NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1604180784|pdb|6H4J|B]
View 

Chain B, Ubiquitin carboxyl-terminal hydrolase 25

Protein Classification

Peptidase_C19I domain-containing protein( domain architecture ID 10119285)

Peptidase_C19I domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-501 1.31e-107

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: 321.43  E-value: 1.31e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 95
Cdd:cd02665   1 GLKNVGNTCWFSAVIQSLF------------------------------------------------------------- 19
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       96 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNG 175
Cdd:cd02665  20 --------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      176 FKDLHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnr 255
Cdd:cd02665  92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ------------ 157
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      256 eitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlps 335
Cdd:cd02665 158 --------IIQ--------------------------------------------------------------------- 160
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      336 tteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqes 415
Cdd:cd02665     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      416 isrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASA 495
Cdd:cd02665 161 ------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSA 222

                ....*.
6H4J_B      496 YCLMYI 501
Cdd:cd02665 223 YCLMYI 228
 
Name Accession Description Interval E-value
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-501 1.31e-107

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: 321.43  E-value: 1.31e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 95
Cdd:cd02665   1 GLKNVGNTCWFSAVIQSLF------------------------------------------------------------- 19
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       96 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNG 175
Cdd:cd02665  20 --------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      176 FKDLHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnr 255
Cdd:cd02665  92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ------------ 157
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      256 eitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlps 335
Cdd:cd02665 158 --------IIQ--------------------------------------------------------------------- 160
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      336 tteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqes 415
Cdd:cd02665     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      416 isrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASA 495
Cdd:cd02665 161 ------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSA 222

                ....*.
6H4J_B      496 YCLMYI 501
Cdd:cd02665 223 YCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
15-271 6.88e-31

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.17  E-value: 6.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B         15 VGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSnaqdlpRNQKEHRNLPFMRELRYLF-ALLVGTKRKYVDPSRAVE 93
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLS------EDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B         94 ILKDAFKS-NDSQQQDVSEFTHKLLDWLEDAFQMKAEEEtdeekPKNPMVELFYGRF------LAVGVlEGKKFEnTEMF 166
Cdd:pfam00443  75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFRGQLksrlkcLSCGE-VSETFE-PFSD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B        167 GQYPLQVNG----FKDLHECLEAAMIE---GEIESLHSENSGKSGQ---EHWFTELPPVLTFELSRFEFNQAlgRPEKIH 236
Cdd:pfam00443 148 LSLPIPGDSaelkTASLQICFLQFSKLeelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKLN 225
                         250       260       270
                  ....*....|....*....|....*....|....*
6H4J_B        237 NKLEFPQVLYLDRYMhrnreiTRIKREEIKRLKDY 271
Cdd:pfam00443 226 TEVEFPLELDLSRYL------AEELKPKTNNLQDY 254
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
3-253 1.64e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 67.20  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B         3 NPYDRKRQdKAPVGLKNVGNTCWFSAVIQSLFNLLEFRRLVlnYKPPSNAQDlPRN------QKEHRNLPFMRElrylfa 76
Cdd:COG5077  183 LNYNSKKE-TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTDHPR-GRDsvalalQRLFYNLQTGEE------ 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B        77 llvgtkrkyvdPSRAVEILKD-AFKSNDS-QQQDVSEFTHKLLDWLEDafQMKaeeetdEEKPKNPMVELFYGRFLAVGV 154
Cdd:COG5077  253 -----------PVDTTELTRSfGWDSDDSfMQHDIQEFNRVLQDNLEK--SMR------GTVVENALNGIFVGKMKSYIK 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       155 LEGKKFEN--TEMFGQYPLQVNGFKDLHECLEAAMiegEIESLHSENSgKSGQEH---------WFTELPPVLTFELSRF 223
Cdd:COG5077  314 CVNVNYESarVEDFWDIQLNVKGMKNLQESFRRYI---QVETLDGDNR-YNAEKHglqdakkgvIFESLPPVLHLQLKRF 389
                        250       260       270
                 ....*....|....*....|....*....|
6H4J_B       224 EFNQALGRPEKIHNKLEFPQVLYLDRYMHR 253
Cdd:COG5077  390 EYDFERDMMVKINDRYEFPLEIDLLPFLDR 419
 
Name Accession Description Interval E-value
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-501 1.31e-107

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: 321.43  E-value: 1.31e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 95
Cdd:cd02665   1 GLKNVGNTCWFSAVIQSLF------------------------------------------------------------- 19
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       96 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNG 175
Cdd:cd02665  20 --------SQQQDVSEFTHLLLDWLEDAFQAAAEAISPGEKSKNPMVQLFYGTFLTEGVLEGKPFCNCETFGQYPLQVNG 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      176 FKDLHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFNQalGRPEKIHNKLEFPQvlyldrymhrnr 255
Cdd:cd02665  92 YGNLHECLEAAMFEGEVELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQ--GRPEKIHDKLEFPQ------------ 157
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      256 eitrikreEIKrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidassppsgsipsqtlps 335
Cdd:cd02665 158 --------IIQ--------------------------------------------------------------------- 160
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      336 tteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrteiendtrdlqes 415
Cdd:cd02665     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      416 isrihrtielmysdksmiQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASA 495
Cdd:cd02665 161 ------------------QVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGGGRNPSA 222

                ....*.
6H4J_B      496 YCLMYI 501
Cdd:cd02665 223 YCLMYI 228
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
15-271 6.88e-31

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 122.17  E-value: 6.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B         15 VGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSnaqdlpRNQKEHRNLPFMRELRYLF-ALLVGTKRKYVDPSRAVE 93
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLS------EDSRYNKDINLLCALRDLFkALQKNSKSSSVSPKMFKK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B         94 ILKDAFKS-NDSQQQDVSEFTHKLLDWLEDAFQMKAEEEtdeekPKNPMVELFYGRF------LAVGVlEGKKFEnTEMF 166
Cdd:pfam00443  75 SLGKLNPDfSGYKQQDAQEFLLFLLDGLHEDLNGNHSTE-----NESLITDLFRGQLksrlkcLSCGE-VSETFE-PFSD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B        167 GQYPLQVNG----FKDLHECLEAAMIE---GEIESLHSENSGKSGQ---EHWFTELPPVLTFELSRFEFNQAlgRPEKIH 236
Cdd:pfam00443 148 LSLPIPGDSaelkTASLQICFLQFSKLeelDDEEKYYCDKCGCKQDaikQLKISRLPPVLIIHLKRFSYNRS--TWEKLN 225
                         250       260       270
                  ....*....|....*....|....*....|....*
6H4J_B        237 NKLEFPQVLYLDRYMhrnreiTRIKREEIKRLKDY 271
Cdd:pfam00443 226 TEVEFPLELDLSRYL------AEELKPKTNNLQDY 254
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
16-501 2.41e-30

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: 119.12  E-value: 2.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFnllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 95
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       96 kdafksndSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAVGVLEGKKFENT----EMFGQYPL 171
Cdd:cd02257  20 --------SEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVstepELFLSLPL 91
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      172 QVNGF--KDLHECLEAAMIEGEIE---SLHSENSGKSG--QEHWFTELPPVLTFELSRFEFNQAlGRPEKIHNKLEFPQV 244
Cdd:cd02257  92 PVKGLpqVSLEDCLEKFFKEEILEgdnCYKCEKKKKQEatKRLKIKKLPPVLIIHLKRFSFNED-GTKEKLNTKVSFPLE 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      245 LYLDRYMhrnreitrikreeikrlkdyltvlqqrlerylsygsgpkrfplvdvlqyalefasskpvctspvddidasspp 324
Cdd:cd02257 171 LDLSPYL------------------------------------------------------------------------- 177
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      325 sgsipsqtlpstteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrte 404
Cdd:cd02257     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      405 iendtrdlqesisrihrTIELMYSDKSMIQVPYRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELV 483
Cdd:cd02257 178 -----------------SEGEKDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVL 240
                       490
                ....*....|....*...
6H4J_B      484 RDsfgGYRNASAYCLMYI 501
Cdd:cd02257 241 EF---GSLSSSAYILFYE 255
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-256 5.70e-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: 111.36  E-value: 5.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFNLLEFRRLVlnYKPPSNAQDLPRNQKE---HRNLPFMRELRYLFALLVGTKRKYVDPSRAV 92
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAV--YECNSTEDAELKNMPPdkpHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       93 eilkDAFKSNDSQQQDVSEFTHKLLDWLEDAFQmkaeeETDEEKPKNPMVELFYGRFLAVGVLE--GKKFENTEMFGQYP 170
Cdd:cd02668  79 ----KALGLDTGQQQDAQEFSKLFLSLLEAKLS-----KSKNPDLKNIVQDLFRGEYSYVTQCSkcGRESSLPSKFYELE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      171 LQVNGFKDLHECLEAAMIEgeiESLHSEN--SGKSGQEH-------WFTELPPVLTFELSRFEFNQALGRPEKIHNKLEF 241
Cdd:cd02668 150 LQLKGHKTLEECIDEFLKE---EQLTGDNqyFCESCNSKtdatrriRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISF 226
                       250
                ....*....|....*
6H4J_B      242 PQVLYLDRYMHRNRE 256
Cdd:cd02668 227 PEILDMGEYLAESDE 241
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
15-502 1.48e-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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 101.57  E-value: 1.48e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       15 VGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQDlprnqKEHRNLPFMRelryLFALLVGTKRKYVDPSRAVEI 94
Cdd:cd02659   3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDD-----NKSVPLALQR----LFLFLQLSESPVKTTELTDKT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       95 LKDAFKSNDS-QQQDVSEFTHKLLDWLEDafQMKAEEEtdeekpKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQV 173
Cdd:cd02659  74 RSFGWDSLNTfEQHDVQEFFRVLFDKLEE--KLKGTGQ------EGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      174 N--GFKDLHECLEAaMIEGEI----ESLHSENSGKSGQEH---WFTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPQV 244
Cdd:cd02659 146 AvkGKKNLEESLDA-YVQGETlegdNKYFCEKCGKKVDAEkgvCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLE 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      245 LYLDRYMHRNREitriKREEIKRLKDYltvlqqrlERYLsygsgpkrfplvdvlqyalefasskpvctspvddidasspp 324
Cdd:cd02659 225 LDMEPYTEKGLA----KKEGDSEKKDS--------ESYI----------------------------------------- 251
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      325 sgsipsqtlpstteqqgalsselpstspssvaaissrsvihkpftqsrippdlpmhpaprhiteeelsvlesclhrwrte 404
Cdd:cd02659     --------------------------------------------------------------------------------
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      405 iendtrdlqesisrihrtielmysdksmiqvpYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVR 484
Cdd:cd02659 252 --------------------------------YELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEE 299
                       490       500       510
                ....*....|....*....|....*....|..
6H4J_B      485 DSFGGY--------------RNASAYCLMYIN 502
Cdd:cd02659 300 ECFGGEetqktydsgprafkRTTNAYMLFYER 331
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
14-501 1.91e-20

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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 92.94  E-value: 1.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       14 PVGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPP--SNAQDLP----------RNQKEHRNLPFMRELRYLFALLVGT 81
Cdd:cd02666   1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESkaELASDYPterriggrevSRSELQRSNQFVYELRSLFNDLIHS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       82 KRKYVDPSRAVEILkdAFKsndsqQQDVSEFTHKLLdwledaFQMKAEEETDEEKPKNPMVELFygrflavgvlegkkfe 161
Cdd:cd02666  81 NTRSVTPSKELAYL--ALR-----QQDVTECIDNVL------FQLEVALEPISNAFAGPDTEDD---------------- 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      162 ntemfgqyPLQVNGFKDLHECLEAAMIEGEIESlhSENSGKSGQEHWFTELPPVltfelsrfefnqalGRPEKIHNKLEF 241
Cdd:cd02666 132 --------KEQSDLIKRLFSGKTKQQLVPESMG--NQPSVRTKTERFLSLLVDV--------------GKKGREIVVLLE 187
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      242 PQVLY--LDRYMHRnreitrikreeikrlkDYLTVLQQRLErylsygsgpkrfplvdvlqyalEFASSKPVCTSPVDDID 319
Cdd:cd02666 188 PKDLYdaLDRYFDY----------------DSLTKLPQRSQ----------------------VQAQLAQPLQRELISMD 229
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      320 assppsgsipsqtlpsTTEQqgalsselpstsPSSVAAISSrsvihkpftqsrippdlpmhpAPRHITEEELSVLEsclh 399
Cdd:cd02666 230 ----------------RYEL------------PSSIDDIDE---------------------LIREAIQSESSLVR---- 256
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      400 rwrtEIENDTRDLQESISRIhrtielmYSDksMIQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSW 479
Cdd:cd02666 257 ----QAQNELAELKHEIEKQ-------FDD--LKSYGYRLHAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPA 323
                       490       500
                ....*....|....*....|..
6H4J_B      480 EELVRDSFGGyrNASAYCLMYI 501
Cdd:cd02666 324 SEVFLFTLGN--TATPYFLVYV 343
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-247 2.06e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 71.37  E-value: 2.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQDlprnqkehrnLPFMRELRYLFALLVGTKRKYVDPSRAV--E 93
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLGDS----------QSVMKKLQLLQAHLMHTQRRAEAPPDYFleA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       94 ILKDAFksNDSQQQDVSEFTHKLLDWLedafqmkaeeetdeekpkNPMVELFYGRFLAVGVL---EGKKFENTEMFGQYP 170
Cdd:cd02664  71 SRPPWF--TPGSQQDCSEYLRYLLDRL------------------HTLIEKMFGGKLSTTIRclnCNSTSARTERFRDLD 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      171 LQVNGFKDLHECLEAAmiegeiESLHSEN-----SGKSGQ----EHWFTELPPVLTFELSRFEFNQALGRPEKIHNKLEF 241
Cdd:cd02664 131 LSFPSVQDLLNYFLSP------EKLTGDNqyyceKCASLQdaekEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSI 204

                ....*.
6H4J_B      242 PQVLYL 247
Cdd:cd02664 205 NEVLSL 210
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-245 1.06e-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 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: 65.82  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPpsnaqdlPRNQKEHRNLPFMRELRYLFALLvGTKRKYVDPSRAVEIL 95
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNP-------ARRGANQSSDNLTNALRDLFDTM-DKKQEPVPPIEFLQLL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       96 KDAF-----KSNDSQ--QQDVSE--------FTHKLL------DWLEDAFQMKAEE---ETDEEKPKNPMVELFYgrFLa 151
Cdd:cd02657  73 RMAFpqfaeKQNQGGyaQQDAEEcwsqllsvLSQKLPgagskgSFIDQLFGIELETkmkCTESPDEEEVSTESEY--KL- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      152 vgvlegkkfeNTEMFGQypLQVNGfkdLHECLEAAMiEGEIEsLHSENSGKSGQ---EHWFTELPPVLTFELSRFEFNQA 228
Cdd:cd02657 150 ----------QCHISIT--TEVNY---LQDGLKKGL-EEEIE-KHSPTLGRDAIytkTSRISRLPKYLTVQFVRFFWKRD 212
                       250
                ....*....|....*..
6H4J_B      229 LGRPEKIHNKLEFPQVL 245
Cdd:cd02657 213 IQKKAKILRKVKFPFEL 229
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
3-253 1.64e-11

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 67.20  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B         3 NPYDRKRQdKAPVGLKNVGNTCWFSAVIQSLFNLLEFRRLVlnYKPPSNAQDlPRN------QKEHRNLPFMRElrylfa 76
Cdd:COG5077  183 LNYNSKKE-TGYVGLRNQGATCYMNSLLQSLFFIAKFRKDV--YGIPTDHPR-GRDsvalalQRLFYNLQTGEE------ 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B        77 llvgtkrkyvdPSRAVEILKD-AFKSNDS-QQQDVSEFTHKLLDWLEDafQMKaeeetdEEKPKNPMVELFYGRFLAVGV 154
Cdd:COG5077  253 -----------PVDTTELTRSfGWDSDDSfMQHDIQEFNRVLQDNLEK--SMR------GTVVENALNGIFVGKMKSYIK 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       155 LEGKKFEN--TEMFGQYPLQVNGFKDLHECLEAAMiegEIESLHSENSgKSGQEH---------WFTELPPVLTFELSRF 223
Cdd:COG5077  314 CVNVNYESarVEDFWDIQLNVKGMKNLQESFRRYI---QVETLDGDNR-YNAEKHglqdakkgvIFESLPPVLHLQLKRF 389
                        250       260       270
                 ....*....|....*....|....*....|
6H4J_B       224 EFNQALGRPEKIHNKLEFPQVLYLDRYMHR 253
Cdd:COG5077  390 EYDFERDMMVKINDRYEFPLEIDLLPFLDR 419
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
437-552 1.52e-10

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 64.12  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       437 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGG--------------YRNASAYCLMYI- 501
Cdd:COG5077  431 YVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGdhpykdkirdhsgiKRFMSAYMLVYLr 510
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
6H4J_B       502 NDKAQFLIQEefnketgqplVGIETLPPDLRDFVEEDNQRFEKELEEWDAQ 552
Cdd:COG5077  511 KSMLDDLLNP----------VAAVDIPPHVEEVLSEEIDKTEVRCKEIDEI 551
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
14-251 2.60e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 61.52  E-value: 2.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       14 PVGLKNVGNTCWFSAVIQSlfnllefrrlvLNYKPPSnAQDLPR----NQKEHRNLPFMRELRYLFALLVGTKRKYVDPS 89
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQC-----------LTHTPPL-ANYLLSrehsKDCCNEGFCMMCALEAHVERALASSGPGSAPR 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       90 RAVEILKdAFKSN--DSQQQDVSEFTHKLLDWLEDA--FQMKAEEETDEE-KPKNPMVELFYGRFLA-VGVLEGKKFENT 163
Cdd:cd02661  69 IFSSNLK-QISKHfrIGRQEDAHEFLRYLLDAMQKAclDRFKKLKAVDPSsQETTLVQQIFGGYLRSqVKCLNCKHVSNT 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      164 -EMFGQYPLQVNGFKDLHECLEAAMiegEIESLHSEN-------SGKSGQEHWFT--ELPPVLTFELSRFEFNQAlgrpE 233
Cdd:cd02661 148 yDPFLDLSLDIKGADSLEDALEQFT---KPEQLDGENkykcercKKKVKASKQLTihRAPNVLTIHLKRFSNFRG----G 220
                       250
                ....*....|....*...
6H4J_B      234 KIHNKLEFPQVLYLDRYM 251
Cdd:cd02661 221 KINKQISFPETLDLSPYM 238
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-268 3.86e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 60.86  E-value: 3.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFnLLEFRRLVLNYKPpsnaqdlprnqkehrnlpfmrelRYLFAllvgtkrkyvdpsravEIL 95
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLS-QTPALRELLSETP-----------------------KELFS----------------QVC 40
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       96 KDAFKSNDSQQQDVSEFTHKLLDWLedafqmkaeeetdeekpkNPMVELFYGRFLAVGV--LEGKKFENT-EMFGQYPLQ 172
Cdd:cd02667  41 RKAPQFKGYQQQDSHELLRYLLDGL------------------RTFIDSIFGGELTSTImcESCGTVSLVyEPFLDLSLP 102
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      173 V----NGFKDLHECL----EAAMIEGEIEsLHSENSGKSGQEHWFTELPPVLTFELSRFeFNQALGRPEKIHNKLEFPQV 244
Cdd:cd02667 103 RsdeiKSECSIESCLkqftEVEILEGNNK-FACENCTKAKKQYLISKLPPVLVIHLKRF-QQPRSANLRKVSRHVSFPEI 180
                       250       260
                ....*....|....*....|....
6H4J_B      245 LYLDRYMHRNREITRIKREEIKRL 268
Cdd:cd02667 181 LDLAPFCDPKCNSSEDKSSVLYRL 204
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
16-240 4.85e-09

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 57.50  E-value: 4.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSL-FNLLEFRRLVLnyKPPSNAQDLprnQKEHRNlPF----MRELRYLFALLVGTKRkyvdpsr 90
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILaLYLPKLDELLD--DLSKELKVL---KNVIRK-PEpdlnQEEALKLFTALWSSKE------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       91 aveiLKDAFKSNDSQQQDVSEFTHKLLDWLEdaFQMKAEEETDEEKPKNPMVELFYGRFLAVGV--LEGKKFENTEMFGQ 168
Cdd:COG5533  68 ----HKVGWIPPMGSQEDAHELLGKLLDELK--LDLVNSFTIRIFKTTKDKKKTSTGDWFDIIIelPDQTWVNNLKTLQE 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6H4J_B      169 YPLQVNGFKDlheclEAAMI-EGEIESLHSENsgKSGQEHWFTELPPVLTFELSRFEFNqalGRPEKIHNKLE 240
Cdd:COG5533 142 FIDNMEELVD-----DETGVkAKENEELEVQA--KQEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVD 204
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
437-501 5.53e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 56.53  E-value: 5.53e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
6H4J_B      437 YRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 501
Cdd:cd02674 174 YDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV--------SSSAYILFYE 230
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
437-501 9.25e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 53.92  E-value: 9.25e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
6H4J_B      437 YRLHAVLVHEGQANAGHYWAYIFDHRESrWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 501
Cdd:cd02660 273 YDLFAVVVHKGTLDTGHYTAYCRQGDGQ-WFKFDDAMITRVSEEEVLK--------SQAYLLFYH 328
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-245 2.50e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 52.71  E-value: 2.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQ-DLPRNQKEHRnlpfMRELRYlfALLVGtkrKYVDPSRAVE- 93
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDvVDPANDLNCQ----LIKLAD--GLLSG---RYSKPASLKSe 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       94 -------ILKDAFKS---------NDSQQQDVSEFTHKLLDWLEDAFQMKAEeetdeekpKNPmVELFygRFLAVGVLEG 157
Cdd:cd02658  72 ndpyqvgIKPSMFKAligkghpefSTMRQQDALEFLLHLIDKLDRESFKNLG--------LNP-NDLF--KFMIEDRLEC 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      158 KKFE--NTEMFGQYPLQVNGFKD----------------LHECLEAAMIEGEIESLHSENSGKSG--QEHWFTELPPVLT 217
Cdd:cd02658 141 LSCKkvKYTSELSEILSLPVPKDeatekeegelvyepvpLEDCLKAYFAPETIEDFCSTCKEKTTatKTTGFKTFPDYLV 220
                       250       260
                ....*....|....*....|....*...
6H4J_B      218 FELSRFEFNQAlGRPEKIHNKLEFPQVL 245
Cdd:cd02658 221 INMKRFQLLEN-WVPKKLDVPIDVPEEL 247
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-248 1.71e-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: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 50.06  E-value: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFNLLEFRRLVLNykppsnaqdlprnQKEHRNLPFMR-------ELRYLFALLVGTKRKyvDP 88
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLS-------------DRHSCTCLSCSpnsclscAMDEIFQEFYYSGDR--SP 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       89 SRAVEILKDAFKSNDS----QQQDVSEFTHKLLDwledafQMKAEEETDEEKPKNPMV------ELFYGRFLAVGVLEGK 158
Cdd:cd02660  67 YGPINLLYLSWKHSRNlagySQQDAHEFFQFLLD------QLHTHYGGDKNEANDESHcnciihQTFSGSLQSSVTCQRC 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      159 KFENT-----------------EMFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSENSG-KSGQEHW----FTELPPVL 216
Cdd:cd02660 141 GGVSTtvdpfldlsldipnkstPSWALGESGVSGTPTLSDCLDRFTRPEKLGDFAYKCSGcGSTQEATkqlsIKKLPPVL 220
                       250       260       270
                ....*....|....*....|....*....|..
6H4J_B      217 TFELSRFEFNQAlGRPEKIHNKLEFPqvLYLD 248
Cdd:cd02660 221 CFQLKRFEHSLN-KTSRKIDTYVQFP--LELN 249
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
437-481 1.71e-06

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 49.80  E-value: 1.71e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
6H4J_B      437 YRLHAVLVHEGQANAGHYWAYIfdHRESRWMKYNDIAVTKSSWEE 481
Cdd:COG5533 225 YDLVGFVLHQGSLEGGHYIAYV--KKGGKWEKANDSDVTPVSEEE 267
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-247 2.34e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 49.62  E-value: 2.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFNLlefrrlvlnykppsnaqdlprnqkehrNLpfMRELRYLFALLVGTKRKY--VDPSRAVE 93
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYFE---------------------------NL--LTCLKDLFESISEQKKRTgvISPKKFIT 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       94 ILKDAFKS-NDSQQQDVSEFTHKLL----DWLEDAFQMKAEEETDEEKPKNPMV-----ELFYG------RFLAVGVLEG 157
Cdd:cd02663  52 RLKRENELfDNYMHQDAHEFLNFLLneiaEILDAERKAEKANRKLNNNNNAEPQptwvhEIFQGiltnetRCLTCETVSS 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      158 KKfentEMFGQYPLQVNGFKDLHECLEAAmieGEIESLHSEN-----SGKSGQEHW----FTELPPVLTFELSRFEFNQA 228
Cdd:cd02663 132 RD----ETFLDLSIDVEQNTSITSCLRQF---SATETLCGRNkfycdECCSLQEAEkrmkIKKLPKILALHLKRFKYDEQ 204
                       250
                ....*....|....*....
6H4J_B      229 LGRPEKIHNKLEFPQVLYL 247
Cdd:cd02663 205 LNRYIKLFYRVVFPLELRL 223
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
437-500 5.01e-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 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: 48.48  E-value: 5.01e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
6H4J_B      437 YRLHAVLVHEGQ-ANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSfGGYRNASAYCLMY 500
Cdd:cd02657 241 YELVAVITHQGRsADSGHYVAWVRRKNDGKWIKFDDDKVSEVTEEDILKLS-GGGDWHIAYILLY 304
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
428-501 5.22e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 45.34  E-value: 5.22e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6H4J_B      428 SDKSMIQVPYRLHAVLVHEG-QANAGHYWAYIFDHREsRWMKYNDIAVTKSSWEELVrdsfggyrNASAYCLMYI 501
Cdd:cd02661 239 SQPNDGPLKYKLYAVLVHSGfSPHSGHYYCYVKSSNG-KWYNMDDSKVSPVSIETVL--------SQKAYILFYI 304
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
105-246 2.95e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 42.74  E-value: 2.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      105 QQQDVSEFTHKLLDWLEDafqmkaeeetdeeKPKNPmvelFYGRF------LAVGVLEGKKFENtemFGQYPLQVNGFKD 178
Cdd:cd02662  33 EQQDAHELFQVLLETLEQ-------------LLKFP----FDGLLasrivcLQCGESSKVRYES---FTMLSLPVPNQSS 92
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6H4J_B      179 LHECLEAAMIEGEIESLHSENSGKSGQEHWFTELPPVLTFELSRFEFN---QALGRPEKIHNKLEFPQVLY 246
Cdd:cd02662  93 GSGTTLEHCLDDFLSTEIIDDYKCDRCQTVIVRLPQILCIHLSRSVFDgrgTSTKNSCKVSFPERLPKVLY 163
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
424-501 3.39e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 43.72  E-value: 3.39e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6H4J_B      424 ELMYSDKSMIqvpYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRdsfggyrnASAYCLMYI 501
Cdd:COG5560 754 EYMVDDPRLI---YDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVT--------SSAYVLFYR 820
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
16-242 1.10e-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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 40.73  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       16 GLKNVGNTCWFSAVIQSLFNllefrrlvlnykppsnaqdlprnqkehrnlpfmrelrylfallvgtkrkyvdpsraveil 95
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B       96 kdafksndsQQQDVSEFTHKLLDWLE----DAF--QMKAEEETDEEKPKNPMVELFYgrFLAVGVLEGKKFENTEMfgqy 169
Cdd:cd02674  21 ---------DQQDAQEFLLFLLDGLHsiivDLFqgQLKSRLTCLTCGKTSTTFEPFT--YLSLPIPSGSGDAPKVT---- 85
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      170 plqvngfkdLHECLEaamiegeiESLHSENSGKSGQEHW--------------FTELPPVLTFELSRFEFNQalGRPEKI 235
Cdd:cd02674  86 ---------LEDCLR--------LFTKEETLDGDNAWKCpkckkkrkatkkltISRLPKVLIIHLKRFSFSR--GSTRKL 146

                ....*..
6H4J_B      236 HNKLEFP 242
Cdd:cd02674 147 TTPVTFP 153
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
437-500 3.45e-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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 39.68  E-value: 3.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6H4J_B      437 YRLHAVLVHEGQANAGHYWAYIFDHR---------------------ESRWMKYNDIAVTKSSWEELVRdsfggyrnASA 495
Cdd:cd02667 202 YRLYGVVEHSGTMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgSGQWYYISDSDVREVSLEEVLK--------SEA 273

                ....*
6H4J_B      496 YCLMY 500
Cdd:cd02667 274 YLLFY 278
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH