NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1465187858|ref|NP_001352408|]
View 

ubiquitin carboxyl-terminal hydrolase 40 isoform 1 [Homo sapiens]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 10119155)

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

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_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
39-344 4.98e-134

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: 412.42  E-value: 4.98e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   39 NLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLT 118
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  119 DSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGL 198
Cdd:cd02659     74 RSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  199 EDALWNmYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLKPFCE 278
Cdd:cd02659    154 EESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTE 232
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1465187858  279 QSE---------LDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHLGNWQFQEEKSKP----DVNLKDLQSEEEIDHP 344
Cdd:cd02659    233 KGLakkegdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPfdpnDAEEECFGGEETQKTY 311
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
39-344 4.98e-134

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: 412.42  E-value: 4.98e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   39 NLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLT 118
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  119 DSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGL 198
Cdd:cd02659     74 RSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  199 EDALWNmYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLKPFCE 278
Cdd:cd02659    154 EESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTE 232
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1465187858  279 QSE---------LDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHLGNWQFQEEKSKP----DVNLKDLQSEEEIDHP 344
Cdd:cd02659    233 KGLakkegdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPfdpnDAEEECFGGEETQKTY 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
42-319 1.49e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 189.96  E-value: 1.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSlgpeelGLFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAA-STADLTDS 120
Cdd:pfam00443    2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSvSPKMFKKS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  121 FGWTSNE--EMRQHDVQELNRILFSALETSLVG---TSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:pfam00443   76 LGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  196 SGLE--DALWNMYVE---EEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFD---FVKCERYKEtscytF 267
Cdd:pfam00443  156 SAELktASLQICFLQfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNrstWEKLNTEVE-----F 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1465187858  268 PLRINLKPFC--EQSELDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNW 319
Cdd:pfam00443  231 PLELDLSRYLaeELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEN-NRW 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
35-319 1.12e-52

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 202.02  E-value: 1.12e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   35 REFTNLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglfeDKDKPDAKvRIIPLQLQRLFAQLLLLDqEAAST 114
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------PTDHPRGR-DSVALALQRLFYNLQTGE-EPVDT 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  115 ADLTDSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKN 194
Cdd:COG5077    257 TELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  195 VSGLEDALWNmYVEEEVFDCDNLYHCGTCDrLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLK 274
Cdd:COG5077    337 MKNLQESFRR-YIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1465187858  275 PF----CEQSELDDleYIYDLFSVIIHKGGCYGGHYHVYIK-DVDhlGNW 319
Cdd:COG5077    415 PFldrdADKSENSD--AVYVLYGVLVHSGDLHEGHYYALLKpEKD--GRW 460
 
Name Accession Description Interval E-value
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
39-344 4.98e-134

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: 412.42  E-value: 4.98e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   39 NLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLT 118
Cdd:cd02659      1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------PPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  119 DSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSGL 198
Cdd:cd02659     74 RSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  199 EDALWNmYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLKPFCE 278
Cdd:cd02659    154 EESLDA-YVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTE 232
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1465187858  279 QSE---------LDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHLGNWQFQEEKSKP----DVNLKDLQSEEEIDHP 344
Cdd:cd02659    233 KGLakkegdsekKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPfdpnDAEEECFGGEETQKTY 311
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
42-319 1.49e-53

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 189.96  E-value: 1.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSlgpeelGLFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAA-STADLTDS 120
Cdd:pfam00443    2 GLVNLGNTCYMNSVLQSLFSIPPFRDYLLR------ISPLSEDSRYNKDINLLCALRDLFKALQKNSKSSSvSPKMFKKS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  121 FGWTSNE--EMRQHDVQELNRILFSALETSLVG---TSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:pfam00443   76 LGKLNPDfsGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  196 SGLE--DALWNMYVE---EEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFD---FVKCERYKEtscytF 267
Cdd:pfam00443  156 SAELktASLQICFLQfskLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYNrstWEKLNTEVE-----F 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1465187858  268 PLRINLKPFC--EQSELDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHlGNW 319
Cdd:pfam00443  231 PLELDLSRYLaeELKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYEN-NRW 283
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
35-319 1.12e-52

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 202.02  E-value: 1.12e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   35 REFTNLSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeelglfeDKDKPDAKvRIIPLQLQRLFAQLLLLDqEAAST 114
Cdd:COG5077    188 KKETGYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGI---------PTDHPRGR-DSVALALQRLFYNLQTGE-EPVDT 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  115 ADLTDSFGWTSNEEMRQHDVQELNRILFSALETSLVGTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKN 194
Cdd:COG5077    257 TELTRSFGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKG 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  195 VSGLEDALWNmYVEEEVFDCDNLYHCGTCDrLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLK 274
Cdd:COG5077    337 MKNLQESFRR-YIQVETLDGDNRYNAEKHG-LQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL 414
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1465187858  275 PF----CEQSELDDleYIYDLFSVIIHKGGCYGGHYHVYIK-DVDhlGNW 319
Cdd:COG5077    415 PFldrdADKSENSD--AVYVLYGVLVHSGDLHEGHYYALLKpEKD--GRW 460
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-325 1.04e-47

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: 173.76  E-value: 1.04e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLG-PEELGLFEDKDKPDAKVRIIPLQLQRLFAQLLLLDQEAASTADLTDS 120
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNsTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  121 FGwTSNEEmrQHDVQELNRILFSALETSLVGTSGHDL---IYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSG 197
Cdd:cd02668     81 LG-LDTGQ--QQDAQEFSKLFLSLLEAKLSKSKNPDLkniVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  198 LEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETSCYTFPLRINLKPFC 277
Cdd:cd02668    158 LEECI-DEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFVFDRKTGAKKKLNASISFPEILDMGEYL 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1465187858  278 EQSELDDleYIYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW-QFQEEK 325
Cdd:cd02668    237 AESDEGS--YVYELSGVLIHQGvSAYSGHYIAHIKD-EQTGEWyKFNDED 283
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
42-339 6.28e-45

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: 163.04  E-value: 6.28e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHftpefrealfslgpeelglfedkdkpdakvriiplqlqrlfaqlllldqeaastadltdsf 121
Cdd:cd02257      1 GLNNLGNTCYLNSVLQALF------------------------------------------------------------- 19
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  122 gwtsneeMRQHDVQELNRILFSALETSLVG--------TSGHDLIYRLYHGTIVNQIVCKECK--NVSERQEDFLDLTVA 191
Cdd:cd02257     20 -------SEQQDAHEFLLFLLDKLHEELKKsskrtsdsSSLKSLIHDLFGGKLESTIVCLECGheSVSTEPELFLSLPLP 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  192 VKNVSG--LEDALwNMYVEEEVFDCDNLYHCGtCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvKCERYKETSCYTFPL 269
Cdd:cd02257     93 VKGLPQvsLEDCL-EKFFKEEILEGDNCYKCE-KKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPL 169
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1465187858  270 RINLKPFCEQSELDDLE----YIYDLFSVIIHKGG-CYGGHYHVYIKDVDHLGNWQFQ----EEKSKPDVNLKDLQSEE 339
Cdd:cd02257    170 ELDLSPYLSEGEKDSDSdngsYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNddkvTEVSEEEVLEFGSLSSS 248
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
41-319 4.13e-37

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: 142.41  E-value: 4.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   41 SGIRNQGGTCYLNSLLQTLHFTPEFREALFSLGpeelglfEDKDKPDAKVRIIpLQLQRLFAQLLLLDQEAASTADLTDS 120
Cdd:cd02661      2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSRE-------HSKDCCNEGFCMM-CALEAHVERALASSGPGSAPRIFSSN 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  121 FGWTSNEEM--RQHDVQELNRILFSALETS----LVGTSGHD-------LIYRLYHGTIVNQIVCKECKNVSERQEDFLD 187
Cdd:cd02661     74 LKQISKHFRigRQEDAHEFLRYLLDAMQKAcldrFKKLKAVDpssqettLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLD 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  188 LTVAVKNVSGLEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvkceRYKETSCYTF 267
Cdd:cd02661    154 LSLDIKGADSLEDAL-EQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFR----GGKINKQISF 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1465187858  268 PLRINLKPFCEQSEldDLEYIYDLFSVIIHKGG-CYGGHYHVYIKDVDhlGNW 319
Cdd:cd02661    229 PETLDLSPYMSQPN--DGPLKYKLYAVLVHSGFsPHSGHYYCYVKSSN--GKW 277
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-319 3.88e-29

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: 119.78  E-value: 3.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGLFEDKDKpdakvrIIPLQLQRLFAQLllldqeaaSTADLTDSF 121
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSPNS------CLSCAMDEIFQEF--------YYSGDRSPY 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  122 G--------WTSNEEM---RQHDVQELNRILFSALETSLVGTSGHD--------LIYRLYHGTIVNQIVCKECKNVSERQ 182
Cdd:cd02660     68 GpinllylsWKHSRNLagySQQDAHEFFQFLLDQLHTHYGGDKNEAndeshcncIIHQTFSGSLQSSVTCQRCGGVSTTV 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  183 EDFLDLTVAVKNVSG---------------LEDALWNMYVEEEVfdCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLL 247
Cdd:cd02660    148 DPFLDLSLDIPNKSTpswalgesgvsgtptLSDCLDRFTRPEKL--GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLK 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1465187858  248 RFNFDFVKCERyKETSCYTFPLRINLKPFCEQSELDDLE-------YIYDLFSVIIHKGGCYGGHYHVYIKdvDHLGNW 319
Cdd:cd02660    226 RFEHSLNKTSR-KIDTYVQFPLELNMTPYTSSSIGDTQDsnsldpdYTYDLFAVVVHKGTLDTGHYTAYCR--QGDGQW 301
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-314 4.61e-28

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: 116.44  E-value: 4.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGlfedkdkpdaKVRIIPLQLQRLFAQLLLLDQEAASTAD--LTD 119
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLG----------DSQSVMKKLQLLQAHLMHTQRRAEAPPDyfLEA 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  120 SF--GWTSNeemRQHDVQELNRILFSALetslvgtsgHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVsg 197
Cdd:cd02664     71 SRppWFTPG---SQQDCSEYLRYLLDRL---------HTLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSV-- 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  198 lEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvKCE-RYK---------------- 260
Cdd:cd02664    137 -QDLL-NYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ-KTHvREKimdnvsinevlslpvr 213
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1465187858  261 -ETSCYTFPLRINLKPFCEQSELDDLEYIYDLFSVIIHKG-GCYGGHYHVYIKDVD 314
Cdd:cd02664    214 vESKSSESPLEKKEEESGDDGELVTRQVHYRLYAVVVHSGySSESGHYFTYARDQT 269
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-325 1.28e-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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 114.33  E-value: 1.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFtpefrEALFSLGPEelgLFEDKDKPDAKVRIIPLQLqrlFAQLLLLDQEAASTADLTDS- 120
Cdd:cd02663      1 GLENFGNTCYCNSVLQALYF-----ENLLTCLKD---LFESISEQKKRTGVISPKK---FITRLKRENELFDNYMHQDAh 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  121 --FGWTSN---EEMRQHDVQELNRILFSALETSlvgTSGHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNV 195
Cdd:cd02663     70 efLNFLLNeiaEILDAERKAEKANRKLNNNNNA---EPQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVEQN 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  196 SGLEDALWNMYvEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDfVKCERYKETScYTFPLRINLKP 275
Cdd:cd02663    147 TSITSCLRQFS-ATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYD-EQLNRYIKLF-YRVVFPLELRL 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1465187858  276 FCEQSELDDLEYIYDLFSVIIHKG-GCYGGHyhvYIKDVDHLGNW-QFQEEK 325
Cdd:cd02663    224 FNTTDDAENPDRLYELVAVVVHIGgGPNHGH---YVSIVKSHGGWlLFDDET 272
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-342 4.69e-26

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 109.40  E-value: 4.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREaLFSLGPEELglfedkdkpdakvriiplqlqrlFAQLLLLDQEaastadltdsF 121
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRE-LLSETPKEL-----------------------FSQVCRKAPQ----------F 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  122 gwtsnEEMRQHDVQELNRILFSALETslvgtsghdLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAV----KNVSG 197
Cdd:cd02667     47 -----KGYQQQDSHELLRYLLDGLRT---------FIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRsdeiKSECS 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  198 LEDALWNMYVEEEVFDcDNLYHCGTCDrlvKAAKSAKLRKLPPFLTVSLLRF----NFDFVKCERYKEtscytFPLRINL 273
Cdd:cd02667    113 IESCLKQFTEVEILEG-NNKFACENCT---KAKKQYLISKLPPVLVIHLKRFqqprSANLRKVSRHVS-----FPEILDL 183
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1465187858  274 KPFCEQSEL---DDLEYIYDLFSVIIHKGGCYGGHYHVYIKDvdhlgnwQFQEEKSKPDVNLKDLQSEEEID 342
Cdd:cd02667    184 APFCDPKCNsseDKSSVLYRLYGVVEHSGTMRSGHYVAYVKV-------RPPQQRLSDLTKSKPAADEAGPG 248
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
130-312 1.07e-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: 106.99  E-value: 1.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  130 RQHDVQELNRILFSALetslvgtsgHDLIYRLYHGTIVNQIVCKECKNVSERQEDFLDLTVAVKNVSG------LEDALw 203
Cdd:cd02674     21 DQQDAQEFLLFLLDGL---------HSIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIPSGSGdapkvtLEDCL- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  204 NMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFvkCERYKETSCYTFPLRI-NLKPFCEQSEL 282
Cdd:cd02674     91 RLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR--GSTRKLTTPVTFPLNDlDLTPYVDTRSF 168
                          170       180       190
                   ....*....|....*....|....*....|
gi 1465187858  283 DDLeYIYDLFSVIIHKGGCYGGHYHVYIKD 312
Cdd:cd02674    169 TGP-FKYDLYAVVNHYGSLNGGHYTAYCKN 197
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
31-311 2.87e-22

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 99.58  E-value: 2.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   31 PPAPREFTNL---SGIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeeLGLFEDKDkpdakvriiplQLQRLFAQLL-L 106
Cdd:cd02671     12 ATSCEKRENLlpfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHL----VSLISSVE-----------QLQSSFLLNPeK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  107 LDQEAASTA---------DLTDSFgwtsnEEMRQHDVQE-LNRILFSAletslvgtsgHDLIYRLYHGTIVNQIVCKECK 176
Cdd:cd02671     77 YNDELANQAprrllnalrEVNPMY-----EGYLQHDAQEvLQCILGNI----------QELVEKDFQGQLVLRTRCLECE 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  177 NVSERQEDFLDLTVAV----------------KNVSGLEDALWNM--YVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKL 238
Cdd:cd02671    142 TFTERREDFQDISVPVqeselskseesseispDPKTEMKTLKWAIsqFASVERIVGEDKYFCENCHHYTEAERSLLFDKL 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1465187858  239 PPFLTVSLLRFNFDFVKCERY----KETSCYTFPLRINLKPFCEQSELDDleyiYDLFSVIIHKGGCYG-GHYHVYIK 311
Cdd:cd02671    222 PEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKLSLEEWSTKPKNDV----YRLFAVVMHSGATISsGHYTAYVR 295
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
42-342 2.26e-17

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 84.08  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHF-TPEFREALFSLgPEELGLFED---KDKPDAKVRiiplQLQRLFAQLLLLDQEaastadl 117
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILALyLPKLDELLDDL-SKELKVLKNvirKPEPDLNQE----EALKLFTALWSSKEH------- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  118 tdSFGWTSNEEmRQHDVQELNRILFSALETSLVGTsghdlIYRLYHGTIVNqivckeckNVSERQEDFLDLTVAVKNVSG 197
Cdd:COG5533     69 --KVGWIPPMG-SQEDAHELLGKLLDELKLDLVNS-----FTIRIFKTTKD--------KKKTSTGDWFDIIIELPDQTW 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  198 LEDalwnmyveEEVFDC--DNLYHCGTCDRLVKAAKSAKLR------------KLPPFLTVSLLRFNFDFVKCERYKETS 263
Cdd:COG5533    133 VNN--------LKTLQEfiDNMEELVDDETGVKAKENEELEvqakqeyevsfvKLPKILTIQLKRFANLGGNQKIDTEVD 204
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1465187858  264 cytFPLRINLKPfcEQSELDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHlgnWqfqEEKSKPDVNLKdlqSEEEID 342
Cdd:COG5533    205 ---EKFELPVKH--DQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKKGGK---W---EKANDSDVTPV---SEEEAI 269
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-325 7.52e-17

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 82.76  E-value: 7.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLgpeELGLFEDKDKPDAKVRIiplQLQRLfAQLLLLDQEAASTADLTDSF 121
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDL---ENKFPSDVVDPANDLNC---QLIKL-ADGLLSGRYSKPASLKSEND 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  122 GWT--------------SNEE---MRQHDVQELNRILFSALETSLVGTSGHDLIyRLYHGTIVNQIVCKECKNV--SERQ 182
Cdd:cd02658     74 PYQvgikpsmfkaligkGHPEfstMRQQDALEFLLHLIDKLDRESFKNLGLNPN-DLFKFMIEDRLECLSCKKVkyTSEL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  183 EDFLDLTV-------------AVKNVSgLEDALwNMYVEEEVFDcdnlYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRF 249
Cdd:cd02658    153 SEILSLPVpkdeatekeegelVYEPVP-LEDCL-KAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRF 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  250 nfDFVKCERYKETSCYTF-PLRINLKPfceqselddleyiYDLFSVIIHKG-GCYGGHYHVYI-KDVDHLGNW-QFQEEK 325
Cdd:cd02658    227 --QLLENWVPKKLDVPIDvPEELGPGK-------------YELIAFISHKGtSVHSGHYVAHIkKEIDGEGKWvLFNDEK 291
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-325 9.47e-17

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 82.38  E-value: 9.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELG--------------LFEDKDK-PDAKVRIIPLQ-LQRLFAQll 105
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARRGanqssdnltnalrdLFDTMDKkQEPVPPIEFLQlLRMAFPQ-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  106 lldqeaastadltdsFGWTSNEEM-RQHDVQELNRILFSALETSLVGTSGH-DLIYRLYHGTIVNQIVCKECKNVSE--- 180
Cdd:cd02657     79 ---------------FAEKQNQGGyAQQDAEECWSQLLSVLSQKLPGAGSKgSFIDQLFGIELETKMKCTESPDEEEvst 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  181 RQEDFLDLTVAVK-NVSGLEDALwNMYVEEEVfdcdnLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFnfdFVKCE-- 257
Cdd:cd02657    144 ESEYKLQCHISITtEVNYLQDGL-KKGLEEEI-----EKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRF---FWKRDiq 214
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1465187858  258 -RYKETSCYTFPLRINLKPFCEQSELddleyiYDLFSVIIHKG-GCYGGHYHVYIKDvDHLGNW-QFQEEK 325
Cdd:cd02657    215 kKAKILRKVKFPFELDLYELCTPSGY------YELVAVITHQGrSADSGHYVAWVRR-KNDGKWiKFDDDK 278
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-309 3.19e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 76.64  E-value: 3.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALfslgpeelglfedkdkpdakvriiplqlqrlfaqlllldqeaastadltdsf 121
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEYL---------------------------------------------------- 28
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  122 gwtsNEEMRQHDVQELNRILFSALETSLVGtsghdliyrLYHGTIVNQIVCKECKNVSE-RQEDFLDLTVAVKNVSG--- 197
Cdd:cd02662     29 ----EEFLEQQDAHELFQVLLETLEQLLKF---------PFDGLLASRIVCLQCGESSKvRYESFTMLSLPVPNQSSgsg 95
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  198 -LEDALWNMYVEEEvfDCDNLyhcgTCDRlvkaaKSAKLRKLPPFLTVSLLRFNFDfVKCERYKETSCYTFPLRINlkpf 276
Cdd:cd02662     96 tTLEHCLDDFLSTE--IIDDY----KCDR-----CQTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP---- 159
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1465187858  277 ceqselddlEYIYDLFSVIIHKGGCYGGHYHVY 309
Cdd:cd02662    160 ---------KVLYRLRAVVVHYGSHSSGHYVCY 183
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
41-311 7.43e-12

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 67.68  E-value: 7.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   41 SGIRNQGGTCYLNSLLQTLHFTPEFRE-ALFSLGPE---------ELG-LF--EDKDKPdakvriIPLQ---LQRLF--- 101
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSHLATEclkehcllcELGfLFdmLEKAKG------KNCQasnFLRALssi 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  102 ---AQLLLLDQEAASTADLTDSfgwtsneemrqHDVQELNRILFS-----ALETSLVGTSGHDLIYRLYHGTIVNQIVCK 173
Cdd:pfam13423   75 peaSALGLLDEDRETNSAISLS-----------SLIQSFNRFLLDqlsseENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  174 ECKNVSERQEDF--LDLTVAVKNVSGLEDALWNMYVE--EEVFDCDNLY--HCGTCDRLVKAAKSAKLRKLPPFLTVSLL 247
Cdd:pfam13423  144 NCGHESVRESSThvLDLIYPRKPSSNNKKPPNQTFSSilKSSLERETTTkaWCEKCKRYQPLESRRTVRNLPPVLSLNAA 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1465187858  248 RFNFDfvkcERYKETSCYTFPLRINLKPFcEQSELDDLEYIYDLFSVIIH-KGGCYGGHYHVYIK 311
Cdd:pfam13423  224 LTNEE----WRQLWKTPGWLPPEIGLTLS-DDLQGDNEIVKYELRGVVVHiGDSGTSGHLVSFVK 283
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
42-312 2.69e-11

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 66.75  E-value: 2.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   42 GIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELGLFEDKDK----PDAKVRIIPL--------QLQRLFAQLLLLDQ 109
Cdd:cd02666      3 GLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTerriGGREVSRSELqrsnqfvyELRSLFNDLIHSNT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  110 EAAS-TADLTdsfgwtsNEEMRQHDVQELNRILFSALETSLVGTSGH-------------DLIYRLYHGTIVNQIVcKEC 175
Cdd:cd02666     83 RSVTpSKELA-------YLALRQQDVTECIDNVLFQLEVALEPISNAfagpdteddkeqsDLIKRLFSGKTKQQLV-PES 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  176 KN----VSERQEDFLDLTVAV------KNVSG----LEDALwnmyveEEVFDcdnlyhcgtCDRLVKA-AKSAKLRKLPP 240
Cdd:cd02666    155 MGnqpsVRTKTERFLSLLVDVgkkgreIVVLLepkdLYDAL------DRYFD---------YDSLTKLpQRSQVQAQLAQ 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  241 FLTVSLLRFNF--------DFVKCERYKETSCYTFPL----RINLKPFCEQSELDDL-EYIYDLFSVIIHKGGCYGGHYH 307
Cdd:cd02666    220 PLQRELISMDRyelpssidDIDELIREAIQSESSLVRqaqnELAELKHEIEKQFDDLkSYGYRLHAVFIHRGEASSGHYW 299

                   ....*
gi 1465187858  308 VYIKD 312
Cdd:cd02666    300 VYIKD 304
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
198-325 1.61e-08

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 59.13  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  198 LEDALwNMYVEEEVFDCDNLYHCGTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDfvKCERYKETSCYTFPL-RINLKPF 276
Cdd:COG5560    677 LQDCL-NEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPIdDLDLSGV 753
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1465187858  277 ceQSELDDLEYIYDLFSVIIHKGGCYGGHYHVYIKDVDHLGNWQFQEEK 325
Cdd:COG5560    754 --EYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSR 800
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
131-338 1.84e-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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 47.55  E-value: 1.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  131 QHDVQELNRILFSALE---------TSLVGTSGHDLiYRLYHGTIVNQIVCKECKnvSERQEDFLDLTVAVKNVSGLEDA 201
Cdd:cd02665     22 QQDVSEFTHLLLDWLEdafqaaaeaISPGEKSKNPM-VQLFYGTFLTEGVLEGKP--FCNCETFGQYPLQVNGYGNLHEC 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  202 LWNMYVEEEVfdcDNLyhcgTCDRLVKAAKSAKLRKLPPFLTVSLLRFNFDFVKCERYKETScyTFPLRINLKPfceqse 281
Cdd:cd02665     99 LEAAMFEGEV---ELL----PSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPEKIHDKL--EFPQIIQQVP------ 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1465187858  282 lddleyiYDLFSVIIHKGGCYGGHYHVYIKDvDHLGNWQFQEEKSKPDVNLKDLQSE 338
Cdd:cd02665    164 -------YELHAVLVHEGQANAGHYWAYIYK-QSRQEWEKYNDISVTESSWEEVERD 212
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
40-190 1.80e-04

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 46.03  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858   40 LSGIRNQGGTCYLNSLLQTLHFTPEFREALFSLGPEELglfEDKDKPDAkvriIPLQLQRLFAQLL--LLDQEAASTADL 117
Cdd:COG5560    265 TCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEES---INEENPLG----MHGSVASAYADLIkqLYDGNLHAFTPS 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1465187858  118 TDSFGWTSNEEM----RQHDVQE------------LNRILFSALETSLVGTSGHD--------------------LIYRL 161
Cdd:COG5560    338 GFKKTIGSFNEEfsgyDQQDSQEfiaflldglhedLNRIIKKPYTSKPDLSPGDDvvvkkkakecwwehlkrndsIITDL 417
                          170       180
                   ....*....|....*....|....*....
gi 1465187858  162 YHGTIVNQIVCKECKNVSERQEDFLDLTV 190
Cdd:COG5560    418 FQGMYKSTLTCPGCGSVSITFDPFMDLTL 446
 
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