NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|84452155|ref|NP_001033678|]
View 

ubiquitin carboxyl-terminal hydrolase 14 isoform 2 [Mus musculus]

Protein Classification

ubiquitin carboxyl-terminal hydrolase( domain architecture ID 13005984)

ubiquitin carboxyl-terminal hydrolase is a C19 family peptidase that deubiquitinates polyubiquitinated target proteins; similar to human ubiquitin carboxyl-terminal hydrolase 14 (USP14) and Arabidopsis thaliana ubiquitin carboxyl-terminal hydrolase 6 (UBP6)

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_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-445 2.30e-175

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: 493.39  E-value: 2.30e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 150
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 151 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsgretdsssapavtPSKKKSLIDQYFGVEFETTMKCTESE-EEE 229
Cdd:cd02657  79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 230 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 309
Cdd:cd02657 141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 310 KDVKFPLMLDVYELCTPelqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 389
Cdd:cd02657 221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 84452155 390 HQGRSSSSGHYVSWVRRK-QDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 445
Cdd:cd02657 249 HQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-65 1.74e-34

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


:

Pssm-ID: 340521  Cd Length: 75  Bit Score: 123.50  E-value: 1.74e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84452155   4 YSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKN 65
Cdd:cd16104   2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKD 64
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-445 2.30e-175

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: 493.39  E-value: 2.30e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 150
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 151 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsgretdsssapavtPSKKKSLIDQYFGVEFETTMKCTESE-EEE 229
Cdd:cd02657  79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 230 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 309
Cdd:cd02657 141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 310 KDVKFPLMLDVYELCTPelqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 389
Cdd:cd02657 221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 84452155 390 HQGRSSSSGHYVSWVRRK-QDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 445
Cdd:cd02657 249 HQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
70-444 1.39e-76

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 241.58  E-value: 1.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155    70 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 147
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   148 FPQFAekgeqgQYLQQDANECWIQMMRVLQQKLEaieddsgretdsssapAVTPSKKKSLIDQYFGVEFETTMKCTESEE 227
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLN----------------GNHSTENESLITDLFRGQLKSRLKCLSCGE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   228 EEVTKGKENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYk 299
Cdd:pfam00443 138 VSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   300 eKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVSFRSkfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnc 379
Cdd:pfam00443 217 -NRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------------------------------------------ 253
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84452155   380 gyYDLQAVLTHQGrSSSSGHYVSWVRRKQD-EWIKFDDDKVSIVTPEDILRLsgggdwHIAYVLLY 444
Cdd:pfam00443 254 --YRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-65 1.74e-34

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 123.50  E-value: 1.74e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84452155   4 YSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKN 65
Cdd:cd16104   2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKD 64
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
71-427 5.65e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 92.56  E-value: 5.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIR-SVPELKDALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 142
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 143 flhmafpqfaekgeqgQYLQQDANEcwiqmmrVLQQKLEAIE-DDSGRETDSSSAPavTPSKKKSLIDQYFGVEFETTMK 221
Cdd:COG5533  76 ----------------MGSQEDAHE-------LLGKLLDELKlDLVNSFTIRIFKT--TKDKKKTSTGDWFDIIIELPDQ 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 222 cteseeeevtKGKENQLQLSCFINQeVKYLF---TGLKLRLQEEITKQSPTLQRNAlyiksskISRLPAYLTIQMVRFFY 298
Cdd:COG5533 131 ----------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEELEVQAKQEYEVS-------FVKLPKILTIQLKRFAN 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 299 kekESVNAKVLKDVkfplmldvyelctpelqekmvsfrskfkdleDKKVNQqpnandknsppkeikyePFSFADDIGSNN 378
Cdd:COG5533 193 ---LGGNQKIDTEV-------------------------------DEKFEL-----------------PVKHDQILNIVK 221
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 84452155 379 CGYYDLQAVLTHQGrSSSSGHYVSWVRRKqDEWIKFDDDKVSIVTPEDI 427
Cdd:COG5533 222 ETYYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEA 268
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
5-57 6.52e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.48  E-value: 6.52e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 84452155      5 SVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDD 57
Cdd:smart00213   2 ELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR 54
 
Name Accession Description Interval E-value
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-445 2.30e-175

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: 493.39  E-value: 2.30e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRasGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQ 150
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPELRDALKNYNPARR--GANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLRMAFPQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 151 FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAieddsgretdsssapavtPSKKKSLIDQYFGVEFETTMKCTESE-EEE 229
Cdd:cd02657  79 FAEKQNQGGYAQQDAEECWSQLLSVLSQKLPG------------------AGSKGSFIDQLFGIELETKMKCTESPdEEE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 230 VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 309
Cdd:cd02657 141 VSTESEYKLQCHISITTEVNYLQDGLKKGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYLTVQFVRFFWKRDIQKKAKIL 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 310 KDVKFPLMLDVYELCTPelqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnCGYYDLQAVLT 389
Cdd:cd02657 221 RKVKFPFELDLYELCTP----------------------------------------------------SGYYELVAVIT 248
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 84452155 390 HQGRSSSSGHYVSWVRRK-QDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYG 445
Cdd:cd02657 249 HQGRSADSGHYVAWVRRKnDGKWIKFDDDKVSEVTEEDILKLSGGGDWHIAYILLYK 305
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
70-444 1.39e-76

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 241.58  E-value: 1.39e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155    70 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQyITAALRDLFDSMDK--TSSSIPPIILLQFLHMA 147
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-LLCALRDLFKALQKnsKSSSVSPKMFKKSLGKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   148 FPQFAekgeqgQYLQQDANECWIQMMRVLQQKLEaieddsgretdsssapAVTPSKKKSLIDQYFGVEFETTMKCTESEE 227
Cdd:pfam00443  80 NPDFS------GYKQQDAQEFLLFLLDGLHEDLN----------------GNHSTENESLITDLFRGQLKSRLKCLSCGE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   228 EEVTKGKENQLQLSCFINQEVK--------YLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYk 299
Cdd:pfam00443 138 VSETFEPFSDLSLPIPGDSAELktaslqicFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSY- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   300 eKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVSFRSkfkdledkkvnqqpnandknsppkeikyepfsfaddigsnnc 379
Cdd:pfam00443 217 -NRSTWEKLNTEVEFPLELDLSRYLAEELKPKTNNLQD------------------------------------------ 253
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84452155   380 gyYDLQAVLTHQGrSSSSGHYVSWVRRKQD-EWIKFDDDKVSIVTPEDILRLsgggdwHIAYVLLY 444
Cdd:pfam00443 254 --YRLVAVVVHSG-SLSSGHYIAYIKAYENnRWYKFDDEKVTEVDEETAVLS------SSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
71-444 1.37e-53

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: 179.99  E-value: 1.37e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVpelkdalkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqflhmafpq 150
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFSE----------------------------------------------------------- 21
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 151 faekgeqgqylQQDANECWIQMmrvlqqkLEAIEDdsgrETDSSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEEEEV 230
Cdd:cd02257  22 -----------QQDAHEFLLFL-------LDKLHE----ELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESV 79
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 231 TKGKENQLQLSCFI-NQEVKYLFTGLKLRLQEEIT----KQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKeSVN 305
Cdd:cd02257  80 STEPELFLSLPLPVkGLPQVSLEDCLEKFFKEEILegdnCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNED-GTK 158
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 306 AKVLKDVKFPLMLDVYELCTPElqekmvsfrskfkdledkkvnqqpnandknsppkeikyepfsFADDIGSNNCGYYDLQ 385
Cdd:cd02257 159 EKLNTKVSFPLELDLSPYLSEG------------------------------------------EKDSDSDNGSYKYELV 196
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 386 AVLTHQGRSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDILRLsgGGDWHIAYVLLY 444
Cdd:cd02257 197 AVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLEF--GSLSSSAYILFY 254
Ubl_USP14_like cd16104
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and ...
4-65 1.74e-34

ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 14 (USP14) and similar proteins; USP14 (EC 3.4.19.12), also termed deubiquitinating enzyme 14, or ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, or ubiquitin carboxyl-terminal hydrolase 14, is a component of proteasome regulatory subunit 19S that regulates deubiquitinated proteins entering inside the proteasome core 20S, which plays an inhibitory role in protein degradation. USP14 is also associated with various signal transduction pathways and tumorigenesis, and thus plays an essential role in the development of various types of cancer. Moreover, USP14 mediates the development of cardiac hypertrophy by promoting GSK-3beta phosphorylation, suggesting a role in cardiac hypertrophy treatment. USP14 contains an N-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, and a C-terminal ubiquitin-specific protease (USP) domain.


Pssm-ID: 340521  Cd Length: 75  Bit Score: 123.50  E-value: 1.74e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84452155   4 YSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGN-IKMKN 65
Cdd:cd16104   2 YKVNVKWGKEKFDDVELDTDEPPLVFKAQLFALTGVPPERQKIMVKGGVLKDDDDLSkLKLKD 64
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
69-444 1.81e-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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 100.04  E-value: 1.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  69 PCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASA-----QYITAALRDlfdsmdkTSSSIPPIILLQF 143
Cdd:cd02661   1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMmcaleAHVERALAS-------SGPGSAPRIFSSN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 144 LHMAFPQFaekgeqGQYLQQDANEcwiqMMRVLQQKLEAIEDDSGRETDSSSapavTPSKKKSLIDQYFGVEFETTMKCT 223
Cdd:cd02661  74 LKQISKHF------RIGRQEDAHE----FLRYLLDAMQKACLDRFKKLKAVD----PSSQETTLVQQIFGGYLRSQVKCL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 224 ESEEEEVTKgkENQLQLSCFINQeVKYLFTGLKLRLQEEITKQSPTLQ--RNALYIKSSK---ISRLPAYLTIQMVRF-- 296
Cdd:cd02661 140 NCKHVSNTY--DPFLDLSLDIKG-ADSLEDALEQFTKPEQLDGENKYKceRCKKKVKASKqltIHRAPNVLTIHLKRFsn 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 297 FYKEKESvnakvlKDVKFPLMLDvyelctpeLQEKMvsfrskfkdledkkvnqqpnANDKNSPPKeikyepfsfaddigs 376
Cdd:cd02661 217 FRGGKIN------KQISFPETLD--------LSPYM--------------------SQPNDGPLK--------------- 247
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84452155 377 nncgyYDLQAVLTHQGRSSSSGHYVSWVRRKQDEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 444
Cdd:cd02661 248 -----YKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQK-------AYILFY 303
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 3.78e-23

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


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 99.75  E-value: 3.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPELKDAL---KRYAGALRASgemaSAQYITAALRDLFDSMDkTSSSIPPIILLQFLHMA 147
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFlsdRHSCTCLSCS----PNSCLSCAMDEIFQEFY-YSGDRSPYGPINLLYLS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 148 FpqFAEKgEQGQYLQQDANECWIQMMRVLQQkleaiedDSGRetdsSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEE 227
Cdd:cd02660  77 W--KHSR-NLAGYSQQDAHEFFQFLLDQLHT-------HYGG----DKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 228 eeVTKGKENQLQLSCFInQEVKYLFTGLKLRLQEEITKQSPTLQR--------NALY-----------IKSSKISRLPAY 288
Cdd:cd02660 143 --VSTTVDPFLDLSLDI-PNKSTPSWALGESGVSGTPTLSDCLDRftrpeklgDFAYkcsgcgstqeaTKQLSIKKLPPV 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 289 LTIQMVRFFYKEKESvNAKVLKDVKFPLMLDVYELCTPELQEKMvsfrskfkdledkkvnqqpnanDKNSPPKEIKYepf 368
Cdd:cd02660 220 LCFQLKRFEHSLNKT-SRKIDTYVQFPLELNMTPYTSSSIGDTQ----------------------DSNSLDPDYTY--- 273
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84452155 369 sfaddigsnncgyyDLQAVLTHQGrSSSSGHYVSWVRRKQDEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 444
Cdd:cd02660 274 --------------DLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVLKSQ-------AYLLFY 327
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
70-444 1.88e-22

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


Pssm-ID: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 97.71  E-value: 1.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  70 CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGA---------------LRASGEMASAQYITAALRDLFDSMDKTSSS 134
Cdd:cd02659   3 VGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTeddddnksvplalqrLFLFLQLSESPVKTTELTDKTRSFGWDSLN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 135 IppiillqflhmafpqfaekgeqgqYLQQDANEcwiqMMRVLQQKLEaieddsgreTDSSSAPAvtpskkKSLIDQYFGV 214
Cdd:cd02659  83 T------------------------FEQHDVQE----FFRVLFDKLE---------EKLKGTGQ------EGLIKNLFGG 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 215 EFETTMKCTE----SEEEEVTkgkenqLQLSCFInQEVKYLFTGLKLRLQEEI-------TKQSPTLQRNAlyIKSSKIS 283
Cdd:cd02659 120 KLVNYIICKEcpheSEREEYF------LDLQVAV-KGKKNLEESLDAYVQGETlegdnkyFCEKCGKKVDA--EKGVCFK 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 284 RLPAYLTIQMVRFFYK----EKESVNAKVlkdvKFPLMLDVYELCTPELqekmvsfrsKFKDLEDKKVNQQPnandknsp 359
Cdd:cd02659 191 KLPPVLTLQLKRFEFDfetmMRIKINDRF----EFPLELDMEPYTEKGL---------AKKEGDSEKKDSES-------- 249
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 360 pkeikYEpfsfaddigsnncgyYDLQAVLTHQGrSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDILRLSGGGD--- 435
Cdd:cd02659 250 -----YI---------------YELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECFGGEetq 308
                       410       420
                ....*....|....*....|.
gi 84452155 436 ------------WHIAYVLLY 444
Cdd:cd02659 309 ktydsgprafkrTTNAYMLFY 329
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
71-427 5.65e-21

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 92.56  E-value: 5.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIR-SVPELKDALKRYAGALRA-------SGEMASAQYITAALRDLFDSMDKTSSSIPPiillq 142
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDELLDDLSKELKVlknvirkPEPDLNQEEALKLFTALWSSKEHKVGWIPP----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 143 flhmafpqfaekgeqgQYLQQDANEcwiqmmrVLQQKLEAIE-DDSGRETDSSSAPavTPSKKKSLIDQYFGVEFETTMK 221
Cdd:COG5533  76 ----------------MGSQEDAHE-------LLGKLLDELKlDLVNSFTIRIFKT--TKDKKKTSTGDWFDIIIELPDQ 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 222 cteseeeevtKGKENQLQLSCFINQeVKYLF---TGLKLRLQEEITKQSPTLQRNAlyiksskISRLPAYLTIQMVRFFY 298
Cdd:COG5533 131 ----------TWVNNLKTLQEFIDN-MEELVddeTGVKAKENEELEVQAKQEYEVS-------FVKLPKILTIQLKRFAN 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 299 kekESVNAKVLKDVkfplmldvyelctpelqekmvsfrskfkdleDKKVNQqpnandknsppkeikyePFSFADDIGSNN 378
Cdd:COG5533 193 ---LGGNQKIDTEV-------------------------------DEKFEL-----------------PVKHDQILNIVK 221
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 84452155 379 CGYYDLQAVLTHQGrSSSSGHYVSWVRRKqDEWIKFDDDKVSIVTPEDI 427
Cdd:COG5533 222 ETYYDLVGFVLHQG-SLEGGHYIAYVKKG-GKWEKANDSDVTPVSEEEA 268
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 2.11e-19

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


Pssm-ID: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 88.63  E-value: 2.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPELKDALkrYAGALRASGEMASAQyitaalrdlfdsMDKTSSSIPPIILLQ--FLHMAF 148
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWFMNLEFRKAV--YECNSTEDAELKNMP------------PDKPHEPQTIIDQLQliFAQLQF 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 149 PQ--------FAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDdsgretdsssapavtpSKKKSLIDQYFGVEFETTM 220
Cdd:cd02668  67 GNrsvvdpsgFVKALGLDTGQQQDAQEFSKLFLSLLEAKLSKSKN----------------PDLKNIVQDLFRGEYSYVT 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 221 KCTESEEEEVTKGKENQLQLSCFINQEVKYLFTG-LKlrlQEEITKQS----PTLQRNALYIKSSKISRLPAYLTIQMVR 295
Cdd:cd02668 131 QCSKCGRESSLPSKFYELELQLKGHKTLEECIDEfLK---EEQLTGDNqyfcESCNSKTDATRRIRLTTLPPTLNFQLLR 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 296 FFYKEKESVNAKVLKDVKFPLMLDVYELCTPELQEKMVsfrskfkdledkkvnqqpnandknsppkeikyepfsfaddig 375
Cdd:cd02668 208 FVFDRKTGAKKKLNASISFPEILDMGEYLAESDEGSYV------------------------------------------ 245
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 376 snncgyYDLQAVLTHQGRSSSSGHYVSWVRRKQ-DEWIKFDDDKVS-----------IVTPEDILRLSGGGDWHI---AY 440
Cdd:cd02668 246 ------YELSGVLIHQGVSAYSGHYIAHIKDEQtGEWYKFNDEDVEempgkplklgnSEDPAKPRKSEIKKGTHSsrtAY 319

                ....
gi 84452155 441 VLLY 444
Cdd:cd02668 320 MLVY 323
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 2.56e-19

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


Pssm-ID: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 88.70  E-value: 2.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQcirsvpelkdalkryagALrasgemASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAfpq 150
Cdd:cd02664   1 GLINLGNTCYMNSVLQ-----------------AL------FMAKDFRRQVLSLNLPRLGDSQSVMKKLQLLQAHLM--- 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 151 faekgeqgqyLQQDANECWIQmmRVLQQKLEAIEDDsGRETDSSSAPAVTPSKKKSLIDQYFGVEFETTMKCTESEEEEV 230
Cdd:cd02664  55 ----------HTQRRAEAPPD--YFLEASRPPWFTP-GSQQDCSEYLRYLLDRLHTLIEKMFGGKLSTTIRCLNCNSTSA 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 231 TKGKENQLQLS-CFINQEVKYLFTGLKLRLQEEITKQSPTLQRNAlyIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVL 309
Cdd:cd02664 122 RTERFRDLDLSfPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDA--EKEMKVTGAPEYLILTLLRFSYDQKTHVREKIM 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 310 KDVKFPLMLDVyelctPELQEKMVSFRSKFKDLEDkkvnqqpnandknsppkeikyepfSFADDIGSNNCGYYDLQAVLT 389
Cdd:cd02664 200 DNVSINEVLSL-----PVRVESKSSESPLEKKEEE------------------------SGDDGELVTRQVHYRLYAVVV 250
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84452155 390 HQGRSSSSGHYVSWVR---------------------RKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLY 444
Cdd:cd02664 251 HSGYSSESGHYFTYARdqtdadstgqecpepkdaeenDESKNWYLFNDSRVTFSSFESVQNVTSRFPKDTPYILFY 326
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 1.08e-16

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: 78.87  E-value: 1.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIrsvpelkdalkryagalrasgemasaqyitaalrdlfdsmdktsssippiillqfLHMafpq 150
Cdd:cd02674   1 GLRNLGNTCYMNSILQCL-------------------------------------------------------SAD---- 21
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 151 faekgeqgqylQQDANECWIQMMRVLQqkleaieddsgretdsssapavtpskkkSLIDQYFGVEFETTMKCTESEEEEV 230
Cdd:cd02674  22 -----------QQDAQEFLLFLLDGLH----------------------------SIIVDLFQGQLKSRLTCLTCGKTST 62
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 231 T----------------KGKENQLQlSCFInqevkyLFTGlKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMV 294
Cdd:cd02674  63 TfepftylslpipsgsgDAPKVTLE-DCLR------LFTK-EETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLK 134
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 295 RFFYKEKESVnaKVLKDVKFPLmldvyelctpelqekmvsfrskfKDLEDKKVnqqPNANDKNSPPKeikyepfsfaddi 374
Cdd:cd02674 135 RFSFSRGSTR--KLTTPVTFPL-----------------------NDLDLTPY---VDTRSFTGPFK------------- 173
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84452155 375 gsnncgyYDLQAVLTHQGrSSSSGHYVSWVRRKQ-DEWIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 444
Cdd:cd02674 174 -------YDLYAVVNHYG-SLNGGHYTAYCKNNEtNDWYKFDDSRVTKVSESSVVSSS-------AYILFY 229
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 1.52e-16

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: 80.05  E-value: 1.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIrsvpelkdalkrYAGALRASgemasaqyitaaLRDLFDSM---DKTSSSIPPIILLQFLHMA 147
Cdd:cd02663   1 GLENFGNTCYCNSVLQAL------------YFENLLTC------------LKDLFESIseqKKRTGVISPKKFITRLKRE 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 148 FPQFaekgeqGQYLQQDANECwiqMMRVLQQKLEAIEDDSGRE-TDSSSAPAVTPSKKKSLIDQYF-GVEFETTmKCTES 225
Cdd:cd02663  57 NELF------DNYMHQDAHEF---LNFLLNEIAEILDAERKAEkANRKLNNNNNAEPQPTWVHEIFqGILTNET-RCLTC 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 226 EEeeVTKGKENQLQLSCFINQEVKyLFTGLKLRLQEEitkqspTL-QRNALYI----------KSSKISRLPAYLTIQMV 294
Cdd:cd02663 127 ET--VSSRDETFLDLSIDVEQNTS-ITSCLRQFSATE------TLcGRNKFYCdeccslqeaeKRMKIKKLPKILALHLK 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 295 RFFYKEKESVNAKVLKDVKFPLMLdvyelctpelqekmvsfrskfkdledkkvnqqpnandknsppkeikyEPFSFADDi 374
Cdd:cd02663 198 RFKYDEQLNRYIKLFYRVVFPLEL-----------------------------------------------RLFNTTDD- 229
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84452155 375 GSNNCGYYDLQAVLTHQGRSSSSGHYVSWVrRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHI-AYVLLY 444
Cdd:cd02663 230 AENPDRLYELVAVVVHIGGGPNHGHYVSIV-KSHGGWLLFDDETVEKIDENAVEEFFGDSPNQAtAYVLFY 299
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-405 3.68e-16

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: 78.58  E-value: 3.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRyagalrasgemasaqyitaALRDLFDSMDKTSssippiillqflhmafPQ 150
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE-------------------TPKELFSQVCRKA----------------PQ 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 151 FaeKGeqgqYLQQDANEcwiqMMRVLQQKLEaieddsgretdsssapavtpskkkSLIDQYFGVEFETTMKCTESEEeeV 230
Cdd:cd02667  46 F--KG----YQQQDSHE----LLRYLLDGLR------------------------TFIDSIFGGELTSTIMCESCGT--V 89
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 231 TKGKENQLQLSC----FINQEV-----KYLFTGlklrlQEEITKQSPTLQRNALY-IKSSKISRLPAYLTIQMVRFFyKE 300
Cdd:cd02667  90 SLVYEPFLDLSLprsdEIKSECsiescLKQFTE-----VEILEGNNKFACENCTKaKKQYLISKLPPVLVIHLKRFQ-QP 163
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 301 KESVNAKVLKDVKFPLMLDVYELCTPelqeKMVSFRSKFKDLedkkvnqqpnandknsppkeikyepfsfaddigsnncg 380
Cdd:cd02667 164 RSANLRKVSRHVSFPEILDLAPFCDP----KCNSSEDKSSVL-------------------------------------- 201
                       330       340
                ....*....|....*....|....*
gi 84452155 381 yYDLQAVLTHQGrSSSSGHYVSWVR 405
Cdd:cd02667 202 -YRLYGVVEHSG-TMRSGHYVAYVK 224
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
64-430 6.47e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 75.70  E-value: 6.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  64 KNMELP-CGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALrasGEMASAQYITAALRDLFDSMDKTSssiPPIILLQ 142
Cdd:cd02671  18 RENLLPfVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLI---SSVEQLQSSFLLNPEKYNDELANQ---APRRLLN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 143 FLHMAFPQFaekgeQGqYLQQDANEcwiqmmrVLQQKLEAIEDdsgretdsssapavtpskkksLIDQYFGVEFETTMKC 222
Cdd:cd02671  92 ALREVNPMY-----EG-YLQHDAQE-------VLQCILGNIQE---------------------LVEKDFQGQLVLRTRC 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 223 TESeeEEVTKGKENQLQLSCFInQEVKYLFTGLKLRLQEEITKQSPTLQRN-ALYIKSSKI------------------- 282
Cdd:cd02671 138 LEC--ETFTERREDFQDISVPV-QESELSKSEESSEISPDPKTEMKTLKWAiSQFASVERIvgedkyfcenchhyteaer 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 283 ----SRLPAYLTIQMVRF--------FYKEKESVNAKVLKdvkfPLMLDVYELCTpelqekmvsfrskfkdledkkvnqq 350
Cdd:cd02671 215 sllfDKLPEVITIHLKCFaangsefdCYGGLSKVNTPLLT----PLKLSLEEWST------------------------- 265
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 351 pnandknSPPKEIkyepfsfaddigsnncgyYDLQAVLTHQGRSSSSGHYVSWVRrkqdeWIKFDDDKVSIVTPEDILRL 430
Cdd:cd02671 266 -------KPKNDV------------------YRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSEVKVTEEKDFLEA 315
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
69-441 1.47e-14

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


Pssm-ID: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 74.45  E-value: 1.47e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  69 PCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRAS-----------------GEMASAQYITAALRDLFDSMDKT 131
Cdd:cd02666   1 PAGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELasdypterriggrevsrSELQRSNQFVYELRSLFNDLIHS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 132 -SSSIPPIILLQFLHMAfpqfaekgeqgqylQQDANECWIQMMRVLQQKLEAIED-DSGRETDSSSApavtpskKKSLID 209
Cdd:cd02666  81 nTRSVTPSKELAYLALR--------------QQDVTECIDNVLFQLEVALEPISNaFAGPDTEDDKE-------QSDLIK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 210 QYFGVEF-ETTMKCTESEEEEVTKGKENQLQLScfinqeVKYLFTGlklrlQEEITKQSPTLQRNAL--YIKSSKISRLP 286
Cdd:cd02666 140 RLFSGKTkQQLVPESMGNQPSVRTKTERFLSLL------VDVGKKG-----REIVVLLEPKDLYDALdrYFDYDSLTKLP 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 287 AYLTIQMVRFFYKEKESvnakvlkdvkfpLMLDVYELctPELQEKMVSFRSkfKDLEDKKVNQQPNANDKNSPPKEIKYE 366
Cdd:cd02666 209 QRSQVQAQLAQPLQREL------------ISMDRYEL--PSSIDDIDELIR--EAIQSESSLVRQAQNELAELKHEIEKQ 272
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 367 pfsFAD--DIGsnncgyYDLQAVLTHQGrSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDI-LRLSGGGD--WHIAY 440
Cdd:cd02666 273 ---FDDlkSYG------YRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYNDETVTVVPASEVfLFTLGNTAtpYFLVY 342

                .
gi 84452155 441 V 441
Cdd:cd02666 343 V 343
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-444 4.03e-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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 70.04  E-value: 4.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPelkdALKRYAGALRASGE--------------------MASAQYITaaLRDLFDSMDK 130
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIP----SFQWRYDDLENKFPsdvvdpandlncqlikladgLLSGRYSK--PASLKSENDP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 131 TSSSIPPIILLQFLHMAFPQFAEKGeqgqylQQDANECWiqmmRVLQQKLEaieddsgRETDSSSAPAVTPSkkkslidq 210
Cdd:cd02658  75 YQVGIKPSMFKALIGKGHPEFSTMR------QQDALEFL----LHLIDKLD-------RESFKNLGLNPNDL-------- 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 211 yFGVEFETTMKCTESEEEEVTKGKENQLQL-------SCFINQEVKYLFTGLKLRLQ-----EEITKQSPTLQRNALYIK 278
Cdd:cd02658 130 -FKFMIEDRLECLSCKKVKYTSELSEILSLpvpkdeaTEKEEGELVYEPVPLEDCLKayfapETIEDFCSTCKEKTTATK 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 279 SSKISRLPAYLTIQMVRFFYKEKESvnakvlkdvkfPLMLDVyelctpelqekmvsfrskfkdledkkvnqqpnandkns 358
Cdd:cd02658 209 TTGFKTFPDYLVINMKRFQLLENWV-----------PKKLDV-------------------------------------- 239
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 359 ppkeikyePFSFADDIGSnncGYYDLQAVLTHQGRSSSSGHYVSWVRRKQD---EWIKFDDDKVSIVT-PEDILRLsggg 434
Cdd:cd02658 240 --------PIDVPEELGP---GKYELIAFISHKGTSVHSGHYVAHIKKEIDgegKWVLFNDEKVVASQdPPEMKKL---- 304
                       410
                ....*....|
gi 84452155 435 dwhiAYVLLY 444
Cdd:cd02658 305 ----GYIYFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
70-231 5.08e-08

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 55.27  E-value: 5.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  70 CGLTNLGNTCYMNATVQCIRSVPELKDAL--KRYAGALRASGEMASAQYITAALRDLFDSM-DKTSSSIPPI----ILLQ 142
Cdd:COG5560 266 CGLRNLGNTCYMNSALQCLMHTWELRDYFlsDEYEESINEENPLGMHGSVASAYADLIKQLyDGNLHAFTPSgfkkTIGS 345
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 143 FLHMAfpqfaeKGeqgqYLQQDANECWIQMMRVLQQKLEAIEDDSGRETDSSSAPAVTPSKKK-------------SLID 209
Cdd:COG5560 346 FNEEF------SG----YDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSPGDDVVVKKKakecwwehlkrndSIIT 415
                       170       180
                ....*....|....*....|..
gi 84452155 210 QYFGVEFETTMKCTESEEEEVT 231
Cdd:COG5560 416 DLFQGMYKSTLTCPGCGSVSIT 437
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
354-435 8.04e-08

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 54.88  E-value: 8.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155  354 NDKNSPPKEIKYEPFSFADDIGSNNCGY-YDLQAVLTHQGrSSSSGHYVSWVR-RKQDEWIKFDDDKVSIVTPEDILRLS 431
Cdd:COG5077  402 NDRYEFPLEIDLLPFLDRDADKSENSDAvYVLYGVLVHSG-DLHEGHYYALLKpEKDGRWYKFDDTRVTRATEKEVLEEN 480

                 ....
gi 84452155  432 GGGD 435
Cdd:COG5077  481 FGGD 484
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
5-57 6.52e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.48  E-value: 6.52e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 84452155      5 SVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDD 57
Cdd:smart00213   2 ELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDR 54
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
6-57 3.13e-06

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 44.51  E-value: 3.13e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 84452155   6 VTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDD 57
Cdd:cd17039   1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDK 52
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
382-444 3.19e-06

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 49.50  E-value: 3.19e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84452155 382 YDLQAVLTHQGrSSSSGHYVSWVRRKQDE-WIKFDDDKVSIVTPEDILRLSgggdwhiAYVLLY 444
Cdd:COG5560 764 YDLYAVDNHYG-GLSGGHYTAYARNFANNgWYLFDDSRITEVDPEDSVTSS-------AYVLFY 819
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
5-56 5.57e-06

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 43.77  E-value: 5.57e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 84452155   5 SVTVKWGKEKFEgVELNTDEPPMVFKAQLFALTGVQPARQKVMVKgGTLKDD 56
Cdd:cd17047   2 DFKVIWNKEKYD-VKFPLDSTIAELKEHIETLTGVPPAMQKLMYK-GLLKDD 51
Ubl_UBLCP1 cd01813
ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 ...
4-57 2.70e-05

ubiquitin-like (Ubl) domain found in ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) and similar proteins; UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. It is localized in the nucleus and it contains conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, which directly interacts with the proteasome. Knockdown of UBLCP1 in cells promotes 26S proteasome assembly and selectively enhances nuclear proteasome activity. UBLCP1 may also play a role in the regulation of phosphorylation state of RNA polymerase II C-terminal domain, a key event during mRNA metabolism.


Pssm-ID: 340511  Cd Length: 74  Bit Score: 42.17  E-value: 2.70e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 84452155   4 YSVTVKWGKEKFEgVELNTDEPPMVFKAQLFALTGVQPARQKV--MVKGGTLKDDD 57
Cdd:cd01813   1 ITLIVKWSGKEYP-VTVLSSDTVLDLKQRIFELTGVLPKRQKLlgLKVKGKPADDD 55
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
355-444 4.30e-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: 44.86  E-value: 4.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 355 DKNSPPKEIKYEPfsfaddigsnncgyYDLQAVLTHQGRsSSSGHYVSWV-RRKQDEWIKFDDDKVSIVTPEDILRLS-G 432
Cdd:cd02665 151 DKLEFPQIIQQVP--------------YELHAVLVHEGQ-ANAGHYWAYIyKQSRQEWEKYNDISVTESSWEEVERDSfG 215
                        90
                ....*....|..
gi 84452155 433 GGDWHIAYVLLY 444
Cdd:cd02665 216 GGRNPSAYCLMY 227
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
276-428 1.70e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 43.85  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 276 YIKSSKISRLPAYLTIQMVRF----FYKEKesvNAKVlkdVKFPLmldvyelctpelqekmvsfrskfKDLEDKKVNQQp 351
Cdd:cd02669 323 SLKRYLISRLPKYLIFHIKRFsknnFFKEK---NPTI---VNFPI-----------------------KNLDLSDYVHF- 372
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84452155 352 nanDKNSPPKEIKyepfsfaddigsnncgyYDLQAVLTHQGRSSSSGHYVSWVRRK-QDEWIKFDDDKVSIVTPEDIL 428
Cdd:cd02669 373 ---DKPSLNLSTK-----------------YNLVANIVHEGTPQEDGTWRVQLRHKsTNKWFEIQDLNVKEVLPQLIF 430
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
71-416 7.46e-04

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 41.49  E-value: 7.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155    71 GLTNLGNTCYMNATVQCIRSVPELKDALKRYAGalrasgemasaqyiTAALRD---------LFDSMDKTSSSIppiilL 141
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPLRNLALSHLA--------------TECLKEhcllcelgfLFDMLEKAKGKN-----C 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   142 Q---FLHmAFPQFAEKGEQG--QYLQQDANECWIQMM-----RVLqqkLEAIEDDsGRETDSSSAPAVTPskkkslIDQY 211
Cdd:pfam13423  63 QasnFLR-ALSSIPEASALGllDEDRETNSAISLSSLiqsfnRFL---LDQLSSE-ENSTPPNPSPAESP------LEQL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   212 FGVEFETTMKCT----ESEEEEVT-----------KGKENQLQLSCFINqevkYLFTGLKlrlQEEITK--------QSP 268
Cdd:pfam13423 132 FGIDAETTIRCSncghESVRESSThvldliyprkpSSNNKKPPNQTFSS----ILKSSLE---RETTTKawcekckrYQP 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155   269 TLQRnalyiksSKISRLPAYLtiqmvrffykekeSVNAKVLKDvkfplmldvyelctpelqekmvsfrskfkdlEDKKVN 348
Cdd:pfam13423 205 LESR-------RTVRNLPPVL-------------SLNAALTNE-------------------------------EWRQLW 233
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84452155   349 QQPNandknSPPKEIKyePFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVR--------RKQDEWIKFDD 416
Cdd:pfam13423 234 KTPG-----WLPPEIG--LTLSDDLQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKvadseledPTESQWYLFND 302
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
382-444 9.84e-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: 40.81  E-value: 9.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84452155 382 YDLQAVLTHQGrSSSSGHYVSWvRRK----------------------QDEWIKFDDDKVSIVTPEDILrLSGGgdwhiA 439
Cdd:cd02662 163 YRLRAVVVHYG-SHSSGHYVCY-RRKplfskdkepgsfvrmregpsstSHPWWRISDTTVKEVSESEVL-EQKS-----A 234

                ....*
gi 84452155 440 YVLLY 444
Cdd:cd02662 235 YMLFY 239
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
382-433 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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 40.59  E-value: 1.10e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 84452155 382 YDLQAVLTHQGRSSSSGHYVSWVRR--KQDEWIKFDDDKVSIVTPEDIL---RLSGG 433
Cdd:cd02673 184 YSLVAVICHLGESPYDGHYIAYTKElyNGSSWLYCSDDEIRPVSKNDVStnaRSSGY 240
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-101 1.23e-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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 40.43  E-value: 1.23e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 84452155  71 GLTNLGNTCYMNATVQCIRSVPELKDALKRY 101
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF 31
 
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