                         170
                  ....*....|..
gi 1063728716 856 IKTSAAYVLFYK 867
Cdd:cd02674   219 VVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
716-866 2.42e-49

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 176.86  E-value: 2.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 716 KRPQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKNKLEAYVDFPLDnL 795
Cdd:pfam00443 156 SAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPLE-L 234
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063728716 796 DLSSYIS---YKNGQTTYRYMLYAISNHYGSMGGGHYTAYV-HHGGDRWYDFDDSHVHQISQEK-IKTSAAYVLFY 866
Cdd:pfam00443 235 DLSRYLAeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIkAYENNRWYKFDDEKVTEVDEETaVLSSSAYILFY 310
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
279-458 2.18e-47

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 171.47  E-value: 2.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 279 TGLQNLGNTCFMNSSLQCLAHTPKLVDFFLgeYSKEINLDNPLGMKGEIALAFGDLLRSLWAPGAST-VAPRTFKAKLAR 357
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLL--RISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSsVSPKMFKKSLGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 358 FAPQFSGFNQHDSQELLAFLLDGLHEDLNrvknkpyveakdgdgrpdaevadeywRNHVARNDSIIVDVCQGQYKSTLVC 437
Cdd:pfam00443  79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLKC 132
                         170       180
                  ....*....|....*....|.
gi 1063728716 438 PICKKVSVMFDPFMYLSLPLP 458
Cdd:pfam00443 133 LSCGEVSETFEPFSDLSLPIP 153
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
717-867 4.26e-38

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: 143.01  E-value: 4.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 717 RPQESVSLFKCLEAFLTEEPLGPDDMWYCPgCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKN-KLEAYVDFPLdNL 795
Cdd:cd02257    94 KGLPQVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGTKeKLNTKVSFPL-EL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 796 DLSSYISYK-----NGQTTYRYMLYAISNHYG-SMGGGHYTAYV-HHGGDRWYDFDDSHVHQISQEKI-----KTSAAYV 863
Cdd:cd02257   172 DLSPYLSEGekdsdSDNGSYKYELVAVVVHSGtSADSGHYVAYVkDPSDGKWYKFNDDKVTEVSEEEVlefgsLSSSAYI 251

                  ....
gi 1063728716 864 LFYK 867
Cdd:cd02257   252 LFYE 255
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
713-867 6.88e-36

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 138.66  E-value: 6.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 713 SGTKRPQESVSLFKCLEAFLTEEPLGPDDmWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRF-MKNKLEAYVDFP 791
Cdd:cd02660   167 LGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNkTSRKIDTYVQFP 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 792 LDnLDLSSYISYKNGQTT--------YRYMLYAISNHYGSMGGGHYTAYVHHGGDRWYDFDDSHVHQISQEKIKTSAAYV 863
Cdd:cd02660   246 LE-LNMTPYTSSSIGDTQdsnsldpdYTYDLFAVVVHKGTLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQAYL 324

                  ....
gi 1063728716 864 LFYK 867
Cdd:cd02660   325 LFYH 328
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
723-866 7.91e-31

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 123.54  E-value: 7.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 723 SLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFmkNKLEAYVDFPlDNLDLSSYIS 802
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFP-ETLDLSPYMS 239
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063728716 803 YKNGQTTyRYMLYAISNHYG-SMGGGHYTAYVHHGGDRWYDFDDSHVHQISQEKIKTSAAYVLFY 866
Cdd:cd02661   240 QPNDGPL-KYKLYAVLVHSGfSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
699-866 2.86e-26

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 109.40  E-value: 2.86e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 699 YDTCLlsSLPEVSKsgtkrPQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEhrqAIKKLDLWRLPEILVIHLKRFSYSR 778
Cdd:cd02667    95 PFLDL--SLPRSDE-----IKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPR 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 779 FMK-NKLEAYVDFPlDNLDLSSYISYKN----GQTTYRYMLYAISNHYGSMGGGHYTAYV--HH---------------- 835
Cdd:cd02667   165 SANlRKVSRHVSFP-EILDLAPFCDPKCnsseDKSSVLYRLYGVVEHSGTMRSGHYVAYVkvRPpqqrlsdltkskpaad 243
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063728716 836 ----GGDRWYDFDDSHVHQISQEKIKTSAAYVLFY 866
Cdd:cd02667   244 eagpGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
279-455 1.36e-25

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 108.13  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 279 TGLQNLGNTCFMNSSLQCLAHTPKLVDFFL-GEYSKEINLDNPLGMKgeialAFGDLLRSLWAPGASTVAPRTFKAKLAR 357
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLsREHSKDCCNEGFCMMC-----ALEAHVERALASSGPGSAPRIFSSNLKQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 358 FAPQFSGFNQHDSQELLAFLLDGLHED-LNRVKNkpyveakdgdgrpdaevadEYWRNHVARNDSIIVDVCQGQYKSTLV 436
Cdd:cd02661    77 ISKHFRIGRQEDAHEFLRYLLDAMQKAcLDRFKK-------------------LKAVDPSSQETTLVQQIFGGYLRSQVK 137
                         170
                  ....*....|....*....
gi 1063728716 437 CPICKKVSVMFDPFMYLSL 455
Cdd:cd02661   138 CLNCKHVSNTYDPFLDLSL 156
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-458 1.78e-24

A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 102.75  E-value: 1.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHtpklvdfflgeyskeinldnplgmkgeialafgdllrslwapgastvaprtfkaklarfa 359
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 360 pqfsgfNQHDSQELLAFLLDGLHedlnrvknkpyveakdgdgrpdaevadeywrnhvarndSIIVDVCQGQYKSTLVCPI 439
Cdd:cd02674    21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
                         170
                  ....*....|....*....
gi 1063728716 440 CKKVSVMFDPFMYLSLPLP 458
Cdd:cd02674    57 CGKTSTTFEPFTYLSLPIP 75
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
723-868 2.66e-22

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 98.87  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 723 SLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYS--RFMKNKLEAYVDFPLDnLDLSSY 800
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLE-LDMEPY 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 801 I----------SYKNGQTTYRYMLYAISNHYGSMGGGHYTAYVH-HGGDRWYDFDDSHV-----HQISQE---------- 854
Cdd:cd02659   231 TekglakkegdSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKdRDDGKWYKFNDDVVtpfdpNDAEEEcfggeetqkt 310
                         170       180
                  ....*....|....*....|.
gi 1063728716 855 -------KIKTSAAYVLFYKR 868
Cdd:cd02659   311 ydsgpraFKRTTNAYMLFYER 331
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
719-867 2.29e-21

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 95.95  E-value: 2.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 719 QESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSR--FMKNKLEAYVDFPLDnLD 796
Cdd:cd02668   153 KGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRktGAKKKLNASISFPEI-LD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 797 LSSYISYKNGQtTYRYMLYAISNHYG-SMGGGHYTAYVHHG-GDRWYDFDDSHVHQISQEKIK----------------- 857
Cdd:cd02668   232 MGEYLAESDEG-SYVYELSGVLIHQGvSAYSGHYIAHIKDEqTGEWYKFNDEDVEEMPGKPLKlgnsedpakprkseikk 310
                         170
                  ....*....|....
gi 1063728716 858 ----TSAAYVLFYK 867
Cdd:cd02668   311 gthsSRTAYMLVYK 324
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-474 2.80e-21

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 95.90  E-value: 2.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHTPKLVDFFLGEyskeiNLDNPLGMKGE---IALAFGDLLRSLWAPGASTvaPRTFKAKLA 356
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSD-----RHSCTCLSCSPnscLSCAMDEIFQEFYYSGDRS--PYGPINLLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 357 RF---APQFSGFNQHDSQELLAFLLDGLHEDLNRVKNKPyveakdgdgrpdaevadeywrNHVARNDSIIVDVCQGQYKS 433
Cdd:cd02660    75 LSwkhSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQS 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063728716 434 TLVCPICKKVSVMFDPFMYLSLPLPCTSMRTMDLTVMSADG 474
Cdd:cd02660   134 SVTCQRCGGVSTTVDPFLDLSLDIPNKSTPSWALGESGVSG 174
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
280-468 5.09e-20

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: 90.62  E-value: 5.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHtpklvdfflgeyskeinldnplgmkgeialafgdllrslwapgastvaprtfkaklarfa 359
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 360 pqfsgfNQHDSQELLAFLLDGLHEDLNRVKNKpyveakdgdgrpdaevadeywRNHVARNDSIIVDVCQGQYKSTLVCPI 439
Cdd:cd02257    21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
                         170       180
                  ....*....|....*....|....*....
gi 1063728716 440 CKKVSVMFDPFMYLSLPLPCTSMRTMDLT 468
Cdd:cd02257    74 CGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-456 3.77e-19

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 88.60  E-value: 3.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHTPKLVDFFLGEyskeinldnplgmkgeialafgdllrslwapgastvaPRTFKAKLARFA 359
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------------------------------------PKELFSQVCRKA 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 360 PQFSGFNQHDSQELLAFLLDGLhedlnrvknkpyveakdgdgrpdaevadeywRNHVarnDSIIVdvcqGQYKSTLVCPI 439
Cdd:cd02667    44 PQFKGYQQQDSHELLRYLLDGL-------------------------------RTFI---DSIFG----GELTSTIMCES 85
                         170
                  ....*....|....*..
gi 1063728716 440 CKKVSVMFDPFMYLSLP 456
Cdd:cd02667    86 CGTVSLVYEPFLDLSLP 102
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
704-867 4.50e-17

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 83.40  E-value: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 704 LSSLPEVSKSGTKRPQESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKN- 782
Cdd:cd02671   162 LSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDc 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 783 -----KLEAYVDFPldnLDLSSYiSYKNGQTTYRYMLYAISNHYG-SMGGGHYTAYVhhggdRWYDFDDSHV-------- 848
Cdd:cd02671   242 ygglsKVNTPLLTP---LKLSLE-EWSTKPKNDVYRLFAVVMHSGaTISSGHYTAYV-----RWLLFDDSEVkvteekdf 312
                         170       180
                  ....*....|....*....|
gi 1063728716 849 -HQISQEKIKTSAAYVLFYK 867
Cdd:cd02671   313 lEALSPNTSSTSTPYLLFYK 332
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
719-867 6.20e-17

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 82.36  E-value: 6.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 719 QESVSLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYS-RFMKN-KLEAYVDFPLD-NL 795
Cdd:cd02663   144 EQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDeQLNRYiKLFYRVVFPLElRL 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 796 DLSSYISYKNGQTtyrYMLYAISNHYGsmGG---GHYTAYVHHGGdRWYDFDDSHVHQISQEKI-------KTSA-AYVL 864
Cdd:cd02663   224 FNTTDDAENPDRL---YELVAVVVHIG--GGpnhGHYVSIVKSHG-GWLLFDDETVEKIDENAVeeffgdsPNQAtAYVL 297

                  ...
gi 1063728716 865 FYK 867
Cdd:cd02663   298 FYQ 300
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
762-867 1.29e-13

A subfamily of Peptidase C19. 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: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 72.75  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 762 RLPEILVIHLKRFSYSRFM--KNKLEAYVDFPLdNLDLSSYISykngqTTYRYMLYAISNHYG-SMGGGHYTAYVHH-GG 837
Cdd:cd02657   195 RLPKYLTVQFVRFFWKRDIqkKAKILRKVKFPF-ELDLYELCT-----PSGYYELVAVITHQGrSADSGHYVAWVRRkND 268
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063728716 838 DRWYDFDDSHVHQISQEKIKTSA-------AYVLFYK 867
Cdd:cd02657   269 GKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
701-866 3.81e-13

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 70.09  E-value: 3.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 701 TCLLSSLPEvsksgtKRPQESVSLFKCLEAFLTEEPLgpDDmwycPGCKEHRQAIKkldlwRLPEILVIHLKRFSYSR-- 778
Cdd:cd02662    81 TMLSLPVPN------QSSGSGTTLEHCLDDFLSTEII--DD----YKCDRCQTVIV-----RLPQILCIHLSRSVFDGrg 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 779 -FMKNKleAYVDFPlDNLdlssyisykngqTTYRYMLYAISNHYGSMGGGHYTAYVHH---------------------G 836
Cdd:cd02662   144 tSTKNS--CKVSFP-ERL------------PKVLYRLRAVVVHYGSHSSGHYVCYRRKplfskdkepgsfvrmregpssT 208
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063728716 837 GDRWYDFDDSHVHQISQEKIK-TSAAYVLFY 866
Cdd:cd02662   209 SHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
723-867 2.04e-12

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 69.06  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 723 SLFKCLEAFLTEEPLGPDDMWYCPGCKEHRQAIKKLDLWRLPEILVIHLKRFSYSR--FMKNKLEAYVDFPLDnLDLSSY 800
Cdd:cd02664   135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQktHVREKIMDNVSINEV-LSLPVR 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 801 ISYKNGQTTYR------------------YMLYAISNHYG-SMGGGHYTAYVHH--GGDR-------------------W 840
Cdd:cd02664   214 VESKSSESPLEkkeeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFTYARDqtDADStgqecpepkdaeendesknW 293
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063728716 841 YDFDDSHVHQISQEKIKT-------SAAYVLFYK 867
Cdd:cd02664   294 YLFNDSRVTFSSFESVQNvtsrfpkDTPYILFYE 327
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
677-867 5.77e-12

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 67.73  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 677 KPVNKSKRLNVLARWPVKELDVYDtcllsslpevsKSGTKRPQESVSLFKCLEAFLTEEPLgpDDmwYCPGCKEHRQAIK 756
Cdd:cd02658   144 KKVKYTSELSEILSLPVPKDEATE-----------KEEGELVYEPVPLEDCLKAYFAPETI--ED--FCSTCKEKTTATK 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 757 KLDLWRLPEILVIHLKRFSYSrfmKN----KLEAYVDFPlDNLDlssyisykNGqttyRYMLYAISNHYG-SMGGGHYTA 831
Cdd:cd02658   209 TTGFKTFPDYLVINMKRFQLL---ENwvpkKLDVPIDVP-EELG--------PG----KYELIAFISHKGtSVHSGHYVA 272
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063728716 832 YV---HHGGDRWYDFDDSHVHQISQEKIKTSAAYVLFYK 867
Cdd:cd02658   273 HIkkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-385 9.96e-12

A subfamily of Peptidase C19. 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: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 66.97  E-value: 9.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHTPKLVDfFLGEYSKeiNLDNPLGMKGEIALAFGDLLRSLwAPGASTVAPRTFKAKLARFA 359
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRD-ALKNYNP--ARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLLRMAF 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063728716 360 PQFS------GFNQHDSQELLAFLLDGLHEDL 385
Cdd:cd02657    77 PQFAekqnqgGYAQQDAEECWSQLLSVLSQKL 108
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
277-482 2.40e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 66.96  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 277 GLTGLQNLGNTCFMNSSLQCLAHTPKLVDFFLGEYSKEINLDNplgmKGEIALAFGDLLRSLWAPGA--STVAPRTFKAK 354
Cdd:cd02669   118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDR----KSELVKRLSELIRKIWNPRNfkGHVSPHELLQA 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 355 LARFAPQFSGFN-QHDSQELLAFLLDGLHEDLNRVKnkpyveakdgdgrpdaevadeywrnhvARNDSIIVDVCQG--QY 431
Cdd:cd02669   194 VSKVSKKKFSITeQSDPVEFLSWLLNTLHKDLGGSK---------------------------KPNSSIIHDCFQGkvQI 246
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063728716 432 KST---------------LVCPICKKVSVMfdPFMYLSLPLPctsmrTMDLTVMSADGSSLP-IPLT 482
Cdd:cd02669   247 ETQkikphaeeegskdkfFKDSRVKKTSVS--PFLLLTLDLP-----PPPLFKDGNEENIIPqVPLK 306
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
748-867 3.62e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 66.19  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 748 CKEHRQAIKKLDLWRLPEILVIHLKRFSYSRFMKNKLEAYVDFPLDNLDLSSYIS--YKNGQTTYRYMLYAISNHYGSMG 825
Cdd:cd02669   317 ETELKDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHfdKPSLNLSTKYNLVANIVHEGTPQ 396
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063728716 826 G-GHYTAYV-HHGGDRWYDFDDSHVHQISQEKIKTSAAYVLFYK 867
Cdd:cd02669   397 EdGTWRVQLrHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-458 3.98e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 65.04  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHTPKLVDFFLGEYSK-EINLDNP-LGMKGEIA-LAFGDL------LRSLWAPGAST---VA 347
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKfPSDVVDPaNDLNCQLIkLADGLLsgryskPASLKSENDPYqvgIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 348 PRTFKAKLARFAPQFSGFNQHDSQELLAFLLDglhedlnrvknkpyveakdgdgrpdaEVADEYWRNHVArNDSIIVDVC 427
Cdd:cd02658    81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLID--------------------------KLDRESFKNLGL-NPNDLFKFM 133
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063728716 428 QGQyksTLVCPICKKVSVMFDPFMYLSLPLP 458
Cdd:cd02658   134 IED---RLECLSCKKVKYTSELSEILSLPVP 161
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
280-385 1.88e-09

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 59.82  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLA-HTPKLvDFFLGEYSKE-------INLDNPLgMKGEIALAFgdlLRSLWAPGastvaprtf 351
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKL-DELLDDLSKElkvlknvIRKPEPD-LNQEEALKL---FTALWSSK--------- 66
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063728716 352 KAKLARFAPQFSgfnQHDSQELLAFLLDGLHEDL 385
Cdd:COG5533    67 EHKVGWIPPMGS---QEDAHELLGKLLDELKLDL 97
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-382 1.89e-09

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 60.20  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHTPKLVDFFLGEYSKEINLDNPLgMKGEIALAFGDLLRSlwapGASTVAPRTFKAklARFA 359
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSV-MKKLQLLQAHLMHTQ----RRAEAPPDYFLE--ASRP 73
                          90       100
                  ....*....|....*....|...
gi 1063728716 360 PQFSGFNQHDSQELLAFLLDGLH 382
Cdd:cd02664    74 PWFTPGSQQDCSEYLRYLLDRLH 96
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
763-848 2.84e-09

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 61.04  E-value: 2.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716  763 LPEILVIHLKRFSYS--RFMKNKLEAYVDFPlDNLDLSSYISY---KNGQTTYRYMLYAISNHYGSMGGGHYTAYVHHGG 837
Cdd:COG5077    378 LPPVLHLQLKRFEYDfeRDMMVKINDRYEFP-LEIDLLPFLDRdadKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEK 456
                           90
                   ....*....|..
gi 1063728716  838 D-RWYDFDDSHV 848
Cdd:COG5077    457 DgRWYKFDDTRV 468
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
274-383 4.98e-08

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 55.67  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 274 GTLGLTGLQNLGNTCFMNSSLQCLAHTPklvdfflGEYSKEINLDNPLGMKGEIALAFgDLLRSLWAPGASTVAPRTFKA 353
Cdd:cd02671    20 NLLPFVGLNNLGNTCYLNSVLQVLYFCP-------GFKHGLKHLVSLISSVEQLQSSF-LLNPEKYNDELANQAPRRLLN 91
                          90       100       110
                  ....*....|....*....|....*....|
gi 1063728716 354 KLARFAPQFSGFNQHDSQELLAFLLDGLHE 383
Cdd:cd02671    92 ALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-314 4.48e-07

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 51.98  E-value: 4.48e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHTPKLVDfFLGEYSKE 314
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIE-YLEEFLEQ 34
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
745-866 1.31e-06

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 50.61  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 745 CPGCKeHRQAIKKLDLWRLPEILVIHLKRFsYSRfmknklEAYVDFPLDNLDlssyiSYKNGQTTY-RYMLYAISNHYG- 822
Cdd:cd02673   129 CSSCK-CESAISSERIMTFPECLSINLKRY-KLR------IATSDYLKKNEE-----IMKKYCGTDaKYSLVAVICHLGe 195
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063728716 823 SMGGGHYTAYVH--HGGDRWYDFDDSHVHQISQEKIK---TSAAYVLFY 866
Cdd:cd02673   196 SPYDGHYIAYTKelYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
277-462 1.89e-05

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 47.64  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 277 GLTGLQNLGNTCFMNSSLQCLAHTPKlvdFFLGEYSKEINLDNPlGMKGEIA---LAFGDLLRSLWAPGASTVAPRTFKa 353
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPE---FRNAVYSIPPTEDDD-DNKSVPLalqRLFLFLQLSESPVKTTELTDKTRS- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 354 klarfapqFSG-----FNQHDSQELLAFLLDGLHEDLnrvknkpyveakdgdgrPDAEVADeywrnhvarndsIIVDVCQ 428
Cdd:cd02659    76 --------FGWdslntFEQHDVQEFFRVLFDKLEEKL-----------------KGTGQEG------------LIKNLFG 118
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063728716 429 GQYKSTLVCPICKKVSVMFDPFMYLSLPL-PCTSM 462
Cdd:cd02659   119 GKLVNYIICKECPHESEREEYFLDLQVAVkGKKNL 153
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
280-457 5.16e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 43.18  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 280 GLQNLGNTCFMNSSLQCLAHTPKLVDFFL---------GEYSKEINLDNPLGMKGEIALAFGDLLRSlwapGASTVAPRT 350
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYecnstedaeLKNMPPDKPHEPQTIIDQLQLIFAQLQFG----NRSVVDPSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 351 FKAKLarfapQFSGFNQHDSQELLAFLLDGLHEDLNRVKNKpyveakdgdgrpdaevadeywrnhVARNdsIIVDVCQGQ 430
Cdd:cd02668    77 FVKAL-----GLDTGQQQDAQEFSKLFLSLLEAKLSKSKNP------------------------DLKN--IVQDLFRGE 125
                         170       180
                  ....*....|....*....|....*..
gi 1063728716 431 YKSTLVCPICKKVSVMFDPFMYLSLPL 457
Cdd:cd02668   126 YSYVTQCSKCGRESSLPSKFYELELQL 152
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
277-381 1.64e-03

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 42.16  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716  277 GLTGLQNLGNTCFMNSSLQCLahtpklvdFFLGEYSK---EINLDNPLGmKGEIALAFGDLLRSLWA---PGASTVAPRT 350
Cdd:COG5077    192 GYVGLRNQGATCYMNSLLQSL--------FFIAKFRKdvyGIPTDHPRG-RDSVALALQRLFYNLQTgeePVDTTELTRS 262
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1063728716  351 FKAKlarfapQFSGFNQHDSQELLAFLLDGL 381
Cdd:COG5077    263 FGWD------SDDSFMQHDIQEFNRVLQDNL 287
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
763-866 3.04e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 40.23  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 763 LPEILVIHLKRFSYSRFMKNKLEAYVDFPLDnldlssyISykngQTTYRymLYAISNHYGSMGGGHYTAYVH-HGGDRWY 841
Cdd:cd02665   128 LPPVLTFELSRFEFNQGRPEKIHDKLEFPQI-------IQ----QVPYE--LHAVLVHEGQANAGHYWAYIYkQSRQEWE 194
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063728716 842 DFDDSHVHQISQEKIKTSA--------AYVLFY 866
Cdd:cd02665   195 KYNDISVTESSWEEVERDSfgggrnpsAYCLMY 227
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
759-867 6.44e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze 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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 39.43  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063728716 759 DLWRLPEILVIHLKRFSYSRFMKNKLEAYVDfPLDNLDLSSYISYKNGQTT---------------------YRYMLYAI 817
Cdd:cd02670    94 VFAKAPSCLIICLKRYGKTEGKAQKMFKKIL-IPDEIDIPDFVADDPRACSkcqlecrvcyddkdfsptcgkFKLSLCSA 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063728716 818 SNHYG-SMGGGHYTAYVHHGGDR------------WYDFDDSHVHQISQEKI------KTSAAYVLFYK 867
Cdd:cd02670   173 VCHRGtSLETGHYVAFVRYGSYSltetdneaynaqWVFFDDMADRDGVSNGFnipaarLLEDPYMLFYQ 241
 
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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