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Conserved domains on  [gi|1063706404|ref|NP_001323724|]
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ubiquitin-specific protease 5 [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];
32-917 1.04e-136

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: 428.92  E-value: 1.04e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404  32 EANSKEGDTFYLITQRWWQEWIEYVNQDqpcntndgsslsehcdsPGSSTLKKPSRIDNSDliydssledpsnTSEIIET 111
Cdd:COG5560    38 AESSKQCEYAVIFAYAWYEGMFDRASCD-----------------GGSPGPIVQGPIVDFE------------PESLKKS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 112 LQEGRDYVLLPQEVWNQLRSWYG-GGPTLARRVISSGlSQTELAVEVYPLRLQLLLMPKSDHSAIR---------ISKKE 181
Cdd:COG5560    89 LREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLP-SESAPEVESYPVVFKLHWLFSINGSLINlghdpvphsASSHG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 182 TIRELHRRACEIFDLDSEHVRIWDYYGHQKYSLMNDLDKTLDDANLQMDQDILVEV----LDINGTLSSAHIQSAQENGL 257
Cdd:COG5560   168 TLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLtrleLFEDRSVLLLSKITRNPDWL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 258 VDgdstsiliepsksslaaaggfsssrnafrtgsvevSQSFDNTYSSTgvttrgSTAGLTGLLNLGNTCFMNSAIQCLVH 337
Cdd:COG5560   248 VD-----------------------------------SIVDDHNRSIN------KEAGTCGLRNLGNTCYMNSALQCLMH 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 338 TPEFASYFQED-YHQEINWQNPLGMVGELALAFGDLLRKLWAPGRTPIAPRPFKAKLARFAPQFSGYNQHDSQELLAFLL 416
Cdd:COG5560   287 TWELRDYFLSDeYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 417 DGLHEDLNRVKHKPYINSRDADGRPDEEV---ADEFWKNHIARNDSIIVDVCQGQYKSTLVCPICNKVSVTFDPFMYLSL 493
Cdd:COG5560   367 DGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTL 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 494 PLQFNTTRAITVTVFSCDKTALPstITVNVSKQGRCRDLIQALTNACSLKQSEELKLAEIRNNFIHRLFEDP-LIPLSSI 572
Cdd:COG5560   447 PLPVSMVWKHTIVVFPESGRRQP--LKIELDASSTIRGLKKLVDAEYGKLGCFEIKVMCIYYGGNYNMLEPAdKVLLQDI 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 573 KDDDHLAAYklSKSSENTTLLRLVLRRRDQKAGER---ESTVQLKpcgtpLLSSASCGDALTKGKIHCLVQNMLspfrre 649
Cdd:COG5560   525 PQTDFVYLY--ETNDNGIEVPVVHLRIEKGYKSKRlfgDPFLQLN-----VLIKASIYDKLVKEFEELLVLVEM------ 591
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 650 esvgKKGNSDSSIPERRSARFnnteeEDKVGG-LKKAKKsnssdlGASKLSLQLIDEDNKtiNLPDNeaeamklpssatV 728
Cdd:COG5560   592 ----KKTDVDLVSEQVRLLRE-----ESSPSSwLKLETE------IDTKREEQVEEEGQM--NFNDA------------V 642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 729 TIYLDWtPELSgmyditcLESLPEVLKYGPTTK-KARSEPLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLW 807
Cdd:COG5560   643 VISCEW-EEKR-------YLSLFSYDPLWTIREiGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELW 714
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 808 RLPEVLVIHLKRFSYSRSMKHKLETFVNFPIHDLDLTKYVANKNLSQpQLYELYALTNHYGGMGSGHYTAHIKLLDDSRW 887
Cdd:COG5560   715 RLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPR-LIYDLYAVDNHYGGLSGGHYTAYARNFANNGW 793
                         890       900       910
                  ....*....|....*....|....*....|
gi 1063706404 888 YNFDDSHISHINEDDVKSGAAYVLFYRRKS 917
Cdd:COG5560   794 YLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
32-917 1.04e-136

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 428.92  E-value: 1.04e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404  32 EANSKEGDTFYLITQRWWQEWIEYVNQDqpcntndgsslsehcdsPGSSTLKKPSRIDNSDliydssledpsnTSEIIET 111
Cdd:COG5560    38 AESSKQCEYAVIFAYAWYEGMFDRASCD-----------------GGSPGPIVQGPIVDFE------------PESLKKS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 112 LQEGRDYVLLPQEVWNQLRSWYG-GGPTLARRVISSGlSQTELAVEVYPLRLQLLLMPKSDHSAIR---------ISKKE 181
Cdd:COG5560    89 LREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLP-SESAPEVESYPVVFKLHWLFSINGSLINlghdpvphsASSHG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 182 TIRELHRRACEIFDLDSEHVRIWDYYGHQKYSLMNDLDKTLDDANLQMDQDILVEV----LDINGTLSSAHIQSAQENGL 257
Cdd:COG5560   168 TLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLtrleLFEDRSVLLLSKITRNPDWL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 258 VDgdstsiliepsksslaaaggfsssrnafrtgsvevSQSFDNTYSSTgvttrgSTAGLTGLLNLGNTCFMNSAIQCLVH 337
Cdd:COG5560   248 VD-----------------------------------SIVDDHNRSIN------KEAGTCGLRNLGNTCYMNSALQCLMH 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 338 TPEFASYFQED-YHQEINWQNPLGMVGELALAFGDLLRKLWAPGRTPIAPRPFKAKLARFAPQFSGYNQHDSQELLAFLL 416
Cdd:COG5560   287 TWELRDYFLSDeYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 417 DGLHEDLNRVKHKPYINSRDADGRPDEEV---ADEFWKNHIARNDSIIVDVCQGQYKSTLVCPICNKVSVTFDPFMYLSL 493
Cdd:COG5560   367 DGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTL 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 494 PLQFNTTRAITVTVFSCDKTALPstITVNVSKQGRCRDLIQALTNACSLKQSEELKLAEIRNNFIHRLFEDP-LIPLSSI 572
Cdd:COG5560   447 PLPVSMVWKHTIVVFPESGRRQP--LKIELDASSTIRGLKKLVDAEYGKLGCFEIKVMCIYYGGNYNMLEPAdKVLLQDI 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 573 KDDDHLAAYklSKSSENTTLLRLVLRRRDQKAGER---ESTVQLKpcgtpLLSSASCGDALTKGKIHCLVQNMLspfrre 649
Cdd:COG5560   525 PQTDFVYLY--ETNDNGIEVPVVHLRIEKGYKSKRlfgDPFLQLN-----VLIKASIYDKLVKEFEELLVLVEM------ 591
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 650 esvgKKGNSDSSIPERRSARFnnteeEDKVGG-LKKAKKsnssdlGASKLSLQLIDEDNKtiNLPDNeaeamklpssatV 728
Cdd:COG5560   592 ----KKTDVDLVSEQVRLLRE-----ESSPSSwLKLETE------IDTKREEQVEEEGQM--NFNDA------------V 642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 729 TIYLDWtPELSgmyditcLESLPEVLKYGPTTK-KARSEPLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLW 807
Cdd:COG5560   643 VISCEW-EEKR-------YLSLFSYDPLWTIREiGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELW 714
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 808 RLPEVLVIHLKRFSYSRSMKHKLETFVNFPIHDLDLTKYVANKNLSQpQLYELYALTNHYGGMGSGHYTAHIKLLDDSRW 887
Cdd:COG5560   715 RLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPR-LIYDLYAVDNHYGGLSGGHYTAYARNFANNGW 793
                         890       900       910
                  ....*....|....*....|....*....|
gi 1063706404 888 YNFDDSHISHINEDDVKSGAAYVLFYRRKS 917
Cdd:COG5560   794 YLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-914 1.52e-55

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: 191.73  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 739 SGMYD-ITCLeSLPEVLKYGPTTKkarsepLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHL 817
Cdd:cd02674    61 STTFEpFTYL-SLPIPSGSGDAPK------VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 818 KRFSYSRSMKHKLETFVNFPIHDLDLTKYVANKNLSQPQLYELYALTNHYGGMGSGHYTAHIKLLDDSRWYNFDDSHISH 897
Cdd:cd02674   134 KRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK 213
                         170
                  ....*....|....*..
gi 1063706404 898 INEDDVKSGAAYVLFYR 914
Cdd:cd02674   214 VSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
761-913 3.26e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.04  E-value: 3.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 761 KKARSEPLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSRSMKHKLETFVNFPIhD 840
Cdd:pfam00443 155 DSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPL-E 233
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706404 841 LDLTKYVA---NKNLSQPQLYELYALTNHYGGMGSGHYTAHIKLLDDSRWYNFDDSHISHI-NEDDVKSGAAYVLFY 913
Cdd:pfam00443 234 LDLSRYLAeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVdEETAVLSSSAYILFY 310
DUSP smart00695
Domain in ubiquitin-specific proteases;
34-147 2.30e-27

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 106.29  E-value: 2.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404   34 NSKEGDTFYLITQRWWQEWIEYVNQDQPcntndgsslsehcdspgsstlKKPSRIDNSDLIydssleDPSNTSEIIETLQ 113
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDG---------------------KDPGPIDNSGIL------CSHGGPRLKEHLV 53
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1063706404  114 EGRDYVLLPQEVWNQLRSWYGGGPT-LARRVISSG 147
Cdd:smart00695  54 EGEDYVLIPEELWNKLVRWYGGGPGpIPRKVVCQG 88
 
Name Accession Description Interval E-value
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
32-917 1.04e-136

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 428.92  E-value: 1.04e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404  32 EANSKEGDTFYLITQRWWQEWIEYVNQDqpcntndgsslsehcdsPGSSTLKKPSRIDNSDliydssledpsnTSEIIET 111
Cdd:COG5560    38 AESSKQCEYAVIFAYAWYEGMFDRASCD-----------------GGSPGPIVQGPIVDFE------------PESLKKS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 112 LQEGRDYVLLPQEVWNQLRSWYG-GGPTLARRVISSGlSQTELAVEVYPLRLQLLLMPKSDHSAIR---------ISKKE 181
Cdd:COG5560    89 LREGIDYSIISGAVWQLLVRWYGlAGLITPRITVLLP-SESAPEVESYPVVFKLHWLFSINGSLINlghdpvphsASSHG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 182 TIRELHRRACEIFDLDSEHVRIWDYYGHQKYSLMNDLDKTLDDANLQMDQDILVEV----LDINGTLSSAHIQSAQENGL 257
Cdd:COG5560   168 TLRDLSERVMNAFVDPSDDFRLWDVVPEIMGLRLGLDSFFRRYRVLASDGRVLHPLtrleLFEDRSVLLLSKITRNPDWL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 258 VDgdstsiliepsksslaaaggfsssrnafrtgsvevSQSFDNTYSSTgvttrgSTAGLTGLLNLGNTCFMNSAIQCLVH 337
Cdd:COG5560   248 VD-----------------------------------SIVDDHNRSIN------KEAGTCGLRNLGNTCYMNSALQCLMH 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 338 TPEFASYFQED-YHQEINWQNPLGMVGELALAFGDLLRKLWAPGRTPIAPRPFKAKLARFAPQFSGYNQHDSQELLAFLL 416
Cdd:COG5560   287 TWELRDYFLSDeYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNEEFSGYDQQDSQEFIAFLL 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 417 DGLHEDLNRVKHKPYINSRDADGRPDEEV---ADEFWKNHIARNDSIIVDVCQGQYKSTLVCPICNKVSVTFDPFMYLSL 493
Cdd:COG5560   367 DGLHEDLNRIIKKPYTSKPDLSPGDDVVVkkkAKECWWEHLKRNDSIITDLFQGMYKSTLTCPGCGSVSITFDPFMDLTL 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 494 PLQFNTTRAITVTVFSCDKTALPstITVNVSKQGRCRDLIQALTNACSLKQSEELKLAEIRNNFIHRLFEDP-LIPLSSI 572
Cdd:COG5560   447 PLPVSMVWKHTIVVFPESGRRQP--LKIELDASSTIRGLKKLVDAEYGKLGCFEIKVMCIYYGGNYNMLEPAdKVLLQDI 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 573 KDDDHLAAYklSKSSENTTLLRLVLRRRDQKAGER---ESTVQLKpcgtpLLSSASCGDALTKGKIHCLVQNMLspfrre 649
Cdd:COG5560   525 PQTDFVYLY--ETNDNGIEVPVVHLRIEKGYKSKRlfgDPFLQLN-----VLIKASIYDKLVKEFEELLVLVEM------ 591
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 650 esvgKKGNSDSSIPERRSARFnnteeEDKVGG-LKKAKKsnssdlGASKLSLQLIDEDNKtiNLPDNeaeamklpssatV 728
Cdd:COG5560   592 ----KKTDVDLVSEQVRLLRE-----ESSPSSwLKLETE------IDTKREEQVEEEGQM--NFNDA------------V 642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 729 TIYLDWtPELSgmyditcLESLPEVLKYGPTTK-KARSEPLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLW 807
Cdd:COG5560   643 VISCEW-EEKR-------YLSLFSYDPLWTIREiGAAERTITLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELW 714
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 808 RLPEVLVIHLKRFSYSRSMKHKLETFVNFPIHDLDLTKYVANKNLSQpQLYELYALTNHYGGMGSGHYTAHIKLLDDSRW 887
Cdd:COG5560   715 RLPMILIIHLKRFSSVRSFRDKIDDLVEYPIDDLDLSGVEYMVDDPR-LIYDLYAVDNHYGGLSGGHYTAYARNFANNGW 793
                         890       900       910
                  ....*....|....*....|....*....|
gi 1063706404 888 YNFDDSHISHINEDDVKSGAAYVLFYRRKS 917
Cdd:COG5560   794 YLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
739-914 1.52e-55

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: 191.73  E-value: 1.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 739 SGMYD-ITCLeSLPEVLKYGPTTKkarsepLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHL 817
Cdd:cd02674    61 STTFEpFTYL-SLPIPSGSGDAPK------VTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 818 KRFSYSRSMKHKLETFVNFPIHDLDLTKYVANKNLSQPQLYELYALTNHYGGMGSGHYTAHIKLLDDSRWYNFDDSHISH 897
Cdd:cd02674   134 KRFSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK 213
                         170
                  ....*....|....*..
gi 1063706404 898 INEDDVKSGAAYVLFYR 914
Cdd:cd02674   214 VSESSVVSSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
761-913 3.26e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 188.04  E-value: 3.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 761 KKARSEPLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSRSMKHKLETFVNFPIhD 840
Cdd:pfam00443 155 DSAELKTASLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNRSTWEKLNTEVEFPL-E 233
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706404 841 LDLTKYVA---NKNLSQPQLYELYALTNHYGGMGSGHYTAHIKLLDDSRWYNFDDSHISHI-NEDDVKSGAAYVLFY 913
Cdd:pfam00443 234 LDLSRYLAeelKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVdEETAVLSSSAYILFY 310
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
317-510 2.61e-52

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 185.72  E-value: 2.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 317 TGLLNLGNTCFMNSAIQCLVHTPEFASYFQEDYHqeINWQNPLGMVGELALAFGDLLRKLWAPGR-TPIAPRPFKAKLAR 395
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISP--LSEDSRYNKDINLLCALRDLFKALQKNSKsSSVSPKMFKKSLGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 396 FAPQFSGYNQHDSQELLAFLLDGLHEDLNRvkhkpyinsrdadgrpdeevadefwkNHIARNDSIIVDVCQGQYKSTLVC 475
Cdd:pfam00443  79 LNPDFSGYKQQDAQEFLLFLLDGLHEDLNG--------------------------NHSTENESLITDLFRGQLKSRLKC 132
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063706404 476 PICNKVSVTFDPFMYLSLPLQFNTTRAITVTVFSC 510
Cdd:pfam00443 133 LSCGEVSETFEPFSDLSLPIPGDSAELKTASLQIC 167
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
766-914 1.76e-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: 144.16  E-value: 1.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 766 EPLSLYACLEAFLREEPLVPDEMWFCPqCNERRQASKKLDLWRLPEVLVIHLKRFSYSRSM-KHKLETFVNFPIhDLDLT 844
Cdd:cd02257    97 PQVSLEDCLEKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNEDGtKEKLNTKVSFPL-ELDLS 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 845 KYVANKNLSQ-----PQLYELYALTNHYGGMG-SGHYTAHIKLLDDSRWYNFDDSHISHINEDDV-----KSGAAYVLFY 913
Cdd:cd02257   175 PYLSEGEKDSdsdngSYKYELVAVVVHSGTSAdSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVlefgsLSSSAYILFY 254

                  .
gi 1063706404 914 R 914
Cdd:cd02257   255 E 255
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
769-913 3.74e-34

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: 133.17  E-value: 3.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 769 SLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSRSmkHKLETFVNFPIHdLDLTKYVA 848
Cdd:cd02661   163 SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRG--GKINKQISFPET-LDLSPYMS 239
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706404 849 NKNlSQPQLYELYALTNHYGG-MGSGHYTAHIKlLDDSRWYNFDDSHISHINEDDVKSGAAYVLFY 913
Cdd:cd02661   240 QPN-DGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQKAYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
741-913 5.45e-33

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: 130.57  E-value: 5.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 741 MYDITcLESLPEVLKYGPTTKKARSEPLSLYACLEAFLREEPLVPDEmWFCPQCNERRQASKKLDLWRLPEVLVIHLKRF 820
Cdd:cd02660   150 FLDLS-LDIPNKSTPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSIKKLPPVLCFQLKRF 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 821 SYS-RSMKHKLETFVNFPIHdLDLTKYVAN-------KNLSQPQL-YELYALTNHYGGMGSGHYTAHIKLLDDSrWYNFD 891
Cdd:cd02660   228 EHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdSNSLDPDYtYDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFD 305
                         170       180
                  ....*....|....*....|..
gi 1063706404 892 DSHISHINEDDVKSGAAYVLFY 913
Cdd:cd02660   306 DAMITRVSEEEVLKSQAYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
769-918 1.02e-27

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: 115.05  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 769 SLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYS--RSMKHKLETFVNFPIHdLDLTKY 846
Cdd:cd02659   152 NLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDfeTMMRIKINDRFEFPLE-LDMEPY 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 847 V----------ANKNLSQPQLYELYALTNHYGGMGSGHYTAHIKLLDDSRWYNFDDSHISHINEDDV------------- 903
Cdd:cd02659   231 TekglakkegdSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAeeecfggeetqkt 310
                         170       180
                  ....*....|....*....|....
gi 1063706404 904 ---------KSGAAYVLFYRRKSD 918
Cdd:cd02659   311 ydsgprafkRTTNAYMLFYERKSP 334
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
317-493 1.76e-27

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: 113.52  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 317 TGLLNLGNTCFMNSAIQCLVHTPEFASYFQ-EDYHQEINWQNPLGMVgelalAFGDLLRKLWAPGRTPIAPRPFKAKLAR 395
Cdd:cd02661     2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLsREHSKDCCNEGFCMMC-----ALEAHVERALASSGPGSAPRIFSSNLKQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 396 FAPQFSGYNQHDSQELLAFLLDGLHedlnRVKHKPYINSRDADgrpdeevadefwknHIARNDSIIVDVCQGQYKSTLVC 475
Cdd:cd02661    77 ISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVD--------------PSSQETTLVQQIFGGYLRSQVKC 138
                         170
                  ....*....|....*...
gi 1063706404 476 PICNKVSVTFDPFMYLSL 493
Cdd:cd02661   139 LNCKHVSNTYDPFLDLSL 156
DUSP smart00695
Domain in ubiquitin-specific proteases;
34-147 2.30e-27

Domain in ubiquitin-specific proteases;


Pssm-ID: 197831  Cd Length: 88  Bit Score: 106.29  E-value: 2.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404   34 NSKEGDTFYLITQRWWQEWIEYVNQDQPcntndgsslsehcdspgsstlKKPSRIDNSDLIydssleDPSNTSEIIETLQ 113
Cdd:smart00695   1 PLEEGLTWYLISTRWYRQWADFVEGKDG---------------------KDPGPIDNSGIL------CSHGGPRLKEHLV 53
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1063706404  114 EGRDYVLLPQEVWNQLRSWYGGGPT-LARRVISSG 147
Cdd:smart00695  54 EGEDYVLIPEELWNKLVRWYGGGPGpIPRKVVCQG 88
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
768-914 5.11e-27

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: 112.90  E-value: 5.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 768 LSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSR-SM-KHKLETFVNFPiHDLDLTK 845
Cdd:cd02668   156 KTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRkTGaKKKLNASISFP-EILDMGE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 846 YVANKNLsQPQLYELYALTNHYG-GMGSGHYTAHIKLLDDSRWYNFDDSHISHI---------NEDDVK----------- 904
Cdd:cd02668   235 YLAESDE-GSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMpgkplklgnSEDPAKprkseikkgth 313
                         170
                  ....*....|.
gi 1063706404 905 -SGAAYVLFYR 914
Cdd:cd02668   314 sSRTAYMLVYK 324
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-510 5.40e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 104.29  E-value: 5.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHtpefasyfqedyhqeinwqnplgmvgelalafgdllrklwapgrtpiaprpfkaklarfa 397
Cdd:cd02674     1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 398 pqfsgyNQHDSQELLAFLLDGLHedlnrvkhkpyinsrdadgrpdeevadefwknhiarndSIIVDVCQGQYKSTLVCPI 477
Cdd:cd02674    21 ------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCLT 56
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1063706404 478 CNKVSVTFDPFMYLSLPLQFNTTRAITVTVFSC 510
Cdd:cd02674    57 CGKTSTTFEPFTYLSLPIPSGSGDAPKVTLEDC 89
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
765-914 2.03e-23

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: 101.31  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 765 SEPLSLYACLEAFLREEPLVPDEMWFCPQCNErrqASKKLDLWRLPEVLVIHLKRFSYSRSMK-HKLETFVNFPiHDLDL 843
Cdd:cd02667   108 KSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFQQPRSANlRKVSRHVSFP-EILDL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 844 TKYV-ANKNLSQPQ---LYELYALTNHYGGMGSGHYTAHIKL---------------------LDDSRWYNFDDSHISHI 898
Cdd:cd02667   184 APFCdPKCNSSEDKssvLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREV 263
                         170
                  ....*....|....*.
gi 1063706404 899 NEDDVKSGAAYVLFYR 914
Cdd:cd02667   264 SLEEVLKSEAYLLFYE 279
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-501 2.51e-23

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: 102.07  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHTPEFASYFQEDYHQeinwQNPLGMVGE--LALAFGDLLRKLWAPG-RTPIAPRPFKAKLA 394
Cdd:cd02660     2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHS----CTCLSCSPNscLSCAMDEIFQEFYYSGdRSPYGPINLLYLSW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 395 RFAPQFSGYNQHDSQELLAFLLDGLHEDLNRVKHKPyinsrdadgrpdeevadefwkNHIARNDSIIVDVCQGQYKSTLV 474
Cdd:cd02660    78 KHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEA---------------------NDESHCNCIIHQTFSGSLQSSVT 136
                         170       180
                  ....*....|....*....|....*..
gi 1063706404 475 CPICNKVSVTFDPFMYLSLPLQFNTTR 501
Cdd:cd02660   137 CQRCGGVSTTVDPFLDLSLDIPNKSTP 163
DUSP pfam06337
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ...
38-144 3.43e-21

DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet.


Pssm-ID: 399383  Cd Length: 80  Bit Score: 88.19  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404  38 GDTFYLITQRWWQEWIEYVNQDQPcntndgsslsehcdspgsstlkKPSRIDNSDLIydssleDPSNTSEIIETLQEGRD 117
Cdd:pfam06337   1 GDKVYLISSKWLNKWKSYVKEPNN----------------------EPGPIDNSDLL------DDESNGQLKPNLQEGVD 52
                          90       100
                  ....*....|....*....|....*..
gi 1063706404 118 YVLLPQEVWNQLRSWYGGGPTLARRVI 144
Cdd:pfam06337  53 YVIVPEEVWEFLVEWYGGGPEIKRNVV 79
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
769-913 7.64e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 93.91  E-value: 7.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 769 SLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSRSMKH--KLETFVNFPihdLDLTKY 846
Cdd:cd02663   148 SITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRyiKLFYRVVFP---LELRLF 224
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706404 847 VANKNLSQP-QLYELYALTNHYG-GMGSGHYTAHIKLldDSRWYNFDDSHISHINEDDVK--------SGAAYVLFY 913
Cdd:cd02663   225 NTTDDAENPdRLYELVAVVVHIGgGPNHGHYVSIVKS--HGGWLLFDDETVEKIDENAVEeffgdspnQATAYVLFY 299
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
318-506 4.24e-19

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: 87.92  E-value: 4.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHtpefasyfqedyhqeinwqnplgmvgelalafgdllrklwapgrtpiaprpfkaklarfa 397
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 398 pqfsgyNQHDSQELLAFLLDGLHEDLNRVKHKpyinsrdadgrpdeevadefwKNHIARNDSIIVDVCQGQYKSTLVCPI 477
Cdd:cd02257    21 ------EQQDAHEFLLFLLDKLHEELKKSSKR---------------------TSDSSSLKSLIHDLFGGKLESTIVCLE 73
                         170       180
                  ....*....|....*....|....*....
gi 1063706404 478 CNKVSVTFDPFMYLSLPLQFNTTRAITVT 506
Cdd:cd02257    74 CGHESVSTEPELFLSLPLPVKGLPQVSLE 102
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-494 1.10e-18

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: 87.44  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHTPEFASYFQEDyhqeinwqnplgmvgelalafgdllrklwapgrtpiaPRPFKAKLARFA 397
Cdd:cd02667     1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------------------------------------PKELFSQVCRKA 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 398 PQFSGYNQHDSQELLAFLLDGLhedlnrvkhKPYInsrdadgrpdeevadefwknhiarnDSIIVdvcqGQYKSTLVCPI 477
Cdd:cd02667    44 PQFKGYQQQDSHELLRYLLDGL---------RTFI-------------------------DSIFG----GELTSTIMCES 85
                         170
                  ....*....|....*..
gi 1063706404 478 CNKVSVTFDPFMYLSLP 494
Cdd:cd02667    86 CGTVSLVYEPFLDLSLP 102
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
718-916 5.73e-16

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 79.46  E-value: 5.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 718 EAMKLPSSATVTIYLDWTpelSGMYDITCLESLPEVLKYGPTTKKARSEPlSLYACLEAFlreEPLVPDEMWFCPQCNER 797
Cdd:COG5533    91 DELKLDLVNSFTIRIFKT---TKDKKKTSTGDWFDIIIELPDQTWVNNLK-TLQEFIDNM---EELVDDETGVKAKENEE 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 798 RQASKKLDLW----RLPEVLVIHLKRFSYSRSmKHKLETFVNFPIHdldLT-KYVANKNLSQPQLYELYALTNHYGGMGS 872
Cdd:COG5533   164 LEVQAKQEYEvsfvKLPKILTIQLKRFANLGG-NQKIDTEVDEKFE---LPvKHDQILNIVKETYYDLVGFVLHQGSLEG 239
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063706404 873 GHYTAHIKLLDDsrWYNFDDSHISHINED---DVKSGAAYVLFYRRK 916
Cdd:COG5533   240 GHYIAYVKKGGK--WEKANDSDVTPVSEEeaiNEKAKNAYLYFYERI 284
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-496 3.06e-15

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: 77.75  E-value: 3.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHTPEFASYFQEDY-HQEINWQNP-LGMVGELA-LAFGDLLRKLWAPGRTP---------IA 385
Cdd:cd02658     1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLEnKFPSDVVDPaNDLNCQLIkLADGLLSGRYSKPASLKsendpyqvgIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 386 PRPFKAKLARFAPQFSGYNQHDSQELLAFLLDglhedlnrvkhkpyinsrdadgrpdeEVADEFWKNHIArNDSIIVDVC 465
Cdd:cd02658    81 PSMFKALIGKGHPEFSTMRQQDALEFLLHLID--------------------------KLDRESFKNLGL-NPNDLFKFM 133
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063706404 466 QGQyksTLVCPICNKVSVTFDPFMYLSLPLQ 496
Cdd:cd02658   134 IED---RLECLSCKKVKYTSELSEILSLPVP 161
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
808-914 9.98e-15

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: 75.83  E-value: 9.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 808 RLPEVLVIHLKRFSYSRSMKHKLETF--VNFPIhDLDLTKYvanknLSQPQLYELYALTNHYG-GMGSGHYTAHIKLLDD 884
Cdd:cd02657   195 RLPKYLTVQFVRFFWKRDIQKKAKILrkVKFPF-ELDLYEL-----CTPSGYYELVAVITHQGrSADSGHYVAWVRRKND 268
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063706404 885 SRWYNFDDSHISHINEDDVKSGA-------AYVLFYR 914
Cdd:cd02657   269 GKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLYK 305
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
774-914 3.86e-14

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: 74.45  E-value: 3.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 774 LEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSR-SMKH-KLETFVNFPIhDLDLTKYVANKN 851
Cdd:cd02664   140 LNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQkTHVReKIMDNVSINE-VLSLPVRVESKS 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 852 LSQPQ------------------LYELYALTNHYG-GMGSGHY-------------------TAHIKLLDDSR-WYNFDD 892
Cdd:cd02664   219 SESPLekkeeesgddgelvtrqvHYRLYAVVVHSGySSESGHYftyardqtdadstgqecpePKDAEENDESKnWYLFND 298
                         170       180
                  ....*....|....*....|....*....
gi 1063706404 893 SHISHINEDDVK-------SGAAYVLFYR 914
Cdd:cd02664   299 SRVTFSSFESVQnvtsrfpKDTPYILFYE 327
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
738-913 9.10e-14

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: 72.01  E-value: 9.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 738 LSGMYDITCLESLPevlkyGPttKKARSEPLSLYACLEAFLREEPLvpdEMWFCPQCnerrqaskKLDLWRLPEVLVIHL 817
Cdd:cd02662    73 SKVRYESFTMLSLP-----VP--NQSSGSGTTLEHCLDDFLSTEII---DDYKCDRC--------QTVIVRLPQILCIHL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 818 KRFSYS-RSMKHKLETFVNFPihdLDLTKYvanknlsqpqLYELYALTNHYGGMGSGHYTAH------------------ 878
Cdd:cd02662   135 SRSVFDgRGTSTKNSCKVSFP---ERLPKV----------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrm 201
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063706404 879 --IKLLDDSRWYNFDDSHISHINEDDVK-SGAAYVLFY 913
Cdd:cd02662   202 reGPSSTSHPWWRISDTTVKEVSESEVLeQKSAYMLFY 239
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
735-914 9.84e-14

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: 73.39  E-value: 9.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 735 TPELSGMYDITC--LES-LPEVLKYGPTTKKARSEPLSLYACLEAFLREEPLVPDEMWFCPQCNERRQASKKLDLWRLPE 811
Cdd:cd02671   144 TERREDFQDISVpvQESeLSKSEESSEISPDPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 812 VLVIHLKRFSYSRSMKH------KLETFVNFPIhDLDLTKYVANKNLsqpQLYELYALTNHYGG-MGSGHYTAHIklldd 884
Cdd:cd02671   224 VITIHLKCFAANGSEFDcygglsKVNTPLLTPL-KLSLEEWSTKPKN---DVYRLFAVVMHSGAtISSGHYTAYV----- 294
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063706404 885 sRWYNFDDSHISHINEDDVK---------SGAAYVLFYR 914
Cdd:cd02671   295 -RWLLFDDSEVKVTEEKDFLealspntssTSTPYLLFYK 332
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
766-914 4.28e-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: 68.12  E-value: 4.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 766 EPLSLYACLEAFLREEPlVPDemwFCPQCNERRQASKKLDLWRLPEVLVIHLKRFSYSR-SMKHKLETFVNFPihdldlt 844
Cdd:cd02658   176 EPVPLEDCLKAYFAPET-IED---FCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLLEnWVPKKLDVPIDVP------- 244
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706404 845 kyvankNLSQPQLYELYALTNHyggMG----SGHYTAHIKLLDD--SRWYNFDDSHISHINEDDVKSGAAYVLFYR 914
Cdd:cd02658   245 ------EELGPGKYELIAFISH---KGtsvhSGHYVAHIKKEIDgeGKWVLFNDEKVVASQDPPEMKKLGYIYFYQ 311
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-423 4.72e-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: 68.13  E-value: 4.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHTPEFASYF-QEDYHQEINWQNPLGMVGELALAFGDLLRKlwapgRTPIAPRPFKAKLARF 396
Cdd:cd02657     1 GLTNLGNTCYLNSTLQCLRSVPELRDALkNYNPARRGANQSSDNLTNALRDLFDTMDKK-----QEPVPPIEFLQLLRMA 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063706404 397 APQFS------GYNQHDSQELLAFLLDGLHEDL 423
Cdd:cd02657    76 FPQFAekqnqgGYAQQDAEECWSQLLSVLSQKL 108
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
809-919 1.20e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 65.66  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404  809 LPEVLVIHLKRFSYS--RSMKHKLETFVNFPIhDLDLTKYV---ANKNLSQPQLYELYALTNHYGGMGSGHYTAHIKLLD 883
Cdd:COG5077    378 LPPVLHLQLKRFEYDfeRDMMVKINDRYEFPL-EIDLLPFLdrdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEK 456
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063706404  884 DSRWYNFDDSHIS---------------HINEDDVKSG-------AAYVLFYRRKSDA 919
Cdd:COG5077    457 DGRWYKFDDTRVTratekevleenfggdHPYKDKIRDHsgikrfmSAYMLVYLRKSML 514
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
801-914 3.02e-10

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: 63.49  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 801 SKKLDLWRLPEVLVIHLKRFSYSRSMKHKLETFVNFPIHDLDLTKYVANKNLSQPQL--YELYALTNHYGGMG-SGHYTA 877
Cdd:cd02669   324 LKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNLStkYNLVANIVHEGTPQeDGTWRV 403
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063706404 878 HIklLDDSR--WYNFDDSHISHINEDDVKSGAAYVLFYR 914
Cdd:cd02669   404 QL--RHKSTnkWFEIQDLNVKEVLPQLIFLSESYIQIWE 440
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-420 1.12e-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: 60.97  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHTPEFASYFQEDYHQEINWQNPLGMVGELALAFgdllrklWAPGRTPIAPRPFKAKLARFA 397
Cdd:cd02664     1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAH-------LMHTQRRAEAPPDYFLEASRP 73
                          90       100
                  ....*....|....*....|...
gi 1063706404 398 PQFSGYNQHDSQELLAFLLDGLH 420
Cdd:cd02664    74 PWFTPGSQQDCSEYLRYLLDRLH 96
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
315-495 1.71e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 57.71  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 315 GLTGLLNLGNTCFMNSAIQCLVHTPEFASYF--QEDYHQEINWQnplgmvGELALAFGDLLRKLWapgrtpiAPRPFKAK 392
Cdd:cd02669   118 GFVGLNNIKNNDYANVIIQALSHVKPIRNFFllYENYENIKDRK------SELVKRLSELIRKIW-------NPRNFKGH 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 393 LA----------RFAPQFSGYNQHDSQELLAFLLDGLHEDLNRVKhkpyinsrdadgrpdeevadefwknhiARNDSIIV 462
Cdd:cd02669   185 VSphellqavskVSKKKFSITEQSDPVEFLSWLLNTLHKDLGGSK---------------------------KPNSSIIH 237
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1063706404 463 DVCQG--QYKSTLVCPICNK-------------VSVTFDPFMYLSLPL 495
Cdd:cd02669   238 DCFQGkvQIETQKIKPHAEEegskdkffkdsrvKKTSVSPFLLLTLDL 285
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
303-421 3.01e-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: 56.44  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 303 SSTGVTTRGSTAGLTGLLNLGNTCFMNSAIQCLvhtpEFASYFQEDYHQEINWqnpLGMVGELALAFgDLLRKLWAPGRT 382
Cdd:cd02671    11 SATSCEKRENLLPFVGLNNLGNTCYLNSVLQVL----YFCPGFKHGLKHLVSL---ISSVEQLQSSF-LLNPEKYNDELA 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063706404 383 PIAPRPFKAKLARFAPQFSGYNQHDSQELLAFLLDGLHE 421
Cdd:cd02671    83 NQAPRRLLNALREVNPMYEGYLQHDAQEVLQCILGNIQE 121
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-513 9.28e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 54.62  E-value: 9.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHtpEFASYFQEDYHQEINWQNPLGMVgelalafgdllrklwapgrtpIAPRPFKAKLARFA 397
Cdd:cd02663     1 GLENFGNTCYCNSVLQALYF--ENLLTCLKDLFESISEQKKRTGV---------------------ISPKKFITRLKREN 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 398 PQFSGYNQHDSQELLAFLLDGLHEDLNRVKHKpyinsrdadgRPDEEVADEFWKNHIARNdsIIVDVCQGQYKSTLVCPI 477
Cdd:cd02663    58 ELFDNYMHQDAHEFLNFLLNEIAEILDAERKA----------EKANRKLNNNNNAEPQPT--WVHEIFQGILTNETRCLT 125
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1063706404 478 CNKVSVTFDPFMYLSLPLQFNTTRAITVTVFSCDKT 513
Cdd:cd02663   126 CETVSSRDETFLDLSIDVEQNTSITSCLRQFSATET 161
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
318-423 2.41e-07

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 53.27  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLV-HTPEFASYFQEDYH------QEINWQNPLgMVGELALAFgdlLRKLWAPGRTpiaprpfk 390
Cdd:COG5533     1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKelkvlkNVIRKPEPD-LNQEEALKL---FTALWSSKEH-------- 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063706404 391 aKLARFAPQfsgYNQHDSQELLAFLLDGLHEDL 423
Cdd:COG5533    69 -KVGWIPPM---GSQEDAHELLGKLLDELKLDL 97
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
315-434 1.17e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 51.49  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 315 GLTGLLNLGNTCFMNSAIQCLVHTPEF--ASYFQEDYHQEINWQN-PLGM--------VGELALAFGDLLRKLWAPGRTP 383
Cdd:cd02659     1 GYVGLKNQGATCYMNSLLQQLYMTPEFrnAVYSIPPTEDDDDNKSvPLALqrlflflqLSESPVKTTELTDKTRSFGWDS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063706404 384 IAPRpfkaklarfapqfsgyNQHDSQELLAFLLDGLHEDLNRVKHKPYINS 434
Cdd:cd02659    81 LNTF----------------EQHDVQEFFRVLFDKLEEKLKGTGQEGLIKN 115
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-500 1.23e-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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 51.65  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHTPEFASYF---------QEDYHQEINWQNPLGMVGELALAFgdllRKLWAPGRTPIAPRP 388
Cdd:cd02668     1 GLKNLGATCYVNSFLQLWFMNLEFRKAVyecnstedaELKNMPPDKPHEPQTIIDQLQLIF----AQLQFGNRSVVDPSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 389 FKAKLarfapQFSGYNQHDSQELLAFLLDGLHEDLnrvkhkpyinsrdadgrpdeevadEFWKNHIARNdsIIVDVCQGQ 468
Cdd:cd02668    77 FVKAL-----GLDTGQQQDAQEFSKLFLSLLEAKL------------------------SKSKNPDLKN--IVQDLFRGE 125
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063706404 469 YKSTLVCPICNKVSVTFDPFMYLSLPLQFNTT 500
Cdd:cd02668   126 YSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
318-347 3.38e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 46.21  E-value: 3.38e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1063706404 318 GLLNLGNTCFMNSAIQCLVHTPEFASYFQE 347
Cdd:cd02662     1 GLVNLGNTCFMNSVLQALASLPSLIEYLEE 30
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
793-914 1.94e-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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 44.05  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 793 QCNERRQASKklDLWRLPEVLVIHLKRFSYSRSMKHKLETFVnFPIHDLDLTKYVANKNL-------------------- 852
Cdd:cd02670    84 QCLEQYFNNS--VFAKAPSCLIICLKRYGKTEGKAQKMFKKI-LIPDEIDIPDFVADDPRacskcqlecrvcyddkdfsp 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 853 -SQPQLYELYALTNHYG-GMGSGHYTAHIK-----------LLDDSRWYNFDDSHISH--INEDDVKSG----AAYVLFY 913
Cdd:cd02670   161 tCGKFKLSLCSAVCHRGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDMADRDgvSNGFNIPAArlleDPYMLFY 240

                  .
gi 1063706404 914 R 914
Cdd:cd02670   241 Q 241
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
791-913 3.83e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 43.29  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 791 CPQCNERRQASKKlDLWRLPEVLVIHLKRFSYSRSMKHKLETfvNFPIhdldLTKYVanknlSQPQLYELYALTNHYG-G 869
Cdd:cd02673   129 CSSCKCESAISSE-RIMTFPECLSINLKRYKLRIATSDYLKK--NEEI----MKKYC-----GTDAKYSLVAVICHLGeS 196
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1063706404 870 MGSGHYTAHIK-LLDDSRWYNFDDSHISHINEDDVK---SGAAYVLFY 913
Cdd:cd02673   197 PYDGHYIAYTKeLYNGSSWLYCSDDEIRPVSKNDVStnaRSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
770-913 2.89e-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: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706404 770 LYACLEAFLREEPLVPDEMWFCPQCNERRQASKkldlwrLPEVLVIHLKRFSYSRSMKHKLETFVNFPihdldltkyvan 849
Cdd:cd02665    95 LHECLEAAMFEGEVELLPSDHSVKSGQERWFTE------LPPVLTFELSRFEFNQGRPEKIHDKLEFP------------ 156
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063706404 850 KNLSQPQlYELYALTNHYGGMGSGHYTAHIKLLDDSRWYNFDDSHISHINEDDVKSGA--------AYVLFY 913
Cdd:cd02665   157 QIIQQVP-YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggrnpsAYCLMY 227
 
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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